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Abz-AAGRK-SLTLnY-amide + H2O
Abz-AAGRK + SLTLnY-amide
-
-
-
-
?
Abz-AAGRKSLTL-3-nitrotyrosine-amide + H2O
Abz-AAGRK + SLTL-3-nitrotyrosine-amide
-
-
-
-
?
Abz-AGRK-SLTnY-amide + H2O
Abz-AGRK + SLTnY-amide
-
-
-
-
?
Abz-AGRK-SnY-amide + H2O
Abz-AGRK + Ser-(3-nitro)Tyr-amide
-
-
-
-
?
Abz-AGRKGTGN-3-nitrotyrosine-amide + H2O
Abz-AGRKGTGN + 3-nitrotyrosine-amide
-
the poorest substrate
-
-
?
Abz-AGRKGTGNnY-amide + H2O
Abz-AGRK + GTGNnY-amide
-
-
-
-
?
Abz-AGRKS-3-nitrotyrosine-amide + H2O
Abz-AGRKS + 3-nitrotyrosine-amide
-
-
-
-
?
Abz-AGRKSLT-3-nitrotyrosine-amide + H2O
Abz-AGRK + SLT-3-nitrotyrosine-amide
-
-
-
-
?
Abz-ARRK-SLTLnY-amide + H2O
Abz-ARRK + SLTLnY-amide
-
-
-
-
?
Abz-ARRKSLTL-3-nitrotyrosine-amide + H2O
Abz-ARRK + SLTL-3-nitrotyrosine-amide
-
-
-
-
?
Abz-FAAGRK-SLTLnY-amide + H2O
Abz-FAAGRK + SLTLnY-amide
-
-
-
-
?
Abz-FAAGRKSLTL-3-nitrotyrosine-amide + H2O
Abz-FAAGRK + SLTL-3-nitrotyrosine-amide
-
-
-
-
?
Abz-GRK-SLTLnY-amide + H2O
Abz-GRK + SLTLnY-amide
-
-
-
-
?
Abz-GRK-SnY-amide + H2O
Abz-GRK + Ser-(3-nitro)Tyr-amide
-
-
-
-
?
Abz-GRKS-3-nitrotyrosine-amide + H2O
Abz-GRK + S-3-nitrotyrosine-amide
-
-
-
-
?
Abz-GRKSLTL-3-nitrotyrosine-amide + H2O
Abz-GRK + SLTL-3-nitrotyrosine-amide
-
-
-
-
?
Abz-KKQR-AGVLnY-amide + H2O
Abz-KKQR + AGVLnY-amide
-
high degree of cleavage efficiency, based on the NS2B/NS3 polyprotein cleavage site
-
-
?
Abz-KKQR-SAGMnY-amide + H2O
Abz-KKQR + SAGMnY-amide
-
-
-
-
?
Abz-KKQRAGVL-3-nitrotyrosine-amide + H2O
Abz-KKQR + AGVL-3-nitrotyrosine-amide
-
is based on the NS2B/NS3 polyprotein cleavage site, shows high degree of cleavage efficiency
-
-
?
Abz-KKQRSAGM-3-nitrotyrosine-amide + H2O
Abz-KKQR + SAGM-3-nitrotyrosine-amide
-
substrates containing the capsid protein prime side sequence SAGM are efficiently hydrolysed
-
-
?
Abz-NRRRR-SAGMnYamide + H2O
?
-
-
-
-
?
Abz-NRRRRSAGM-3-nitrotyrosine-amide + H2O
Abz-NRRRR + SAGM-3-nitrotyrosine-amide
-
-
-
-
?
Abz-RK-SLTLnY-amide + H2O
Abz-RK + SLTLnY-amide
-
-
-
-
?
Abz-RK-SnY-amide + H2O
Abz-RK + SnY-amide
-
-
-
-
?
Abz-RKS-3-nitrotyrosine-amide + H2O
Abz-RK + S-3-nitrotyrosine-amide
-
-
-
-
?
Abz-RKSLTL-3-nitrotyrosine-amide + H2O
Abz-RK + SLTL-3-nitrotyrosine-amide
-
-
-
-
?
Abz-RRRR-3-nitrotyrosine-amide + H2O
Abz-RRRR + 3-nitrotyrosine-amide
-
marginal activity
-
-
?
Abz-RRRR-nY-amide + H2O
Abz-RRRR + 3-nitro-L-tyrosine amide
-
-
-
-
?
Abz-RRRR-SAGMnY-amide + H2O
Abz-RRRR + SAGMnY-amide
-
-
-
-
?
Abz-RRRR-SAGnY-amide + H2O
Abz-RRRR + SAGnY-amide
-
efficient substrate of the NS3 protease, based on the Dengue virus capsid protein processing site
-
-
?
Abz-RRRR-SLTLnY-amide + H2O
Abz-RRRR + SLTLnY-amide
-
-
-
-
?
Abz-RRRR-SnY-amide + H2O
Abz-RRRR + Ser-(3-nitro)Tyr-amide
-
-
-
-
?
Abz-RRRRS-3-nitrotyrosine-amide + H2O
Abz-RRRR + S-3-nitrotyrosine-amide
-
-
-
-
?
Abz-RRRRSAG-3-nitrotyrosine-amide + H2O
Abz-RRRR + SAG-3-nitrotyrosine-amide
-
most efficiently hydrolysed substrate, which contains the tetrabasic non-prime side sequence RRRR of the dengue virus capsid protein
-
-
?
Abz-RRRRSAGM-3-nitrotyrosine-amide + H2O
Abz-RRRR + SAGM-3-nitrotyrosine-amide
-
-
-
-
?
Abz-RRRRSLTL-3-nitrotyrosineamide + H2O
Abz-RRRR + SLTL-3-nitrotyrosineamide
-
-
-
-
?
Abz-SKKR-AGVLnY-amide + H2O
Abz-SKKR + AGVLnY-amide
-
-
-
-
?
Abz-SKKR-SAGMnY-amide + H2O
Abz-SKKR + SAGMnY-amide
-
-
-
-
?
Abz-SKKRAGVL-3-nitrotyrosine-amide + H2O
Abz-SKKR + AGVL-3-nitrotyrosine-amide
-
-
-
-
?
Abz-SKKRSAGM-3-nitrotyrosine-amide + H2O
Abz-SKKR + SAGM-3-nitrotyrosine-amide
-
-
-
-
?
Ac-Arg-Lys-Lys-Arg-7-amido-4-carbamoylmethylcoumarin + H2O
?
-
-
-
?
Ac-D-Arg-Lys-Orn-Arg(Me)-7-amido-4-carbamoylmethylcoumarin + H2O
?
-
-
-
?
Ac-D-Arg-Lys-Orn-Arg-7-amido-4-carbamoylmethylcoumarin + H2O
?
substrate profiling of the P1 position using Ac-Ala-Arg-Leu-X-7-amido-4-carbamoylmethylcoumarin (X is natural or unnatural amino acid)
-
-
?
Ac-D-Lys-Lys-Orn-Arg-7-amido-4-carbamoylmethylcoumarin + H2O
?
-
-
-
?
Ac-Nle-Lys-Lys-Arg-7-amido-4-carbamoylmethylcoumarin + H2O
?
-
-
-
?
Ac-Thr-Arg-Arg-7-amido-4-methylcoumarin + H2O
Ac-Thr-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-Nle-Lys-Arg-Arg-4-methylcoumarin 7-amide + H2O
acetyl-Nle-Lys-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
ADP ATOO-647N + H2O
?
-
affinity of complete NS3 molecule fused to 18 residues of the NS2B cofactor is 10fold higher than that of NS3 helicase
-
-
?
AQRRGRIG + H2O
?
-
three individual batches of the peptide results in 45%, 37%, and 36% cleavages
-
-
?
AQRRGRIG + H2O
AQRR + GRIG
-
three individual batches of the peptide results in AQRR2GRIG 3%, 2%, and 0% cleavages
-
-
?
ATP ATOO-647N + H2O
?
-
affinity of complete NS3 molecule fused to 18 residues of the NS2B cofactor is 10fold higher than that of NS3 helicase
-
-
?
benzoyl-Nle-Lys-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzoyl-Nle-Lys-Arg-Arg + 7-amino-4-methylcoumarin
benzoyl-Nle-Lys-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin + H2O
benzoyl-Nle-Lys-Arg-Arg + 7-amino-3-carbamoylmethyl-4-methylcoumarin
-
-
-
-
?
benzoyl-Nle-Lys-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzoyl-Nle-Lys-Arg-Arg + 7-amino-4-methylcoumarin
benzoyl-Nle-Lys-Arg-Arg-thiobenzylester + H2O
benzoyl-Nle-Lys-Arg-Arg + thiobenzoic acid
-
-
-
-
?
benzoyl-Nle-Lys-Thr-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin + H2O
benzoyl-Nle-Lys-Thr-Arg + 7-amino-3-carbamoylmethyl-4-methylcoumarin
-
-
-
-
?
benzoyl-Nle-Thr-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin + H2O
benzoyl-Nle-Thr-Arg-Arg + 7-amino-3-carbamoylmethyl-4-methylcoumarin
-
-
-
-
?
benzoyl-norleucyl-lysyl-lysyl-argininyl-7-amido-4-methylcoumarin + H2O
benzoyl-norleucyl-lysyl-lysyl-arginine + 7-amino-4-methylcoumarin
benzoyl-Thr-Lys-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin + H2O
benzoyl-Thr-Lys-Arg-Arg + 7-amino-3-carbamoylmethyl-4-methylcoumarin
-
-
-
-
?
benzoyl-Thr-Thr-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin + H2O
benzoyl-Thr-Thr-Arg-Arg + 7-amino-3-carbamoylmethyl-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Gly-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Gly-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Gly-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-Arg-Arg + 7-amino-4-methylcoumarin
-
substrate of isoform DENV-2
-
-
?
Boc-Gly-Arg-Arg-4-methylcoumaryl-7-amide + H2O
Boc-Gly-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Boc-Gly-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Boc-Gly-Arg-Arg-7-amido-4-methylcoumarin + H2O
Boc-Gly-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Boc-Gly-L-Arg-L-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
butyloxycarbonyl-Arg-Val-Arg-Arg-7-amido-4-methylcoumarin + H2O
butyloxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
Bz-Arg-Arg-4-methylcoumaryl-7-amide + H2O
Bz-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Bz-Nle-Lys-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
-
10fold higher affinity for the tetrapeptide than for the tripeptide Boc-Gly-Arg-Arg-7-amido-4-methylcoumarin, and processes it with 34fold greater efficiency
-
-
?
CFP-LQYTKRGGVLWD-YFP + H2O
CFP-LQYTKR + GGVLWD-YFP
CFP-SAAQRRGRIGRN-YFP + H2O
CFP-SAAQRR + GRIGRN-YFP
Dengue virus DEN4 polyprotein + H2O
?
-
involved in processing of downstream nonstructural proteins of the Dengue virus DEN4 polyprotein precursor
-
-
?
Dengue virus polyprotein + H2O
Dengue virus proteins NS3 and NS5
DSSTKRGGSW + H2O
DSSTKR + GGSW
-
each substrate plasmid contains the ER membrane-anchoring domain, a specific cleavage sequence that includes the P6-P1 P19-P49 residues and a fluorescent reporter group (DsRed)
-
-
?
FAEGRRGAAEVLQ + H2O
FAEGRR + GAAEVLQ
-
-
-
-
?
flavivirus polyprotein + H2O
?
-
-
-
?
Flavivirus sp. polyproteins + H2O
?
GLKRFGAK + H2O
GLKR + FGAK
-
-
-
-
?
GLKRGSAK + H2O
GLKR + GSAK
GLKRTGAK + H2O
GLKR + TGAK
Gly-Arg-Arg-4-methylcoumarin 7-amide + H2O
Gly-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
human neural transcription factor Sox2 + H2O
?
the substrate protein exhibits likely cleavage sites for NS2B-NS3pro: K95RLR-A99 and R110PRRK-T115
-
-
?
KKQRAGVL + H2O
?
-
cleaved with 11% efficiency
-
-
?
KLAQRRVFHGVAQ + H2O
KLAQRR + VFHGVAQ
-
-
-
-
?
KPGLKRGGAK + H2O
KPGLKR + GGAK
-
each substrate plasmid contains the ER membrane-anchoring domain, a specific cleavage sequence that includes the P6-P1 P19-P49 residues and a fluorescent reporter group (DsRed)
-
-
?
L-pGlu-L-Arg-L-Thr-L-Lys-L-Arg-7-amido-4-methylcoumarin + H2O
L-pGlu-L-Arg-L-Thr-L-Lys-L-Arg + 7-amino-4-methylcoumarin
LQYTKRGGVLWD + H2O
LQYTKR + GGVLWD
LYKRYGGF + H2O
?
-
cleaved with 48% efficiency
-
-
?
MKTGRRGSANGKQ + H2O
MKTGRR + GSANGKQ
-
-
-
-
?
MLKRGMPR + H2O
?
-
cleaved with 49% efficiency
-
-
?
myelin basic protein + H2O
?
N-(2-aminobenzoyl)-L-valyl-L-lysyl-L-lysyl-N-(3-carbamoyl-4-nitrophenyl)-L-argininamide + H2O
N-(2-aminobenzoyl)-L-valyl-L-lysyl-L-lysyl-L-arginine + 5-amino-2-nitrobenzamide
substrate binding structure in the enzyme's active site (PDB ID 5LC0), modeling. The peptidic substrate with the sequence ABZ-Val-Lys-Lys-Arg-ANB-NH2 is selected as the most efficient peptidic substrate with the nonprimed binding sites of ZIKV NS3 protease
-
-
ir
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin + H2O
N-acetyl-Gly-Arg-Arg + 7-amino-4-methylcoumarin
N-alpha-benzoyl-L-arginine-p-nitroanilide + H2O
N-alpha-benzoyl-L-arginine + p-nitroaniline
N-benzoyl-3-(4-aminocyclohexyl)-L-Ala-L-Arg-4-methylcoumaryl-7-amide + H2O
N-benzoyl-3-(4-aminocyclohexyl)-L-Ala-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzoyl-3-(4-piperidinyl)-L-Ala-L-Arg-4-methylcoumaryl-7-amide + H2O
N-benzoyl-3-(4-piperidinyl)-L-Ala-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzoyl-3-(trans-aminomethylcyclohexyl)-L-Ala-L-Arg-4-methylcoumaryl-7-amide + H2O
N-benzoyl-3-(trans-aminomethylcyclohexyl)-L-Ala-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzoyl-3-pyridyl-L-Ala-L-Arg-4-methylcoumaryl-7-amide + H2O
N-benzoyl-3-pyridyl-L-Ala-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzoyl-4-(aminomethyl)-L-Phe-L-Arg-4-methylcoumaryl-7-amide + H2O
N-benzoyl-4-(aminomethyl)-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzoyl-4-(aminomethyl-N-isopropyl)-L-Phe-L-Arg-4-methylcoumaryl-7-amide + H2O
N-benzoyl-4-(aminomethyl-N-isopropyl)-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzoyl-4-(guanidino)-L-Phe-L-Arg-4-methylcoumaryl-7-amide + H2O
N-benzoyl-4-(guanidino)-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-benzyloxycarbonyl-Arg-Arg-4-methylcoumaryl-7-amide + H2O
N-benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
NQKRYGGF + H2O
?
-
cleaved with 7% efficiency
-
-
?
NRKR + GGPA + H2O
NRKRGGPA
-
two individual batches of the peptide results in 78 and 77% cleavages
-
-
?
NS2B-3181-polyproteins + H2O
?
-
effect of mutations within Gly-Ala-Arg-Arg-+-Ser sequence on cis-cleavage (mutations at P1', P1, P2, P3 and P4), the term-+- depicts the point of cleavage
-
-
?
o-aminobenzoyl-AGKKSAQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AGKK + SAQ-N-(2,4-dinitrophenyl)-ethylenediamine
o-aminobenzoyl-AGKRSAQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AGKR + SAQ-N-(2,4-dinitrophenyl)-ethylenediamine
o-aminobenzoyl-AGRKSAQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AGRK + SAQ-N-(2,4-dinitrophenyl)-ethylenediamine
o-aminobenzoyl-AGRRSAQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AGRR + SAQ-N-(2,4-dinitrophenyl)-ethylenediamine
o-aminobenzoyl-AKKKSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AKKK + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
o-aminobenzoyl-AKKRSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AKKR + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
o-aminobenzoyl-AKRKSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AKRK + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
o-aminobenzoyl-AKRRSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AKRR + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
o-aminobenzoyl-ARKKSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-ARKK + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
o-aminobenzoyl-ARKRSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-ARKR + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
o-aminobenzoyl-ARRKSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-ARRK + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
o-aminobenzoyl-ARRRSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-ARRR + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
o-aminobenzoyl-EVKKQRAGVLWDQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-EVKKQR + AGVLWDQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-FAAGRKSLTLNLQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-FAAGRK + SLTLNLQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-FAAQRRGRIGRNQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
-
-
-
-
?
o-aminobenzoyl-HRREKRSVALQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-HRREKR + SVALQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
is poorly hydrolyzed
-
-
?
o-aminobenzoyl-KKRSSKQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-KKR + SSKQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-KRRSSKQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-KRR + SSKQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-LNRRRRTAGMIIQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-LNRRRR + TAGMIIQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-RTSKKRSWPLNEQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-RTSKKR + SWPLNEQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-SAAGRRGRIGRNQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
-
-
-
-
?
o-aminobenzoyl-SAAQRKGRIGRNQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
-
-
-
-
?
o-aminobenzoyl-SAAQRRGLIGRNQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
-
-
-
-
?
o-aminobenzoyl-SAAQRRGRIGNNQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
-
-
-
-
?
o-aminobenzoyl-SAAQRRGRIGRLQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
-
-
-
-
?
o-aminobenzoyl-SAAQRRGRIGRNQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
-
-
-
-
?
o-aminobenzoyl-SAAQRRGRILRNQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
-
-
-
-
?
o-aminobenzoyl-SAAQRRGRTGRNQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
-
-
-
-
?
o-aminobenzoyl-SAAQRRSRIGRNQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
-
-
-
-
?
o-aminobenzoyl-TTSTRRGTGNIGQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-TTSTRR + GTGNIGQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
PhAc-Lys-Arg-Arg-7-amido-4-methylcoumarin + H2O
PhAc-Lys-Arg-Arg + 7-amino-4-methylcoumarin
-
substrate of isoform DENV-3
-
-
?
phenylacetyl-Lys-Lys-Arg-4-nitroanilide + H2O
phenylacetyl-Lys-Lys-Arg + 4-nitroaniline
protein C of tick-borne encephalitis virus + H2O
?
-
the protein contains two amino acid sequence motifs within the carboxy-terminal region that match the canonical NS2B/3 recognition site. The downstream site is necessary and sufficient for efficient cleavage and virion assembly. In contrast, the upstream site is dispensable and placed in a structural context that renders it largely inaccessible to the viral protease. The NS2B/3 protease predominantly uses the downstream cleavage motif R95-R96-S97 for cleavage
-
-
?
Pyr-Arg-Thr-Lys-Arg-4-methylcoumarin 7-amide + H2O
Pyr-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Pyr-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
Pyr-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
Pyr-RTKR-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
pyroglutamic acid-Arg-Thr-Lys-Arg-4-methylcoumarin 7-amide + H2O
pyroglutamic acid-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
pyroglutamic acid-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
?
pyroglutamic acid-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
pyroglutamic acid-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
pyroglutamic acid-L-Arg-L-Thr-L-Lys-L-Arg-7-amido-4-methylcoumarin + H2O
pyroglutamic acid-L-Arg-L-Thr-L-Lys-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
QRRRGGTA + H2O
QRRR + GGTA
-
two individual batches of the peptide results in 58% cleavage
-
-
?
RIFGRRSIPVNEQ + H2O
RIFGRR + SIPVNEQ
-
-
-
-
?
SAAQRRGRIGRNQ + H2O
SAAQRRGRIGRNQ
-
-
-
-
?
SSRKRRSHDVLTQ + H2O
SSRKRR + SHDVLTQ
-
-
-
-
?
t-butoxycarbonyl-Arg-Val-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine + 7-amino-4-methylcoumarin
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine + 7-amino-4-methylcoumarin
tert-butoxycarbonyl-Gly-Arg-Arg-4-methylcoumarin 7-amide + H2O
tert-butoxycarbonyl-Gly-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
VRGARRSGDVLWQ + H2O
VRGARR + SGDVLWQ
-
-
-
-
?
Yellow fever virus protein + H2O
?
YF17D virus protein + H2O
?
-
cleavage site: Gln-Gln-Arg-+-Ser, i.e. 4A/2K site, this cleavage is prerequisite for processing at the downstream signalase site, determinants of cleavage site specificity for 2B/3 cleavage (site: Gly-Ala-Arg-Arg-+-Ser), the term-+- depicts the point of cleavage
-
-
?
additional information
?
-
ATG16L1 + H2O
?
-
human autophagy-related protein 16-1, high activity
-
-
?
ATG16L1 + H2O
?
-
human autophagy-related protein 16-1
-
-
?
benzoyl-Nle-Lys-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzoyl-Nle-Lys-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzoyl-Nle-Lys-Arg-Arg-4-methylcoumarin 7-amide + H2O
benzoyl-Nle-Lys-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzoyl-Nle-Lys-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzoyl-Nle-Lys-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzoyl-Nle-Lys-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzoyl-Nle-Lys-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzoyl-Nle-Lys-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzoyl-Nle-Lys-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzoyl-norleucyl-lysyl-lysyl-argininyl-7-amido-4-methylcoumarin + H2O
benzoyl-norleucyl-lysyl-lysyl-arginine + 7-amino-4-methylcoumarin
-
-
-
?
benzoyl-norleucyl-lysyl-lysyl-argininyl-7-amido-4-methylcoumarin + H2O
benzoyl-norleucyl-lysyl-lysyl-arginine + 7-amino-4-methylcoumarin
Zika virus Brazilian isolate BeH823339
-
-
-
?
butyloxycarbonyl-Arg-Val-Arg-Arg-7-amido-4-methylcoumarin + H2O
butyloxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
butyloxycarbonyl-Arg-Val-Arg-Arg-7-amido-4-methylcoumarin + H2O
butyloxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
CFP-LQYTKRGGVLWD-YFP + H2O
CFP-LQYTKR + GGVLWD-YFP
-
the artificial substrate contains the natural sequence of the NS2B/NS3 junction and is cleaved efficiently
-
-
?
CFP-LQYTKRGGVLWD-YFP + H2O
CFP-LQYTKR + GGVLWD-YFP
-
the artificial substrate contains the natural sequence of the NS2B/NS3 junction and is cleaved efficiently
-
-
?
CFP-SAAQRRGRIGRN-YFP + H2O
CFP-SAAQRR + GRIGRN-YFP
-
cleavage is barely detectable
-
-
?
CFP-SAAQRRGRIGRN-YFP + H2O
CFP-SAAQRR + GRIGRN-YFP
-
cleavage is barely detectable
-
-
?
Dengue virus polyprotein + H2O
Dengue virus proteins NS3 and NS5
-
-
-
-
?
Dengue virus polyprotein + H2O
Dengue virus proteins NS3 and NS5
-
cleaves NS3/NS4A and NS4B/NS5 junctions, not NS4A/4B junction, cleavage site consists of 2 basic amino acids followed by Gly, Ala or Ser, e.g. Arg-Arg-/-Gly
-
?
eIF4G1 protein + H2O
?
-
human eukaryotic translation initiation factor 4 gamma 1, high activity
-
-
?
eIF4G1 protein + H2O
?
-
human eukaryotic translation initiation factor 4 gamma 1
-
-
?
Flavivirus sp. polyproteins + H2O
?
-
cleavage sites consist of Lys-Arg, Arg-Lys or Arg-Arg (Dengue virus: Gln-Arg) usually followed by Gln, Ala or Ser, cleavage sites: NS2A/2B, NS2B/3, NS3/4A (not SLE virus), NS4B/5 (not SLE virus)
-
-
?
Flavivirus sp. polyproteins + H2O
?
-
involved in processing of downstream nonstructural proteins of the virus polyprotein
-
-
?
GLKRGSAK + H2O
GLKR + GSAK
-
cleaved with 82% efficiency
-
-
?
GLKRGSAK + H2O
GLKR + GSAK
-
cleaved with 9% efficiency
-
-
?
GLKRTGAK + H2O
GLKR + TGAK
-
cleaved with 77% efficiency
-
-
?
GLKRTGAK + H2O
GLKR + TGAK
-
cleaved with 2% efficiency
-
-
?
L-pGlu-L-Arg-L-Thr-L-Lys-L-Arg-7-amido-4-methylcoumarin + H2O
L-pGlu-L-Arg-L-Thr-L-Lys-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-pGlu-L-Arg-L-Thr-L-Lys-L-Arg-7-amido-4-methylcoumarin + H2O
L-pGlu-L-Arg-L-Thr-L-Lys-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
LQYTKRGGVLWD + H2O
LQYTKR + GGVLWD
-
the artificial substrate contains the natural sequence of the NS2B/NS3 junction and is cleaved efficiently
-
-
?
LQYTKRGGVLWD + H2O
LQYTKR + GGVLWD
-
the artificial substrate contains the natural sequence of the NS2B/NS3 junction and is cleaved efficiently
-
-
?
myelin basic protein + H2O
?
-
-
-
?
myelin basic protein + H2O
?
-
-
-
?
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin + H2O
N-acetyl-Gly-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin + H2O
N-acetyl-Gly-Arg-Arg + 7-amino-4-methylcoumarin
Dengue virus type 2 Thailand/16681/1984
-
-
-
?
N-alpha-benzoyl-L-arginine-p-nitroanilide + H2O
N-alpha-benzoyl-L-arginine + p-nitroaniline
-
no substrate-dependent precipitation for either Alkhurma virus mutants or chimeric proteins
-
-
?
N-alpha-benzoyl-L-arginine-p-nitroanilide + H2O
N-alpha-benzoyl-L-arginine + p-nitroaniline
-
-
-
-
?
N-alpha-benzoyl-L-arginine-p-nitroanilide + H2O
N-alpha-benzoyl-L-arginine + p-nitroaniline
-
-
-
?
N-alpha-benzoyl-L-arginine-p-nitroanilide + H2O
N-alpha-benzoyl-L-arginine + p-nitroaniline
-
-
-
?
N-alpha-benzoyl-L-arginine-p-nitroanilide + H2O
N-alpha-benzoyl-L-arginine + p-nitroaniline
-
-
-
?
N-alpha-benzoyl-L-arginine-p-nitroanilide + H2O
N-alpha-benzoyl-L-arginine + p-nitroaniline
dengue virus type I D1/H/IMTSSA/98/606
-
-
-
?
N-alpha-benzoyl-L-arginine-p-nitroanilide + H2O
N-alpha-benzoyl-L-arginine + p-nitroaniline
-
-
-
?
N-alpha-benzoyl-L-arginine-p-nitroanilide + H2O
N-alpha-benzoyl-L-arginine + p-nitroaniline
-
-
-
?
N-alpha-benzoyl-L-arginine-p-nitroanilide + H2O
N-alpha-benzoyl-L-arginine + p-nitroaniline
-
-
-
-
?
N-alpha-benzoyl-L-arginine-p-nitroanilide + H2O
N-alpha-benzoyl-L-arginine + p-nitroaniline
-
-
-
-
?
N-alpha-benzoyl-L-arginine-p-nitroanilide + H2O
N-alpha-benzoyl-L-arginine + p-nitroaniline
-
-
-
-
?
N-alpha-benzoyl-L-arginine-p-nitroanilide + H2O
N-alpha-benzoyl-L-arginine + p-nitroaniline
-
-
-
-
?
N-alpha-benzoyl-L-arginine-p-nitroanilide + H2O
N-alpha-benzoyl-L-arginine + p-nitroaniline
-
-
-
-
?
N-alpha-benzoyl-L-arginine-p-nitroanilide + H2O
N-alpha-benzoyl-L-arginine + p-nitroaniline
-
-
-
-
?
o-aminobenzoyl-AGKKSAQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AGKK + SAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-AGKKSAQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AGKK + SAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-AGKRSAQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AGKR + SAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-AGKRSAQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AGKR + SAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-AGRKSAQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AGRK + SAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-AGRKSAQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AGRK + SAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-AGRRSAQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AGRR + SAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-AGRRSAQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AGRR + SAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-AKKKSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AKKK + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-AKKKSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AKKK + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-AKKRSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AKKR + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-AKKRSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AKKR + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-AKRKSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AKRK + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-AKRKSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AKRK + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-AKRRSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AKRR + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
is most efficiently cleaved. Substrates containing two or three basic amino acids (Arg or Lys) in tandem are best
-
-
?
o-aminobenzoyl-AKRRSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AKRR + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-ARKKSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-ARKK + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-ARKKSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-ARKK + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-ARKRSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-ARKR + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-ARKRSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-ARKR + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-ARRKSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-ARRK + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-ARRKSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-ARRK + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-ARRRSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-ARRR + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-ARRRSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-ARRR + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
phenylacetyl-Lys-Lys-Arg-4-nitroanilide + H2O
phenylacetyl-Lys-Lys-Arg + 4-nitroaniline
-
-
-
-
?
phenylacetyl-Lys-Lys-Arg-4-nitroanilide + H2O
phenylacetyl-Lys-Lys-Arg + 4-nitroaniline
-
chromogenic substrate
-
-
?
Pyr-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
Pyr-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Pyr-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
Pyr-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Pyr-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
Pyr-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
?
pyroglutamic acid-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
pyroglutamic acid-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
?
Dengue virus type 2 16681
-
-
-
-
?
pyroglutamic acid-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
pyroglutamic acid-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
?
-
efficiently cleaved
-
-
?
pyroglutamic acid-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
pyroglutamic acid-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
pyroglutamic acid-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
?
pyroglutamic acid-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
pyroglutamic acid-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
?
t-butoxycarbonyl-Arg-Val-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
t-butoxycarbonyl-Arg-Val-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
?
