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acetyl-FR-7-amido-4-trifluoromethyl coumarin + H2O
acetyl-FR + 7-amino-4-trifluoromethyl coumarin
-
-
-
?
benzoyl-Phe-Val-Arg-4-methylcoumarinyl-7-amide + H2O
benzoyl-Phe-Val-Arg + 7-amino-4-methylcoumarin
-
cathepsin L1
-
-
?
benzoyl-Phe-Val-Arg-7-amido-4-methylcoumarin + H2O
benzoyl-Phe-Val-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Arg-4-methylcoumarinyl-7-amide + H2O
benzyloxycarbonyl-Arg + 7-amino-4-methylcoumarin
-
cathepsin L1
-
-
?
benzyloxycarbonyl-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Arg-Arg-4-methylcoumarinyl-7-amide + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
cathepsin L1
-
-
?
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-L-Leu-L-Arg-4-methylcoumarinyl-7-amide + H2O
benzyloxycarbonyl-L-Leu-L-Arg + 7-amino-4-methylcoumarin
FheCL1
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-4-methylcoumarinyl-7-amide + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-L-phenylalanyl-L-arginine 4-methylcoumarinyl-7-amide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-L-Pro-L-Arg-4-methylcoumarinyl-7-amide + H2O
benzyloxycarbonyl-L-Pro-L-Arg + 7-amino-4-methylcoumarin
FheCL1
-
-
?
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Leu-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarinyl-7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
cleaved by cathepsin L2 with much greater affinity than by cathepsin L1
-
-
?
benzyloxycarbonyl-Phe-Arg-4-nitroanilide + H2O
benzyloxycarbonyl-Phe-Arg + 4-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Phe-Arg-7-amido-4-trifluoromethylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-trifluoromethylcoumarin
-
best substrate
-
-
?
benzyloxycarbonyl-Phe-Phe-Arg-7-amido-4-methylcoumarin + H2O
?
-
renatured CPFhW
-
-
?
benzyloxycarbonyl-Pro-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Collagen + H2O
?
whereas FheCL1 produces clear degradation fragments, FheCL2 degrades the collagen completely, particularly at pH 4.0, indicating that only the latter cleaves efficiently within the helical structures
-
-
?
Collagen type I + H2O
?
-
-
-
?
Collagen type III + H2O
?
-
-
-
?
collagen type IV + H2O
?
-
-
-
?
Fibrinogen + H2O
?
enzyme FhCL3 is capable of degradation of the fibrinogen alpha-chain, beta-chain, and gamma-chain
-
-
?
Fibronectin + H2O
?
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
H-Leu-Val-Tyr-4-methylcoumarinyl-7-amide + H2O
H-Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
cleaved by cathepsin L2 with much greater affinity than by cathepsin L1
-
-
?
H-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
H-Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
human IgG + H2O
?
-
both cathepsins L produce similar degradation patterns and cleave all human IgG subclasses at the hinge region, yielding at pH 7.3 and 37°C Fab and Fc fragments in the case of IgG1 and IgG3 or Fab(2) and Fc in IgG2 and IgG4. Both liver fluke cathepsins L cleave the peptide bonds 237His-Thr, 237Glu-Cys, 233Gly-Asp, and 241Ser-Cys of the gamma1, gamma2, gamma3, and gamma4 H chains, respectively. Therefore, the enzymes are interacting with the following P3-P'3 sequences, Lys-Thr-His-Thr-Cys-Pro, Cys-Val-Glu-Asp-Pro-Pro, Pro-Leu-Gly-Asp-Thr-Thr, and Cys-Pro-Ser-Cys-Pro-Ala. The specificity of the liver fluke cathepsins L for peptide bonds in proteins is less defined. The P1 position, for instance, can be occupied by hydrophobic, hydrophilic, acidic, or basic residues. The P3 and P2 positions are occupied by hydrophobic amino acids with the exception of the gamma1 sequence which contains a basic lysine and a hydrophilic threonine, respectively. In addition the specificity between the enzyme and its substrate would depend on which of the amino acids of the substrate can be really exposed to the active site
-
-
?
Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
cleaved by cathepsin L2 with much greater affinity than by cathepsin L1
-
-
?