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
?
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
?
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine + 7-amino-4-methylcoumarin
dengue virus type I D1/H/IMTSSA/98/606
-
-
-
?
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
?
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
?
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
?
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
?
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
?
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine + 7-amino-4-methylcoumarin
dengue virus type I D1/H/IMTSSA/98/606
-
-
-
?
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
?
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
?
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
Yellow fever virus protein + H2O
?
-
-
-
-
?
Yellow fever virus protein + H2O
?
-
cleavage sites: 2A/2B, 2B/3, 3/4A and 4B/5, 4 dibasic sites in nonstructural region of viral polyprotein
-
-
?
additional information
?
-
-
amino-terminal third of NS3 acts as serine protease on nonstructural viral proteins
-
-
?
additional information
?
-
-
strong preference for basic amino acid residues (Arg/Lys) at the P1 position, preference for the P2-4 sites are in the order of Arg > Thr > Gln/Asn/Lys for P2, Lys > Arg > Asn for P3, and Nle > Leu > Lys > Xaa for P4. The prime site substrate specificity is for small and polar amino acids in P1' and P3'
-
-
?
additional information
?
-
-
o-aminobenzoyl-EPEKQRTPQDNQQ-N-(2,4-dinitrophenyl)-ethylenediamine, o-aminobenzoyl-AGRRPAQ-N-(2,4-dinitrophenyl)-ethylenediamine and o-aminobenzoyl-AKRRRPQ-N-(2,4-dinitrophenyl)-ethylenediamine are not hydrolyzed
-
-
?
additional information
?
-
-
peptides with a similar sequence, including GIKRGETD, LQKRGIVE, LSKRQHPG, LVTAGHGQ, and MLKKGMTT, are completely resistant to proteolysis
-
-
?
additional information
?
-
-
the recombinant NS2B-NS3 protease is subject to autolytic cleavage
-
-
?
additional information
?
-
-
preferred substrate size for the dengue virus NS3 protease encompasses the residues from P4 to P3'. The presence of basic residues at the P3 and P4 positions significantly promotes reactivity. Serine is the preferred P1' residue
-
-
?
additional information
?
-
-
preferred substrate size for the Dengue virus NS3 protease encompasses the residues from P4 to P3'. Serine is the preferred P1' residue
-
-
?
additional information
?
-
molecular dynamics simulations of the NS2B/NS3 protease complexes with six peptide substrates (capsid, intNS3, 2A/2B, 4B/5, 3/4A and 2B/3 containing the proteolytic site between P1 and P1' subsites) of DENV type 2 to compare the specificity of the protein-substrate binding recognition
-
-
?
additional information
?
-
-
NS2B-NS3 protease is a trypsin-like protease with a serine protease catalytic triad (His51, Asp75, Ser135) that has a polybasic substrate recognition profile
-
-
?
additional information
?
-
molecular dynamics simulations of the NS2B/NS3 protease complexes with six peptide substrates (capsid, intNS3, 2A/2B, 4B/5, 3/4A and 2B/3 containing the proteolytic site between P1 and P1' subsites) of DENV type 2 to compare the specificity of the protein-substrate binding recognition
-
-
?
additional information
?
-
-
the recombinant NS2B-NS3 protease is subject to autolytic cleavage
-
-
?
additional information
?
-
-
amino-terminal third of NS3 acts as serine protease on nonstructural viral proteins
-
-
?
additional information
?
-
-
NS2/3 auto-cleavage and NS3 protease activity
-
-
?
additional information
?
-
-
interaction of human brain proteins with the Japanese encephalitis virus NS2B-NS3 protease could be involved in the Japanese encephalitis virus induced pathogenesis
-
-
?
additional information
?
-
-
the recombinant NS2B-NS3 protease is subject to autolytic cleavage
-
-
?
additional information
?
-
-
enzyme is highly specific toward lysines at the P2 and P3 positions
-
-
?
additional information
?
-
-
NS3 alone triggers the apoptotic pathways involving caspases-8 and -3. Activation of caspase-8 is essential to initiate apoptotic signaling in NS3-expressing cells
-
-
?
additional information
?
-
-
during purification, incomplete autolytic conversion of the 36 kDa NS2B-NS3pro construct into the individual 30 kDa NS3pro and the NS2B sequence (5-6 kDa). Undergoes self-cleavage during expression and purification at the K48G-G site of the glycine linker
-
-
?
additional information
?
-
-
peptides with a similar sequence, including GIKRGETD, LQKRGIVE, LSKRQHPG, LVTAGHGQ, and MLKKGMTT, are completely resistant to proteolysis. Peptides GLKRFGAK, KKQRAGVL, LYKRYGGF, MLKRGMPR, and NQKRYGGF are also not cleaved
-
-
?
additional information
?
-
-
strict substrate specificity, the (K/R)(K/R)R-GG amino acid motif is optimal. Efficiently cleaves peptides derived from the West Nile virus and Dengue virus capsid protein C, from the NS2A/NS2B junction region and NS4B/NS5 junction region and from NS2B/NS3
-
-
?
additional information
?
-
-
the recombinant NS2B-NS3 protease is subject to autolytic cleavage. It catalyzes two autolytic cleavages. The NS2B/NS3 junction is cleaved before protein purification. A second site at Arg4592Gly460 within the C-terminal helicase region of NS3 is cleaved more slowly. Intramolecular cleavage of both the N-terminal site and the internal helicase site of recombinant NS2B-NS3. The artificial substrates CFP-LQYTHMGGVLWD-YFP and CFP-GGGGHMGGVLWD-YFP are not cleaved
-
-
?
additional information
?
-
-
the substrate that corresponds to the NS4B/NS5 junction site is cleaved in trans, whereas the remaining substrates that correspond to the NS2A/NS2B,NS2B/NS3, and NS3/NS4A proprotein junction sites are poorly processed in trans under experimental conditions
-
-
?
additional information
?
-
-
enzyme is highly specific toward lysines at the P2 and P3 positions
-
-
?
additional information
?
-
-
strict substrate specificity, the (K/R)(K/R)R-GG amino acid motif is optimal. Efficiently cleaves peptides derived from the West Nile virus and Dengue virus capsid protein C, from the NS2A/NS2B junction region and NS4B/NS5 junction region and from NS2B/NS3
-
-
?
additional information
?
-
-
the recombinant NS2B-NS3 protease is subject to autolytic cleavage. It catalyzes two autolytic cleavages. The NS2B/NS3 junction is cleaved before protein purification. A second site at Arg4592Gly460 within the C-terminal helicase region of NS3 is cleaved more slowly. Intramolecular cleavage of both the N-terminal site and the internal helicase site of recombinant NS2B-NS3. The artificial substrates CFP-LQYTHMGGVLWD-YFP and CFP-GGGGHMGGVLWD-YFP are not cleaved
-
-
?
additional information
?
-
-
viral serine protease consisting of viral protein NS2B and NS3
-
-
?
additional information
?
-
-
amino-terminal third of NS3 acts as serine protease on nonstructural viral proteins
-
-
?
additional information
?
-
-
cleavage preference for substrates containing basic amino acids
-
?
additional information
?
-
-
the recombinant NS2B-NS3 protease is subject to autolytic cleavage
-
-
?
additional information
?
-
-
docking studies of the bioactive compounds at the active site of NS2B-NS3 complex also indicate 4-hydroxypanduratin A as potential lead compound for drug development
-
-
?
additional information
?
-
analysis of substrate specificity at substrate positions P1, P2, P3, and P4, and cleavage site parameters, detailed overview. Enzyme cleavage sequence is Ac-Ala-Arg-Leu-X-7-amido-4-carbamoylmethylcoumarin (X is a natural or nonnatural amino acid). The P4-P1 optimal sequence is D-Arg-Lys-Orn-Arg. Most preferred amino acid residues at P1 are L-Arg(Me) and L-Arg. At P2, the NS2B-NS3 protease displays also a very high level of specificity. The most preferred amino acids are the non-proteinogenic L-Orn (100%) and L-Arg(Z)2 (40%). Natural amino acids interact significantly weaker with the S2 pocket, and only L-Lys and L-Arg are recognized (38% and 17%, respectively). Similarly to the S2 and S1 pockets, the S3 site exhibits very narrow specificity. L-Lys is the most preferentially recognized residue at P3 among all tested amino acids. Other amino acids such as L-Orn, L-Arg, L-Arg(Z)2, L-hArg, L-Agp or L-Phe(guan) are recognized with significantly lower affinity. However, all these amino acids have basic side chains. The S4 site exhibits very broad substrate specificity. Almost all amino acids, including unnatural ones, are recognized at the same level at P4 position
-
-
?
additional information
?
-
-
analysis of substrate specificity at substrate positions P1, P2, P3, and P4, and cleavage site parameters, detailed overview. Enzyme cleavage sequence is Ac-Ala-Arg-Leu-X-7-amido-4-carbamoylmethylcoumarin (X is a natural or nonnatural amino acid). The P4-P1 optimal sequence is D-Arg-Lys-Orn-Arg. Most preferred amino acid residues at P1 are L-Arg(Me) and L-Arg. At P2, the NS2B-NS3 protease displays also a very high level of specificity. The most preferred amino acids are the non-proteinogenic L-Orn (100%) and L-Arg(Z)2 (40%). Natural amino acids interact significantly weaker with the S2 pocket, and only L-Lys and L-Arg are recognized (38% and 17%, respectively). Similarly to the S2 and S1 pockets, the S3 site exhibits very narrow specificity. L-Lys is the most preferentially recognized residue at P3 among all tested amino acids. Other amino acids such as L-Orn, L-Arg, L-Arg(Z)2, L-hArg, L-Agp or L-Phe(guan) are recognized with significantly lower affinity. However, all these amino acids have basic side chains. The S4 site exhibits very broad substrate specificity. Almost all amino acids, including unnatural ones, are recognized at the same level at P4 position
-
-
?
additional information
?
-
-
identification of 31 human proteins that are cleaved by the NS2B-NS3 protease. The cofactor NS2B is the principal determinant in ZVP substrate selection
-
-
?
additional information
?
-
no activity with human maltose binding protein
-
-
?
additional information
?
-
-
no activity with human maltose binding protein
-
-
?
additional information
?
-
screening for potential intracellular substrates of NS3, substrate specificity analysis of recombinant enzyme NS2BLNNS3pr using synthesized FRET-type substrate libraries, peptide library preparation. Profiling of the P1-P4 substrate specificity of the NS2B-NS3 protease using a combinatorial chemistry approach and the split-and-mix method. Arg is the only preferred P1 residue of the enzyme, preference for Val at P4, and Lys at P3 and P2, no activity for Trp, Tyr, Asp, and Pro at P3 position, structure-function analysis, overview
-
-
?
additional information
?
-
-
screening for potential intracellular substrates of NS3, substrate specificity analysis of recombinant enzyme NS2BLNNS3pr using synthesized FRET-type substrate libraries, peptide library preparation. Profiling of the P1-P4 substrate specificity of the NS2B-NS3 protease using a combinatorial chemistry approach and the split-and-mix method. Arg is the only preferred P1 residue of the enzyme, preference for Val at P4, and Lys at P3 and P2, no activity for Trp, Tyr, Asp, and Pro at P3 position, structure-function analysis, overview
-
-
?
additional information
?
-
the enzyme performs self-cleavage processes viral polyproteins. Protease activity analysis of gZiPro, eZiPro and bZiPro
-
-
?
additional information
?
-
-
the enzyme performs self-cleavage processes viral polyproteins. Protease activity analysis of gZiPro, eZiPro and bZiPro
-
-
?
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(1'R,2R,4'S,6S,8'R,10'E,12'S,14'E,16'E,21'R)-6-[(2S)-butan-2-yl]-12'-[[(2R,4S,5R,6R)-5-[[(2S,4S,5R,6S)-4,5-dihydroxy-6-methyltetrahydro-2H-pyran-2-yl]oxy]-4,6-dihydroxytetrahydro-2H-pyran-2-yl]oxy]-21',24'-dihydroxy-11',22'-dimethyl-3,4,5,6-tetrahydro-2'H-spiro[pyran-2,6'-[3,7,19]trioxatetracyclo[15.6.1.14,8.020,24]pentacosa[10,14,16,22]tetraen]-2'-one
-
-
(2aE,4E,5'S,6S,6'S,7S,8E,11R,13S,15S,17aS,20Z,20aR)-6'-cyclohexyl-20b-hydroxy-5',6,8,11,19-pentamethyl-20-(methylimino)-17-oxo-3',4',5',6,6',10,11,14,15,17,17a,20,20a,20b-tetradecahydro-2H,7H-spiro[11,15-methanofuro[4,3,2-pq][2,6]benzodioxacyclooctadecine
-
-
(2S)-4-[3-(aminomethyl)phenyl]-2-([(2S)-4-[3-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]butanamide
(2S)-4-[4-(aminomethyl)phenyl]-2-([(2S)-4-[4-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]butanamide
(2S)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-4-[3-(carbamimidamidomethyl)phenyl]-2-([(2S)-4-[3-(carbamimidamidomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)butanamide
(2S)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-4-[4-(carbamimidamidomethyl)phenyl]-2-([(2S)-4-[4-(carbamimidamidomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)butanamide
(3R,7aS)-2,3-bis(4-nitrophenyl)hexahydro-1H-pyrrolo-[1,2-c]imidazol-1-one
-
crystal structure analysis
(3R,7aS)-2-(4-nitrophenyl)-3-(4-(trifluoromethyl)-phenyl)-hexahydro-1H- pyrrolo[1,2-c]-imidazol-1-one
-
below 50% inhibition
(3R,7aS)-2-(4-nitrophenyl)-3-phenylhexahydro-1H-pyrrolo[1,2-c]imidazol-1-one
-
67% inhibition
(3R,7aS)-3-(3-nitrophenyl)-2-(4-nitrophenyl)hexahydro-1H-pyrrolo[1,2-c]imidazol-1-one
-
below 50% inhibition
(3R,7aS)-3-(4-chlorophenyl)-2-(4-nitrophenyl)hexahydro-1H-pyrrolo[1,2-c]-imidazol-1-one
-
below 50% inhibition, crystal structure analysis
(3R,7aS)-3-(4-isopropylphenyl)-2-(4-nitrophenyl)-hexahydro-1H-pyrrolo[1,2-c]imidazol-1-one
-
below 50% inhibition
(3R,7aS)-3-(4-methoxyphenyl)-2-(4-nitrophenyl)hexahydro-1H-pyrrolo[1,2-c]imidazol-1-one
-
below 50% inhibition
(3R,7aS)-3-(4-nitrobenzyl)-2-(4-nitrophenyl)hexahydro-1Hpyrrolo[1,2-c]-imidaz-ol-1-one
-
below 50% inhibition
(3R,7aS)-3-benzyl-2-(4-nitrophenyl)hexahydro-1H-pyrrolo[1,2-c]imidazol-1-one
-
42% inhibition
(3R,7aS)-3-ethyl-2-(4-nitrophenyl)hexahydro-1H-pyrrolo[1,2-c]imidazol-1-one
-
60% inhibition
(3R,7aS)-3-isopropyl-2-(4-nitrophenyl)hexahydro-1H-pyrrolo[1,2-c]imidazol-1-one
-
34% inhibition
(3R,7aS)-3-methyl-2-(4-nitrophenyl)hexahydro-1H-pyrrolo[1,2-c]imidazol-1-one
-
42% inhibition
(3S,7aS)-2,3-bis(4-nitrophenyl)hexahydro-1H-pyrrolo-[1,2-c]imidazol-1-one
-
below 50% inhibition
(3S,7aS)-2-(4-nitrophenyl)-3-(4-(trifluoromethyl)-phenyl)hexahydro-1H- pyrrolo[1,2-c]-imidazol-1-one
-
below 50% inhibition
(3S,7aS)-3-(4-chlorophenyl)-2-(4-nitrophenyl)hexa-hydro-1H-pyrrolo[1,2-c]imidazol-1-one
-
below 50% inhibition
(5-amino-1-phenylsulfonylpyrazol-3-yl) 2-bromobenzoate
-
100.8% inhibition at 0.05 mM
(5-amino-1-phenylsulfonylpyrazol-3-yl)thiophene-2-carboxylate
-
101.4% inhibition at 0.05 mM
(E)-N-(5-(benzylsulfanyl)-1,3,4-thiadiazol-2-yl)-2-cyano-3-(1-((2-cyanophenyl)methyl)-1H-indol-3-yl)prop-2-enamide
-
-
(E)-N-(5-(benzylsulfanyl)-1,3,4-thiadiazol-2-yl)-2-cyano-3-(1-((2-fluorophenyl)methyl)-1H-indol-3-yl)prop-2-enamide
-
-
(E)-N-(5-(benzylsulfanyl)-1,3,4-thiadiazol-2-yl)-2-cyano-3-(1-((4-fluorophenyl)methyl)-1H-indol-3-yl)prop-2-enamide
-
-
(S)-2-(4-nitrophenyl)hexahydro-1H-pyrrolo[1,2-c]imida-zol-1-one
-
39% inhibition
(S)-2-acetamido-6-amino-N-((S)-5-guanidino-1-oxopentan-2-yl)hexanamide
-
inhibitor-enzyme interaction analysis, crystal structure analysis of the complex, NMR spectrometry, overview
1,10-phenanthroline
-
zinc-selective chelator, inhibits NS2/3 auto-cleavage and NS3 protease activity
1-(2,6-difluorophenyl)-2-[1-(4-methoxybenzyl)-3-methyl-1H-pyrazol-5-yl]ethanol
-
-
1-(2,6-difluorophenyl)-2-[1-(4-methoxybenzyl)-3-methyl-1H-pyrazol-5-yl]ethanone
-
-
1-(2-fluorophenyl)-2-[1-(4-methoxybenzyl)-3-methyl-1H-pyrazol-5-yl]ethanone
-
-
1-(3-[[2-(1H-benzimidazol-2-yl)hydrazinyl]methyl]-4-hydroxy-5-[(E)-[2-(3H-indol-2-yl)hydrazinylidene]methyl]phenyl)butane-1,2-dione
-
-
1-(4-methoxybenzyl)-3-methyl-1H-pyrazol-5-yl 2,6-difluoro-3-methylbenzoate
-
-
1-(4-methoxybenzyl)-3-methyl-1H-pyrazol-5-yl 2,6-difluorobenzoate
-
-
1-(4-methoxybenzyl)-3-methyl-1H-pyrazol-5-yl benzoate
-
-
1-(4-[3-[4-(furan-3-yl)phenyl]-5-(piperidin-4-ylmethoxy)pyrazin-2-yl]phenyl)methanamine
1-benzyl-3-methyl-1H-pyrazol-5-yl 2,6-difluoro-3-methylbenzoate
-
-
1-benzyl-3-methyl-1H-pyrazol-5-yl 2,6-difluorobenzoate
-
-
1-[(4-[2-[5-(4-fluorophenyl)-3-(thiophen-2-yl)-4,5-dihydro-1H-pyrazol-1-yl]-1,3-thiazol-4-yl]phenyl)sulfonyl]piperidine
-
-
1-[5-[(4-chloro-5-methyl-3-nitro-1H-pyrazol-1-yl)methyl]furan-2-yl]-2-[1-[2-(diethylamino)ethyl]-1H-benzimidazol-2-yl]ethanone
-
-
2,6-difluoro-benzoyl-Nle-Lys-Arg-Arg-CF3-ketone
-
-
2-(3,4-dihydroxyphenyl)-3,5,7-trihydroxy-4H-chromen-4-one
-
-
2-([[3,6-bis(2,6-dimethylphenyl)-7-oxo-2-thioxo-2,3,6,7-tetrahydro[1,3]thiazolo[4,5-d]pyrimidin-5-yl]sulfanyl]methyl)-7-chloro-4H-pyrido[1,2-a]pyrimidin-4-one
-
-
2-benzyl-N-[2-methyl-4-(4-methylpiperazin-1-yl)phenyl]-1,2,3,4-tetrahydrobenzo[b][1,6]naphthyridine-10-carboxamide
-
compound identified by a pharmacophore model based on X-ray crystal structure and predicted binding patterns. Compound shows good cell-based bioactivity
2-[(E)-[2-(3-bromophenyl)hydrazinylidene]methyl]-N'-[(1E)-2-phenylethylidene]quinoline-4-carbohydrazide
-
-
2-[1-(4-methoxybenzyl)-3-methyl-1H-pyrazol-5-yl]-1-phenylethanol
-
-
2-[1-(4-methoxybenzyl)-3-methyl-1H-pyrazol-5-yl]-1-phenylethanone
-
-
2-[1-(5-methyl-1,3,4-oxadiazol-2-yl)ethyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[[(4-methoxyphenyl)amino]methylidene]cyclohexane-1,3-dione
-
56% inhibition at 0.05 mM
3-[(8-benzoyl-1-methyl[1,2,4]triazolo[4,3-a]quinoxalin-4-yl)amino]benzoic acid
-
-
3-[[6-(3-fluorophenyl)pyridazin-3-yl]amino]-N-[2-(piperidin-1-yl)ethyl]benzamide
-
-
4-(aminomethyl)-Nalpha-benzoyl-N-[(1R)-4-carbamimidamido-1-(dihydroxyboranyl)butyl]-L-phenylalaninamide
cn-716, ZIKV protease in complex with a peptidomimetic boronic acid inhibitor reveals a cyclic diester between the boronic acid and glycerol, enzyme binding structure, binds to the active site, crystal structure analysis, detailed overview
4-(guanidinomethyl)-phenylacetyl-Lys-Lys-Arg-NH2
4-aminobenzoyl-Lys-Arg-Arg
4-aminobenzoyl-Lys-Lys-Arg
4-aminophenylacetyl-Lys-Arg-Arg
4-guanidino-benzoic acid 4-nitrophenyl ester
-
the fold of Dengue NS2B-NS3pro in solution with and without bound inhibitor by nuclear magnetic resonance spectroscopy is analyzed. Multiple paramagnetic lanthanide tags are attached to different sites to generate pseudocontact shifts (PCS). The PCSs show, that in the presence of a positively charged low-molecular weight inhibitor, the enzyme assumes a closed state that is very similar to the closed state previously observed for the West Nile virus protease. To assess the open state, a binding site for a Gd3+ complex is created and paramagnetic relaxation enhancements is measured. The results show that the specific open conformation displayed in the crystal of DEN NS2B-NS3pro is barely populated in solution
4-hydroxypanduratin A
-
cyclohexenyl chalcone derivative, competetive inhibitor, compound from Boesenbergia rotunda (L.) Mansf. Kulturpfl.
4-methylumbelliferyl-alpha-D-mannopyranoside
-
i.e. compound 4282211 of ZINC database, identified by molecular docking. Inhibitor can efficiently bind to the NS2b/NS3 protease without changing the conformation of the protein, most active inhibitor identified, acitve against serotypes DENV1, DENV2, DENV3
4-phenylphenylacetyl-Lys-Arg-Arg
4-phenylphenylacetyl-Lys-Lys-Arg
4-[3-acetyl-5-(2-phenylquinolin-4-yl)-2,3-dihydro-1,3,4-oxadiazol-2-yl]benzoic acid
4-[[3-(azepan-1-yl)-6-oxo-6H-anthra[1,9-cd][1,2]oxazol-5-yl]amino]butanoic acid
-
-
5,6-dichloro-2H-triazolo[4,5-b]pyrazine
NSC157058, the inhibitor decreases ZIKV infection in mice
5-amino-1-((4-methoxyphenyl)sulfonyl)-1H-pyrazol-3-ol
-
-
5-amino-1-((4-methoxyphenyl)sulfonyl)-1H-pyrazol-3-yl benzoate
-
the benzoyl moiety of the inhibitor forms a covalent bond with the side chain of S135. Structure and dynamics of bZiPro-inhibitor complex in solution
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2,3,4-trifluorobenzoate
-
-
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2,3,5,6-tetrafluoro-4-methylbenzoate
-
-
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2,3,6-trifluorobenzoate
-
-
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2,4,5-trifluorobenzoate
-
-
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2,4,6-trifluorobenzoate
-
-
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2,4-difluorobenzoate
-
-
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2,5-difluorobenzoate
-
-
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2,6-dichlorobenzoate
-
-
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2,6-difluoro-3-methylbenzoate
-
-
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2,6-difluorobenzoate
-
-
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2-ethoxybenzoate
-
-
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2-fluoro-3-(trifluoromethyl)benzoate
-
-
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2-methylbenzoate
-
-
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2-nitrobenzoate
-
-
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 3-chlorothiophene-2-carboxylate
-
-
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl thiophene-3-carboxylate
-
-
5-methyl-2-[4-[(4-[[4-(4-methyl-4,5-dihydro-1H-imidazol-3-ium-2-yl)phenyl]amino]-4a,8a-dihydrophthalazin-1-yl)amino]phenyl]-4,5-dihydro-1H-imidazol-3-ium
-
-
5-[(4-chloro-3-nitro-1H-pyrazol-1-yl)methyl]-N-[1-[2-(diethylamino)ethyl]-1H-benzimidazol-2-yl]furan-2-carboxamide
-
-
5-[(E)-2-(2,6-difluorophenyl)ethenyl]-1-(4-methoxybenzyl)-3-methyl-1H-pyrazole
-
-
6-(4-chlorophenyl)-3-[[3-[[6-(4-chlorophenyl)-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazol-3-yl]methoxy]phenoxy]methyl]-[1,2,4]triazolo[3,4-b][1,3,4]thiadiazole
NSC716903
6-methoxy-3-methyl-1H-benzo[de]cinnoline
-
98.2% inhibition at 0.05 mM
7-[(1,3-benzothiazol-2-ylamino)(2-hydroxyphenyl)methyl]quinolin-8-ol
-
-
7-[(1,3-benzothiazol-2-ylamino)(phenyl)methyl]quinolin-8-ol
-
-
7-[(3-hydroxyphenyl)(1,3-thiazol-2-ylamino)methyl]quinolin-8-ol
-
-
7-[1-(methylamino)ethyl]quinolin-8-ol
-
-
acetyl-K-agmatine
-
acetyl-K-agmatine is weakly bound by the ZIKV protease and does inhibit the enzyme. The Arg and Lys residues of acyl-KR-COOH occupy the S1 and S2 sites of the protease, respectively
agathisflavone
-
binds to a specific allosteric binding site of the enzyme
alpinetin
-
compound from Boesenbergia rotunda (L.) Mansf. Kulturpfl.
benzoyl-Lys-Lys(acetyl)-Arg
benzoyl-Lys-Lys(benzoyl)-Arg
benzoyl-Lys-Lys(benzyl)-Arg
benzoyl-Lys-Lys(p-anisoyl)-Arg
benzoyl-Nle-KRR
homology model of the DV2 NS2B/NS3pro complexed with the peptidic inhibitor based on West nile virus structure
benzoyl-Nle-Lys-Arg-Arg-B(OH)2
-
dynamics of NS2B and NS3pro in the presence of the peptidic inhibitor
benzoyl-Nle-Lys-Thr-Arg-H
-
-
Bovine pancreatic trypsin inhibitor
-
Bowman-Birk inhibitor
-
from mung bean
Bz-D-Nle-Lys-Arg-Arg-H
-
-
Bz-N-Me-Nle-Lys-Arg-Arg-H
-
-
Bz-Nle-(3-amino)-Phe-(3-imino)-Phe-(3,4-dimethoxy)-Phe
-
-
Bz-Nle-(3-guanidino)-Phe-(4-guanidino)-Phe-(4-guanidino)-Phe
-
-
Bz-Nle-(4-amino)-Phe-(3-guanidino)-Phe-(4-amino)-Phe
-
-
Bz-Nle-(4-amino)-Phe-(3-guanidino)-Phe-Arg
-
-
Bz-Nle-(4-amino)-Phe-(3-imino)-Phe-Arg
-
-
Bz-Nle-(4-amino)-Phe-(4-guanidino)-Phe-Trp
-
-
Bz-Nle-Arg-(3-guanidino)-Phe-(4-amino)-Phe
-
-
Bz-Nle-D-Lys-Arg-Arg-H
-
-
Bz-Nle-His-(3-guanidino)-Phe-(4-guanidino)-Phe
-
-
Bz-Nle-His-(3-guanidino)-Phe-beta-(2-naphthyl)-Ala
-
-
Bz-Nle-His-(3-imino)-Phe-Arg
-
-
Bz-Nle-His-(4-guanidino)-Phe-(4-guanidino)-Phe
-
-
Bz-Nle-His-(4-guanidino)-Phe-Trp
-
-
Bz-Nle-homo-His-(3-guanidino)-Phe-(4-guanidino)-Phe
-
-
Bz-Nle-homoHis-(3-guanidino)-Phe-Arg
-
-
Bz-Nle-homoHis-(4-guanidino)-Phe-(4-phenyl)-Phe
-
-
Bz-Nle-Lys-Arg-(p-Cl)Phe-H
-
-
Bz-Nle-Lys-Arg-(p-CN)Phe-H
-
-
Bz-Nle-Lys-Arg-(p-guanidinyl)Phe-H
-
-
Bz-Nle-Lys-Arg-(p-Me)Phe-H
-
-
Bz-Nle-Lys-Arg-(p-Ph)Phe-H
-
-
Bz-Nle-Lys-Arg-Arg(OH)-CONH-Bn
-
-
Bz-Nle-Lys-Arg-Arg-B(OH)2
-
-
Bz-Nle-Lys-Arg-Arg-benzoxazole
-
-
Bz-Nle-Lys-Arg-Arg-CF3
-
-
Bz-Nle-Lys-Arg-Arg-NH2
-
-
Bz-Nle-Lys-Arg-Arg-NHSO2CF3
-
-
Bz-Nle-Lys-Arg-Arg-OH
-
-
Bz-Nle-Lys-Arg-Arg-thiazole
-
-
Bz-Nle-Lys-Arg-D-Arg-H
-
-
Bz-Nle-Lys-Arg-homoPhe-H
-
-
Bz-Nle-Lys-D-Arg-Arg-H
-
-
Bz-Nle-Lys-Lys-Arg-B(OH)2
-
-
Bz-Nle-Lys-N-Me-Arg-Arg-H
-
-
Bz-Nle-Lys-Thr-Arg-NH2
-
-
Bz-Nle-Lys-Thr-Arg-OH
-
-
Bz-Nle-N-Me-Lys-Arg-Arg-H
-
-
CaCl2
-
strongly inhibits
cardamonin
-
chalcone, non-competetive inhibitor, compound from Boesenbergia rotunda (L.) Mansf. Kulturpfl.
Cbz-Lys-Arg-(4-GuPhe)P(OPh)2
-
-
Cbz-Lys-Arg-(4-GuPhg)P(OPh)2
-
-
Cbz-Lys-Arg-ArgP(OPh)2
-
-
Cbz-Lys-Arg-LysP(OPh)2
-
-
cyclo(D-arginyl-L-arginyl-L-arginyl-L-lysyl-L-seryl-4-phenyl-L-phenylalanyl-L-seryl-D-arginyl)
-
-
cyclo(D-arginyl-L-arginyl-L-arginyl-L-lysyl-L-seryl-4-phenyl-L-phenylalanyl-L-seryl-D-phenylalanyl)
-
-
cyclo(L-alanylglycyl-L-alanyl-L-arginyl-L-lysyl-L-serylglycyl-L-cysteinyl)
-
-
cyclo(L-alanylglycyl-L-lysyl-L-alanyl-L-lysyl-L-serylglycyl-L-cysteinyl)
-
-
cyclo(L-alanylglycyl-L-lysyl-L-arginyl-L-alanyl-L-serylglycyl-L-cysteinyl)
-
-
cyclo(L-alanylglycyl-L-lysyl-L-arginyl-L-lysyl-L-alanylglycyl-L-cysteinyl)
-
-
cyclo(L-alanylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-L-phenylalanyl-L-cysteinyl)
-
-
cyclo(L-alanylglycyl-L-lysyl-L-arginyl-L-lysyl-L-serylglycyl-L-alanyl)
-
-
cyclo(L-alanylglycyl-L-lysyl-L-arginyl-L-lysyl-L-serylglycyl-L-cysteinyl)
-
-
cyclo(L-arginyl-L-lysyl-L-seryl-4-phenyl-L-phenylalanyl-L-seryl-D-phenylalanyl-D-prolyl-L-arginyl)
-
-
cyclo(L-arginyl-L-lysyl-L-seryl-4-phenyl-L-phenylalanyl-L-seryl-D-phenylalanyl-D-prolyl-L-lysyl)
-
-
cyclo-[L-Pro-L-Phe-L-Leu-L-Lys-Gly-L-Val-L-Tyr-L-Glu-L-Asp-L-Phe-L-Phe-Gly]
-
-
cyclopropionyl-Lys-Lys-Arg
cyclo[3-(1-naphthyl)-L-alanyl-D-phenylalanyl-D-arginyl-L-arginyl-L-arginyl-L-lysyl-L-alanyl-(2S)-2-amino-4-phenylbutanoyl]
-
-
cyclo[3-(1-naphthyl)-L-alanyl-D-phenylalanyl-D-arginyl-L-arginyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl]
-
-
cyclo[3-(1-naphthyl)-L-alanyl-D-phenylalanyl-D-arginyl-L-arginyl-L-arginyl-L-lysyl-N6-[CH2NH]-L-alanyl-(2S)-2-amino-4-phenylbutanoyl]
-
-
cyclo[3-(2-naphthyl)-D-alanyl-D-arginyl-L-arginyl-L-arginyl-L-lysyl-3-(2-naphthyl)-D-alanyl-(2S)-2-amino-4-phenylbutanoyl-L-phenylalanyl]
-
-
cyclo[3-(2-naphthyl)-D-alanyl-D-arginyl-L-arginyl-L-arginyl-L-lysyl-D-phenylalanyl-(2S)-2-amino-4-phenylbutanoyl-L-phenylalanyl]
-
-
cyclo[3-(2-naphthyl)-L-alanyl-D-phenylalanyl-D-arginyl-L-arginyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl]
-
-
cyclo[3-(2-naphthyl)-L-alanyl-L-seryl-D-phenylalanyl-D-prolyl-L-lysyl-L-arginyl-L-lysyl-L-seryl]
-
-
cyclo[D-alanyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl-L-seryl-D-phenylalanyl]
-
-
cyclo[L-alany-(2R)-2-phenylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl]
-
-
cyclo[L-alany-(2S)-2-phenylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl]
-
-
cyclo[L-alanyl-(2R)-2-amino-4-phenylbutanoylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl]
-
-
cyclo[L-alanyl-(2S)-2-amino-4-phenylbutanoylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl]
-
-
cyclo[L-alanyl-D-phenylalanylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl]
-
-
cyclo[L-alanyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl-L-seryl-D-phenylalanyl]
-
-
cyclo[L-alanyl-L-phenylalanylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl]
-
-
cyclo[L-alanylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2R)-2-amino-4-phenylbutanoyl-L-cysteinyl]
-
-
cyclo[L-alanylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl-L-alanyl]
-
-
cyclo[L-alanylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl-L-cysteinyl]
-
-
cyclo[L-alanylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-phenylglycyl-L-cysteinyl]
-
-
cyclo[L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl-L-seryl-D-phenylalanyl-D-prolyl-L-lysyl]
-
-
cyclo[L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl-L-seryl-D-phenylalanyl-L-prolyl-L-lysyl]
-
-
cyclo[L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl-L-seryl-D-phenylalanylglycyl-L-lysyl]
-
-
D-methionyl-N-(4-nitrobenzyl)-L-prolinamide
-
64% inhibition
D-methionyl-N-benzyl-L-prolinamide
-
42% inhibition
D-methionyl-N-phenyl-L-prolinamide
-
below 50% inhibition
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
completely inhibits autolysis of the NS2B-NS3pro construct
diphenyl (1-[[(benzyloxy)carbonyl]amino]-3-carbamimidamidopropyl)phosphonate
-
-
diphenyl (1-[[(benzyloxy)carbonyl]amino]-4-carbamimidamidobutyl)phosphonate
-
12% inhibition
diphenyl (3-amino-1-[[(benzyloxy)carbonyl]amino]-3-oxopropyl)phosphonate
-
15% inhibition
diphenyl (3-amino-1-[[(benzyloxy)carbonyl]amino]propyl)phosphonate
-
12% inhibition
diphenyl (5-amino-1-[[(benzyloxy)carbonyl]amino]pentyl)phosphonate
-
-
diphenyl ([4-(1H-benzimidazol-1-yl)phenyl][[(benzyloxy)carbonyl]amino]methyl)phosphonate
-
4% inhibition
diphenyl ([[(benzyloxy)carbonyl]amino][4-(1H-pyrazol-1-yl)phenyl]methyl)phosphonate
-
5% inhibition
diphenyl ([[(benzyloxy)carbonyl]amino][4-(4-methylpiperazin-1-yl)phenyl]methyl)phosphonate
-
3% inhibition
diphenyl ([[(benzyloxy)carbonyl]amino][4-(morpholin-4-yl)phenyl]methyl)phosphonate
-
1% inhibition
diphenyl [(3-aminophenyl)[[(benzyloxy)carbonyl]amino]methyl]phosphonate
-
8% inhibition
diphenyl [(4-aminophenyl)[[(benzyloxy)carbonyl]amino]methyl]phosphonate
-
16% inhibition
diphenyl [1-[[(benzyloxy)carbonyl]amino]-3-(carbamimidoylsulfanyl)propyl]phosphonate
-
22% inhibition
diphenyl [2-(4-aminophenyl)-1-[[(benzyloxy)carbonyl]amino]ethyl]phosphonate
diphenyl [[[(benzyloxy)carbonyl]amino](3-carbamimidamidophenyl)methyl]phosphonate
-
11% inhibition
diphenyl [[[(benzyloxy)carbonyl]amino](3-nitrophenyl)methyl]phosphonate
-
4% inhibition
diphenyl [[[(benzyloxy)carbonyl]amino](4-carbamimidamidophenyl)methyl]phosphonate
-
-
diphenyl [[[(benzyloxy)carbonyl]amino](4-carbamimidoylphenyl)methyl]phosphonate
-
22% inhibition
diphenyl [[[(benzyloxy)carbonyl]amino](4-cyanophenyl)methyl]phosphonate
-
8% inhibition
diphenyl [[[(benzyloxy)carbonyl]amino](4-nitrophenyl)methyl]phosphonate
-
3% inhibition
diphenyl [[[(benzyloxy)carbonyl]amino](6-carbamimidoylnaphthalen-2-yl)methyl]phosphonate
-
12% inhibition
diphenyl [[[(benzyloxy)carbonyl]amino](6-cyanonaphthalen-2-yl)methyl]phosphonate
-
2% inhibition
diphenyl [[[(benzyloxy)carbonyl]amino](carbamimidamido)methyl]phosphonate
-
-
EDTA
-
zinc-selective chelator, inhibits NS2/3 auto-cleavage and NS3 protease activity
L-methionyl-N-(4-nitrophenyl)-L-prolinamide
-
68% inhibition
myricetin
-
binds to a specific allosteric binding site of the enzyme
N'-(2-ethylhexyl)-N'-(6-[N'-[N-(3-methylheptan-2-yl)carbamimidoyl]carbamimidamido]hexyl)imidodicarbonimidic diamide (non-preferred name)
-
-
N-(6-nitro-2,3-dihydro-1,3-benzothiazol-2-yl)-2-([4-(trifluoromethyl)phenyl]sulfanyl)benzamide
-
EC50 value 0.1 microM
N-(6-nitro-2,3-dihydro-1,3-benzothiazol-2-yl)-3-[(4-nitrophenyl)sulfanyl]benzamide
-
EC50 value 0.3 microM
N-(9-ethylcarbazol-3-yl)-2-[(4-ethyl-5-furan-2-yl-1,2,4-triazol-3-yl)sulfanyl]acetamide
-
68.8% inhibition at 0.05 mM
N-benzyl-N,N-dimethyl-2-[2-[4-(2,2,3-trimethylpentan-3-yl)phenoxy]ethoxy]ethanaminium
-
-
N-[(2S)-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-4-(4-carbamimidamidophenyl)-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-lysinamide
N-[(2S)-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-4-[3-(carbamimidamidomethyl)cyclohexa-1,5-dien-1-yl]-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-lysinamide
N-[(2S)-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-4-[4-(carbamimidamidomethyl)phenyl]-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-lysinamide
N-[(2S)-4-[3-(aminomethyl)phenyl]-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-lysinamide
N-[(2S)-4-[4-(aminomethyl)phenyl]-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-ornithinamide
N-[(2S)-6-amino-1-([(2S)-6-amino-1-[(3R)-3-(carbamimidamidomethyl)pyrrolidin-1-yl]-1-oxohexan-2-yl]amino)-1-oxohexan-2-yl]-2-(biphenyl-4-yl)acetamide
-
-
N-[(2S)-6-amino-1-([(2S)-6-amino-1-[(3S)-3-(carbamimidamidomethyl)pyrrolidin-1-yl]-1-oxohexan-2-yl]amino)-1-oxohexan-2-yl]-2-(biphenyl-4-yl)acetamide
-
-
N-[(2S)-6-amino-1-([(2S)-6-amino-1-[4-(carbamimidamidomethyl)piperidin-1-yl]-1-oxohexan-2-yl]amino)-1-oxohexan-2-yl]-2-(biphenyl-4-yl)acetamide
-
-
N-[(trans-4-carbamimidamidocyclohexyl)methyl]-N2-[(2S)-4-(3-carbamimidamidophenyl)-2-[(phenylacetyl)amino]butanoyl]-L-lysinamide
N-[(trans-4-carbamimidamidocyclohexyl)methyl]-N2-[(2S)-4-[3-(carbamimidamidomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]-L-lysinamide
N-[(trans-4-carbamimidamidocyclohexyl)methyl]-N2-[(2S)-4-[4-(carbamimidamidomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]-L-lysinamide
N-[4-[5-(4-acetamidophenyl)pentyl]phenyl]acetamide
NSC86414
N2-(1,3-benzodioxol-5-ylacetyl)-L-lysyl-L-lysinamide
N2-(1,3-thiazol-2-yl)-L-arginyl-N-[(1S)-2-amino-2-oxo-1-(4-[[4-(trifluoromethyl)benzyl]oxy]phenyl)ethyl]-L-lysinamide
-
-
N2-(4-[(Z)-[3-(cyclohexylmethyl)-2,4-dioxo-1,3-thiazolidin-5-ylidene]methyl]benzoyl)-L-lysyl-N-[(1S)-2-amino-2-oxo-1-phenylethyl]-L-lysinamide
-
-
N2-(adamant-1-yl(amino)acetyl)-L-lysyl-L-lysinamide
N2-(adamant-1-ylacetyl)-L-lysyl-L-lysinamide
N2-(biphenyl-3-ylacetyl)-L-lysyl-N-[(1-carbamimidoylpiperidin-4-yl)methyl]-L-lysinamide
-
C-terminal agmatine peptidomimetic inhibitor, competitive
N2-(biphenyl-4-ylacetyl)-L-lysyl-L-Lys-L-Arg-aldehyde
-
-
N2-(biphenyl-4-ylacetyl)-L-lysyl-L-lysinamide
N2-(biphenyl-4-ylacetyl)-L-lysyl-N-(4-carbamimidamidobutyl)-L-lysinamide
-
-
N2-(biphenyl-4-ylacetyl)-L-lysyl-N-(trans-4-carbamimidamidocyclohexyl)-L-lysinamide
-
-
N2-(biphenyl-4-ylacetyl)-L-lysyl-N-[(2E)-4-carbamimidamidobut-2-en-1-yl]-L-lysinamide
-
-
N2-(biphenyl-4-ylcarbonyl)-L-lysyl-N-(2-carbamimidamidoethyl)-L-lysinamide
-
-
N2-(biphenyl-4-ylcarbonyl)-L-lysyl-N-(3-carbamimidamidopropyl)-L-lysinamide
-
-
N2-(biphenyl-4-ylcarbonyl)-L-lysyl-N-(5-carbamimidamidopentyl)-L-lysinamide
-
-
N2-(cyclohexylacetyl)-L-lysyl-L-lysinamide
N2-(phenylacetyl)-L-lysyl-L-lysinamide
N2-(phenylacetyl)-L-lysyl-L-lysine
N2-(phenylacetyl)-L-lysyl-L-lysyl-3-methylvalinamide
N2-(phenylacetyl)-L-lysyl-L-lysyl-D-alaninamide
N2-(phenylacetyl)-L-lysyl-L-lysyl-L-alaninamide
N2-(phenylacetyl)-L-lysyl-L-lysyl-L-prolinamide
N2-(phenylacetyl)-L-lysyl-L-lysyl-L-valinamide
N2-(phenylacetyl)-L-lysyl-L-lysyl-N2-methylglycinamide
N2-(phenylacetyl)-L-lysyl-L-lysylglycinamide
N2-(phenylacetyl)-L-lysyl-N-(2-aminoprop-2-en-1-yl)-L-lysinamide
N2-(phenylacetyl)-L-lysyl-N-(4-amino-4-oxobutyl)-L-lysinamide
N2-(phenylacetyl)-L-lysyl-N-(5-amino-5-oxopentyl)-L-lysinamide
N2-(phenylacetyl)-L-ornithyl-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-L-lysinamide
N2-(thiophen-2-ylcarbonyl)-L-arginyl-N-[(1S)-2-amino-2-oxo-1-(4-[[4-(trifluoromethyl)benzyl]oxy]phenyl)ethyl]-L-lysinamide
the compound inhibits both unlinked and linked protease with similar potency
N2-acetyl-L-lysyl-N-(4-carbamimidamidobutyl)-L-lysinamide
-
-
N2-phenylacetyl-L-Lys-L-Lys-L-Arg-aldehyde
-
-
N2-[(2S)-4-[3-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-L-lysinamide
N2-[(2S)-4-[4-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-L-lysinamide
N2-[(3,4-dichlorophenyl)acetyl]-L-lysyl-N-[(1S)-1-(1-carbamimidoylpiperidin-4-yl)-2-oxoethyl]-L-lysinamide
-
-
N2-[(3,4-dichlorophenyl)acetyl]-L-ornithyl-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-L-lysinamide
-
-
N2-[(3,4-dimethylphenyl)acetyl]-L-lysyl-L-lysinamide
N2-[(3,4-dimethylphenyl)acetyl]-L-lysyl-L-lysylglycinamide
N2-[(3-aminophenyl)acetyl]-L-lysyl-L-lysinamide
N2-[(4-hydroxyphenyl)acetyl]-L-lysyl-L-lysinamide
N2-[(acetylamino)(phenyl)acetyl]-L-lysyl-L-lysinamide
N2-[amino(phenyl)acetyl]-L-lysyl-L-lysinamide
N2-[[3-(aminomethyl)phenyl]acetyl]-L-lysyl-L-lysinamide
N2-[[3-(carbamimidamidomethyl)phenyl]acetyl]-L-lysyl-L-lysinamide
N2-[[4-(aminomethyl)phenyl]acetyl]-L-lysyl-L-lysinamide
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-3-methyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-L-arginyl-N-(4-carbamimidoylbenzyl)-L-argininamide
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-L-lysyl-N-(4-carbamimidoylbenzyl)-L-argininamide
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-lysyl-L-lysinamide
Na2SO4
-
kosmotropic salts of the Hofmeisters series strongly inhibit in decreasing order: sodium citrate, SO42-, acetate, Cl-
NaOAc
-
kosmotropic salts of the Hofmeisters series strongly inhibit in decreasing order: sodium citrate, SO42-, acetate, Cl-
nona-D-Arg-amide
-
completely inhibits autolysis of the NS2B-NS3pro construct
phenylpropionyl-Lys-Arg-Arg
pinocembrin
-
compound from Boesenbergia rotunda (L.) Mansf. Kulturpfl.
pinostrobin
-
flavanone, non-competetive inhibitor, compound from Boesenbergia rotunda (L.) Mansf. Kulturpfl.
Sodium citrate
-
kosmotropic salts of the Hofmeisters series strongly inhibit in decreasing order: sodium citrate, SO42-, acetate, Cl-
trifluoroacetyl-Lys-Lys-Arg
[2-(2-cyanoethyl)-5-methylpyrazol-3-yl] benzoate
-
105.9% inhibition at 0.05 mM
[4-(2,3-dimethylphenyl)piperazin-1-yl]-(2-ethylsulfonyl-3,4-dihydro-1H-isoquinolin-3-yl)methanone
-
51.6% inhibition at 0.05 mM
[4-methyl-5-(3-methylbut-2-en-1-yl)-6-phenylcyclohex-3-en-1-yl](2,4,6-trimethoxyphenyl)methanone
-
-
[5-(3-methylbut-2-en-1-yl)-6-phenylcyclohex-3-en-1-yl](2,4,6-trimethoxyphenyl)methanone
-
-
[5-amino-1-(4-fluorophenyl)sulfonylpyrazol-3-yl] furan-2-carboxylate
-
107.7% inhibition at 0.05 mM
[5-amino-1-(4-fluorophenyl)sulfonylpyrazol-3-yl] thiophene-2-carboxylate
-
99.1% inhibition at 0.05 mM
[5-amino-1-(4-methoxyphenyl)sulfonylpyrazol-3-yl] 2-bromobenzoate
-
112.5% inhibition at 0.05 mM
[5-amino-1-(4-methoxyphenyl)sulfonylpyrazol-3-yl] benzoate
-
115.6% inhibition at 0.05 mM
[5-amino-1-(4-methoxyphenyl)sulfonylpyrazol-3-yl] furan-2-carboxylate
-
99.3% inhibition at 0.05 mM
[5-amino-1-(4-methoxyphenyl)sulfonylpyrazol-3-yl] thiophene-2-carboxylate
-
116.3% inhibition at 0.05 mM
[5-amino-1-(4-methylphenyl)sulfonylpyrazol-3-yl] furan-2-carboxylate
-
96.6% inhibition at 0.05 mM
[5-amino-1-(4-methylphenyl)sulfonylpyrazol-3-yl] thiophene-2-carboxylate
-
86.8% inhibition at 0.05 mM
[6-(4-methoxyphenyl)-4-methyl-5-(3-methylbut-2-en-1-yl)cyclohex-3-en-1-yl](2,4,6-trimethoxyphenyl)methanone
-
-
(2S)-4-[3-(aminomethyl)phenyl]-2-([(2S)-4-[3-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]butanamide
-
5.5% inhibition
(2S)-4-[3-(aminomethyl)phenyl]-2-([(2S)-4-[3-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]butanamide
-
-
(2S)-4-[4-(aminomethyl)phenyl]-2-([(2S)-4-[4-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]butanamide
-
10.8% inhibition
(2S)-4-[4-(aminomethyl)phenyl]-2-([(2S)-4-[4-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]butanamide
-
-
(2S)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-4-[3-(carbamimidamidomethyl)phenyl]-2-([(2S)-4-[3-(carbamimidamidomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)butanamide
-
-
(2S)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-4-[3-(carbamimidamidomethyl)phenyl]-2-([(2S)-4-[3-(carbamimidamidomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)butanamide
-
-
(2S)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-4-[4-(carbamimidamidomethyl)phenyl]-2-([(2S)-4-[4-(carbamimidamidomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)butanamide
-
17.1% inhibition
(2S)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-4-[4-(carbamimidamidomethyl)phenyl]-2-([(2S)-4-[4-(carbamimidamidomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)butanamide
-
-
1-(4-[3-[4-(furan-3-yl)phenyl]-5-(piperidin-4-ylmethoxy)pyrazin-2-yl]phenyl)methanamine
-
-
1-(4-[3-[4-(furan-3-yl)phenyl]-5-(piperidin-4-ylmethoxy)pyrazin-2-yl]phenyl)methanamine
-
-
1-(4-[3-[4-(furan-3-yl)phenyl]-5-(piperidin-4-ylmethoxy)pyrazin-2-yl]phenyl)methanamine
-
-
2-naphthoyl-Lys-Arg-Arg
-
-
2-naphthoyl-Lys-Arg-Arg
-
-
4-(guanidinomethyl)-phenylacetyl-Lys-Lys-Arg-NH2
-
-
4-(guanidinomethyl)-phenylacetyl-Lys-Lys-Arg-NH2
-
-
4-aminobenzoyl-Lys-Arg-Arg
-
-
4-aminobenzoyl-Lys-Arg-Arg
-
-
4-aminobenzoyl-Lys-Lys-Arg
-
-
4-aminobenzoyl-Lys-Lys-Arg
-
-
4-aminophenylacetyl-Lys-Arg-Arg
-
-
4-aminophenylacetyl-Lys-Arg-Arg
-
-
4-phenylphenylacetyl-Lys-Arg-Arg
-
-
4-phenylphenylacetyl-Lys-Arg-Arg
-
-
4-phenylphenylacetyl-Lys-Lys-Arg
-
-
4-phenylphenylacetyl-Lys-Lys-Arg
-
-
4-[3-acetyl-5-(2-phenylquinolin-4-yl)-2,3-dihydro-1,3,4-oxadiazol-2-yl]benzoic acid
-
-
4-[3-acetyl-5-(2-phenylquinolin-4-yl)-2,3-dihydro-1,3,4-oxadiazol-2-yl]benzoic acid
-
-
acetyl-Ala-Arg-agmatine
-
-
acetyl-Ala-Arg-agmatine
-
-
acetyl-Ala-Lys-agmatine
-
-
acetyl-Ala-Lys-agmatine
-
-
acetyl-Arg-Lys-agmatine
-
-
acetyl-Arg-Lys-agmatine
-
-
acetyl-Lys-Arg-Arg
-
-
acetyl-Lys-Lys-agmatine
-
-
acetyl-Lys-Lys-agmatine
-
-
acetyl-Lys-Lys-Arg
-
-
acetyl-Trp-Lys-agmatine
-
-
acetyl-Trp-Lys-agmatine
-
-
Aprotinin
-
-
Aprotinin
bovine pancreatic trypsin inhibitor, BPTI
Aprotinin
-
non-specific inhibitor of NS2B-NS3pro, full inhibition at 0.001 mM
Aprotinin
-
completely inhibits autolysis of the NS2B-NS3pro construct
Aprotinin
bovine pancreatic trypsin inhibitor, BPTI
Aprotinin
a 60-amino acid bovine pancreatic trypsin inhibitor and an efficient inhibitor of ZIKV NS2B-NS3pro
benzoyl-Lys-Lys(acetyl)-Arg
-
-
benzoyl-Lys-Lys(acetyl)-Arg
-
-
benzoyl-Lys-Lys(benzoyl)-Arg
-
-
benzoyl-Lys-Lys(benzoyl)-Arg
-
-
benzoyl-Lys-Lys(benzyl)-Arg
-
-
benzoyl-Lys-Lys(benzyl)-Arg
-
-
benzoyl-Lys-Lys(p-anisoyl)-Arg
-
-
benzoyl-Lys-Lys(p-anisoyl)-Arg
-
-
benzoyl-Lys-Lys-Arg
-
-
benzoyl-Nle-Lys-Arg-Arg
-
-
benzoyl-Nle-Lys-Arg-Arg
-
-
benzoyl-Nle-Lys-Arg-Arg
-
-
Bovine pancreatic trypsin inhibitor
pseudocontact shifts from a lanthanide tag show that NS2Bc remains in the closed conformation also in the complex with
-
Bovine pancreatic trypsin inhibitor
-
BPTI
-
Bovine pancreatic trypsin inhibitor
BPTI
-
cinnamoyl-Lys-Arg-Arg
-
-
cinnamoyl-Lys-Arg-Arg
-
-
cyclopropionyl-Lys-Lys-Arg
-
-
cyclopropionyl-Lys-Lys-Arg
-
-
diphenyl [2-(4-aminophenyl)-1-[[(benzyloxy)carbonyl]amino]ethyl]phosphonate
-
-
diphenyl [2-(4-aminophenyl)-1-[[(benzyloxy)carbonyl]amino]ethyl]phosphonate
-
11% inhibition
N-[(2S)-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-4-(4-carbamimidamidophenyl)-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-lysinamide
-
14.7% inhibition
N-[(2S)-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-4-(4-carbamimidamidophenyl)-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-lysinamide
-
-
N-[(2S)-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-4-[3-(carbamimidamidomethyl)cyclohexa-1,5-dien-1-yl]-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-lysinamide
-
-
N-[(2S)-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-4-[3-(carbamimidamidomethyl)cyclohexa-1,5-dien-1-yl]-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-lysinamide
-
-
N-[(2S)-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-4-[4-(carbamimidamidomethyl)phenyl]-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-lysinamide
-
-
N-[(2S)-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-4-[4-(carbamimidamidomethyl)phenyl]-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-lysinamide
-
-
N-[(2S)-4-[3-(aminomethyl)phenyl]-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-lysinamide
-
-
N-[(2S)-4-[3-(aminomethyl)phenyl]-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-lysinamide
-
-
N-[(2S)-4-[4-(aminomethyl)phenyl]-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-ornithinamide
-
-
N-[(2S)-4-[4-(aminomethyl)phenyl]-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-ornithinamide
-
-
N-[(trans-4-carbamimidamidocyclohexyl)methyl]-N2-[(2S)-4-(3-carbamimidamidophenyl)-2-[(phenylacetyl)amino]butanoyl]-L-lysinamide
-
-
N-[(trans-4-carbamimidamidocyclohexyl)methyl]-N2-[(2S)-4-(3-carbamimidamidophenyl)-2-[(phenylacetyl)amino]butanoyl]-L-lysinamide
-
-
N-[(trans-4-carbamimidamidocyclohexyl)methyl]-N2-[(2S)-4-[3-(carbamimidamidomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]-L-lysinamide
-
31.1% inhibition
N-[(trans-4-carbamimidamidocyclohexyl)methyl]-N2-[(2S)-4-[3-(carbamimidamidomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]-L-lysinamide
-
-
N-[(trans-4-carbamimidamidocyclohexyl)methyl]-N2-[(2S)-4-[4-(carbamimidamidomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]-L-lysinamide
-
-
N-[(trans-4-carbamimidamidocyclohexyl)methyl]-N2-[(2S)-4-[4-(carbamimidamidomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]-L-lysinamide
-
-
N2-(1,3-benzodioxol-5-ylacetyl)-L-lysyl-L-lysinamide
-
19.9% inhibition
N2-(1,3-benzodioxol-5-ylacetyl)-L-lysyl-L-lysinamide
-
-
N2-(adamant-1-yl(amino)acetyl)-L-lysyl-L-lysinamide
-
14.6% inhibition
N2-(adamant-1-yl(amino)acetyl)-L-lysyl-L-lysinamide
-
-
N2-(adamant-1-ylacetyl)-L-lysyl-L-lysinamide
-
24.2% inhibition
N2-(adamant-1-ylacetyl)-L-lysyl-L-lysinamide
-
-
N2-(biphenyl-4-ylacetyl)-L-lysyl-L-lysinamide
-
27.1% inhibition
N2-(biphenyl-4-ylacetyl)-L-lysyl-L-lysinamide
-
-
N2-(cyclohexylacetyl)-L-lysyl-L-lysinamide
-
31.7% inhibition; 36.7% inhibition
N2-(cyclohexylacetyl)-L-lysyl-L-lysinamide
-
-
N2-(phenylacetyl)-L-lysyl-L-lysinamide
-
20.8% inhibition
N2-(phenylacetyl)-L-lysyl-L-lysinamide
-
-
N2-(phenylacetyl)-L-lysyl-L-lysine
-
-
N2-(phenylacetyl)-L-lysyl-L-lysine
-
-
N2-(phenylacetyl)-L-lysyl-L-lysyl-3-methylvalinamide
-
6.4% inhibition
N2-(phenylacetyl)-L-lysyl-L-lysyl-3-methylvalinamide
-
-
N2-(phenylacetyl)-L-lysyl-L-lysyl-D-alaninamide
-
12.0% inhibition
N2-(phenylacetyl)-L-lysyl-L-lysyl-D-alaninamide
-
-
N2-(phenylacetyl)-L-lysyl-L-lysyl-L-alaninamide
-
5.6% inhibition
N2-(phenylacetyl)-L-lysyl-L-lysyl-L-alaninamide
-
-
N2-(phenylacetyl)-L-lysyl-L-lysyl-L-prolinamide
-
5.2% inhibition
N2-(phenylacetyl)-L-lysyl-L-lysyl-L-prolinamide
-
-
N2-(phenylacetyl)-L-lysyl-L-lysyl-L-valinamide
-
12.0% inhibition
N2-(phenylacetyl)-L-lysyl-L-lysyl-L-valinamide
-
-
N2-(phenylacetyl)-L-lysyl-L-lysyl-N2-methylglycinamide
-
3.2% inhibition
N2-(phenylacetyl)-L-lysyl-L-lysyl-N2-methylglycinamide
-
-
N2-(phenylacetyl)-L-lysyl-L-lysylglycinamide
-
30.7% inhibition
N2-(phenylacetyl)-L-lysyl-L-lysylglycinamide
-
-
N2-(phenylacetyl)-L-lysyl-N-(2-aminoprop-2-en-1-yl)-L-lysinamide
-
35.1% inhibition
N2-(phenylacetyl)-L-lysyl-N-(2-aminoprop-2-en-1-yl)-L-lysinamide
-
-
N2-(phenylacetyl)-L-lysyl-N-(4-amino-4-oxobutyl)-L-lysinamide
-
26.3% inhibition
N2-(phenylacetyl)-L-lysyl-N-(4-amino-4-oxobutyl)-L-lysinamide
-
-
N2-(phenylacetyl)-L-lysyl-N-(5-amino-5-oxopentyl)-L-lysinamide
-
-
N2-(phenylacetyl)-L-lysyl-N-(5-amino-5-oxopentyl)-L-lysinamide
-
-
N2-(phenylacetyl)-L-ornithyl-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-L-lysinamide
-
-
N2-(phenylacetyl)-L-ornithyl-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-L-lysinamide
-
-
N2-[(2S)-4-[3-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-L-lysinamide
-
-
N2-[(2S)-4-[3-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-L-lysinamide
-
-
N2-[(2S)-4-[4-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-L-lysinamide
-
12.4% inhibition
N2-[(2S)-4-[4-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-L-lysinamide
-
-
N2-[(3,4-dimethylphenyl)acetyl]-L-lysyl-L-lysinamide
-
25.1% inhibition
N2-[(3,4-dimethylphenyl)acetyl]-L-lysyl-L-lysinamide
-
-
N2-[(3,4-dimethylphenyl)acetyl]-L-lysyl-L-lysylglycinamide
-
45.0% inhibition
N2-[(3,4-dimethylphenyl)acetyl]-L-lysyl-L-lysylglycinamide
-
-
N2-[(3-aminophenyl)acetyl]-L-lysyl-L-lysinamide
-
27.5% inhibition
N2-[(3-aminophenyl)acetyl]-L-lysyl-L-lysinamide
-
-
N2-[(4-hydroxyphenyl)acetyl]-L-lysyl-L-lysinamide
-
27.5% inhibition
N2-[(4-hydroxyphenyl)acetyl]-L-lysyl-L-lysinamide
-
-
N2-[(acetylamino)(phenyl)acetyl]-L-lysyl-L-lysinamide
-
-
N2-[(acetylamino)(phenyl)acetyl]-L-lysyl-L-lysinamide
-
-
N2-[amino(phenyl)acetyl]-L-lysyl-L-lysinamide
-
-
N2-[amino(phenyl)acetyl]-L-lysyl-L-lysinamide
-
-
N2-[[3-(aminomethyl)phenyl]acetyl]-L-lysyl-L-lysinamide
-
12.4% inhibition
N2-[[3-(aminomethyl)phenyl]acetyl]-L-lysyl-L-lysinamide
-
-
N2-[[3-(carbamimidamidomethyl)phenyl]acetyl]-L-lysyl-L-lysinamide
-
32.3% inhibition
N2-[[3-(carbamimidamidomethyl)phenyl]acetyl]-L-lysyl-L-lysinamide
-
-
N2-[[4-(aminomethyl)phenyl]acetyl]-L-lysyl-L-lysinamide
-
31.7% inhibition
N2-[[4-(aminomethyl)phenyl]acetyl]-L-lysyl-L-lysinamide
-
-
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-3-methyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
-
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-3-methyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
-
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-L-arginyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
-
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-L-arginyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
-
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-L-lysyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
-
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-L-lysyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
-
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
-
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
-
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-lysyl-L-lysinamide
-
65.0% inhibition
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-lysyl-L-lysinamide
-
-
NaCl
-
decreases activity by more than 40% at 50 mM and more than 70% at 250 mM
NaCl
-
kosmotropic salts of the Hofmeisters series strongly inhibit in decreasing order: sodium citrate, SO42-, acetate, Cl-
NaCl
decreases activity by more than 40% at 50 mM and more than 70% at 250 mM
NaCl
decreases activity by more than 40% at 50 mM and more than 70% at 250 mM
NaCl
decreases activity less than 25% at 250 mM
NaCl
-
decreases activity by more than 40% at 50 mM and more than 70% at 250 mM
NaCl
-
decreases activity by more than 40% at 50 mM and more than 70% at 250 mM
panduratin A
-
-
panduratin A
-
cyclohexenyl chalcone derivative, competetive inhibitor, compound from Boesenbergia rotunda (L.) Mansf. Kulturpfl.