N-benzyloxycarbonyl-FR-4-nitroanilide + H2O
N-benzyloxycarbonyl-FR + 4-nitroaniline
-
-
-
?
N-benzyloxycarbonyl-FR-7-amido-4-trifluoromethylcoumarin + H2O
N-benzyloxycarbonyl-FR + 7-amino-4-trifluoromethylcoumarin
best substrate
-
-
?
N-benzyloxycarbonyl-GPR-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-GPR + 7-amino-4-methylcoumarin
-
-
-
?
N-benzyloxycarbonyl-VVR-7-amido-4-methylcoumarin + H2O
N-benzyloxycarbonyl-VVR + 7-amino-4-methylcoumarin
-
-
-
?
procathepsin L1 + H2O
?
-
procathepsin L1 autocatalytically processes and activates to its mature enzyme (FheCL1) over a wide pH range 4.0-7.3. Activation is more rapid at low pH. Maturation initiates with cleavages of a small proportion of molecules within the central region of the prosegment, possibly by intramolecular events. Activation to fully mature enzymes is achieved by a precise intermolecular cleavage at a Leu12-Ser11-/-His10 sequence within the nonconserved C-terminal region of the prosegment. Active site variant FheproCL1C26G and a double variant FheproCL1L12P/C26G cannot autocatalytically process. The former is susceptible to trans-processing at a Leu12-Ser11-/-His10 sequence by preactivated FheCL1, but the latter is not
-
-
?
succinyl-Ala-Phe-Lys-4-methylcoumarinyl-7-amide + H2O
succinyl-Ala-Phe-Lys + 7-amino-4-methylcoumarin
-
cathepsin L1
-
-
?
succinyl-Ala-Phe-Lys-7-amido-4-methylcoumarin + H2O
tosyl-Ala-Phe-Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-4-methylcoumarinyl-7-amide + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
cathepsin L1
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
t-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
t-butyloxycarbonyl-Val-Leu-Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
t-butyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin + H2O
t-butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
-
cleaved by cathepsin L2 with much greater affinity than by cathepsin L1
-
-
?
tert-butoxycarbonyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide + H2O
tert-butoxycarbonyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
FheCL1
-
-
?
tert-butyloxycarbonyl-Val-Leu-Lys-4-methylcoumarinyl-7-amide + H2O
tert-butyloxycarbonyl-Val-Leu-Lys + 7-amino-4-methylcoumarin
-
cathepsin L1
-
-
?
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumarinyl-7-amide + H2O
tert-butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
-
cleaved by cathepsin L2 with much greater affinity than by cathepsin L1
-
-
?
tosyl-Ala-Phe-Lys-4-methylcoumarinyl-7-amide + H2O
tosyl-Ala-Phe-Lys + 7-amino-4-methylcoumarin
-
cathepsin L1
-
-
?
tosyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide + H2O
tosyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
tosyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
-
cleaved by cathepsin L2 with much greater affinity than by cathepsin L1
-
-
?
tosyl-Gly-Pro-Lys-4-methylcoumarinyl-7-amide + H2O
tosyl-Gly-Pro-Lys + 7-amino-4-methylcoumarin
-
cleaved by cathepsin L2 with much greater affinity than by cathepsin L1
-
-
?
tosyl-Gly-Pro-Lys-7-amido-4-methylcoumarin + H2O
tosyl-Gly-Pro-Lys + 7-amino-4-methylcoumarin
-
cleaved by cathepsin L2 with much greater affinity than by cathepsin L1
-
-
?
Z-Phe-Arg-OMe + SerNH2
Z-Phe-Arg-Ser-NH2 + methanol
-
peptide synthesis
-
-
?
additional information
?
-
benzyloxycarbonyl-L-Phe-L-Arg-4-methylcoumarinyl-7-amide + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
FheCL1
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-4-methylcoumarinyl-7-amide + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
FheCL1
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
cleaved by cathepsin L2 with much greater affinity than by cathepsin L1
-
-
?
Hemoglobin + H2O
?
-
-
-
-
?
Hemoglobin + H2O
?