phenylacetyl-Lys-Arg-Arg
-
-
phenylacetyl-Lys-Arg-Arg
-
-
phenylacetyl-Lys-Lys-Arg
-
-
phenylacetyl-Lys-Lys-Arg
-
-
phenylpropionyl-Lys-Arg-Arg
-
-
phenylpropionyl-Lys-Arg-Arg
-
-
propionyl-Lys-Arg-Arg
-
-
propionyl-Lys-Arg-Arg
-
-
propionyl-Lys-Lys-Arg
-
-
propionyl-Lys-Lys-Arg
-
-
quercetin
-
molecular docking study. A total of six hydrogen bonds are formed, key residues are Asn152, Ala164, Lys74, Asn167, Leu149 and Gly87
quercetin
-
dissociation constant Kd is 0.02 microM
trifluoroacetyl-Lys-Lys-Arg
-
-
trifluoroacetyl-Lys-Lys-Arg
-
-
additional information
-
N-alpha-benzoyl-L-arginine-p-nitroanilide causes precipitation of the recombinant protease and is therefore not appropiate for enzymatic analysis
-
additional information
-
cleavage products and their analogs do not appreciably inhibit the Dengue NS3 protease. Inhibitors with electrophilic warheads, such as aldehyde, trifluoromethyl ketone, and boronic acid, are needed to see effective inhibition of the enzyme activity. Among warheads, tetrapeptide boronic acid has the highest affinity
-
additional information
-
P2 Arg residue is more important for enzyme interactions than P1 Arg. Tri- and dipeptide aldehyde inhibitors afford low micromolar activity
-
additional information
-
discovery, X-ray crystallography and antiviral activity of allosteric inhibitors of flavivirus NS2B-NS3 protease. Compound screening followed by medicinal chemistry yield a series of drug-like, broadly active inhibitors of flavivirus proteases with IC50 as low as 120 nM. The inhibitors exhibit significant antiviral activities in cells (EC68: 300-600 nM). X-ray studies reveal that the inhibitors bind to an allosteric, mostly hydrophobic pocket of dengue NS3 and hold the protease in an open, catalytically inactive conformation
-
additional information
-
inhibitor screening, a strong inhibitory potency is found for simple phenylacetyl-capped tripeptides containing a C-terminal P1 arginyl amide moiety and for their elongated derivatives with one or two glycine residues in the P1' and P2' positions. Inhibitory potencies of synthesized compounds, comparison to human furin, and West nile virus, structure-activity relationships, overview
-
additional information
-
unlinked NS2B-NS3 complex bound to a peptidic boronic acid inhibitor
-
additional information
enzyme ligand binding structure analysis
-
additional information
-
in silico screening, alanine mutation, and density functional theory approaches for identification of NS2B/NS3 protease inhibitors, using molecular docking, free energy calculations, and simulation protocols in computational inhibitor screening, determination of ligand binding affinitites and protein interactions, overview
-
additional information
-
discovery of cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity. The introduction of aromatic residues at the appropriate positions and conformational restriction generates the most promising cyclic peptide. Cyclic peptides with proper positioning of additional arginines and aromatic residues exhibit antiviral activity against DENV. Replacing the C-terminal amide bond of the polybasic amino acid sequence with an amino methylene moiety stabilizes the cyclic peptides against hydrolysis by NS2BNS3 protease, while maintaining their enzyme inhibitory activity and antiviral activity
-
additional information
-
identification of fused bicyclic derivatives of pyrrolidine and imidazolidinone as dengue virus-2 NS2B-NS3 protease inhibitors. The preliminary structure-activity relationship reveals that a substituent and its stereochemistry at C-3 position, substitution (X) at N-2 arene and a linker (Y) between C-3 position and its attached arene are important for the fused-ring scaffold of pyrrolidino [1,2-c]imidazolidinone to block the active site of NS2B-NS3 protease. The linear dipeptide L-methionyl-N-(4-nitrophenyl)-L-prolinamide) and the non-peptidic fused ring L-methionyl-N-(4-nitrophenyl)-L-prolinamide) show comparable activities against DENV-2 NS2B-NS3 protease and wild-type DENV-2 virus in a viral replication assay
-
additional information
N-alpha-benzoyl-L-arginine-p-nitroanilide causes precipitation of the recombinant protease and is therefore not appropiate for enzymatic analysis
-
additional information
enzyme ligand binding structure analysis
-
additional information
structure-based identification of key residues and binding sites for inhibitor binding, design of non-competitive inhibitors for Dengue virus type 3 NS2b-NS3-protease, overview. The identified residues include 1. amino acids close to the beta sheet-loop-beta sheet known to be important in its closed conformation for NS2b 2. residues close to the active site, 3. several residues evenly spread on the NS2b-NS3 contact surface, and 4. some inner residues most likely related to the overall stability of the protease. Computational alanine scanning mutagenesis and similarity analysis based on sequence and structure homology, modeling. On the DENV NS3 protease, the residues Tyr23, Gly37, Phe46, Thr48, His51, Thr53, Leu58, Asp75, Tyr79, Trp89, and Thr156 are identified as class A and as the eleven highest ranked residues by both MLP models
-
additional information
enzyme ligand binding structure analysis
-
additional information
N-alpha-benzoyl-L-arginine-p-nitroanilide causes precipitation of the recombinant protease and is therefore not appropiate for enzymatic analysis
-
additional information
enzyme ligand binding structure analysis
-
additional information
-
EGTA or inhibitors of bacterial and mammalian metalloendopeptidases, aminopeptidase, angiotensin converting enzyme, and metalloprotease-disintegrins have no effect on NS2/3 auto-cleavage and NS3 protease activity. No inhibitory effect of the NS4A peptide on NS2/3 auto-cleavage. NS4A does not significantly affect the sensitivity of NS2/3 autocleavage to zinc chelation, but has a marked effect on NS3 protease activity, rendering this activity approximately 3fold more resistant to zinc chelation
-
additional information
enzyme ligand binding structure analysis
-
additional information
enzyme ligand binding structure analysis
-
additional information
enzyme ligand binding structure analysis
-
additional information
N-alpha-benzoyl-L-arginine-p-nitroanilide causes precipitation of the recombinant protease and is therefore not appropiate for enzymatic analysis
-
additional information
enzyme ligand binding structure analysis
-
additional information
-
N-alpha-benzoyl-L-arginine-p-nitroanilide causes precipitation of the recombinant protease and is therefore not appropiate for enzymatic analysis
-
additional information
-
product inhibition of the protease by the cleaved C-terminus of NS2B. The reaction product Lys-Arg-COO- remains in the P2-P1 site after cleavage and effectively blocks the active site for both cis and trans substrates
-
additional information
enzyme ligand binding structure analysis
-
additional information
-
discovery, X-ray crystallography and antiviral activity of allosteric inhibitors of flavivirus NS2B-NS3 protease. Compound screening followed by medicinal chemistry yield a series of drug-like, broadly active inhibitors of flavivirus proteases with IC50 as low as 120 nM. The inhibitors exhibit significant antiviral activities in cells (EC68: 300-600 nM). X-ray studies reveal that the inhibitors bind to an allosteric, mostly hydrophobic pocket of dengue NS3 and hold the protease in an open, catalytically inactive conformation
-
additional information
-
inhibitor screening, a strong inhibitory potency is found for simple phenylacetyl-capped tripeptides containing a C-terminal P1 arginyl amide moiety and for their elongated derivatives with one or two glycine residues in the P1' and P2' positions. The compounds seem to be poor substrates of the WNV NS2BNS3 protease and therefore, act as competitive inhibitors. Inhibitory potencies of synthesized compounds, comparison to human furin, and West nile virus, structure-activity relationships, overview
-
additional information
-
development of a series of alpha-aminoalkylphosphonate diphenyl esters and their peptidyl derivatives as potent inhibitors of the NS2B/NS3 protease. Inhibitor synthesis and mechanism of serine proteases inhibition by alpha-aminoalkylphosphonate diphenyl esters involving the oxyanion hole, overview. Molecular docking
-
additional information
-
inhibitor potency is driven predominantely by interactions with amino acid residues in the S1 and S2 pockets, as substitutions in the P1 and P2 sites have the greates impact on inhibitor potency. P1 and P2 positions are most important for inhibitor binding, whilst the P3 and P4 positions have much less effect
-
additional information
-
N-alpha-benzoyl-L-arginine-p-nitroanilide causes precipitation of the recombinant protease and is therefore not appropiate for enzymatic analysis
-
additional information
enzyme ligand binding structure analysis
-
additional information
-
N-alpha-benzoyl-L-arginine-p-nitroanilide causes precipitation of the recombinant protease and is therefore not appropiate for enzymatic analysis
-
additional information
identification of structural scaffolds for allosteric small-molecule inhibitors of this protease, overview. Molecular modeling of the protease-inhibitor complexes suggests that these compounds bind to the druggable cavity in the NS2B-NS3 protease interface and affect productive interactions of the protease domain with its cofactor. The most potent compound demonstrate efficient inhibition of ZIKV propagation in vitro in human fetal neural progenitor cells and in vivo in SJL mice. Docking study and in silico modeling of ZIKV NS2B-NS3pro complexed with inhibitors
-
additional information
-
identification of structural scaffolds for allosteric small-molecule inhibitors of this protease, overview. Molecular modeling of the protease-inhibitor complexes suggests that these compounds bind to the druggable cavity in the NS2B-NS3 protease interface and affect productive interactions of the protease domain with its cofactor. The most potent compound demonstrate efficient inhibition of ZIKV propagation in vitro in human fetal neural progenitor cells and in vivo in SJL mice. Docking study and in silico modeling of ZIKV NS2B-NS3pro complexed with inhibitors
-
additional information
screening for potential intracellular substrates of NS3 and development of specific inhibitors of ZIKV protease, overview
-
additional information
-
screening for potential intracellular substrates of NS3 and development of specific inhibitors of ZIKV protease, overview
-
additional information
-
discovery, X-ray crystallography and antiviral activity of allosteric inhibitors of flavivirus NS2B-NS3 protease. Compound screening followed by medicinal chemistry yield a series of drug-like, broadly active inhibitors of flavivirus proteases with IC50 as low as 120 nM. The inhibitors exhibit significant antiviral activities in cells (EC68: 300-600 nM) and in a mouse model of Zika virus infection. X-ray studies reveal that the inhibitors bind to an allosteric, mostly hydrophobic pocket of dengue NS3 and hold the protease in an open, catalytically inactive conformation
-
additional information
-
structural dynamics of Zika virus NS2B-NS3 protease binding to dipeptide inhibitors, overview. The unlinked protease forms the closed conformation and the aldehyde group from the inhibitor forms a covalent bond with the side chain of S135. Compounds derived from protease substrate bind to the protease active site. Nuclear magnetic resonance studies demonstrate that the protease-inhibitor complex is in the closed conformation in solution. No inhibition by acyl-KR-COOH
-
additional information
-
structural insights into the inhibition of Zika virus NS2B-NS3 protease by a small-molecule inhibitor, structure and dynamics, overview. 5-amino-1-((4-methoxyphenyl)sulfonyl)-1H-pyrazol-3-yl benzoate stabilizes the closed conformation of ZIKV protease. Upon hydrolysis in situ into two fragments, the benzoyl group of the inhibitor forms a covalent bond with the side chain of catalytic residue S135, whereas the second fragment exhibits no obvious molecular interactions with the protease, detailed mechanism of action of a covalent inhibitor. Unique adduct of the benzoyl moiety to residue S135
-
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0.089
Abz-KKQRAGVL-3-nitrotyrosine-amide
-
-
0.0045
Abz-RRRRSAG-3-nitrotyrosine-amide
-
-
0.0045
Abz-RRRRSAGnY-amide
-
-
0.00418
Ac-Arg-Lys-Lys-Arg-7-amido-4-carbamoylmethylcoumarin
pH 8.5, 22°C
0.006
Ac-D-Arg-Lys-Orn-Arg(Me)-7-amido-4-carbamoylmethylcoumarin
pH 8.5, 22°C
0.0042
Ac-D-Arg-Lys-Orn-Arg-7-amido-4-carbamoylmethylcoumarin
pH 8.5, 22°C
0.00799
Ac-D-Lys-Lys-Orn-Arg-7-amido-4-carbamoylmethylcoumarin
pH 8.5, 22°C
0.01385
Ac-Nle-Lys-Lys-Arg-7-amido-4-carbamoylmethylcoumarin
pH 8.5, 22°C
0.1
acetyl-Nle-Lys-Arg-Arg-4-methylcoumarin 7-amide
-
pH 9.5, 37°C
0.0016 - 8.6
benzoyl-Nle-Lys-Arg-Arg-4-methylcoumarin 7-amide
0.0062 - 7.3
benzoyl-Nle-Lys-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
6
benzoyl-Nle-Lys-Arg-Arg-thiobenzylester
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 4
0.034 - 52
benzoyl-Nle-Lys-Thr-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
0.046 - 72
benzoyl-Nle-Thr-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
0.0066 - 8.6
benzoyl-Thr-Lys-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
0.076 - 210
benzoyl-Thr-Thr-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
0.143 - 0.707
benzyloxycarbonyl-Gly-Arg-Arg-4-methylcoumarin 7-amide
0.1422
Boc-Gly-Arg-Arg-7-amido-4-methylcoumarin
-
-
0.004 - 0.03
butyloxycarbonyl-Arg-Val-Arg-Arg-7-amido-4-methylcoumarin
0.247
Bz-Arg-Arg-4-methylcoumaryl-7-amide
-
-
0.0146
Bz-Nle-Lys-Arg-Arg-7-amido-4-methylcoumarin
-
-
0.015
FAEGRRGAAEVLQ
-
pH 9.0, 37°C
0.146
Gly-Arg-Arg-4-methylcoumarin 7-amide
-
pH 9.0, 37°C, wild-type NS3 protease with wild-tyüe NS2B cofactor
0.0027
KLAQRRVFHGVAQ
-
pH 9.0, 37°C
0.0013 - 0.089
L-pGlu-L-Arg-L-Thr-L-Lys-L-Arg-7-amido-4-methylcoumarin
0.0025
MKTGRRGSANGKQ
-
pH 9.0, 37°C
0.111 - 0.444
N-(2-aminobenzoyl)-L-valyl-L-lysyl-L-lysyl-N-(3-carbamoyl-4-nitrophenyl)-L-argininamide
0.03 - 0.08
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
0.3 - 15.9
N-alpha-benzoyl-L-arginine-p-nitroanilide
0.027
N-benzoyl-3-(4-aminocyclohexyl)-L-Ala-L-Arg-4-methylcoumaryl-7-amide
-
-
0.216
N-benzoyl-3-(4-piperidinyl)-L-Ala-L-Arg-4-methylcoumaryl-7-amide
-
-
0.298
N-benzoyl-3-(trans-aminomethylcyclohexyl)-L-Ala-L-Arg-4-methylcoumaryl-7-amide
-
-
0.043
N-benzoyl-3-pyridyl-L-Ala-L-Arg-4-methylcoumaryl-7-amide
-
-
0.026
N-benzoyl-4-(aminomethyl)-L-Phe-L-Arg-4-methylcoumaryl-7-amide
-
-
0.354
N-benzoyl-4-(aminomethyl-N-isopropyl)-L-Phe-L-Arg-4-methylcoumaryl-7-amide
-
-
0.49
N-benzoyl-4-(guanidino)-L-Phe-L-Arg-4-methylcoumaryl-7-amide
-
-
0.247
N-benzyloxycarbonyl-Arg-Arg-4-methylcoumaryl-7-amide
-
-
0.0087 - 0.0588
o-aminobenzoyl-AGKKSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
0.0073 - 0.038
o-aminobenzoyl-AGKRSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
0.005 - 0.0213
o-aminobenzoyl-AGRKSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
0.02
o-aminobenzoyl-AGRRSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
0.0066 - 0.0692
o-aminobenzoyl-AKKKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
0.0076 - 0.0532
o-aminobenzoyl-AKKRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
0.0006 - 0.0237
o-aminobenzoyl-AKRKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
0.002 - 0.0314
o-aminobenzoyl-AKRRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
0.00013 - 0.0673
o-aminobenzoyl-ARKKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
0.014 - 0.058
o-aminobenzoyl-ARKRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
0.0015 - 0.0183
o-aminobenzoyl-ARRKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
0.0096 - 0.0256
o-aminobenzoyl-ARRRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
0.0088
o-aminobenzoyl-EVKKQRAGVLWDQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
NS3 protease from strain NGC
0.0177
o-aminobenzoyl-FAAGRKSLTLNLQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
NS3 protease from strain NGC
0.0074
o-aminobenzoyl-FAAQRRGRIGRNQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.026
o-aminobenzoyl-HRREKRSVALQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
NS3 protease from strain NGC
0.012
o-aminobenzoyl-KKRSSKQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.0021
o-aminobenzoyl-KRRSSKQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.0039
o-aminobenzoyl-LNRRRRTAGMIIQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
NS3 protease from strain NGC
0.03
o-aminobenzoyl-RTSKKRSWPLNEQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
NS3 protease from strain NGC
0.004
o-aminobenzoyl-SAAGRRGRIGRNQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.0098
o-aminobenzoyl-SAAQRKGRIGRNQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.0072
o-aminobenzoyl-SAAQRRGLIGRNQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.0046
o-aminobenzoyl-SAAQRRGRIGNNQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.0045
o-aminobenzoyl-SAAQRRGRIGRLQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.0138
o-aminobenzoyl-SAAQRRGRIGRNQ-N-(2,4-dinitrophenyl)-ethylenediamine
0.0069
o-aminobenzoyl-SAAQRRGRILRNQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.0165
o-aminobenzoyl-SAAQRRGRTGRNQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.0059
o-aminobenzoyl-SAAQRRSRIGRNQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.027
o-aminobenzoyl-TTSTRRGTGNIGQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
NS3 protease from strain NGC
0.0475 - 0.06
phenylacetyl-Lys-Lys-Arg-4-nitroanilide
0.059
Pyr-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin
-
pH 8.5, 37°C
0.004 - 0.071
pyroglutamic acid-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin
0.02
RIFGRRSIPVNEQ
-
pH 9.0, 37°C
0.0088
SAAQRRGRIGRNQ
-
pH 9.0, 37°C
0.0022
SSRKRRSHDVLTQ
-
pH 9.0, 37°C
0.036 - 0.04
t-butoxycarbonyl-Arg-Val-Arg-Arg-7-amido-4-methylcoumarin
0.324 - 2.7
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide
0.181 - 3.74
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide
0.12 - 180
tert-butoxycarbonyl-Gly-Arg-Arg-4-methylcoumarin 7-amide
0.0085
VRGARRSGDVLWQ
-
pH 9.0, 37°C
additional information
additional information
-
0.0016
benzoyl-Nle-Lys-Arg-Arg-4-methylcoumarin 7-amide
-
pH 7.5, 37°C
8.6
benzoyl-Nle-Lys-Arg-Arg-4-methylcoumarin 7-amide
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 4
0.0062
benzoyl-Nle-Lys-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 1
0.012
benzoyl-Nle-Lys-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 2
0.012
benzoyl-Nle-Lys-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 3
7.3
benzoyl-Nle-Lys-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 4
0.034
benzoyl-Nle-Lys-Thr-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 2
0.18
benzoyl-Nle-Lys-Thr-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 3
0.202
benzoyl-Nle-Lys-Thr-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 1
52
benzoyl-Nle-Lys-Thr-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 4
0.046
benzoyl-Nle-Thr-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 2
0.053
benzoyl-Nle-Thr-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 3
0.071
benzoyl-Nle-Thr-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 1
72
benzoyl-Nle-Thr-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 4
0.0066
benzoyl-Thr-Lys-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 1
0.011
benzoyl-Thr-Lys-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 2
0.013
benzoyl-Thr-Lys-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 3
8.6
benzoyl-Thr-Lys-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 4
0.076
benzoyl-Thr-Thr-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 2
0.22
benzoyl-Thr-Thr-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 3
0.36
benzoyl-Thr-Thr-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 1
210
benzoyl-Thr-Thr-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 4
0.143
benzyloxycarbonyl-Gly-Arg-Arg-4-methylcoumarin 7-amide
-
serovar DENV2, pH 9.5, temperature not specified in the publication
0.707
benzyloxycarbonyl-Gly-Arg-Arg-4-methylcoumarin 7-amide
-
serovar DENV3, pH 9.0, temperature not specified in the publication
0.004
butyloxycarbonyl-Arg-Val-Arg-Arg-7-amido-4-methylcoumarin
mutant G22S
0.03
butyloxycarbonyl-Arg-Val-Arg-Arg-7-amido-4-methylcoumarin
wild-type
0.0013
L-pGlu-L-Arg-L-Thr-L-Lys-L-Arg-7-amido-4-methylcoumarin
-
mutant enzyme T52V, in 20 mM Tris/HCl buffer, pH 8.0, at 22°C
0.0588
L-pGlu-L-Arg-L-Thr-L-Lys-L-Arg-7-amido-4-methylcoumarin
-
mutant enzyme K48A, in 20 mM Tris/HCl buffer, pH 8.0, at 22°C
0.071
L-pGlu-L-Arg-L-Thr-L-Lys-L-Arg-7-amido-4-methylcoumarin
-
wild type enzyme, in 20 mM Tris/HCl buffer, pH 8.0, at 22°C
0.089
L-pGlu-L-Arg-L-Thr-L-Lys-L-Arg-7-amido-4-methylcoumarin
-
mutant enzyme R76L, in 20 mM Tris/HCl buffer, pH 8.0, at 22°C
0.111
N-(2-aminobenzoyl)-L-valyl-L-lysyl-L-lysyl-N-(3-carbamoyl-4-nitrophenyl)-L-argininamide
pH 7.4, 37°C, phosphate buffer
0.444
N-(2-aminobenzoyl)-L-valyl-L-lysyl-L-lysyl-N-(3-carbamoyl-4-nitrophenyl)-L-argininamide
pH 8.5, 37°C, Tris-CHAPS-glycerol buffer
0.03
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant linked form mutant A125C/V162C
0.03
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant linked form mutant S75C/K117C
0.04
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant linked form mutant I73C/P106C
0.04
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant linked form mutant K117A
0.04
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant linked form mutant S75C
0.04
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant unlinked form mutant S75C/K117C
0.04
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant unlinked form wild-type enzyme
0.05
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant linked form mutant K117C
0.05
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant linked form mutant K117R
0.05
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant unlinked form mutant A125C/V162C
0.05
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant unlinked form mutant I73C/P106C
0.07
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant linked form wild-type enzyme
0.08
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant unlinked form mutant K117A
0.3
N-alpha-benzoyl-L-arginine-p-nitroanilide
-
mutant G68A
0.3
N-alpha-benzoyl-L-arginine-p-nitroanilide
-
mutant G81A
0.4
N-alpha-benzoyl-L-arginine-p-nitroanilide
-
mutant V88D
0.4
N-alpha-benzoyl-L-arginine-p-nitroanilide
-
mutant W60A
0.6
N-alpha-benzoyl-L-arginine-p-nitroanilide
-
deltaNS2B-NS3pro
1.7
N-alpha-benzoyl-L-arginine-p-nitroanilide
-
mutant L73A
2.2
N-alpha-benzoyl-L-arginine-p-nitroanilide
-
mutant V88K
2.6
N-alpha-benzoyl-L-arginine-p-nitroanilide
-
chimeric proteases with the NS2B cofactor from Langat virus replacing the Alkhurma virus sequence
15.9
N-alpha-benzoyl-L-arginine-p-nitroanilide
-
mutant Q77A
0.0087
o-aminobenzoyl-AGKKSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.0588
o-aminobenzoyl-AGKKSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.0073
o-aminobenzoyl-AGKRSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.038
o-aminobenzoyl-AGKRSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.005
o-aminobenzoyl-AGRKSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.0213
o-aminobenzoyl-AGRKSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.02
o-aminobenzoyl-AGRRSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.02
o-aminobenzoyl-AGRRSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.0066
o-aminobenzoyl-AKKKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.0692
o-aminobenzoyl-AKKKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.0076
o-aminobenzoyl-AKKRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.0532
o-aminobenzoyl-AKKRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.0006
o-aminobenzoyl-AKRKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.0237
o-aminobenzoyl-AKRKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.002
o-aminobenzoyl-AKRRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.0314
o-aminobenzoyl-AKRRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.00013
o-aminobenzoyl-ARKKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.0673
o-aminobenzoyl-ARKKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.014
o-aminobenzoyl-ARKRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.058
o-aminobenzoyl-ARKRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.0015
o-aminobenzoyl-ARRKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.0183
o-aminobenzoyl-ARRKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.0096
o-aminobenzoyl-ARRRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.0256
o-aminobenzoyl-ARRRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.0138
o-aminobenzoyl-SAAQRRGRIGRNQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.0138
o-aminobenzoyl-SAAQRRGRIGRNQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
NS3 protease from strain NGC
0.0475
phenylacetyl-Lys-Lys-Arg-4-nitroanilide
-
pH 8.5, 22°C
0.06
phenylacetyl-Lys-Lys-Arg-4-nitroanilide
-
pH 8.5, 22°C
0.004
pyroglutamic acid-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin
mutant G22S
0.03
pyroglutamic acid-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin
wild-type
0.0586
pyroglutamic acid-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin
-
-
0.059
pyroglutamic acid-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin
-
mutant K48A
0.071
pyroglutamic acid-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin
-
wild-type
0.036
t-butoxycarbonyl-Arg-Val-Arg-Arg-7-amido-4-methylcoumarin
-
mutant K48A
0.04
t-butoxycarbonyl-Arg-Val-Arg-Arg-7-amido-4-methylcoumarin
-
wild-type
0.324
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide
-
0.415
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide
-
-
0.417
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide
-
-
0.465
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide
-
-
0.505
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide
-
2.18
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide
-
-
2.7
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide
-
0.181
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide
-
0.53
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide
-
-
0.563
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide
-
-
0.65
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide
-
-
1.249
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide
-
-
3.74
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide
-
0.12
tert-butoxycarbonyl-Gly-Arg-Arg-4-methylcoumarin 7-amide
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 1
0.125
tert-butoxycarbonyl-Gly-Arg-Arg-4-methylcoumarin 7-amide
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 3
0.15
tert-butoxycarbonyl-Gly-Arg-Arg-4-methylcoumarin 7-amide
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 2
180
tert-butoxycarbonyl-Gly-Arg-Arg-4-methylcoumarin 7-amide
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 4