-
Fasciola hepatica secretes cathepsin L cysteine proteases to invade its host, migrate through tissues and digest hemoglobin, its main source of amino acids. FheCL1 can degrade hemoglobin to small peptides, predominantly of 414 residues, but cannot release free amino acids. It is suggested that hemoglobin degradation is not completed in the gut lumen but the resulting peptides are absorbed by the gut epithelial cells for further processing by intracellular di- and amino-peptidases to free amino acids that are distributed through the parasite tissue for protein anabolism. The action of FheCL1 is enhanced by glutathione, the major reducing agent found in red blood cells
-
-
?
Hemoglobin + H2O
?
FhCL1 cleaves substrates with hydrophobic residues (Phe and Leu) in the P2 position with catalytic rates (kcat/Km) that are 25- and eightfold greater, respectively, than FhCL2. In comparison to human cathepsin L, which can accommodate a wide range of amino acids in the S2 subsite, the S2 subsite of FhCL1 is restricted. Hydrophobic residues are most susceptible to cleavage, in the order Leu > Val > Ala > Phe. Together, these four residues make up about 42% of the hemoglobin molecule and, therefore, it seems that FhCL1 has been specifically adapted to degrade the host substrate, which it exploits as nutrient. Substrates with proline in the P2 position, which are good substrates for FhCL2 are poorly cleaved by FhCL1 (and not at all by human cathepsin L)
-
-
?
Hemoglobin + H2O
?
-
FheCL1 can degrade hemoglobin to small peptides, predominantly of 414 residues, but cannot release free amino acids. FheCL1 can not cleave its natural substrate hemoglobin in the pH range pH 5.5 and pH 7.0. Digestion occurs only at or below pH 4.5, which coincides with pH-induced dissociation of the hemoglobin tetramer. The acidic pH of the parasite relaxes the hemoglobin structure, making it susceptible to proteolysis by FheCL1. The P1 position could be occupied by many amino acids but most preferentially Leu. FheCL1 preferentially cleaves bonds where the P2 position is occupied with hydrophobic residues (in order of decreasing efficiency: Leu, Val, Ala, Phe) and is observed for the digestion of both hemoglobin-alpha and hemoglobin-beta
-
-
?
Hemoglobin + H2O
?
-
enzyme does not cleave its natural substrate hemoglobin in the pH range pH 5.5 and pH 7.0. Digestion occurs only at pH 4.5, which coincides with pH-induced dissociation of the hemoglobin tetramer
degradation to small peptides of 4-14 residues, no release of free amino acids
-
?
Hemoglobin + H2O
?
purified recombinant CL1 is not able to hydrolyze hemoglobin
-
-
?
ovalbumin + H2O
?
-
-
-
-
?
ovalbumin + H2O
?
-
FheCL1 can degrade ovalbumin from pH 3.5 to pH 8.0
-
-
?
tosyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide + H2O
tosyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tosyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide + H2O
tosyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
-
cleaved by cathepsin L2 with much greater affinity than by cathepsin L1
-
-
?
tosyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide + H2O
tosyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
FheCL1
-
-
?
additional information
?
-
-
benzyloxycarbonyl-Gly-Pro-Atg-7-amido-4-methylcoumarin and benzyloxycarbonyl-Val-Val-Arg-7-amido-4-methylcoumarin are not hydrolyzed
-
-
?
additional information
?
-
-
does not hydrolyze Arg-4-nitroanilide, N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide, benzyloxycarbonyl-Gly-Pro-Arg-7-amido-4-methylcoumarin, and benzyloxycarbonyl-Val-Val-Arg-7-amido-4-methylcoumarin
-
-
?
additional information
?
-
substrate specificity supports the hypothesis that Diaprepes abbreviatus CTSL1 is a unique basic cathepsin L and protease inhibitor studies also suggest unique activity, unlike other characterized acidic cathepsin Ls. No activity with N-succinyl-AAPF-4-nitroanilide and HR-4-nitroanilide
-
-
?
additional information
?
-
-
substrate specificity supports the hypothesis that Diaprepes abbreviatus CTSL1 is a unique basic cathepsin L and protease inhibitor studies also suggest unique activity, unlike other characterized acidic cathepsin Ls. No activity with N-succinyl-AAPF-4-nitroanilide and HR-4-nitroanilide
-
-
?
additional information
?
-
-
the enzyme mediates kinin release from high molecular weight kininigen
-
-
?
additional information
?
-
-
the enzyme facilitates the penetration of the parasite though the tissue of its host, and also participates in functions such as feeding and immune evasion
-
-
?
additional information
?
-
-
cathepsin L1 and cathepsin L2 proteinases may be the prime mechanism by which the parasite penetrates tissue
-
-
?
additional information
?
-
-
renatured enzyme shows no activity with benzyloxycarbonyl-Phe-Arg-beta-naphthylamide
-
-
?
additional information
?
-
wild-type FheCL1 shows clear preference for Arg at P1. Other residues accommodated in this position including Lys, Glu, Thr, and Met are all cleaved at similar relative rates to that observed for human cathepsin L and cathepsin K. Similar results are obtained for the variants FheCL1 L67Y and FheCL1 L205A. FheCL1 shows distinct preference for hydrophobic amino acids in the P2, Leu is favored. FheCL1 and FheCL2 are similar to cathepsin K with regard to their preference for a P2 Leu over Phe (human cathepsin L has a preference for P2 Phe over Leu). Both enzymes can accommodate Pro in the P2 position, but this is more readily accepted by FheCL2 compared with FheCL1. Neither enzyme, however, cleaves substrates with this residue in the P2 position as readily as human cathepsin K
-
-
?
additional information
?
-
-
wild-type FheCL1 shows clear preference for Arg at P1. Other residues accommodated in this position including Lys, Glu, Thr, and Met are all cleaved at similar relative rates to that observed for human cathepsin L and cathepsin K. Similar results are obtained for the variants FheCL1 L67Y and FheCL1 L205A. FheCL1 shows distinct preference for hydrophobic amino acids in the P2, Leu is favored. FheCL1 and FheCL2 are similar to cathepsin K with regard to their preference for a P2 Leu over Phe (human cathepsin L has a preference for P2 Phe over Leu). Both enzymes can accommodate Pro in the P2 position, but this is more readily accepted by FheCL2 compared with FheCL1. Neither enzyme, however, cleaves substrates with this residue in the P2 position as readily as human cathepsin K
-
-
?
additional information
?
-
-
enzyme preferentially cleaves bonds where the P2 position is occupied with hydrophobic residues, this preference follows the order Leu>Val>Ala>Phe, and is observed for the digestion of both hemoglobin-alpha and hemoglobin-beta
-
-
?
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benzyloxycarbonyl-L-phenylalanyl-L-alanine-diazomethylketone(-CHN2)
-
-
Benzyloxycarbonyl-Phe-Ala-CHN2
-
-
benzyloxycarbonyl-Phe-Ala-diazomethyl ketone
FheCL1
cathepsin K inhibitor II
FheCL1
N-2,3,4,5,6-pentafluorobenzoyl-L-leucyl-glycine nitrile
-
-
N-2,3,4,5-tetrafluorobenzoyl-L-leucyl-glycine nitrile
-
-
N-2,3,4-trifluorobenzoyl-L-leucyl-glycine nitrile
-
-
N-2,3,6-trifluorobenzoyl-L-leucyl-glycine nitrile
-
-
N-2,3-difluorobenzoyl-L-leucyl-glycine nitrile
-
-
N-2,4,5-trifluorobenzoyl-L-leucyl-glycine nitrile
-
-
N-2,4-difluorobenzoyl-L-leucyl-glycine nitrile
-
-
N-2,5-difluorobenzoyl-L-leucyl-glycine nitrile
-
-
N-2,6-difluorobenzoyl-L-leucyl-glycine nitrile
-
-
N-2-fluorobenzoyl-L-alanine-beta-alanine nitrile
-
-
N-2-fluorobenzoyl-L-alanine-glycine nitrile
-
-
N-2-fluorobenzoyl-L-leucine-beta-alanine benzyl ester
-
-
N-2-fluorobenzoyl-L-leucine-beta-alanine nitrile
-
-
N-2-fluorobenzoyl-L-leucine-gamma-aminobutyric acid benzyl ester
-
-
N-2-fluorobenzoyl-L-leucyl-glycine benzyl ester
-
-
N-2-fluorobenzoyl-L-leucyl-glycine nitrile
-
-
N-2-trifluoromethylbenzoyl-L-leucyl-glycine nitrile
-
-
N-3,4,5-trifluorobenzoyl-L-leucyl-glycine nitrile
-
-
N-3,4-difluorobenzoyl-L-leucyl-glycine nitrile
-
-