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
kinetics of cysteine-substituted mutant variants
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.005
Abz-AGRK-SLTnY-amide
-
-
0.001
Abz-AGRK-SnY-amide
-
-
0.001
Abz-AGRKS-3-nitrotyrosine-amide
-
-
0.005
Abz-AGRKSLT-3-nitrotyrosine-amide
-
-
0.0967
Abz-KKQR-SAGMnY-amide
-
-
0.0967
Abz-KKQRAGVL-3-nitrotyrosine-amide
-
-
0.0045
Abz-SKKR-AGVLnY-amide
-
-
0.045
Abz-SKKR-SAGMnY-amide
-
-
0.0045
Abz-SKKRAGVL-3-nitrotyrosine-amide
-
-
0.045
Abz-SKKRSAGM-3-nitrotyrosine-amide
-
-
1.08
Ac-Arg-Lys-Lys-Arg-7-amido-4-carbamoylmethylcoumarin
pH 8.5, 22°C
5.43
Ac-D-Arg-Lys-Orn-Arg(Me)-7-amido-4-carbamoylmethylcoumarin
pH 8.5, 22°C
4.64
Ac-D-Arg-Lys-Orn-Arg-7-amido-4-carbamoylmethylcoumarin
pH 8.5, 22°C
7.99
Ac-D-Lys-Lys-Orn-Arg-7-amido-4-carbamoylmethylcoumarin
pH 8.5, 22°C
4.4
Ac-Nle-Lys-Lys-Arg-7-amido-4-carbamoylmethylcoumarin
pH 8.5, 22°C
0.112
acetyl-Nle-Lys-Arg-Arg-4-methylcoumarin 7-amide
-
pH 9.5, 37°C
2.9
benzoyl-Nle-Lys-Arg-Arg-4-methylcoumarin 7-amide
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 4
0.32 - 2.8
benzoyl-Nle-Lys-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
300
benzoyl-Nle-Lys-Arg-Arg-thiobenzylester
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 4
0.97 - 4.9
benzoyl-Nle-Lys-Thr-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
0.28 - 1.1
benzoyl-Nle-Thr-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
0.05 - 0.43
benzoyl-Thr-Lys-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
0.17 - 0.48
benzoyl-Thr-Thr-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
0.034
Boc-Gly-Arg-Arg-7-amido-4-methylcoumarin
-
-
0.109
Bz-Arg-Arg-4-methylcoumaryl-7-amide
-
-
0.111
Bz-Nle-Lys-Arg-Arg-7-amido-4-methylcoumarin
-
-
0.001
FAEGRRGAAEVLQ
-
pH 9.0, 37°C
0.02
Gly-Arg-Arg-4-methylcoumarin 7-amide
-
pH 9.0, 37°C, wild-type NS3 protease with wild-tyüe NS2B cofactor
0.003
KLAQRRVFHGVAQ
-
pH 9.0, 37°C
0.013 - 7.3
L-pGlu-L-Arg-L-Thr-L-Lys-L-Arg-7-amido-4-methylcoumarin
0.012
MKTGRRGSANGKQ
-
pH 9.0, 37°C
25.94 - 343.73
N-(2-aminobenzoyl)-L-valyl-L-lysyl-L-lysyl-N-(3-carbamoyl-4-nitrophenyl)-L-argininamide
0.006 - 0.09
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
0.0004 - 0.015
N-alpha-benzoyl-L-arginine-p-nitroanilide
0.013
N-benzoyl-3-(4-aminocyclohexyl)-L-Ala-L-Arg-4-methylcoumaryl-7-amide
-
-
0.014
N-benzoyl-3-(4-piperidinyl)-L-Ala-L-Arg-4-methylcoumaryl-7-amide
-
-
0.172
N-benzoyl-3-(trans-aminomethylcyclohexyl)-L-Ala-L-Arg-4-methylcoumaryl-7-amide
-
-
0.002
N-benzoyl-3-pyridyl-L-Ala-L-Arg-4-methylcoumaryl-7-amide
-
-
0.013
N-benzoyl-4-(aminomethyl)-L-Phe-L-Arg-4-methylcoumaryl-7-amide
-
-
0.022
N-benzoyl-4-(aminomethyl-N-isopropyl)-L-Phe-L-Arg-4-methylcoumaryl-7-amide
-
-
0.035
N-benzoyl-4-(guanidino)-L-Phe-L-Arg-4-methylcoumaryl-7-amide
-
-
0.11
N-benzyloxycarbonyl-Arg-Arg-4-methylcoumaryl-7-amide
-
-
0.001 - 0.02
o-aminobenzoyl-AGKKSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
0.01 - 0.2
o-aminobenzoyl-AGKRSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
0.005 - 0.13
o-aminobenzoyl-AGRKSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
0.061 - 0.21
o-aminobenzoyl-AGRRSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
0.004 - 0.04
o-aminobenzoyl-AKKKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
0.07 - 0.097
o-aminobenzoyl-AKKRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
0.012 - 0.04
o-aminobenzoyl-AKRKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
0.026 - 1
o-aminobenzoyl-AKRRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
0.002 - 0.05
o-aminobenzoyl-ARKKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
0.06 - 0.07
o-aminobenzoyl-ARKRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
0.005 - 0.09
o-aminobenzoyl-ARRKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
0.12 - 0.38
o-aminobenzoyl-ARRRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
0.03
o-aminobenzoyl-EVKKQRAGVLWDQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
NS3 protease from strain NGC
0.02
o-aminobenzoyl-FAAGRKSLTLNLQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
NS3 protease from strain NGC
0.14
o-aminobenzoyl-FAAQRRGRIGRNQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.04
o-aminobenzoyl-HRREKRSVALQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
NS3 protease from strain NGC
0.012
o-aminobenzoyl-KKRSSKQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.025
o-aminobenzoyl-KRRSSKQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.04
o-aminobenzoyl-LNRRRRTAGMIIQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
NS3 protease from strain NGC
0.17
o-aminobenzoyl-RTSKKRSWPLNEQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
NS3 protease from strain NGC
0.09
o-aminobenzoyl-SAAGRRGRIGRNQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.04
o-aminobenzoyl-SAAQRKGRIGRNQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.11
o-aminobenzoyl-SAAQRRGLIGRNQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.11
o-aminobenzoyl-SAAQRRGRIGNNQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.16
o-aminobenzoyl-SAAQRRGRIGRLQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.29
o-aminobenzoyl-SAAQRRGRIGRNQ-N-(2,4-dinitrophenyl)-ethylenediamine
0.18
o-aminobenzoyl-SAAQRRGRILRNQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.34
o-aminobenzoyl-SAAQRRGRTGRNQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.14
o-aminobenzoyl-SAAQRRSRIGRNQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.04
o-aminobenzoyl-TTSTRRGTGNIGQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
NS3 protease from strain NGC
5.3 - 6.3
pyroglutamic acid-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin
0.005
RIFGRRSIPVNEQ
-
pH 9.0, 37°C
0.016
SAAQRRGRIGRNQ
-
pH 9.0, 37°C
0.069
SSRKRRSHDVLTQ
-
pH 9.0, 37°C
0.18 - 0.22
t-butoxycarbonyl-Arg-Val-Arg-Arg-7-amido-4-methylcoumarin
0.007 - 0.163
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide
0.006 - 0.153
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide
0.03 - 0.13
tert-butoxycarbonyl-Gly-Arg-Arg-4-methylcoumarin 7-amide
0.041
VRGARRSGDVLWQ
-
pH 9.0, 37°C
0.32
benzoyl-Nle-Lys-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 1
0.61
benzoyl-Nle-Lys-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 3
1.4
benzoyl-Nle-Lys-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 2
2.8
benzoyl-Nle-Lys-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 4
0.97
benzoyl-Nle-Lys-Thr-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 1
1.1
benzoyl-Nle-Lys-Thr-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 3
1.4
benzoyl-Nle-Lys-Thr-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 2
4.9
benzoyl-Nle-Lys-Thr-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 4
0.28
benzoyl-Nle-Thr-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 1
0.58
benzoyl-Nle-Thr-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 3
0.76
benzoyl-Nle-Thr-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 2
1.1
benzoyl-Nle-Thr-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 4
0.05
benzoyl-Thr-Lys-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 1
0.1
benzoyl-Thr-Lys-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 3
0.2
benzoyl-Thr-Lys-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 2
0.43
benzoyl-Thr-Lys-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 4
0.17
benzoyl-Thr-Thr-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 2
0.21
benzoyl-Thr-Thr-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 1
0.33
benzoyl-Thr-Thr-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 3
0.48
benzoyl-Thr-Thr-Arg-Arg-7-amido-3-carbamoylmethyl-4-methylcoumarin
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 4
0.013
L-pGlu-L-Arg-L-Thr-L-Lys-L-Arg-7-amido-4-methylcoumarin
-
mutant enzyme T52V, in 20 mM Tris/HCl buffer, pH 8.0, at 22°C
5.25
L-pGlu-L-Arg-L-Thr-L-Lys-L-Arg-7-amido-4-methylcoumarin
-
mutant enzyme K48A, in 20 mM Tris/HCl buffer, pH 8.0, at 22°C
6.3
L-pGlu-L-Arg-L-Thr-L-Lys-L-Arg-7-amido-4-methylcoumarin
-
wild type enzyme, in 20 mM Tris/HCl buffer, pH 8.0, at 22°C
7.3
L-pGlu-L-Arg-L-Thr-L-Lys-L-Arg-7-amido-4-methylcoumarin
-
mutant enzyme R76L, in 20 mM Tris/HCl buffer, pH 8.0, at 22°C
25.94
N-(2-aminobenzoyl)-L-valyl-L-lysyl-L-lysyl-N-(3-carbamoyl-4-nitrophenyl)-L-argininamide
pH 7.4, 37°C, phosphate buffer
343.73
N-(2-aminobenzoyl)-L-valyl-L-lysyl-L-lysyl-N-(3-carbamoyl-4-nitrophenyl)-L-argininamide
pH 8.5, 37°C, Tris-CHAPS-glycerol buffer
0.006
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant linked form mutant K117A
0.01
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant unlinked form mutant A125C/V162C
0.02
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant linked form mutant A125C/V162C
0.02
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant linked form mutant K117C
0.02
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant linked form mutant S75C/K117C
0.03
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant linked form mutant I73C/P106C
0.04
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant linked form mutant K117R
0.05
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant linked form mutant S75C
0.05
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant linked form wild-type enzyme
0.05
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant unlinked form mutant K117A
0.07
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant unlinked form mutant S75C/K117C
0.08
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant unlinked form mutant I73C/P106C
0.09
N-acetyl-Gly-Arg-Arg-7-amido-4-methylcoumarin
pH 8.5, 37°C, recombinant unlinked form wild-type enzyme
0.0004
N-alpha-benzoyl-L-arginine-p-nitroanilide
-
mutant V88D
0.0006
N-alpha-benzoyl-L-arginine-p-nitroanilide
-
mutant V88K
0.0018
N-alpha-benzoyl-L-arginine-p-nitroanilide
-
mutant G81A
0.0018
N-alpha-benzoyl-L-arginine-p-nitroanilide
-
mutant W60A
0.0051
N-alpha-benzoyl-L-arginine-p-nitroanilide
-
chimeric proteases with the NS2B cofactor from Langat virus replacing the Alkhurma virus sequence
0.0058
N-alpha-benzoyl-L-arginine-p-nitroanilide
-
mutant G68A
0.008
N-alpha-benzoyl-L-arginine-p-nitroanilide
-
mutant Q77A
0.0089
N-alpha-benzoyl-L-arginine-p-nitroanilide
-
mutant L73A
0.015
N-alpha-benzoyl-L-arginine-p-nitroanilide
-
deltaNS2B-NS3pro
0.001
o-aminobenzoyl-AGKKSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.02
o-aminobenzoyl-AGKKSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.01
o-aminobenzoyl-AGKRSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.2
o-aminobenzoyl-AGKRSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.005
o-aminobenzoyl-AGRKSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.13
o-aminobenzoyl-AGRKSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.061
o-aminobenzoyl-AGRRSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.21
o-aminobenzoyl-AGRRSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.004
o-aminobenzoyl-AKKKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.04
o-aminobenzoyl-AKKKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.07
o-aminobenzoyl-AKKRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.097
o-aminobenzoyl-AKKRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.012
o-aminobenzoyl-AKRKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.04
o-aminobenzoyl-AKRKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.026
o-aminobenzoyl-AKRRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
1
o-aminobenzoyl-AKRRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.002
o-aminobenzoyl-ARKKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.05
o-aminobenzoyl-ARKKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.06
o-aminobenzoyl-ARKRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.07
o-aminobenzoyl-ARKRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.005
o-aminobenzoyl-ARRKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.09
o-aminobenzoyl-ARRKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.12
o-aminobenzoyl-ARRRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.38
o-aminobenzoyl-ARRRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.29
o-aminobenzoyl-SAAQRRGRIGRNQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
0.29
o-aminobenzoyl-SAAQRRGRIGRNQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
NS3 protease from strain NGC
5.3
pyroglutamic acid-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin
-
mutant K48A
6.3
pyroglutamic acid-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin
-
wild-type
0.18
t-butoxycarbonyl-Arg-Val-Arg-Arg-7-amido-4-methylcoumarin
-
mutant K48A
0.22
t-butoxycarbonyl-Arg-Val-Arg-Arg-7-amido-4-methylcoumarin
-
wild-type
0.007
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide
-
0.013
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide
-
-
0.044
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide
-
-
0.073
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide
-
-
0.075
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide
-
-
0.101
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide
-
0.163
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide
-
0.006
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide
-
-
0.007
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide
-
0.039
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide
-
-
0.083
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide
-
-
0.088
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide
-
-
0.153
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide
-
0.03
tert-butoxycarbonyl-Gly-Arg-Arg-4-methylcoumarin 7-amide
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 1
0.07
tert-butoxycarbonyl-Gly-Arg-Arg-4-methylcoumarin 7-amide
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 4
0.09
tert-butoxycarbonyl-Gly-Arg-Arg-4-methylcoumarin 7-amide
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 3
0.13
tert-butoxycarbonyl-Gly-Arg-Arg-4-methylcoumarin 7-amide
-
pH 8.5, 37°C, enzyme from Dengue virus serotype 2
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0442 - 5.5
(2S)-4-[3-(aminomethyl)phenyl]-2-([(2S)-4-[3-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]butanamide
0.0136 - 10.8
(2S)-4-[4-(aminomethyl)phenyl]-2-([(2S)-4-[4-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]butanamide
0.0216
(2S)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-4-[3-(carbamimidamidomethyl)phenyl]-2-([(2S)-4-[3-(carbamimidamidomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)butanamide
-
pH 8.5, 22°C
0.0853 - 17.1
(2S)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-4-[4-(carbamimidamidomethyl)phenyl]-2-([(2S)-4-[4-(carbamimidamidomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)butanamide
0.0034
2-([[3,6-bis(2,6-dimethylphenyl)-7-oxo-2-thioxo-2,3,6,7-tetrahydro[1,3]thiazolo[4,5-d]pyrimidin-5-yl]sulfanyl]methyl)-7-chloro-4H-pyrido[1,2-a]pyrimidin-4-one
-
serotype 4, pH 7.5, 37°C
0.00011
4-(guanidinomethyl)-phenylacetyl-Lys-Lys-Arg-NH2
-
pH 8.5, 22°C
0.021
4-hydroxypanduratin
-
pH and temperature not specified in the publication
0.021
4-hydroxypanduratin A
-
-
0.0049
4-[3-acetyl-5-(2-phenylquinolin-4-yl)-2,3-dihydro-1,3,4-oxadiazol-2-yl]benzoic acid
-
serotype 4, pH 7.5, 37°C
0.00082
5,6-dichloro-2H-triazolo[4,5-b]pyrazine
pH 8.0, 20°C
0.004
5-[(4-chloro-3-nitro-1H-pyrazol-1-yl)methyl]-N-[1-[2-(diethylamino)ethyl]-1H-benzimidazol-2-yl]furan-2-carboxamide
-
serotype 4, pH 7.5, 37°C
0.0667
Ac-EVKKQR-NH2
-
pH 9.0, 37°C
0.0259
Ac-FAAGRK-NH2
-
pH 9.0, 37°C
0.1523
Ac-GKR-NH2
-
pH 9.0, 37°C
0.0223
Ac-KKR-NH2
-
pH 9.0, 37°C
0.1215
Ac-KR-NH2
-
pH 9.0, 37°C
0.0121
Ac-RTSKKR-NH2
-
pH 9.0, 37°C
0.1876
Ac-SKKR-NH2
-
pH 9.0, 37°C
0.046
Ac-TTSTRR-NH2
-
pH 9.0, 37°C
0.0111 - 0.0153
agathisflavone
0.000264
antibody D05320
-
wild type enzyme, in 20 mM Tris/HCl buffer, pH 8.0, at 22°C
-
0.0004
antibody D05321
-
wild type enzyme, in 20 mM Tris/HCl buffer, pH 8.0, at 22°C
-
0.00017
antibody D05322
-
wild type enzyme, in 20 mM Tris/HCl buffer, pH 8.0, at 22°C
-
0.000031
antibody D05323
-
wild type enzyme, in 20 mM Tris/HCl buffer, pH 8.0, at 22°C
-
0.000058
antibody D05444
-
wild type enzyme, in 20 mM Tris/HCl buffer, pH 8.0, at 22°C
-
0.000035
antibody D05445
-
wild type enzyme, in 20 mM Tris/HCl buffer, pH 8.0, at 22°C
-
0.000288
antibody D05446
-
wild type enzyme, in 20 mM Tris/HCl buffer, pH 8.0, at 22°C
-
0.000000079 - 0.00007
Aprotinin
0.00075
Bz-Ala-Lys-Arg-Arg
-
-
0.0053
Bz-Ala-Lys-Arg-Arg-H
-
-
0.0094
Bz-D-Nle-Lys-Arg-Arg-H
-
-
0.0004
Bz-Lys-Arg-Arg
-
-
0.0015
Bz-Lys-Arg-Arg-H
-
-
0.0437
Bz-N-Me-Nle-Lys-Arg-Arg-H
-
-
0.0013
Bz-Nle-(3-amino)-Phe-(3-imino)-Phe-(3,4-dimethoxy)-Phe
-
predicted inhibition constant, pH and temperature not specified in the publication
0.0018
Bz-Nle-(3-guanidino)-Phe-(4-guanidino)-Phe-(4-guanidino)-Phe
-
predicted inhibition constant, pH and temperature not specified in the publication
0.0002
Bz-Nle-(4-amino)-Phe-(3-guanidino)-Phe-(4-amino)-Phe
-
predicted inhibition constant, pH and temperature not specified in the publication
0.002
Bz-Nle-(4-amino)-Phe-(3-guanidino)-Phe-Arg
-
predicted inhibition constant, pH and temperature not specified in the publication
0.0017
Bz-Nle-(4-amino)-Phe-(3-imino)-Phe-Arg
-
predicted inhibition constant, pH and temperature not specified in the publication
0.0018
Bz-Nle-(4-amino)-Phe-(4-guanidino)-Phe-Trp
-
predicted inhibition constant, pH and temperature not specified in the publication
0.0009
Bz-Nle-Ala-Arg-Arg
-
-
0.0221
Bz-Nle-Ala-Arg-Arg-H
-
-
0.0015
Bz-Nle-Arg-(3-guanidino)-Phe-(4-amino)-Phe
-
predicted inhibition constant, pH and temperature not specified in the publication
0.0286
Bz-Nle-D-Lys-Arg-Arg-H
-
-
0.0001
Bz-Nle-His-(3-guanidino)-Phe-(4-guanidino)-Phe
-
predicted inhibition constant, pH and temperature not specified in the publication
0.0008
Bz-Nle-His-(3-guanidino)-Phe-beta-(2-naphthyl)-Ala
-
predicted inhibition constant, pH and temperature not specified in the publication
0.0017
Bz-Nle-His-(3-imino)-Phe-Arg
-
predicted inhibition constant, pH and temperature not specified in the publication
0.0018
Bz-Nle-His-(4-guanidino)-Phe-(4-guanidino)-Phe
-
predicted inhibition constant, pH and temperature not specified in the publication
0.0009
Bz-Nle-His-(4-guanidino)-Phe-Trp
-
predicted inhibition constant, pH and temperature not specified in the publication
0.0005
Bz-Nle-homo-His-(3-guanidino)-Phe-(4-guanidino)-Phe
-
predicted inhibition constant, pH and temperature not specified in the publication
0.0019
Bz-Nle-homoHis-(3-guanidino)-Phe-Arg
-
predicted inhibition constant, pH and temperature not specified in the publication
0.0014
Bz-Nle-homoHis-(4-guanidino)-Phe-(4-phenyl)-Phe
-
predicted inhibition constant, pH and temperature not specified in the publication
0.125
Bz-Nle-Lys-Ala-Arg
-
-
0.5
Bz-Nle-Lys-Ala-Arg-H
-
-
0.138
Bz-Nle-Lys-Arg-(p-Cl)Phe-H
-
-
0.0186
Bz-Nle-Lys-Arg-(p-CN)Phe-H
-
-
0.0028
Bz-Nle-Lys-Arg-(p-guanidinyl)Phe-H
-
-
0.006
Bz-Nle-Lys-Arg-(p-Me)Phe-H
-
-
0.0116
Bz-Nle-Lys-Arg-(p-Ph)Phe-H
-
-
0.03315
Bz-Nle-Lys-Arg-Ala
-
-
0.193
Bz-Nle-Lys-Arg-Ala-H
-
-
0.0004
Bz-Nle-Lys-Arg-Arg
-
-
0.178
Bz-Nle-Lys-Arg-Arg(OH)-CONH-Bn
-
-
0.000043
Bz-Nle-Lys-Arg-Arg-B(OH)2
-
-
0.0829
Bz-Nle-Lys-Arg-Arg-benzoxazole
-
-
0.00085
Bz-Nle-Lys-Arg-Arg-CF3
-
-
0.0058
Bz-Nle-Lys-Arg-Arg-H
-
-
0.1275
Bz-Nle-Lys-Arg-Arg-NH2
-
-
0.5
Bz-Nle-Lys-Arg-Arg-NHSO2CF3
-
-
0.5
Bz-Nle-Lys-Arg-Arg-OH
-
-
0.0428
Bz-Nle-Lys-Arg-Arg-thiazole
-
-
0.051
Bz-Nle-Lys-Arg-D-Arg-H
-
-
0.5
Bz-Nle-Lys-Arg-homoPhe-H
-
-
0.0112
Bz-Nle-Lys-Arg-Lys
-
-
0.0205
Bz-Nle-Lys-Arg-Lys-H
-
-
0.062
Bz-Nle-Lys-Arg-Phe
-
-
0.0159
Bz-Nle-Lys-Arg-Phe-H
-
-
0.033
Bz-Nle-Lys-Arg-Phg-H
-
-
0.0016
Bz-Nle-Lys-Arg-Trp
-
predicted inhibition constant, pH and temperature not specified in the publication
0.0075
Bz-Nle-Lys-Arg-Trp-H
-
-
0.115
Bz-Nle-Lys-D-Arg-Arg-H
-
-
0.0012
Bz-Nle-Lys-Lys-Arg
-
-
0.00005
Bz-Nle-Lys-Lys-Arg-B(OH)2
-
-
0.0413
Bz-Nle-Lys-Lys-Arg-H
-
-
0.0474
Bz-Nle-Lys-N-Me-Arg-Arg-H
-
-
0.0156
Bz-Nle-Lys-Phe-Arg
-
-
0.0407
Bz-Nle-Lys-Phe-Arg-H
-
-
0.109
Bz-Nle-Lys-Pro-Arg-H
-
-
0.5
Bz-Nle-Lys-Thr-Arg-H
-
-
0.5
Bz-Nle-Lys-Thr-Arg-NH2
-
-
0.5
Bz-Nle-Lys-Thr-Arg-OH
-
-
0.1133
Bz-Nle-N-Me-Lys-Arg-Arg-H
-
-
0.0015
Bz-Nle-Phe-Arg-Arg
-
-
0.0158
Bz-Nle-Phe-Arg-Arg-H
-
-
0.0614
Bz-Nle-Pro-Arg-Arg-H
-
-
0.00025
Bz-Phe-Lys-Arg-Arg
-
-
0.0068
Bz-Phe-Lys-Arg-Arg-H
-
-
0.0004
Cbz-Lys-Arg-(4-GuPhe)P(OPh)2
-
pH 8.5, 37°C
0.0007
Cbz-Lys-Arg-(4-GuPhg)P(OPh)2
-
pH 8.5, 37°C
0.00012
Cbz-Lys-Arg-Arg
-
pH 8.5, 37°C
0.003
Cbz-Lys-Arg-ArgP(OPh)2
-
pH 8.5, 37°C
0.008
Cbz-Lys-Arg-LysP(OPh)2
-
pH 8.5, 37°C
0.0004
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
-
0.013
diphenyl (1-[[(benzyloxy)carbonyl]amino]-3-carbamimidamidopropyl)phosphonate
-
pH 8.5, 37°C
0.022
diphenyl (5-amino-1-[[(benzyloxy)carbonyl]amino]pentyl)phosphonate
-
pH 8.5, 37°C
0.01
diphenyl [[[(benzyloxy)carbonyl]amino](4-carbamimidamidophenyl)methyl]phosphonate
-
pH 8.5, 37°C
0.004
diphenyl [[[(benzyloxy)carbonyl]amino](carbamimidamido)methyl]phosphonate
-
pH 8.5, 37°C
0.0047 - 0.0257
myricetin
0.0182 - 14.7
N-[(2S)-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-4-(4-carbamimidamidophenyl)-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-lysinamide
0.0994
N-[(2S)-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-4-[3-(carbamimidamidomethyl)cyclohexa-1,5-dien-1-yl]-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-lysinamide
-
pH 8.5, 22°C
0.0756
N-[(2S)-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-4-[4-(carbamimidamidomethyl)phenyl]-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-lysinamide
-
pH 8.5, 22°C
0.134
N-[(2S)-4-[3-(aminomethyl)phenyl]-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-lysinamide
-
pH 8.5, 22°C
0.0289
N-[(2S)-4-[4-(aminomethyl)phenyl]-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-ornithinamide
-
pH 8.5, 22°C
0.0298
N-[(trans-4-carbamimidamidocyclohexyl)methyl]-N2-[(2S)-4-(3-carbamimidamidophenyl)-2-[(phenylacetyl)amino]butanoyl]-L-lysinamide
-
pH 8.5, 22°C
0.0296 - 31.1
N-[(trans-4-carbamimidamidocyclohexyl)methyl]-N2-[(2S)-4-[3-(carbamimidamidomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]-L-lysinamide
0.044
N-[(trans-4-carbamimidamidocyclohexyl)methyl]-N2-[(2S)-4-[4-(carbamimidamidomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]-L-lysinamide
-
pH 8.5, 22°C
0.00068
N2-(1,3-benzodioxol-5-ylacetyl)-L-lysyl-L-lysinamide
-
pH 8.5, 22°C
0.000039
N2-(1,3-thiazol-2-yl)-L-arginyl-N-[(1S)-2-amino-2-oxo-1-(4-[[4-(trifluoromethyl)benzyl]oxy]phenyl)ethyl]-L-lysinamide
-
pH 8.5, 37°C
0.00075
N2-(4-[(Z)-[3-(cyclohexylmethyl)-2,4-dioxo-1,3-thiazolidin-5-ylidene]methyl]benzoyl)-L-lysyl-N-[(1S)-2-amino-2-oxo-1-phenylethyl]-L-lysinamide
-
pH 8.5, 37°C
0.07
N2-(adamant-1-yl(amino)acetyl)-L-lysyl-L-lysinamide
-
pH 8.5, 22°C
0.0138
N2-(adamant-1-ylacetyl)-L-lysyl-L-lysinamide
-
pH 8.5, 22°C
0.0025
N2-(biphenyl-3-ylacetyl)-L-lysyl-N-[(1-carbamimidoylpiperidin-4-yl)methyl]-L-lysinamide
-
pH 8.0, 25°C
0.000006
N2-(biphenyl-4-ylacetyl)-L-lysyl-L-Lys-L-Arg-aldehyde
-
pH 8.5, 37°C
0.00053
N2-(biphenyl-4-ylacetyl)-L-lysyl-L-lysinamide
-
pH 8.5, 22°C
0.0048 - 0.0263
N2-(cyclohexylacetyl)-L-lysyl-L-lysinamide
0.00247
N2-(phenylacetyl)-L-lysyl-L-lysinamide
-
pH 8.5, 22°C
0.027
N2-(phenylacetyl)-L-lysyl-L-lysine
-
pH 8.5, 22°C
0.14
N2-(phenylacetyl)-L-lysyl-L-lysyl-3-methylvalinamide
-
pH 8.5, 22°C
0.075
N2-(phenylacetyl)-L-lysyl-L-lysyl-D-alaninamide
-
pH 8.5, 22°C
0.025
N2-(phenylacetyl)-L-lysyl-L-lysyl-L-alaninamide
-
pH 8.5, 22°C
0.2
N2-(phenylacetyl)-L-lysyl-L-lysyl-L-prolinamide
-
pH 8.5, 22°C
0.105
N2-(phenylacetyl)-L-lysyl-L-lysyl-L-valinamide
-
pH 8.5, 22°C
0.05
N2-(phenylacetyl)-L-lysyl-L-lysyl-N2-methylglycinamide
-
pH 8.5, 22°C
0.00256
N2-(phenylacetyl)-L-lysyl-L-lysylglycinamide
-
pH 8.5, 22°C
0.00156
N2-(phenylacetyl)-L-lysyl-N-(2-aminoprop-2-en-1-yl)-L-lysinamide
-
pH 8.5, 22°C
0.015
N2-(phenylacetyl)-L-lysyl-N-(4-amino-4-oxobutyl)-L-lysinamide
-
pH 8.5, 22°C
0.017
N2-(phenylacetyl)-L-lysyl-N-(5-amino-5-oxopentyl)-L-lysinamide
-
pH 8.5, 22°C
0.0012
N2-(phenylacetyl)-L-ornithyl-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-L-lysinamide
-
pH 8.5, 22°C
0.000009
N2-phenylacetyl-L-Lys-L-Lys-L-Arg-aldehyde
-
pH 8.5, 37°C
0.0222
N2-[(2S)-4-[3-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-L-lysinamide
-
pH 8.5, 22°C
0.00471 - 12.4
N2-[(2S)-4-[4-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-L-lysinamide
0.00013
N2-[(3,4-dichlorophenyl)acetyl]-L-lysyl-N-[(1S)-1-(1-carbamimidoylpiperidin-4-yl)-2-oxoethyl]-L-lysinamide
-
pH 8.5, 37°C
0.00011
N2-[(3,4-dichlorophenyl)acetyl]-L-ornithyl-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-L-lysinamide
-
pH 8.5, 22°C
0.00113
N2-[(3,4-dimethylphenyl)acetyl]-L-lysyl-L-lysinamide
-
pH 8.5, 22°C
0.0018
N2-[(3,4-dimethylphenyl)acetyl]-L-lysyl-L-lysylglycinamide
-
pH 8.5, 22°C
0.0012
N2-[(3-aminophenyl)acetyl]-L-lysyl-L-lysinamide
-
pH 8.5, 22°C
0.00054
N2-[(4-hydroxyphenyl)acetyl]-L-lysyl-L-lysinamide
-
pH 8.5, 22°C
0.00418
N2-[(acetylamino)(phenyl)acetyl]-L-lysyl-L-lysinamide
-
pH 8.5, 22°C
0.0036
N2-[amino(phenyl)acetyl]-L-lysyl-L-lysinamide
-
pH 8.5, 22°C
0.00036
N2-[[3-(aminomethyl)phenyl]acetyl]-L-lysyl-L-lysinamide
-
pH 8.5, 22°C
0.00018
N2-[[3-(carbamimidamidomethyl)phenyl]acetyl]-L-lysyl-L-lysinamide
-
pH 8.5, 22°C
0.00038
N2-[[4-(aminomethyl)phenyl]acetyl]-L-lysyl-L-lysinamide
-
pH 8.5, 22°C
0.00645 - 0.0831
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-3-methyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
0.00065 - 0.0116
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-L-arginyl-N-(4-carbamimidoylbenzyl)-L-argininamide
0.00082 - 0.00122
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-L-lysyl-N-(4-carbamimidoylbenzyl)-L-argininamide
0.0057 - 0.0773
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
0.00011
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-lysyl-L-lysinamide
-
pH 8.5, 22°C
0.000006
nona-D-Arg-amide
-
-
0.0199 - 0.0227
quercetin
0.01984
[4-methyl-5-(3-methylbut-2-en-1-yl)-6-phenylcyclohex-3-en-1-yl](2,4,6-trimethoxyphenyl)methanone
-
pH and temperature not specified in the publication
0.02436
[5-(3-methylbut-2-en-1-yl)-6-phenylcyclohex-3-en-1-yl](2,4,6-trimethoxyphenyl)methanone
-
pH and temperature not specified in the publication
0.03968
[6-(4-methoxyphenyl)-4-methyl-5-(3-methylbut-2-en-1-yl)cyclohex-3-en-1-yl](2,4,6-trimethoxyphenyl)methanone
-
pH and temperature not specified in the publication
additional information
additional information
-
0.0442
(2S)-4-[3-(aminomethyl)phenyl]-2-([(2S)-4-[3-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]butanamide
-
pH 8.5, 22°C
5.5
(2S)-4-[3-(aminomethyl)phenyl]-2-([(2S)-4-[3-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]butanamide
-
pH 8.5, 22°C
0.0136
(2S)-4-[4-(aminomethyl)phenyl]-2-([(2S)-4-[4-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]butanamide
-
pH 8.5, 22°C
10.8
(2S)-4-[4-(aminomethyl)phenyl]-2-([(2S)-4-[4-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]butanamide
-
pH 8.5, 22°C
0.0853
(2S)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-4-[4-(carbamimidamidomethyl)phenyl]-2-([(2S)-4-[4-(carbamimidamidomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)butanamide
-
pH 8.5, 22°C
17.1
(2S)-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-4-[4-(carbamimidamidomethyl)phenyl]-2-([(2S)-4-[4-(carbamimidamidomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]amino)butanamide