N-3,5-difluorobenzoyl-L-leucyl-glycine nitrile
-
-
N-3-fluorobenzoyl-L-leucine-beta-alanine benzyl ester
-
-
N-3-fluorobenzoyl-L-leucine-gamma-aminobutyric acid benzyl ester
-
-
N-3-fluorobenzoyl-L-leucyl-glycine benzyl ester
-
-
N-3-fluorobenzoyl-L-leucyl-glycine nitrile
-
-
N-3-trifluoromethylbenzoyl-L-leucyl-glycine nitrile
-
-
N-4-fluorobenzoyl-L-leucine-beta-alanine benzyl ester
-
-
N-4-fluorobenzoyl-L-leucine-beta-alanine nitrile
-
-
N-4-fluorobenzoyl-L-leucine-gamma-aminobutyric acid benzyl ester
-
-
N-4-fluorobenzoyl-L-leucyl-glycine benzyl ester
-
-
N-4-fluorobenzoyl-L-leucyl-glycine nitrile
-
-
N-4-trifluoromethylbenzoyl-L-leucyl-glycine nitrile
-
-
N-benzoyl-L-leucyl-glycine
-
-
N-benzyloxycarbonyl-FY(tert-butyl)-diazomethylketone
40.6% inhibition at 0.05 mM
N-benzyloxycarbonylphenylalanyl-t-butyl-tryrosyl diazomethylketone
-
40.6% inhibition at 0.05 mM
N-cinnamoyl-L-leucyl-glycine nitrile
-
-
N-pentafluorobenzoyl-L-alanine-beta-alanine nitrile
-
-
N-pentafluorobenzoyl-L-alanine-glycine nitrile
-
-
N-pentafluorobenzoyl-L-leucine-beta-alanine benzyl ester
-
-
N-pentafluorobenzoyl-L-leucine-gamma-aminobutyric acid benzyl ester
-
-
N-pentafluorobenzoyl-L-leucyl-glycine benzyl ester
-
-
Aprotinin
-
complete inhibition at 50 nM at a molar ratio of enzyme to inhibitor of 17:1; inhibits enzyme activity almost completely at a molar ratio of enzyme to inhibitor of 17:1
CA074
-
25.3% inhibition at 0.05 mM
CA074
25.3% inhibition at 0.05 mM
chymostatin
-
85.6% inhibition at 0.05 mM
chymostatin
85.6% inhibition at 0.05 mM
cystatin
-
47.5% inhibition at 0.05 mM
-
cystatin
47.5% inhibition at 0.05 mM
-
E-64
-
i.e. L-trans-epoxysuccinyl-leucyamido(4-guanidino) butane, 26.6% inhibition at 0.05 mM
E-64
26.6% inhibition at 0.05 mM
additional information
-
cathepsin L2 is completely inactivated by 4 mM tetranitromethane, cathepsin L1 is not inactivated
-
additional information
the enzyme's fibrinolytic activity is inhibited by plasma. Addition of GSH to plasma cannot counteract the inhibitory effect of plasma components for FhCL1
-
additional information
-
the enzyme's fibrinolytic activity is inhibited by plasma. Addition of GSH to plasma cannot counteract the inhibitory effect of plasma components for FhCL1
-
additional information
inhibitory interactions of human family 1 and 2 cystatins with cathepsin L1 are predicted and their stability and viability are verified through protein docking and comparative molecular dynamics, overview. The key amino acid residues surfaced via interaction energy, hydrogen bonding and solvent accessible surface area analysis for each cystatin-cathepsin L1 complex influence the mode of binding and thus control the diverse inhibitory affinity of cystatins towards cysteine proteases. Docking outputs of cathepsin L1 complexes with stefin A, stefin B, cystatin C, cystatin D, cystatin F, cystatin M/E, cystatin S, cystatin SA, and cystatin SN
-
additional information
-
inhibitory interactions of human family 1 and 2 cystatins with cathepsin L1 are predicted and their stability and viability are verified through protein docking and comparative molecular dynamics, overview. The key amino acid residues surfaced via interaction energy, hydrogen bonding and solvent accessible surface area analysis for each cystatin-cathepsin L1 complex influence the mode of binding and thus control the diverse inhibitory affinity of cystatins towards cysteine proteases. Docking outputs of cathepsin L1 complexes with stefin A, stefin B, cystatin C, cystatin D, cystatin F, cystatin M/E, cystatin S, cystatin SA, and cystatin SN
-
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COVID-19
Multi-organ proteomic landscape of COVID-19 autopsies.