-
pH 8.5, 22°C
0.0111
agathisflavone
-
serovar DENV2, pH 9.5, temperature not specified in the publication
0.0153
agathisflavone
-
serovar DENV3, pH 9.0, temperature not specified in the publication
0.000000079
Aprotinin
-
enzyme from Dengue virus serotype 1
0.00002
Aprotinin
-
wild type enzyme, in 20 mM Tris/HCl buffer, pH 8.0, at 22°C
0.00007
Aprotinin
pH 8.0, 20°C
0.0047
myricetin
-
serovar DENV2, pH 9.5, temperature not specified in the publication
0.0257
myricetin
-
serovar DENV3, pH 9.0, temperature not specified in the publication
0.0182
N-[(2S)-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-4-(4-carbamimidamidophenyl)-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-lysinamide
-
pH 8.5, 22°C
14.7
N-[(2S)-1-[[(trans-4-carbamimidamidocyclohexyl)methyl]amino]-4-(4-carbamimidamidophenyl)-1-oxobutan-2-yl]-N2-(phenylacetyl)-L-lysinamide
-
pH 8.5, 22°C
0.0296
N-[(trans-4-carbamimidamidocyclohexyl)methyl]-N2-[(2S)-4-[3-(carbamimidamidomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]-L-lysinamide
-
pH 8.5, 22°C
31.1
N-[(trans-4-carbamimidamidocyclohexyl)methyl]-N2-[(2S)-4-[3-(carbamimidamidomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]-L-lysinamide
-
pH 8.5, 22°C
0.0048
N2-(cyclohexylacetyl)-L-lysyl-L-lysinamide
-
pH 8.5, 22°C
0.0263
N2-(cyclohexylacetyl)-L-lysyl-L-lysinamide
-
pH 8.5, 22°C
0.00471
N2-[(2S)-4-[4-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-L-lysinamide
-
pH 8.5, 22°C
12.4
N2-[(2S)-4-[4-(aminomethyl)phenyl]-2-[(phenylacetyl)amino]butanoyl]-N-[(trans-4-carbamimidamidocyclohexyl)methyl]-L-lysinamide
-
pH 8.5, 22°C
0.00645
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-3-methyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
pH 8.5, 22°C
0.0831
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-3-methyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
pH 8.5, 22°C
0.00065
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-L-arginyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
pH 8.5, 22°C
0.0116
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-L-arginyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
pH 8.5, 22°C
0.00082
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-L-lysyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
pH 8.5, 22°C
0.00122
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-L-lysyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
pH 8.5, 22°C
0.0057
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
pH 8.5, 22°C
0.0773
N2-[[4-(carbamimidamidomethyl)phenyl]acetyl]-L-arginyl-L-valyl-N-(4-carbamimidoylbenzyl)-L-argininamide
-
pH 8.5, 22°C
0.025
panduratin A
-
-
0.025
panduratin A
-
pH and temperature not specified in the publication
0.0199
quercetin
-
serovar DENV3, pH 9.0, temperature not specified in the publication
0.0227
quercetin
-
serovar DENV2, pH 9.5, temperature not specified in the publication
additional information
additional information
inhibition kinetics
-
additional information
additional information
-
inhibition kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0012
(3R,7aS)-2,3-bis(4-nitrophenyl)hexahydro-1H-pyrrolo-[1,2-c]imidazol-1-one
Dengue virus type 2
-
pH and temperature not specified in the publication
0.001263
(5-amino-1-phenylsulfonylpyrazol-3-yl) 2-bromobenzoate
West Nile virus
-
-
0.002376
(5-amino-1-phenylsulfonylpyrazol-3-yl)thiophene-2-carboxylate
West Nile virus
-
-
0.0036
(E)-N-(5-(benzylsulfanyl)-1,3,4-thiadiazol-2-yl)-2-cyano-3-(1-((2-fluorophenyl)methyl)-1H-indol-3-yl)prop-2-enamide
Dengue virus
-
pH 8.5, 37°C
0.0022
(E)-N-(5-(benzylsulfanyl)-1,3,4-thiadiazol-2-yl)-2-cyano-3-(1-((4-fluorophenyl)methyl)-1H-indol-3-yl)prop-2-enamide
Dengue virus
-
pH 8.5, 37°C
0.000208
(S)-2-acetamido-6-amino-N-((S)-5-guanidino-1-oxopentan-2-yl)hexanamide
Zika virus
-
pH and temperature not specified in the publication
0.89 - 5.9
1,10-phenanthroline
0.1
1-(2,6-difluorophenyl)-2-[1-(4-methoxybenzyl)-3-methyl-1H-pyrazol-5-yl]ethanol
West Nile virus
-
IC50 above 0.1 mM, in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.0239
1-(2,6-difluorophenyl)-2-[1-(4-methoxybenzyl)-3-methyl-1H-pyrazol-5-yl]ethanone
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.0388
1-(2-fluorophenyl)-2-[1-(4-methoxybenzyl)-3-methyl-1H-pyrazol-5-yl]ethanone
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.00926
1-(4-methoxybenzyl)-3-methyl-1H-pyrazol-5-yl 2,6-difluoro-3-methylbenzoate
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.00871
1-(4-methoxybenzyl)-3-methyl-1H-pyrazol-5-yl 2,6-difluorobenzoate
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.00403
1-(4-methoxybenzyl)-3-methyl-1H-pyrazol-5-yl benzoate
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.00943
1-benzyl-3-methyl-1H-pyrazol-5-yl 2,6-difluoro-3-methylbenzoate
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.00804
1-benzyl-3-methyl-1H-pyrazol-5-yl 2,6-difluorobenzoate
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.000019
2,6-difluoro-benzoyl-Nle-Lys-Arg-Arg-CF3-ketone
Dengue virus
-
pH 7.4, temperature not specified in the publication, versus the linked NS2B-NS3 complex
0.0039
2-([[3,6-bis(2,6-dimethylphenyl)-7-oxo-2-thioxo-2,3,6,7-tetrahydro[1,3]thiazolo[4,5-d]pyrimidin-5-yl]sulfanyl]methyl)-7-chloro-4H-pyrido[1,2-a]pyrimidin-4-one
Dengue virus
-
serotype 4, pH 7.5, 37°C
0.0018 - 0.0267
2-naphthoyl-Lys-Arg-Arg
0.1
2-[1-(4-methoxybenzyl)-3-methyl-1H-pyrazol-5-yl]-1-phenylethanol
West Nile virus
-
IC50 above 0.1 mM, in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.1
2-[1-(4-methoxybenzyl)-3-methyl-1H-pyrazol-5-yl]-1-phenylethanone
West Nile virus
-
IC50 above 0.1 mM, in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.03409
2-[[(4-methoxyphenyl)amino]methylidene]cyclohexane-1,3-dione
West Nile virus
-
-
0.0224 - 0.201
4-aminobenzoyl-Lys-Arg-Arg
0.0335 - 0.3
4-aminobenzoyl-Lys-Lys-Arg
0.0019 - 0.0112
4-aminophenylacetyl-Lys-Arg-Arg
0.00099 - 0.0234
4-phenylphenylacetyl-Lys-Arg-Arg
0.000056 - 0.0122
4-phenylphenylacetyl-Lys-Lys-Arg
0.0125
4-[3-acetyl-5-(2-phenylquinolin-4-yl)-2,3-dihydro-1,3,4-oxadiazol-2-yl]benzoic acid
Dengue virus
-
serotype 4, pH 7.5, 37°C
0.0015
5-amino-1-((4-methoxyphenyl)sulfonyl)-1H-pyrazol-3-yl benzoate
Zika virus
-
20xa0mM Tris pH 8.5, 10% glycerol, 0.01% Triton X-100, 37°C
0.01192
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2,3,4-trifluorobenzoate
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.01069
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2,3,5,6-tetrafluoro-4-methylbenzoate
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.00097
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2,3,6-trifluorobenzoate
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.02618
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2,4,5-trifluorobenzoate
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.00183
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2,4,6-trifluorobenzoate
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.00196
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2,4-difluorobenzoate
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.0049
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2,5-difluorobenzoate
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.1
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2,6-dichlorobenzoate
West Nile virus
-
IC50 above 0.1 mM, in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.00428
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2,6-difluoro-3-methylbenzoate
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.00031
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2,6-difluorobenzoate
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.1
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2-ethoxybenzoate
West Nile virus
-
IC50 above 0.1 mM, in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.04549
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2-fluoro-3-(trifluoromethyl)benzoate
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.00355
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2-methylbenzoate
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.1
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 2-nitrobenzoate
West Nile virus
-
IC50 above 0.1 mM, in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.00122
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl 3-chlorothiophene-2-carboxylate
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.005
5-amino-1-[(4-methoxyphenyl)sulfonyl]-1H-pyrazol-3-yl thiophene-3-carboxylate
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.0156
5-[(4-chloro-3-nitro-1H-pyrazol-1-yl)methyl]-N-[1-[2-(diethylamino)ethyl]-1H-benzimidazol-2-yl]furan-2-carboxamide
Dengue virus
-
serotype 4, pH 7.5, 37°C
0.0138
5-[(E)-2-(2,6-difluorophenyl)ethenyl]-1-(4-methoxybenzyl)-3-methyl-1H-pyrazole
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.01007
6-methoxy-3-methyl-1H-benzo[de]cinnoline
West Nile virus
-
-
0.0471 - 0.0532
acetyl-Ala-Arg-agmatine
0.0312 - 0.0382
acetyl-Ala-Lys-agmatine
0.0237 - 0.0271
acetyl-Arg-Lys-agmatine
0.0024 - 0.058
acetyl-Lys-Arg-Arg
0.0168 - 0.0187
acetyl-Lys-Lys-agmatine
0.00097 - 0.115
acetyl-Lys-Lys-Arg
0.0268 - 0.0305
acetyl-Trp-Lys-agmatine
0.0151 - 0.0175
agathisflavone
0.0001024
Aprotinin
West Nile virus
-
-
0.112 - 0.3
benzoyl-Lys-Lys(acetyl)-Arg
0.033 - 0.3
benzoyl-Lys-Lys(benzoyl)-Arg
0.0242 - 0.3
benzoyl-Lys-Lys(benzyl)-Arg
0.0083 - 0.3
benzoyl-Lys-Lys(p-anisoyl)-Arg
0.00042 - 0.127
benzoyl-Lys-Lys-Arg
0.0026 - 0.0095
benzoyl-Nle-Lys-Arg-Arg
0.000038
benzoyl-Nle-Lys-Arg-Arg-B(OH)2
Dengue virus
-
pH 7.4, temperature not specified in the publication, versus the linked NS2B-NS3 complex
0.0014 - 0.0158
cinnamoyl-Lys-Arg-Arg
0.0023
cyclo(D-arginyl-L-arginyl-L-arginyl-L-lysyl-L-seryl-4-phenyl-L-phenylalanyl-L-seryl-D-arginyl)
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0037
cyclo(D-arginyl-L-arginyl-L-arginyl-L-lysyl-L-seryl-4-phenyl-L-phenylalanyl-L-seryl-D-phenylalanyl)
Dengue virus type 2
-
pH and temperature not specified in the publication
0.2
cyclo(L-alanylglycyl-L-alanyl-L-arginyl-L-lysyl-L-serylglycyl-L-cysteinyl)
Dengue virus type 2
-
pH and temperature not specified in the publication
0.2
cyclo(L-alanylglycyl-L-lysyl-L-alanyl-L-lysyl-L-serylglycyl-L-cysteinyl)
Dengue virus type 2
-
pH and temperature not specified in the publication
0.2
cyclo(L-alanylglycyl-L-lysyl-L-arginyl-L-alanyl-L-serylglycyl-L-cysteinyl)
Dengue virus type 2
-
pH and temperature not specified in the publication
0.2
cyclo(L-alanylglycyl-L-lysyl-L-arginyl-L-lysyl-L-alanylglycyl-L-cysteinyl)
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0393
cyclo(L-alanylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-L-phenylalanyl-L-cysteinyl)
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0574
cyclo(L-alanylglycyl-L-lysyl-L-arginyl-L-lysyl-L-serylglycyl-L-alanyl)
Dengue virus type 2
-
pH and temperature not specified in the publication
0.114
cyclo(L-alanylglycyl-L-lysyl-L-arginyl-L-lysyl-L-serylglycyl-L-cysteinyl)
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0038
cyclo(L-arginyl-L-lysyl-L-seryl-4-phenyl-L-phenylalanyl-L-seryl-D-phenylalanyl-D-prolyl-L-arginyl)
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0038
cyclo(L-arginyl-L-lysyl-L-seryl-4-phenyl-L-phenylalanyl-L-seryl-D-phenylalanyl-D-prolyl-L-lysyl)
Dengue virus type 2
-
pH and temperature not specified in the publication
0.00038 - 0.172
cyclopropionyl-Lys-Lys-Arg
0.0017
cyclo[3-(1-naphthyl)-L-alanyl-D-phenylalanyl-D-arginyl-L-arginyl-L-arginyl-L-lysyl-L-alanyl-(2S)-2-amino-4-phenylbutanoyl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0016
cyclo[3-(1-naphthyl)-L-alanyl-D-phenylalanyl-D-arginyl-L-arginyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0021
cyclo[3-(1-naphthyl)-L-alanyl-D-phenylalanyl-D-arginyl-L-arginyl-L-arginyl-L-lysyl-N6-[CH2NH]-L-alanyl-(2S)-2-amino-4-phenylbutanoyl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0011
cyclo[3-(2-naphthyl)-D-alanyl-D-arginyl-L-arginyl-L-arginyl-L-lysyl-3-(2-naphthyl)-D-alanyl-(2S)-2-amino-4-phenylbutanoyl-L-phenylalanyl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0017
cyclo[3-(2-naphthyl)-D-alanyl-D-arginyl-L-arginyl-L-arginyl-L-lysyl-D-phenylalanyl-(2S)-2-amino-4-phenylbutanoyl-L-phenylalanyl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0015
cyclo[3-(2-naphthyl)-L-alanyl-D-phenylalanyl-D-arginyl-L-arginyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0026
cyclo[3-(2-naphthyl)-L-alanyl-L-seryl-D-phenylalanyl-D-prolyl-L-lysyl-L-arginyl-L-lysyl-L-seryl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0033
cyclo[D-alanyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl-L-seryl-D-phenylalanyl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0151
cyclo[L-alany-(2R)-2-phenylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0222
cyclo[L-alany-(2S)-2-phenylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0162
cyclo[L-alanyl-(2R)-2-amino-4-phenylbutanoylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0256
cyclo[L-alanyl-(2S)-2-amino-4-phenylbutanoylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0076
cyclo[L-alanyl-D-phenylalanylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0285
cyclo[L-alanyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl-L-seryl-D-phenylalanyl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0198
cyclo[L-alanyl-L-phenylalanylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0387
cyclo[L-alanylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2R)-2-amino-4-phenylbutanoyl-L-cysteinyl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0184
cyclo[L-alanylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl-L-alanyl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0092
cyclo[L-alanylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl-L-cysteinyl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0221
cyclo[L-alanylglycyl-L-lysyl-L-arginyl-L-lysyl-L-seryl-(2S)-2-phenylglycyl-L-cysteinyl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.00095
cyclo[L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl-L-seryl-D-phenylalanyl-D-prolyl-L-lysyl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.052
cyclo[L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl-L-seryl-D-phenylalanyl-L-prolyl-L-lysyl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.005
cyclo[L-arginyl-L-lysyl-L-seryl-(2S)-2-amino-4-phenylbutanoyl-L-seryl-D-phenylalanylglycyl-L-lysyl]
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0012
L-methionyl-N-(4-nitrophenyl)-L-prolinamide
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0223 - 0.0293
myricetin
0.021 - 0.022
N-(6-nitro-2,3-dihydro-1,3-benzothiazol-2-yl)-2-([4-(trifluoromethyl)phenyl]sulfanyl)benzamide
0.026
N-(6-nitro-2,3-dihydro-1,3-benzothiazol-2-yl)-3-[(4-nitrophenyl)sulfanyl]benzamide
Dengue virus
-
protease of serotype DENV-2, pH not specified in the publication, temperature not specified in the publication
0.04771
N-(9-ethylcarbazol-3-yl)-2-[(4-ethyl-5-furan-2-yl-1,2,4-triazol-3-yl)sulfanyl]acetamide
West Nile virus
-
-
0.1
N-[(2S)-6-amino-1-([(2S)-6-amino-1-[(3R)-3-(carbamimidamidomethyl)pyrrolidin-1-yl]-1-oxohexan-2-yl]amino)-1-oxohexan-2-yl]-2-(biphenyl-4-yl)acetamide
West Nile virus
-
pH 8.0, 37°C, value above
0.02
N-[(2S)-6-amino-1-([(2S)-6-amino-1-[(3S)-3-(carbamimidamidomethyl)pyrrolidin-1-yl]-1-oxohexan-2-yl]amino)-1-oxohexan-2-yl]-2-(biphenyl-4-yl)acetamide
West Nile virus
-
pH 8.0, 37°C
0.1
N-[(2S)-6-amino-1-([(2S)-6-amino-1-[4-(carbamimidamidomethyl)piperidin-1-yl]-1-oxohexan-2-yl]amino)-1-oxohexan-2-yl]-2-(biphenyl-4-yl)acetamide
West Nile virus
-
pH 8.0, 37°C, value above
0.0049
N2-(biphenyl-3-ylacetyl)-L-lysyl-N-[(1-carbamimidoylpiperidin-4-yl)methyl]-L-lysinamide
Murray Valley encephalitis virus
-
pH 8.0, 25°C
0.0047
N2-(biphenyl-4-ylacetyl)-L-lysyl-N-(4-carbamimidamidobutyl)-L-lysinamide
West Nile virus
-
pH 8.0, 37°C
0.1
N2-(biphenyl-4-ylacetyl)-L-lysyl-N-(trans-4-carbamimidamidocyclohexyl)-L-lysinamide
West Nile virus
-
pH 8.0, 37°C, value above
0.0612
N2-(biphenyl-4-ylacetyl)-L-lysyl-N-[(2E)-4-carbamimidamidobut-2-en-1-yl]-L-lysinamide
West Nile virus
-
pH 8.0, 37°C
0.1
N2-(biphenyl-4-ylcarbonyl)-L-lysyl-N-(2-carbamimidamidoethyl)-L-lysinamide
West Nile virus
-
pH 8.0, 37°C, value above
0.1
N2-(biphenyl-4-ylcarbonyl)-L-lysyl-N-(3-carbamimidamidopropyl)-L-lysinamide
West Nile virus
-
pH 8.0, 37°C, value above
0.1
N2-(biphenyl-4-ylcarbonyl)-L-lysyl-N-(5-carbamimidamidopentyl)-L-lysinamide
West Nile virus
-
pH 8.0, 37°C, value above
0.00104 - 0.00106
N2-(thiophen-2-ylcarbonyl)-L-arginyl-N-[(1S)-2-amino-2-oxo-1-(4-[[4-(trifluoromethyl)benzyl]oxy]phenyl)ethyl]-L-lysinamide
0.0182
N2-acetyl-L-lysyl-N-(4-carbamimidamidobutyl)-L-lysinamide
West Nile virus
-
pH 8.0, 37°C
0.00039 - 0.0067
phenylacetyl-Lys-Arg-Arg
0.0007 - 0.167
phenylacetyl-Lys-Lys-Arg
0.0197 - 0.3
phenylpropionyl-Lys-Arg-Arg
0.0085 - 0.218
propionyl-Lys-Arg-Arg
0.00085 - 0.3
propionyl-Lys-Lys-Arg
0.0227 - 0.0352
quercetin
0.001353
SID-3717586
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.00011
SID-4245669
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.000105
SID-852843
West Nile virus
-
in 10 mM Tris-HCl buffer, pH 8.0, containing 20% (v/v) glycerol and 0.005% Brij 35
0.0018 - 0.274
trifluoroacetyl-Lys-Lys-Arg
0.001353
[2-(2-cyanoethyl)-5-methylpyrazol-3-yl] benzoate
West Nile virus
-
-
0.03857
[4-(2,3-dimethylphenyl)piperazin-1-yl]-(2-ethylsulfonyl-3,4-dihydro-1H-isoquinolin-3-yl)methanone
West Nile virus
-
-
0.001161
[5-amino-1-(4-fluorophenyl)sulfonylpyrazol-3-yl] thiophene-2-carboxylate
West Nile virus
-
-
0.001651
[5-amino-1-(4-fluorophenyl)sulfonylpyrazol-3-yl]furan-2-carboxylate
West Nile virus
-
-
0.000297
[5-amino-1-(4-methoxyphenyl)sulfonylpyrazol-3-yl] 2-bromobenzoate
West Nile virus
-
-
0.000105
[5-amino-1-(4-methoxyphenyl)sulfonylpyrazol-3-yl] benzoate
West Nile virus
-
-
0.000553
[5-amino-1-(4-methoxyphenyl)sulfonylpyrazol-3-yl] furan-2-carboxylate
West Nile virus
-
-
0.00011
[5-amino-1-(4-methoxyphenyl)sulfonylpyrazol-3-yl] thiophene-2-carboxylate
West Nile virus
-
-
0.01439
[5-amino-1-(4-methylphenyl)sulfonylpyrazol-3-yl] furan-2-carboxylate
West Nile virus
-
-
0.002405
[5-amino-1-(4-methylphenyl)sulfonylpyrazol-3-yl] thiophene-2-carboxylate
West Nile virus
-
-
0.89
1,10-phenanthroline
Hepacivirus C
-
inhibition of NS2/3 auto-cleavage
5.9
1,10-phenanthroline
Hepacivirus C
-
inhibition of NS3 protease activity
0.0018
2-naphthoyl-Lys-Arg-Arg
West Nile virus
-
pH 8.5, 20°C
0.0267
2-naphthoyl-Lys-Arg-Arg
Dengue virus
-
pH 8.5, 20°C
0.0224
4-aminobenzoyl-Lys-Arg-Arg
West Nile virus
-
pH 8.5, 20°C
0.201
4-aminobenzoyl-Lys-Arg-Arg
Dengue virus
-
pH 8.5, 20°C
0.0335
4-aminobenzoyl-Lys-Lys-Arg
West Nile virus
-
pH 8.5, 20°C
0.3
4-aminobenzoyl-Lys-Lys-Arg
Dengue virus
-
pH 8.5, 20°C, value above
0.0019
4-aminophenylacetyl-Lys-Arg-Arg
West Nile virus
-
pH 8.5, 20°C
0.0112
4-aminophenylacetyl-Lys-Arg-Arg
Dengue virus
-
pH 8.5, 20°C
0.00099
4-phenylphenylacetyl-Lys-Arg-Arg
West Nile virus
-
pH 8.5, 20°C
0.0234
4-phenylphenylacetyl-Lys-Arg-Arg
Dengue virus
-
pH 8.5, 20°C
0.000056
4-phenylphenylacetyl-Lys-Lys-Arg
West Nile virus
-
pH 8.5, 20°C
0.0122
4-phenylphenylacetyl-Lys-Lys-Arg
Dengue virus
-
pH 8.5, 20°C
0.0471
acetyl-Ala-Arg-agmatine
Murray Valley encephalitis virus
-
pH 8.0, 25°C
0.0532
acetyl-Ala-Arg-agmatine
West Nile virus
-
pH 8.0, 25°C
0.0312
acetyl-Ala-Lys-agmatine
Murray Valley encephalitis virus
-
pH 8.0, 25°C
0.0382
acetyl-Ala-Lys-agmatine
West Nile virus
-
pH 8.0, 25°C
0.0237
acetyl-Arg-Lys-agmatine
Murray Valley encephalitis virus
-
pH 8.0, 25°C
0.0271
acetyl-Arg-Lys-agmatine
West Nile virus
-
pH 8.0, 25°C
0.0024
acetyl-Lys-Arg-Arg
West Nile virus
-
pH 8.5, 20°C
0.058
acetyl-Lys-Arg-Arg
Dengue virus
-
pH 8.5, 20°C
0.0168
acetyl-Lys-Lys-agmatine
Murray Valley encephalitis virus
-
pH 8.0, 25°C
0.0187
acetyl-Lys-Lys-agmatine
West Nile virus
-
pH 8.0, 25°C
0.00097
acetyl-Lys-Lys-Arg
West Nile virus
-
pH 8.5, 20°C
0.115
acetyl-Lys-Lys-Arg
Dengue virus
-
pH 8.5, 20°C
0.0268
acetyl-Trp-Lys-agmatine
Murray Valley encephalitis virus
-
pH 8.0, 25°C
0.0305
acetyl-Trp-Lys-agmatine
West Nile virus
-
pH 8.0, 25°C
0.0151
agathisflavone
Dengue virus
-
serovar DENV2, pH 9.5, temperature not specified in the publication
0.0175
agathisflavone
Dengue virus
-
serovar DENV3, pH 9.0, temperature not specified in the publication
0.112
benzoyl-Lys-Lys(acetyl)-Arg
West Nile virus
-
pH 8.5, 20°C
0.3
benzoyl-Lys-Lys(acetyl)-Arg
Dengue virus
-
pH 8.5, 20°C, value above
0.033
benzoyl-Lys-Lys(benzoyl)-Arg
West Nile virus
-
pH 8.5, 20°C
0.3
benzoyl-Lys-Lys(benzoyl)-Arg
Dengue virus
-
pH 8.5, 20°C, value above
0.0242
benzoyl-Lys-Lys(benzyl)-Arg
West Nile virus
-
pH 8.5, 20°C
0.3
benzoyl-Lys-Lys(benzyl)-Arg
Dengue virus
-
pH 8.5, 20°C, value above
0.0083
benzoyl-Lys-Lys(p-anisoyl)-Arg
West Nile virus
-
pH 8.5, 20°C
0.3
benzoyl-Lys-Lys(p-anisoyl)-Arg
Dengue virus
-
pH 8.5, 20°C, value above
0.00042
benzoyl-Lys-Lys-Arg
West Nile virus
-
pH 8.5, 20°C
0.127
benzoyl-Lys-Lys-Arg
Dengue virus
-
pH 8.5, 20°C
0.0026
benzoyl-Nle-Lys-Arg-Arg
West Nile virus
-
pH 8.5, 20°C
0.0095
benzoyl-Nle-Lys-Arg-Arg
Dengue virus
-
pH 8.5, 20°C
0.0014
cinnamoyl-Lys-Arg-Arg
West Nile virus
-
pH 8.5, 20°C
0.0158
cinnamoyl-Lys-Arg-Arg
Dengue virus
-
pH 8.5, 20°C
0.00038
cyclopropionyl-Lys-Lys-Arg
West Nile virus
-
pH 8.5, 20°C
0.172
cyclopropionyl-Lys-Lys-Arg
Dengue virus
-
pH 8.5, 20°C
0.0223
myricetin
Dengue virus
-
serovar DENV2, pH 9.5, temperature not specified in the publication
0.0293
myricetin
Dengue virus
-
serovar DENV3, pH 9.0, temperature not specified in the publication
0.021
N-(6-nitro-2,3-dihydro-1,3-benzothiazol-2-yl)-2-([4-(trifluoromethyl)phenyl]sulfanyl)benzamide
Dengue virus
-
protease of serotype DENV-3, pH not specified in the publication, temperature not specified in the publication
0.022
N-(6-nitro-2,3-dihydro-1,3-benzothiazol-2-yl)-2-([4-(trifluoromethyl)phenyl]sulfanyl)benzamide
Dengue virus
-
protease of serotype DENV-2, pH not specified in the publication, temperature not specified in the publication
0.00104
N2-(thiophen-2-ylcarbonyl)-L-arginyl-N-[(1S)-2-amino-2-oxo-1-(4-[[4-(trifluoromethyl)benzyl]oxy]phenyl)ethyl]-L-lysinamide
Zika virus
recombinant linked protease, pH 8.5, 37°C
0.00106
N2-(thiophen-2-ylcarbonyl)-L-arginyl-N-[(1S)-2-amino-2-oxo-1-(4-[[4-(trifluoromethyl)benzyl]oxy]phenyl)ethyl]-L-lysinamide
Zika virus
recombinant unlinked protease, pH 8.5, 37°C
0.00039
phenylacetyl-Lys-Arg-Arg
West Nile virus
-
pH 8.5, 20°C
0.0067
phenylacetyl-Lys-Arg-Arg
Dengue virus
-
pH 8.5, 20°C
0.0007
phenylacetyl-Lys-Lys-Arg
West Nile virus
-
pH 8.5, 20°C
0.167
phenylacetyl-Lys-Lys-Arg
Dengue virus
-
pH 8.5, 20°C
0.0197
phenylpropionyl-Lys-Arg-Arg
West Nile virus
-
pH 8.5, 20°C
0.3
phenylpropionyl-Lys-Arg-Arg
Dengue virus
-
pH 8.5, 20°C, value above
0.0085
propionyl-Lys-Arg-Arg
West Nile virus
-
pH 8.5, 20°C
0.218
propionyl-Lys-Arg-Arg
Dengue virus
-
pH 8.5, 20°C
0.00085
propionyl-Lys-Lys-Arg
West Nile virus
-
pH 8.5, 20°C
0.3
propionyl-Lys-Lys-Arg
Dengue virus
-
pH 8.5, 20°C, value above
0.0227
quercetin
Dengue virus
-
serovar DENV3, pH 9.0, temperature not specified in the publication
0.0352
quercetin
Dengue virus
-
serovar DENV2, pH 9.5, temperature not specified in the publication
0.0018
trifluoroacetyl-Lys-Lys-Arg
West Nile virus
-
pH 8.5, 20°C
0.274
trifluoroacetyl-Lys-Lys-Arg
Dengue virus
-
pH 8.5, 20°C
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evolution
comparative analysis of the substrate specificity reveals that ZIKV NS3 protease follows the typical pattern for flaviviruses
evolution
-
the flavivirus NS2B-NS3 protease is highly conserved in Zika, West Nile, and Dengue viruses
evolution
-
the flavivirus NS2B-NS3 protease is highly conserved in Zika, West Nile, and Dengue viruses
evolution
-
the flavivirus NS2B-NS3 protease is highly conserved in Zika, West Nile, and Dengue viruses
physiological function
-
required for viral replication
physiological function
-
autophagy-related protein 16-1 (ATG16L1) and eukaryotic translation initiation factor 4 gamma 1 (eIF4G1) are dramatically depleted during Zika virus infection. ATG16L1 and eIF4G1 mediate type-II interferon production and host-cell translation, respectively, likely aiding immune system evasion and driving the Zika life cycle
physiological function
enzyme NS2B-NS3pro has a critical role in polyprotein maturation and viral infectivity
physiological function
NS2B-NS3 protease consists of the NS2B cofactor and the NS3 protease domain and is essential for cleavage of the ZIKV polyprotein precursor and generation of fully functional viral proteins. Cell toxicity assays. The enzyme cleaves human Sox2 protein, which plays a critical role in neural stem cells by maintaining the activity of multiple genes involved in self-renewal and by priming the epigenetic landscape for the onset of neuronal differentiation. Sox2 is cleaved by ZIKV NS2B-NS3pro only at a very high enzyme/substrate ratio Sox2 insufficiency results in a plethora of developmental neuronal malformations in the human brain
physiological function
-
the complex of NS2B and NS3 (NS2B/NS3) in the serine protease enzyme is essential for viral replication
physiological function
the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response
physiological function
the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response
physiological function
the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response
physiological function
the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response
physiological function
the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response
physiological function
the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response
physiological function
the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response
physiological function
the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response
physiological function
the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response
physiological function
the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response
physiological function
the NS2B-NS3 protease is essential for the dengue virus (DENV) replication process
physiological function
-
the two-component viral protease NS2B-NS3 is required for the production of mature viruses and plays a key role in maintaining infectivity
physiological function
the viral protease that processes viral polyproteins
physiological function
the virus possesses a two-component (NS2B/NS3) serine protease that cleaves the viral precursor proteins
physiological function
the Zika virus (ZIKV) relies on its NS2B/NS3 protease for polyprotein processing
physiological function
the ZIKV NS2B/NS3 protease is responsible for cleavage of the viral polyprotein at five sites
physiological function
-
viral NS2B-NS3 protease processes viral polyprotein and is essential for the virus replication
physiological function
ZIKV expresses the serine protease NS3 which is responsible for viral protein processing and replication
physiological function
Dengue virus type 2 Thailand/16681/1984
-
enzyme NS2B-NS3pro has a critical role in polyprotein maturation and viral infectivity
-
physiological function