Endometritis
Endometrial expression of various genes (ISGs, PPARs, RXRs and MUC1) on day 16 post-ovulation in repeat breeder cows, with or without subclinical endometritis.
Endometritis
mRNA Expressions of Candidate Genes in Gestational Day 16 Conceptus and Corresponding Endometrium in Repeat Breeder Dairy Cows with Suboptimal Uterine Environment Following Transfer of Different Quality Day 7 Embryos.
Fascioliasis
Design and synthesis of a new peptide derived from Fasciola gigantica cathepsin L1 with potential application in serodiagnosis of fascioliasis.
Fascioliasis
Immunodiagnosis of Fasciola hepatica infection (fascioliasis) in a human population in the Bolivian Altiplano using purified cathepsin L cysteine proteinase.
Fascioliasis
Potent epitopes derived from Fasciola gigantica cathepsin L1 in peptide-based immunoassay for the serodiagnosis of human fascioliasis.
Fascioliasis
Serodiagnosis of human fascioliasis by a cystatin capture enzyme-linked immunosorbent assay with recombinant Fasciola gigantica cathepsin L antigen.
Fascioliasis
Short report: Immunodiagnosis of human fascioliasis using recombinant Fasciola hepatica cathepsin L1 cysteine proteinase.
Glioma
Viability screen on pediatric low grade glioma cell lines unveils a novel anti-cancer drug of the steroid biosynthesis inhibitor family.
Infections
Cathepsin L1 mimotopes with adjuvant Quil A induces a Th1/Th2 immune response and confers significant protection against Fasciola hepatica infection in goats.
Infections
Differences in the antibody response to adult Fasciola hepatica excretory/secretory products in experimentally and naturally infected cattle and sheep.
Infections
Early and Late Peritoneal and Hepatic Changes in Goats Immunized with Recombinant Cathepsin L1 and Infected with Fasciola hepatica.
Infections
Expression of free radicals by peritoneal cells of sheep during the early stages of Fasciola hepatica infection.
Infections
Humoral immune response in goats immunised with cathepsin L1, peroxiredoxin and Sm14 antigen and experimentally challenged with Fasciola hepatica.
Infections
Identification of protective peptides of Fasciola hepatica-derived cathepsin L1 (FhCL1) in vaccinated sheep by a linear B-cell epitope mapping approach.
Infections
Identification of reference genes for real-time PCR cytokine gene expression studies in sheep experimentally infected with Fasciola hepatica.
Infections
Immune responses of cattle to experimental anti-Fasciola hepatica vaccines.
Infections
Immunodiagnosis of Fasciola gigantica Infection Using Monoclonal Antibody-Based Sandwich ELISA and Immunochromatographic Assay for Detection of Circulating Cathepsin L1 Protease.
Infections
Protection of cattle against a natural infection of Fasciola hepatica by vaccination with recombinant cathepsin L1 (rFhCL1).
Infections
Th1/Th2 balance in the liver and hepatic lymph nodes of vaccinated and unvaccinated sheep during acute stages of infection with Fasciola hepatica.
Infections
The combined recombinant cathepsin L1H and cathepsin B3 vaccine against Fasciola gigantica infection.
Insulin Resistance
Cathepsin gene expression in abdominal subcutaneous adipose tissue of obese/overweight humans.
Lymphoma
[Mechanism of renal injury and apoptosis in rats with nephrotic syndrome induced by mercury].
Neoplasm Metastasis
The lnc-CTSLP8 upregulates CTSL1 as a competitive endogenous RNA and promotes ovarian cancer metastasis.