Dengue virus type 2 Thailand/16681/1984
-
the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response
-
physiological function
-
the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response
-
physiological function
-
the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response
-
physiological function
-
the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response
-
physiological function
-
the NS2B-NS3 protease is essential for the dengue virus (DENV) replication process
-
physiological function
Zika virus Puerto Rico isolate
-
the ZIKV NS2B/NS3 protease is responsible for cleavage of the viral polyprotein at five sites
-
physiological function
dengue virus type I Nauru/West Pac/1974
-
the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response
-
physiological function
-
the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response
-
physiological function
-
the virus possesses a two-component (NS2B/NS3) serine protease that cleaves the viral precursor proteins
-
physiological function
Zika virus Brazilian isolate BeH823339
-
the Zika virus (ZIKV) relies on its NS2B/NS3 protease for polyprotein processing
-
physiological function
-
the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response
-
physiological function
-
the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response
-
additional information
enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis
additional information
enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis
additional information
enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis
additional information
enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis
additional information
enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis
additional information
enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis
additional information
enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis
additional information
enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis
additional information
enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis
additional information
enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis
additional information
increased activity of unlinked Zika virus NS2B/NS3 protease compared to linked Zika virus protease. Enzyme structure homology modeling and molecular dynamics simulations of linked and unlinked protease, overview
additional information
-
increased activity of unlinked Zika virus NS2B/NS3 protease compared to linked Zika virus protease. Enzyme structure homology modeling and molecular dynamics simulations of linked and unlinked protease, overview
additional information
molecular dynamics simulations of the NS2B/NS3 protease complexes with six peptide substrates (capsid, intNS3, 2A/2B, 4B/5, 3/4A and 2B/3 containing the proteolytic site between P1 and P1' subsites) of DENV type 2 to compare the specificity of the protein-substrate binding recognition, overview. Although all substrates are in the active conformation for cleavage reaction by NS2B/NS3 protease, their binding strength is different. The simulated results of intermolecular hydrogen bonds and decomposition energies suggest that among the ten substrate residues (P5-P5') the P1 and P2 subsites play a major role in the binding with the focused protease. The arginine residue at these two subsites shows preferential binding at the active site. Besides, the P3, P1', P2' and P4' subsites show a less contribution in binding interaction. The catalytic water is detected nearby the carbonyl oxygen of the P1 reacting center of the capsid, intNS3, 2A/2B and 4B/5 peptides. The order of absolute binding free energy between these substrates and the NS2B/NS3 protease is capsid, intNS3, 2A/2B, 4B/5, 3/4A, 2B/3 in descending order in a relative correspondence with previous experimentally derived values. Hydrogen bond patterns of substrate binding
additional information
-
solution NMR spectrum of recombinant gZiPro enzyme without inhibitor, overview. The inhibitor-bound gZiPro-AcKR-H complex adopts the closed conformation
additional information
structure of the NS2B-NS3 protease from Zika virus after self-cleavage. Analysis of the post-proteolysis state structure of the enzyme during viral polyprotein processing providing insights into peptide substrate recognition by the protease, Protease activity analysis of gZiPro, eZiPro and bZiPro
additional information
-
structure of the NS2B-NS3 protease from Zika virus after self-cleavage. Analysis of the post-proteolysis state structure of the enzyme during viral polyprotein processing providing insights into peptide substrate recognition by the protease, Protease activity analysis of gZiPro, eZiPro and bZiPro
additional information
structure-function studies of ZIKV NS2B-NS3 protease
additional information
-
structure-function studies of ZIKV NS2B-NS3 protease
additional information
-
the enzyme is a complex of NS2B cofactor and NS3 protein. It adopts an open or closed conformation in crystal structures with different NS2B C-terminus (NS2Bc) positioning. In solution, NS2B-NS3p forms a mixture of open, closed and maybe other intermediate conformations. Analysis of the conformational changes using 19F NMR spectroscopy and enzyme mutant H51A/S75C. Low pH or bovine pancreatic trypsin inhibitor (BPTI) binding promote the conformation change from open to closed, showing the importance of charge forces in the interaction between NS2Bc and NS3p. NS3p residue His51 plays a crucial role in the pH-dependent conformational exchange by charge interacting with NS2Bc
additional information
the protease is a two-component system such that a portion of NS2B in addition to the protease portion of NS3 is also required for proteolytic activity. The enzymatic activity appears to be dependent on the movement of NS2B and may rely on the flexibility of the protease core. Locking the enzyme into the closed conformation dramatically increases the activity, strongly suggesting that the closed conformation is the active conformation. The observed resting state of the enzyme depends largely on the construct used to express the NS2B-NS3pro complex. In an unlinked construct, in which the NS2B and NS3 regions exist as independent, co-expressed polypeptides, the enzyme rests predominantly in a closed, active conformation. In contrast, in a linked construct, in which NS2B and NS3 are attached by a nine-amino acid linker, NS2B-NS3pro adopts a more relaxed, alternative conformation. Nevertheless, even the unlinked construct samples both the closed and other alternative conformations. 4-(2-Aminoethyl)benzenesulfonyl fluoride (AEBSF) induction of the closed conformation. Structure-function analysis, overview
additional information
-
the unique cofactor region of zika virus NS2B-NS3 protease facilitates cleavage of key host proteins
additional information
-
the unlinked NS2B-NS3 protease adopts a closed conformation in which NS2B engages NS3 to form an empty substrate-binding site
additional information
-
the viral protease is a two-component serine protease formed by the N-terminal part of NS3 and the cofactor region of NS2B, a membrane protein essential for the membrane location of NS3
additional information
-
the viral protease is a two-component serine protease formed by the N-terminal part of NS3 and the cofactor region of NS2B, a membrane protein essential for the membrane location of NS3
additional information
Dengue virus type 2 Thailand/16681/1984
-
the protease is a two-component system such that a portion of NS2B in addition to the protease portion of NS3 is also required for proteolytic activity. The enzymatic activity appears to be dependent on the movement of NS2B and may rely on the flexibility of the protease core. Locking the enzyme into the closed conformation dramatically increases the activity, strongly suggesting that the closed conformation is the active conformation. The observed resting state of the enzyme depends largely on the construct used to express the NS2B-NS3pro complex. In an unlinked construct, in which the NS2B and NS3 regions exist as independent, co-expressed polypeptides, the enzyme rests predominantly in a closed, active conformation. In contrast, in a linked construct, in which NS2B and NS3 are attached by a nine-amino acid linker, NS2B-NS3pro adopts a more relaxed, alternative conformation. Nevertheless, even the unlinked construct samples both the closed and other alternative conformations. 4-(2-Aminoethyl)benzenesulfonyl fluoride (AEBSF) induction of the closed conformation. Structure-function analysis, overview
-
additional information
Dengue virus type 2 Thailand/16681/1984
-
enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis
-
additional information
-
enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis
-
additional information
-
enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis
-
additional information
-
enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis
-
additional information
Zika virus Puerto Rico isolate
-
increased activity of unlinked Zika virus NS2B/NS3 protease compared to linked Zika virus protease. Enzyme structure homology modeling and molecular dynamics simulations of linked and unlinked protease, overview
-
additional information
dengue virus type I Nauru/West Pac/1974
-
enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis
-
additional information
-
enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis
-
additional information
-
molecular dynamics simulations of the NS2B/NS3 protease complexes with six peptide substrates (capsid, intNS3, 2A/2B, 4B/5, 3/4A and 2B/3 containing the proteolytic site between P1 and P1' subsites) of DENV type 2 to compare the specificity of the protein-substrate binding recognition, overview. Although all substrates are in the active conformation for cleavage reaction by NS2B/NS3 protease, their binding strength is different. The simulated results of intermolecular hydrogen bonds and decomposition energies suggest that among the ten substrate residues (P5-P5') the P1 and P2 subsites play a major role in the binding with the focused protease. The arginine residue at these two subsites shows preferential binding at the active site. Besides, the P3, P1', P2' and P4' subsites show a less contribution in binding interaction. The catalytic water is detected nearby the carbonyl oxygen of the P1 reacting center of the capsid, intNS3, 2A/2B and 4B/5 peptides. The order of absolute binding free energy between these substrates and the NS2B/NS3 protease is capsid, intNS3, 2A/2B, 4B/5, 3/4A, 2B/3 in descending order in a relative correspondence with previous experimentally derived values. Hydrogen bond patterns of substrate binding
-
additional information
-
enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis
-
additional information
-
enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis
-
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deltaV88
-
deletion mutant
G68A
-
substitution in the NS2B sequence, decreased activity compared with that of the wild-type enzyme
G81A
-
substitution in the NS2B sequence, decreased activity compared with that of the wild-type enzyme
L73A
-
substitution in the NS2B sequence, decreased activity compared with that of the wild-type enzyme
Q77A
-
substitution in the NS2B sequence, mutation has greater effects on substrate binding than on the reaction rate
V88D
-
reduced activity compared with that of the wild-type
V88K
-
reduced activity compared with that of the wild-type
W60A
-
substitution in the NS2B sequence, decreased activity compared with that of the wild-type enzyme
D129A
-
mutant shows 39fold reduction in catalytic efficacy compared to wild-type
D129E
-
no significant loss of activity
D129L
-
no significant loss of activity
D129R
-
no significant loss of activity
D129S
-
no significant loss of activity
G133A
-
mutant shows 10fold reduced catalytic activity
G148A
-
mutant exhibits impaired autolytic activity
I165A
-
mutant shows a drastic decrease in catalytic efficacy and a drastic increase in Km
K26A
-
mutant exhibits impaired autolytic activity
L115A
-
mutant shows activity comparable to wild-type
N152A
-
mutant shows no a complete inactivation but a 60fold reduced catalytic activity
S163A
-
mutant shows 12fold reduction in catalytic efficacy compared to wild-type
T134A
-
mutant shows 2.2fold reduction in catalytic efficacy compared to wild-type
A125C/V162C
site-directed mutagenesis, the mutant shows 32% reduction in activity due to the cysteine substitution. Linked A125C/V162C, in which both mutations are within the protease domain, does not migrate differently without DTT. The unlinked either trap does not form intermolecular disulfide bonds
H51A
-
site-directed mutagenesis, the mutation of NS3 protein impairs the charge interaction and the pH dependence of the conformational changes. It stabilizes the open conformation, while the addition of BPTI still converts NS2B-NS3p from open to closed conformation
H51A/S75C
-
complex mutations
I73C/P106C
site-directed mutagenesis, the linked open trap mutant does not form intermolecular disulfide bonds appreciably, as evidenced by the lack of higher-molecular weight bands. Unlinked I73C/P106C forms a small amount of NS2BS-SNS3pro, which shows retarded migration as NS2B and NS3pro electrophorese as a single disulfide-bonded complex
K117A
site-directed mutagenesis
K117C
site-directed mutagenesis
K117R
site-directed mutagenesis
K117R/T122R
-
mutant is analyzed by 15N-HSQC spectra with and without inhibitor 4-guanidino-benzoic acid-4-nitrophenyl ester
K15A
-
autocleavage detected by SDS-PAGE is supressed
P176G
-
mutation in the 11-amino acid linker region (169-179): a 70% reduction in luciferase reporter signal and a similar reduction in the level of viral RNA synthesis are observed
S75C/K117C
site-directed mutagenesis, linked S75C/K117C is induced to form the NS2BS-SNS3pro closed conformation in the presence of active site inhibitor 4-(2-aminoethyl)benzenesulfonyl fluoride, suggesting that the mutation forms a disulfide bond when the enzyme is resting in the active conformation. The S75C/K117C pair is close together in the closed conformation but far apart in the open conformation and should therefore trap this variant in the closed conformation upon intramolecular disulfide bond formation
A125C/V162C
Dengue virus type 2 Thailand/16681/1984
-
site-directed mutagenesis, the mutant shows 32% reduction in activity due to the cysteine substitution. Linked A125C/V162C, in which both mutations are within the protease domain, does not migrate differently without DTT. The unlinked either trap does not form intermolecular disulfide bonds
-
I73C/P106C
Dengue virus type 2 Thailand/16681/1984
-
site-directed mutagenesis, the linked open trap mutant does not form intermolecular disulfide bonds appreciably, as evidenced by the lack of higher-molecular weight bands. Unlinked I73C/P106C forms a small amount of NS2BS-SNS3pro, which shows retarded migration as NS2B and NS3pro electrophorese as a single disulfide-bonded complex
-
K117A
Dengue virus type 2 Thailand/16681/1984
-
site-directed mutagenesis
-
S75C/K117C
Dengue virus type 2 Thailand/16681/1984
-
site-directed mutagenesis, linked S75C/K117C is induced to form the NS2BS-SNS3pro closed conformation in the presence of active site inhibitor 4-(2-aminoethyl)benzenesulfonyl fluoride, suggesting that the mutation forms a disulfide bond when the enzyme is resting in the active conformation. The S75C/K117C pair is close together in the closed conformation but far apart in the open conformation and should therefore trap this variant in the closed conformation upon intramolecular disulfide bond formation
-
C1123A
-
results in dramatic reductions in both auto-cleavage of the NS2/3 precursor and NS3 protease activities to levels that are close to the background of the assay
C1125A
-
results in dramatic reductions in both auto-cleavage of the NS2/3 precursor and NS3 protease activities to levels that are close to the background of the assay
C1171A
-
results in dramatic reductions in both auto-cleavage of the NS2/3 precursor and NS3 protease activities to levels that are close to the background of the assay
C1185A
-
has no effect on either auto-cleavage of the NS2/3 precursor and NS3 protease activities
C184A
-
mutation in the NS2 active site, is defective in NS2-3 processing. When Hepatitis C virus polyproteins with NS2 containing a C184A mutation are co-expressed, NS2 and NS3 cleavage products are detected
C922A
-
reduces NS2/3 auto-cleavage, but has no significant effect on NS3 protease activity
H1175A
-
reduces NS3 protease activity. Auto-cleavage activity is indistinguishable from wild-type
H143A
-
mutation in the NS2 active site, is defective in NS2-3 processing. When Hepatitis C virus polyproteins with NS2 containing a H143A mutation are co-expressed, NS2 and NS3 cleavage products are detected
H143A/C184A
-
mixing wild-type Flag-NS2-3 with double-mutant HA-NS2-3(H143A/C184A) or vice versa yields only cleaved wild-type NS2, whereas the double-mutant polypeptide remains unprocessed because neither of the composite active sites is functional, when a wild-type and a double-mutant NS2-3 dimerize
H952A
-
totally abolishes auto-cleavage of the NS2/3 precursor, whereas NS3 protease activity is not abolished
L1026P/A1027P
-
totally abolishes auto-cleavage of the NS2/3 precursor, whereas NS3 protease activity is not abolished
S1165A
-
completely abrogates NS3 protease activity, but has no effect on NS2/3 auto-cleavage
D42G
has no dramatic effect on either the catalytic activity (50% of wild-type) or self-proteolysis of NS2B-NS3pro. Aprotinin efficiently inhibits proteolytic activity
G460L
-
no autolytic cleavage, but is an efficient enzyme against the artificial substrate CFP-LQYTKRGGVLWD-YFP
P131K/T132P
-
decrease in kcat, which is partially compensated by an improvement in the substrate binding. Shift of the cleavage preferences toward that of the Dengue virus proteinase
D42G
-
has no dramatic effect on either the catalytic activity (50% of wild-type) or self-proteolysis of NS2B-NS3pro. Aprotinin efficiently inhibits proteolytic activity
-
G460L
-
no autolytic cleavage, but is an efficient enzyme against the artificial substrate CFP-LQYTKRGGVLWD-YFP
-
R76L
-
the mutant displays reduced catalytic efficiency compared to the wild type enzyme
-
S135A
-
no autolytic cleavage, is enzymatically inactive
-
T52V
-
the mutant displays increased catalytic efficiency compared to the wild type enzyme
-
S138A
-
is inactive towards Bz-Nle-Lys-Arg-Arg-7-amino-4-methylcoumarin
C143S
-
site-directed mutagenesis, the NS2B mutant cannot form the disulfide bond between C143 residues of neighboring NS3
S135A
-
inactive
S75C
site-directed mutagenesis
S75C
-
site-directed mutagenesis, the mutation of NS2B protein
G22S
-
no activity
G22S
resistant to autoproteolysis at the flexible linker region, retains 3% residual activity
H51A
-
no activity
H51A
-
devoid of any proteolytic activity and incapable of autolytically cleaving either the NS2B sequence or the NS3pro-hel boundary. Resistant to the proteolysis in trans by the external, highly active NS2B-NS3pro construct
K48A
-
autolysis-resistant
K48A
-
is a single-chain protein and fully resistant to autolysis at the linker region, exhibits high stability and functional activity, cleaves pyroglutamic acid-Arg-Thr-Lys-Arg-7-amino-4-methylcoumarin
K48A
-
mutation of the C-terminal amino acid residue of the NS2B sequence, inactivates the autolytic cleavage site. Does not have any significant effect on the catalytic activity. Readily cleaved in cis by the integral NS2B-NS3pro activity
K48A
resistant to autoproteolysis at the flexible linker region. Aprotinin efficiently inhibits proteolytic activity
K48A
-
the mutant displays slightly increased catalytic efficiency compared to the wild type enzyme
R76L
-
kinetic parameters are similar to those of the wild-type. Shift of the cleavage preferences toward that of the Dengue virus proteinase
R76L
-
the mutant displays reduced catalytic efficiency compared to the wild type enzyme
S135A
-
inactive mutant
S135A
-
no autolytic cleavage, is enzymatically inactive
T52V
-
exhibits a significant loss of kcat, which is compensated by an improvement in substrate binding. Does not cause any significant differences in the cleavage subsite specificity. Cleavage preferences of the T52V mutant construct are similar to those of the original West Nile virus proteinase
T52V
-
the mutant displays increased catalytic efficiency compared to the wild type enzyme
G22S
-
no activity
-
G22S
-
resistant to autoproteolysis at the flexible linker region, retains 3% residual activity
-
H51A
-
devoid of any proteolytic activity and incapable of autolytically cleaving either the NS2B sequence or the NS3pro-hel boundary. Resistant to the proteolysis in trans by the external, highly active NS2B-NS3pro construct
-
K48A
-
mutation of the C-terminal amino acid residue of the NS2B sequence, inactivates the autolytic cleavage site. Does not have any significant effect on the catalytic activity. Readily cleaved in cis by the integral NS2B-NS3pro activity
-
K48A
-
the mutant displays slightly increased catalytic efficiency compared to the wild type enzyme
-
K48A
-
resistant to autoproteolysis at the flexible linker region. Aprotinin efficiently inhibits proteolytic activity
-
R95*A/R29G
construction of a complex containing residues 45 to 95 of the NS2B cofactor linked via a Gly-Gly-Gly-Gly-Ser-Gly-Gly-Gly-Gly (G4SG4) linker to the NS3 protease to avoid auto-proteolysis and create the linked protease, the last arginine residue of the NS2B cofactor before the G4SG4 linker is mutated to alanine (R95*A), and arginine 29 of the NS3 protease domain is mutated to glycine (R29G)
R95*A/R29G
Zika virus Puerto Rico isolate
-
construction of a complex containing residues 45 to 95 of the NS2B cofactor linked via a Gly-Gly-Gly-Gly-Ser-Gly-Gly-Gly-Gly (G4SG4) linker to the NS3 protease to avoid auto-proteolysis and create the linked protease, the last arginine residue of the NS2B cofactor before the G4SG4 linker is mutated to alanine (R95*A), and arginine 29 of the NS3 protease domain is mutated to glycine (R29G)
-
additional information
-
mutation at G153 results in inactivation
additional information
-
random mutagenesis study. Among 103 clones, 58 represent functionally inactive mutants. All tested alanine-substituted mutants exhibit impaired autolytic activity
additional information
-
separate expression of dengue virus NS3 protease and its NS2B cofactor domain and efficient co-refolding to form a stable complex, method evaluation, overview. This straightforward and robust method allows for separate isotope labeling of the two proteins, facilitating analysis by NMR spectroscopy, detailed overview. Unlinked NS2B-NS3pro behaves better in NMR spectroscopy than linked NS2B-NS3pro, which has resulted in the backbone resonance assignment of the unlinked NS2B-NS3 complex bound to a peptidic boronic acid inhibitor
additional information
-
16 possible mutants bearing and an exchanged Ile to Val are analyzed by 15N-HSQC spectra with and without inhibitor 4-guanidino-benzoic acid-4-nitrophenyl ester
additional information
-
7 Ser to Ala mutants are analyzed by 15N-HSQC spectra with and without inhibitor 4-guanidino-benzoic acid-4-nitrophenyl ester
additional information
multiple types of protein constructs have been used for NS2B-NS3pro expression. In one type, a Gly4SerGly4 linker joins NS2B to NS3pro, reported to improve expression and purification, while another type requires co-expression of the unlinked NS2B and NS3 regions. The catalytic activity is slightly different between the linked and unlinked protein constructs, with the unlinked form showing activity approximately 0-5fold greater than that of the linked form, likely due to constraints introduced by the synthetic linker
additional information
Dengue virus type 2 Thailand/16681/1984
-
multiple types of protein constructs have been used for NS2B-NS3pro expression. In one type, a Gly4SerGly4 linker joins NS2B to NS3pro, reported to improve expression and purification, while another type requires co-expression of the unlinked NS2B and NS3 regions. The catalytic activity is slightly different between the linked and unlinked protein constructs, with the unlinked form showing activity approximately 0-5fold greater than that of the linked form, likely due to constraints introduced by the synthetic linker
-
additional information
mutation in the 11-amino acid linker region (169-179): a Gly residue before Pro174 is introduced in DENV4 NS2B18NS3: The mutant protein having a glycine insertion in its linker region adopts another conformation where the protease domain has not rotated by an angle of 161° relative to the helicase domain
additional information
D(32)DD(34) substitution for AAA inactivates NS2B-NS3pro, retains 1% residual activity
additional information
-
D(32)DD(34) substitution for AAA inactivates NS2B-NS3pro, retains 1% residual activity
additional information
-
D(32)DD(34) substitution for AAA inactivates NS2B-NS3pro, retains 1% residual activity
-
additional information
-
mutation studies at the residues His94, Asp118 and Ser176 reveal that Asp118-His94 bond play an important role in the structural stability of NS2B-NS3 complex
additional information
construction of eZiPro that contains the NS2B cofactor region (residues 45-96) linked with NS3 protein (residues 1-177) through the last five residues of NS2B (K126TGKR130), and the gZiPro construct, which is similar except that the G4SG4 linker replaced K126TGKR130 of NS2B. Protease activity analysis of gZiPro, eZiPro and bZiPro
additional information
-
construction of eZiPro that contains the NS2B cofactor region (residues 45-96) linked with NS3 protein (residues 1-177) through the last five residues of NS2B (K126TGKR130), and the gZiPro construct, which is similar except that the G4SG4 linker replaced K126TGKR130 of NS2B. Protease activity analysis of gZiPro, eZiPro and bZiPro
additional information
-
construction of the NS2B cofactor region linked to the NS3 protease domain via a glycine-rich flexible linker (Gly4-Ser-Gly4 linker), structural dynamics of this conventional Zika protease (gZiPro) using NMR spectroscopy, overview. Although the glycine-rich linker in gZiPro does not alter the overall folding of the protease in solution, gZiPro is not homogenous in ion exchange chromatography. Compared to the unlinked protease construct, the artificial linker affects the chemical environment of many residues including H51 in the catalytic triad. Direct comparison of ZIKV protease constructs with and without an artificial linker, namely gZiPro (with the Gly4-Ser-Gly4 linker), bZiPro (unlinked NS2B NS3protease), and eZiPro (NS2B-NS3 junction sequence KTGKR as the linker). Solution NMR spectrum of recombinant gZiPro enzyme without inhibitor, overview. The inhibitor-bound gZiPro-AcKR-H complex adopts the closed conformation. Effect of the linker on the chemical environment of residues, dynamics of the linked protease, overview
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Chambers, T.J.; Hahn, C.S.; Galler, R.; Rice, C.M.
Flavivirus genome organization, expression, and replication
Annu. Rev. Microbiol.
44
649-688
1990
Dengue virus, Flavivirus sp., Yellow fever virus
brenda
Cah, A.; Falgout, B.; Lai, C.J.
Cleavage of the dengue virus polyprotein at the NS3/NS4A and NS4B/NS5 junctions is mediated by viral protease NS2B-NS3, whereas NS4A/NS4B may be processed by a cellular protease
J. Virol.
66
1535-1542
1992
Dengue virus
brenda
Lin, C.; Amberg, S.M.; Chambers, T.J.; Rice, C.M.
Cleavage at a novel site in the NS4A region by the yellow fever virus NS2B-3 proteinase is a prerequisite for processing at the downstream 4A/4B signalase site
J. Virol.
67
2327-2335
1993
Yellow fever virus
brenda
Chambers, T.J.; Nestorowicz, A.; Rice, C.M.
Mutagenesis of the yellow fever virus NS2B/3 cleavage site: determinants of cleavage site specificity and effects on polyprotein processing and viral replication
J. Virol.
69
1600-1605
1995
Yellow fever virus
brenda
Murthy, H.M.K.; Judge, K.; DeLucas, L.; Clum, S.; Padmanabhan, R.
Crystallization, characterization and measurement of MAD data on crystals of dengue virus NS3 serine protease complexed with mung-bean Bowman-Birk inhibitor
Acta Crystallogr. Sect. D
55
1370-1372
1999
Dengue virus
-
brenda
Krishna Murthy, H.M.; Clum, S.; Padmanabhan, R.
Dengue virus NS3 serine protease. Crystal structure and insights into interaction of the active site with substrates by molecular modeling and structural analysis of mutational effects
J. Biol. Chem.
274
5573-5580
1999
Dengue virus
brenda
Droll, D.A.; Krishna Murthy, H.M.; Chambers, T.J.
Yellow fever virus NS2B-NS3 protease: charged-to-alanine mutagenesis and deletion analysis define regions important for protease complex formation and function
Virology
275
335-347
2000
Yellow fever virus
brenda
D'Arcy, A.; Chaillet, M.; Schiering, N.; Villard, F.; Lim, S.P.; Lefeuvre, P.; Erbel, P.
Purification and crystallization of dengue and West Nile virus NS2B-NS3 complexes
Acta Crystallogr. Sect. F
62
157-162
2006
Dengue virus, West Nile virus
brenda
Li, J.; Lim, S.P.; Beer, D.; Patel, V.; Wen, D.; Tumanut, C.; Tully, D.C.; Williams, J.A.; Jiricek, J.; Priestle, J.P.; Harris, J.L.; Vasudevan, S.G.
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Dengue virus type 2
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Host cell killing by the West Nile Virus NS2B-NS3 proteolytic complex: NS3 alone is sufficient to recruit caspase-8-based apoptotic pathway
Virology
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West Nile virus
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Lin, C.W.; Lin, K.H.; Lyu, P.C.; Chen, W.J.
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Virus Res.
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Japanese encephalitis virus
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Chanprapaph, S.; Saparpakorn, P.; Sangma, C.; Niyomrattanakit, P.; Hannongbua, S.; Angsuthanasombat, C.; Katzenmeier, G.
Competitive inhibition of the dengue virus NS3 serine protease by synthetic peptides representing polyprotein cleavage sites
Biochem. Biophys. Res. Commun.
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Dengue virus
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Gouvea, I.E.; Izidoro, M.A.; Judice, W.A.; Cezari, M.H.; Caliendo, G.; Santagada, V.; dos Santos, C.N.; Queiroz, M.H.; Juliano, M.A.; Young, P.R.; Fairlie, D.P.; Juliano, L.
Substrate specificity of recombinant dengue 2 virus NS2B-NS3 protease: influence of natural and unnatural basic amino acids on hydrolysis of synthetic fluorescent substrates
Arch. Biochem. Biophys.
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Dengue virus
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Johnston, P.A.; Phillips, J.; Shun, T.Y.; Shinde, S.; Lazo, J.S.; Huryn, D.M.; Myers, M.C.; Ratnikov, B.I.; Smith, J.W.; Su, Y.; Dahl, R.; Cosford, N.D.; Shiryaev, S.A.; Strongin, A.Y.
HTS identifies novel and specific uncompetitive inhibitors of the two-component NS2B-NS3 proteinase of West Nile virus
Assay Drug Dev. Technol.
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West Nile virus
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Shiryaev, S.A.; Kozlov, I.A.; Ratnikov, B.I.; Smith, J.W.; Lebl, M.; Strongin, A.Y.
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Biochem. J.
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West Nile virus, Dengue virus type 2, Dengue virus type 2 16681, West Nile virus NY99
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Othman, R.; Wahab, H.A.; Yusof, R.; Rahman, N.A.
Analysis of secondary structure predictions of dengue virus type 2 NS2B/NS3 against crystal structure to evaluate the predictive power of the in silico methods
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Dengue virus type 2
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Bera, A.K.; Kuhn, R.J.; Smith, J.L.
Functional characterization of cis and trans activity of the Flavivirus NS2B-NS3 protease
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Japanese encephalitis virus, West Nile virus, Yellow fever virus, Dengue virus type 2, Dengue virus type 4, West Nile virus NY99
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Pastorino, B.A.; Peyrefitte, C.N.; Grandadam, M.; Thill, M.C.; Tolou, H.J.; Bessaud, M.
Mutagenesis analysis of the NS2B determinants of the Alkhurma virus NS2B-NS3 protease activation
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Alkhumra hemorrhagic fever virus
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Loehr, K.; Knox, J.E.; Phong, W.Y.; Ma, N.L.; Yin, Z.; Sampath, A.; Patel, S.J.; Wang, W.L.; Chan, W.L.; Rao, K.R.; Wang, G.; Vasudevan, S.G.; Keller, T.H.; Lim, S.P.
Yellow fever virus NS3 protease: peptide-inhibition studies
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Yellow fever virus
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Radichev, I.; Shiryaev, S.A.; Aleshin, A.E.; Ratnikov, B.I.; Smith, J.W.; Liddington, R.C.; Strongin, A.Y.
Structure-based mutagenesis identifies important novel determinants of the NS2B cofactor of the West Nile virus two-component NS2B-NS3 proteinase
J. Gen. Virol.
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West Nile virus (P06935), West Nile virus, West Nile virus NY99 (P06935)
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Tedbury, P.R.; Harris, M.
Characterisation of the role of zinc in the hepatitis C virus NS2/3 auto-cleavage and NS3 protease activities
J. Mol. Biol.
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Hepacivirus C
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Shiryaev, S.A.; Ratnikov, B.I.; Aleshin, A.E.; Kozlov, I.A.; Nelson, N.A.; Lebl, M.; Smith, J.W.; Liddington, R.C.; Strongin, A.Y.
Switching the substrate specificity of the two-component NS2B-NS3 flavivirus proteinase by structure-based mutagenesis
J. Virol.
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Dengue virus, West Nile virus
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Luo, D.; Xu, T.; Hunke, C.; Grueber, G.; Vasudevan, S.G.; Lescar, J.
Crystal structure of the NS3 protease-helicase from dengue virus
J. Virol.
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Dengue virus type 4
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Lorenz, I.C.; Marcotrigiano, J.; Dentzer, T.G.; Rice, C.M.
Structure of the catalytic domain of the hepatitis C virus NS2-3 protease
Nature
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Hepacivirus C
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Shiryaev, S.A.; Aleshin, A.E.; Ratnikov, B.I.; Smith, J.W.; Liddington, R.C.; Strongin, A.Y.
Expression and purification of a two-component flaviviral proteinase resistant to autocleavage at the NS2B-NS3 junction region
Protein Expr. Purif.
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West Nile virus
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Bessaud, M.; Pastorino, B.A.; Peyrefitte, C.N.; Rolland, D.; Grandadam, M.; Tolou, H.J.
Functional characterization of the NS2B/NS3 protease complex from seven viruses belonging to different groups inside the genus Flavivirus
Virus Res.
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Yellow fever virus, Zika virus, Saint Louis encephalitis virus, Bussuquara virus, Langat virus (P29837), Dengue virus type 3 (Q6YMS4), dengue virus type I (Q91NH1), Yellow fever virus Asibi, Dengue virus type 3 Sri Lanka/1266/2000 (Q6YMS4), dengue virus type I D1/H/IMTSSA/98/606 (Q91NH1), Langat virus TP21 (P29837), Zika virus Ar-D-41644, Saint Louis encephalitis virus MSI-7
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Niyomrattanakit, P.; Yahorava, S.; Mutule, I.; Mutulis, F.; Petrovska, R.; Prusis, P.; Katzenmeier, G.; Wikberg, J.E.
Probing the substrate specificity of the dengue virus type 2 NS3 serine protease by using internally quenched fluorescent peptides
Biochem. J.
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Dengue virus type 2
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Kiat, T.S.; Pippen, R.; Yusof, R.; Ibrahim, H.; Khalid, N.; Rahman, N.A.
Inhibitory activity of cyclohexenyl chalcone derivatives and flavonoids of fingerroot, Boesenbergia rotunda (L.), towards dengue-2 virus NS3 protease
Bioorg. Med. Chem. Lett.
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Dengue virus type 2
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Yin, Z.; Patel, S.J.; Wang, W.; Wang, G.; Chan, W.; Rao, K.R.; Alam, J.; Jeyaraj, D.A.; Ngew, X.; Patel, V.; Beer, D.; Lim, S.P.; Vasudevan, S.G.; Keller, T.H.
Peptide inhibitors of dengue virus NS3 protease. Part 1: Warhead
Bioorg. Med. Chem. Lett.
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Dengue virus
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Yin, Z.; Patel, S.J.; Wang, W.; Chan, W.; Ranga Rao, K.R.; Wang, G.; Ngew, X.; Patel, V.; Beer, D.; Knox, J.E.; Ma, N.L.; Ehrhardt, C.; Lim, S.P.; Vasudevan, S.G.; Keller, T.H.
Peptide inhibitors of dengue virus NS3 protease. Part 2: SAR study of tetrapeptide aldehyde inhibitors
Bioorg. Med. Chem. Lett.
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Dengue virus
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Schrauf, S.; Schlick, P.; Skern, T.; Mandl, C.W.
Functional analysis of potential carboxy-terminal cleavage sites of tick-borne encephalitis virus capsid protein
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Flavivirus sp.
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Shiryaev, S.A.; Radichev, I.A.; Ratnikov, B.I.; Aleshin, A.E.; Gawlik, K.; Stec, B.; Frisch, C.; Knappik, A.; Strongin, A.Y.
Isolation and characterization of selective and potent human Fab inhibitors directed to the active-site region of the two-component NS2B-NS3 proteinase of West Nile virus
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West Nile virus, West Nile virus NY99
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Sidique, S.; Shiryaev, S.A.; Ratnikov, B.I.; Herath, A.; Su, Y.; Strongin, A.Y.; Cosford, N.D.
Structure-activity relationship and improved hydrolytic stability of pyrazole derivatives that are allosteric inhibitors of West Nile Virus NS2B-NS3 proteinase
Bioorg. Med. Chem. Lett.
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West Nile virus
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Schueller, A.; Yin, Z.; Brian Chia, C.S.; Doan, D.N.; Kim, H.K.; Shang, L.; Loh, T.P.; Hill, J.; Vasudevan, S.G.
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Dengue virus, West Nile virus
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Kondo, M.Y.; Oliveira, L.C.; Okamoto, D.N.; de Araujo, M.R.; Duarte dos Santos, C.N.; Juliano, M.A.; Juliano, L.; Gouvea, I.E.
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Biochem. Biophys. Res. Commun.
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Yellow fever virus
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Kannappan, P.; Narayanan, S.
Mutation and docking studies on NS2b-NS3 complex from yellow fever virus towards drug discovery
Bioinformation
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Yellow fever virus
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Condotta, S.A.; Martin, M.M.; Boutin, M.; Jean, F.
Detection and in-cell selectivity profiling of the full-length West Nile virus NS2B/NS3 serine protease using membrane-anchored fluorescent substrates
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West Nile virus
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Phong, W.Y.; Moreland, N.J.; Lim, S.P.; Wen, D.; Paradkar, P.N.; Vasudevan, S.G.
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Dengue virus type 2
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Lim, H.A.; Joy, J.; Hill, J.; San Brian Chia, C.
Novel agmatine and agmatine-like peptidomimetic inhibitors of the West Nile virus NS2B/NS3 serine protease
Eur. J. Med. Chem.
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West Nile virus
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Frimayanti, N.; Chee, C.F.; Zain, S.M.; Rahman, N.A.
Design of new competitive dengue ns2b/ns3 protease inhibitors-a computational approach
Int. J. Mol. Sci.
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Dengue virus
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de la Cruz, L.; Nguyen, T.H.; Ozawa, K.; Shin, J.; Graham, B.; Huber, T.; Otting, G.
Binding of Low Molecular Weight Inhibitors Promotes Large Conformational Changes in the Dengue Virus NS2B-NS3 Protease: Fold Analysis by Pseudocontact Shifts
J. Am. Chem. Soc.
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Dengue virus type 2
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Luo, D.; Wei, N.; Doan, D.N.; Paradkar, P.N.; Chong, Y.; Davidson, A.D.; Kotaka, M.; Lescar, J.; Vasudevan, S.G.
Flexibility between the protease and helicase domains of the dengue virus NS3 protein conferred by the linker region and its functional implications
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Dengue virus type 2, Dengue virus type 4 (Q2YHF0)
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Salaemae, W.; Junaid, M.; Angsuthanasombat, C.; Katzenmeier, G.
Structure-guided mutagenesis of active site residues in the dengue virus two-component protease NS2B-NS3
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Dengue virus
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Frecer, V.; Miertus, S.
Design, structure-based focusing and in silico screening of combinatorial library of peptidomimetic inhibitors of Dengue virus NS2B-NS3 protease
J. Comput. Aided Mol. Des.
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Dengue virus type 2
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Wu, H.; Bock, S.; Snitko, M.; Berger, T.; Weidner, T.; Holloway, S.; Kanitz, M.; Diederich, W.E.; Steuber, H.; Walter, C.; Hofmann, D.; Weissbrich, B.; Spannaus, R.; Acosta, E.G.; Bartenschlager, R.; Engels, B.; Schirmeister, T.; Bodem, J.
Novel dengue virus NS2B/NS3 protease inhibitors
Antimicrob. Agents Chemother.
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2015
Dengue virus
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Verma, R.; Jatav, V.; Sharma, S.
Identification of inhibitors of dengue virus (Denv1, Denv2 and Denv3) NS2B/NS3 serine protease: A molicular docking and simulation approach
Asian J. Pharm. Clin. Res.
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2015
Dengue virus
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Junaid, M.; Angsuthanasombat, C.; Wikberg, J.E.; Ali, N.; Katzenmeier, G.
A straightforward experimental approach to expression, purification, refolding, and enzymatic analysis of recombinant dengue virus NS2B(H)-NS3pro protease
Biochemistry (Moscow)
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2013
Dengue virus
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Choksupmanee, O.; Hodge, K.; Katzenmeier, G.; Chimnaronk, S.
Structural platform for the autolytic activity of an intact NS2B-NS3 protease complex from dengue virus
Biochemistry
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2012
Dengue virus
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Senthilvel, P.; Lavanya, P.; Kumar, K.M.; Swetha, R.; Anitha, P.; Bag, S.; Sarveswari, S.; Vijayakumar, V.; Ramaiah, S.; Anbarasu, A.
Flavonoid from Carica papaya inhibits NS2B-NS3 protease and prevents Dengue 2 viral assembly
Bioinformation
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889-895
2013
Dengue virus
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Liu, H.; Wu, R.; Sun, Y.; Ye, Y.; Chen, J.; Luo, X.; Shen, X.; Liu, H.
Identification of novel thiadiazoloacrylamide analogues as inhibitors of dengue-2 virus NS2B/NS3 protease
Bioorg. Med. Chem.
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Dengue virus
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de Sousa, L.R.; Wu, H.; Nebo, L.; Fernandes, J.B.; da Silva, M.F.; Kiefer, W.; Kanitz, M.; Bodem, J.; Diederich, W.E.; Schirmeister, T.; Vieira, P.C.
Flavonoids as noncompetitive inhibitors of Dengue virus NS2B-NS3 protease: inhibition kinetics and docking studies
Bioorg. Med. Chem.
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2015
Dengue virus
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Li, L.; Basavannacharya, C.; Chan, K.W.; Shang, L.; Vasudevan, S.G.; Yin, Z.
Structure-guided discovery of a novel non-peptide inhibitor of dengue virus NS2B-NS3 protease
Chem. Biol. Drug Des.
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2015
Dengue virus
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Ang, M.J.; Yong, G.H.; Poulsen, A.; Then, S.W.; Li, Z.; Joy, J.; Hill, J.; Chia, C.S.
Substrate-based peptidomimetic inhibitors of the Murray Valley encephalitis virus NS2B/NS3 serine protease: a P1-P4 SAR study
Eur. J. Med. Chem.
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Murray Valley encephalitis virus
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de la Cruz, L.; Chen, W.N.; Graham, B.; Otting, G.
Binding mode of the activity-modulating C-terminal segment of NS2B to NS3 in the dengue virus NS2B-NS3 protease
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Dengue virus (Q91H74), Dengue virus
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Chen, W.N.; Loscha, K.V.; Nitsche, C.; Graham, B.; Otting, G.
The dengue virus NS2B-NS3 protease retains the closed conformation in the complex with BPTI
FEBS Lett.
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Dengue virus (Q91H74), Dengue virus
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Nguyen, T.; Lee, S.; Wang, H.; Chen, H.; Wu, Y.; Lin, S.; Kim, D.; Kim, D.
In vitro evaluation of novel inhibitors against the NS2B-NS3 protease of dengue fever virus type 4
Molecules
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15600-15612
2013
Dengue virus
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Ang, M.J.; Li, Z.; Lim, H.A.; Ng, F.M.; Then, S.W.; Wee, J.L.; Joy, J.; Hill, J.; Chia, C.S.
A P2 and P3 substrate specificity comparison between the Murray Valley encephalitis and West Nile virus NS2B/NS3 protease using C-terminal agmatine dipeptides
Peptides
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49-52
2014
West Nile virus, Murray Valley encephalitis virus
brenda
Huang, Q.; Li, Q.; Joy, J.; Chen, A.S.; Ruiz-Carrillo, D.; Hill, J.; Lescar, J.; Kang, C.
Lyso-myristoyl phosphatidylcholine micelles sustain the activity of Dengue non-structural (NS) protein 3 protease domain fused with the full-length NS2B
Protein Expr. Purif.
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2013
Dengue virus
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Hill, M.E.; Kumar, A.; Wells, J.A.; Hobman, T.C.; Julien, O.; Hardy, J.A.
The unique cofactor region of zika virus NS2B-NS3 protease facilitates cleavage of key host proteins
ACS Chem. Biol.
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Zika virus
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Luo, D.; Vasudevan, S.G.; Lescar, J.
The flavivirus NS2B-NS3 protease-helicase as a target for antiviral drug development
Antiviral Res.
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Yellow fever virus (P03314), Murray Valley encephalitis virus (P05769), West Nile virus (P06935), Kunjin virus (P14335), dengue virus type I (P17763), Japanese encephalitis virus (P27395), Dengue virus type 2 (P29990), Dengue virus type 4 (Q2YHF0), Kokobera virus (Q32ZD5), Dengue virus type 3 (Q6YMS3), Dengue virus type 2 Thailand/16681/1984 (P29990), Dengue virus type 3 Martinique/1243/1999 (Q6YMS3), Yellow fever virus 17D vaccine (P03314), Dengue virus type 4 Thailand/0348/1991 (Q2YHF0), dengue virus type I Nauru/West Pac/1974 (P17763), Japanese encephalitis virus SA-14 (P27395), Kunjin virus MRM61C (P14335), Murray Valley encephalitis virus MVE-1-51 (P05769)
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Rut, W.; Zhang, L.; Kasperkiewicz, P.; Poreba, M.; Hilgenfeld, R.; Drag, M.
Extended substrate specificity and first potent irreversible inhibitor/activity-based probe design for Zika virus NS2B-NS3 protease
Antiviral Res.
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2017
Zika virus (A0A024B7W1), Zika virus
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Shiryaev, S.A.; Farhy, C.; Pinto, A.; Huang, C.T.; Simonetti, N.; Elong Ngono, A.; Dewing, A.; Shresta, S.; Pinkerton, A.B.; Cieplak, P.; Strongin, A.Y.; Terskikh, A.V.
Characterization of the Zika virus two-component NS2B-NS3 protease and structure-assisted identification of allosteric small-molecule antagonists
Antiviral Res.
143
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Zika virus (A0A024B7W1), Zika virus
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Zhu, L.; Yang, J.; Li, H.; Sun, H.; Liu, J.; Wang, J.
Conformational change study of dengue virus NS2B-NS3 protease using 19F NMR spectroscopy
Biochem. Biophys. Res. Commun.
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Dengue virus type 2
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Aguilera-Pesantes, D.; Robayo, L.E.; Mendez, P.E.; Mollocana, D.; Marrero-Ponce, Y.; Torres, F.J.; Mendez, M.A.
Discovering key residues of dengue virus NS2b-NS3-protease new binding sites for antiviral inhibitors design
Biochem. Biophys. Res. Commun.
492
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Dengue virus type 3 (Q5UB51), Dengue virus type 3 Singapore/8120/1995 (Q5UB51)
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Kuiper, B.D.; Slater, K.; Spellmon, N.; Holcomb, J.; Medapureddy, P.; Muzzarelli, K.M.; Yang, Z.; Ovadia, R.; Amblard, F.; Kovari, I.A.; Schinazi, R.F.; Kovari, L.C.
Increased activity of unlinked Zika virus NS2B/NS3 protease compared to linked Zika virus protease
Biochem. Biophys. Res. Commun.
492
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2017
Zika virus (A0A384KRS4), Zika virus, Zika virus Puerto Rico isolate (A0A384KRS4)
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Balajee, R.; Srinivasadesikan, V.; Sakthivadivel, M.; Gunasekaran, P.
In silico screening, alanine mutation, and DFT approaches for identification of NS2B/NS3 protease inhibitors
Biochem. Res. Int.
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Dengue virus type 2
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Hill, M.E.; Yildiz, M.; Hardy, J.A.
Cysteine disulfide traps reveal distinct conformational ensembles in dengue virus NS2B-NS3 protease
Biochemistry
58
776-787
2019
Dengue virus type 2 (P29990), Dengue virus type 2 Thailand/16681/1984 (P29990)
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Takagi, Y.; Matsui, K.; Nobori, H.; Maeda, H.; Sato, A.; Kurosu, T.; Orba, Y.; Sawa, H.; Hattori, K.; Higashino, K.; Numata, Y.; Yoshida, Y.
Discovery of novel cyclic peptide inhibitors of dengue virus NS2B-NS3 protease with antiviral activity
Bioorg. Med. Chem. Lett.
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3586-3590
2017
Dengue virus type 2
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Weng, Z.; Shao, X.; Graf, D.; Wang, C.; Klein, C.D.; Wang, J.; Zhou, G.C.
Identification of fused bicyclic derivatives of pyrrolidine and imidazolidinone as dengue virus-2 NS2B-NS3 protease inhibitors
Eur. J. Med. Chem.
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2017
Dengue virus type 2
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Gruba, N.; Rodriguez Martinez, J.I.; Grzywa, R.; Wysocka, M.; Skorenski, M.; Burmistrz, M.; Lecka, M.; Lesner, A.; Sienczyk, M.; Pyrc, K.
Substrate profiling of Zika virus NS2B-NS3 protease
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Zika virus (Q32ZE1), Zika virus
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Li, Y.; Phoo, W.W.; Loh, Y.R.; Zhang, Z.; Ng, E.Y.; Wang, W.; Keller, T.H.; Luo, D.; Kang, C.
Structural characterization of the linked NS2B-NS3 protease of Zika virus
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Zika virus
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Yao, Y.; Huo, T.; Lin, Y.L.; Nie, S.; Wu, F.; Hua, Y.; Wu, J.; Kneubehl, A.R.; Vogt, M.B.; Rico-Hesse, R.; Song, Y.
Discovery, X-ray crystallography and antiviral activity of allosteric inhibitors of flavivirus NS2B-NS3 protease
J. Am. Chem. Soc.
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Dengue virus, West Nile virus, Zika virus
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Kouretova, J.; Hammamy, M.Z.; Epp, A.; Hardes, K.; Kallis, S.; Zhang, L.; Hilgenfeld, R.; Bartenschlager, R.; Steinmetzer, T.
Effects of NS2B-NS3 protease and furin inhibition on West Nile and Dengue virus replication
J. Enzyme Inhib. Med. Chem.
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Dengue virus, West Nile virus
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Skorenski, M.; Milewska, A.; Pyrc, K.; Sienczyk, M.; Oleksyszyn, J.
Phosphonate inhibitors of West Nile virus NS2B/NS3 protease
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West Nile virus
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Yotmanee, P.; Rungrotmongkol, T.; Wichapong, K.; Choi, S.B.; Wahab, H.A.; Kungwan, N.; Hannongbua, S.
Binding specificity of polypeptide substrates in NS2B/NS3pro serine protease of dengue virus type 2 A molecular dynamics study
J. Mol. Graph. Model.
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Dengue virus type 2 (Q91H74), Dengue virus type 2 Thailand/NGS-C/1944 (Q91H74)
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Phoo, W.W.; Li, Y.; Zhang, Z.; Lee, M.Y.; Loh, Y.R.; Tan, Y.B.; Ng, E.Y.; Lescar, J.; Kang, C.; Luo, D.
Structure of the NS2B-NS3 protease from Zika virus after self-cleavage
Nat. Commun.
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Zika virus (H8XX12), Zika virus
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Woestenenk, E.; Agback, P.; Unnerstale, S.; Henderson, I.; Agback, T.
Co-refolding of a functional complex of Dengue NS3 protease and NS2B co-factor domain and backbone resonance assignment by solution NMR
Protein Expr. Purif.
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Dengue virus
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Lei, J.; Hansen, G.; Nitsche, C.; Klein, C.D.; Zhang, L.; Hilgenfeld, R.
Crystal structure of Zika virus NS2B-NS3 protease in complex with a boronate inhibitor
Science
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2016
Zika virus (A0A140DLX4), Zika virus, Zika virus Brazilian isolate BeH823339 (A0A140DLX4)
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Zhang, Z.; Li, Y.; Loh, Y.R.; Phoo, W.W.; Hung, A.W.; Kang, C.; Luo, D.
Crystal structure of unlinked NS2B-NS3 protease from Zika virus
Science
354
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2016
Zika virus
brenda
Li, Y.; Zhang, Z.; Phoo, W.W.; Loh, Y.R.; Wang, W.; Liu, S.; Chen, M.W.; Hung, A.W.; Keller, T.H.; Luo, D.; Kang, C.
Structural dynamics of Zika virus NS2B-NS3 protease binding to dipeptide inhibitors
Structure
25
1242-1250
2017
Zika virus
brenda
Li, Y.; Zhang, Z.; Phoo, W.W.; Loh, Y.R.; Li, R.; Yang, H.Y.; Jansson, A.E.; Hill, J.; Keller, T.H.; Nacro, K.; Luo, D.; Kang, C.
Structural insights into the inhibition of Zika virus NS2B-NS3 protease by a small-molecule inhibitor
Structure
26
555-564.e3
2018
Zika virus
brenda