Neoplasms
Biomarkers of blood cadmium and incidence of cardiovascular events in non-smokers: results from a population-based proteomics study.
Neoplasms
Candidate serological biomarkers for cancer identified from the secretomes of 23 cancer cell lines and the human protein atlas.
Neoplasms
Proteomic profiling for detection of early-stage heart failure in the community.
Neoplasms
The Biomarkers NT-proBNP and CA-125 are Elevated in Patients with Idiopathic Atrial Fibrillation.
Neoplasms
Using multimarker screening to identify biomarkers associated with cardiovascular death in patients with atrial fibrillation.
Ovarian Neoplasms
The lnc-CTSLP8 upregulates CTSL1 as a competitive endogenous RNA and promotes ovarian cancer metastasis.
Schistosomiasis
Computer-Aided Drug Design for the Identification of Novel Antischistosomal Compounds.
Starvation
Molecular cloning and mRNA expression of the liver-specific cathepsin L1 gene of the olive flounder, Paralichthys olivaceus.
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0.0093
benzoyl-Phe-Val-Arg-4-methylcoumarinyl-7-amide
-
pH 7.0, 37°C, cathepsin L1
0.0093
benzoyl-Phe-Val-Arg-7-amido-4-methylcoumarin
-
pH 7.0, 37°C
0.0204
benzyloxycarbonyl-Arg-4-methylcoumarinyl-7-amide
-
pH 7.0, 37°C, cathepsin L1
0.0204
benzyloxycarbonyl-Arg-7-amido-4-methylcoumarin
-
pH 7.0, 37°C
0.0656
benzyloxycarbonyl-Arg-Arg-4-methylcoumarinyl-7-amide
-
pH 7.0, 37°C, cathepsin L1
0.0656
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin
-
pH 7.0, 37°C
0.38 - 4.35
benzyloxycarbonyl-L-Leu-L-Arg-4-methylcoumarinyl-7-amide
8.16 - 24.18
benzyloxycarbonyl-L-Phel-L-Arg-4-methylcoumarinyl-7-amide
48.41 - 191.2
benzyloxycarbonyl-L-Pro-L-Arg-4-methylcoumarinyl-7-amide
0.0036 - 0.0044
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin
0.0147
benzyloxycarbonyl-Phe-Arg-4-methylcoumarinyl-7-amide
-
pH 7.0, 37°C, cathepsin L1
0.003 - 0.0242
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
0.1819 - 0.1912
benzyloxycarbonyl-Pro-Arg-7-amido-4-methylcoumarin
0.0054
H-Leu-Val-Tyr-4-methylcoumarinyl-7-amide
-
pH 7.0, 37°C, cathepsin L1
0.0054
H-Leu-Val-Tyr-7-amido-4-methylcoumarin
-
pH 7.0, 37°C
0.0653
succinyl-Ala-Phe-Lys-4-methylcoumarinyl-7-amide
-
pH 7.0, 37°C, cathepsin L1
0.0653
succinyl-Ala-Phe-Lys-7-amido-4-methylcoumarin
-
pH 7.0, 37°C
0.0385
succinyl-Leu-Leu-Val-Tyr-4-methylcoumarinyl-7-amide
-
pH 7.0, 37°C, cathepsin L1
0.0385
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
-
pH 7.0, 37°C
0.0347
t-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
-
pH 7.0, 37°C
0.0436
t-butyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin
-
pH 7.0, 37°C
10.43 - 21.57
tert-butoxycarbonyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide
0.0347
tert-butyloxycarbonyl-Val-Leu-Lys-4-methylcoumarinyl-7-amide
-
pH 7.0, 37°C, cathepsin L1
0.0436
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumarinyl-7-amide
-
pH 7.0, 37°C, cathepsin L1
0.026 - 20.35
tosyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide
0.026
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin
-
pH 7.0, 37°C
0.1069
tosyl-Gly-Pro-Lys-4-methylcoumarinyl-7-amide
-
pH 7.0, 37°C, cathepsin L1
0.1069
tosyl-Gly-Pro-Lys-7-amido-4-methylcoumarin
-
pH 7.0, 37°C
0.38
benzyloxycarbonyl-L-Leu-L-Arg-4-methylcoumarinyl-7-amide
mutant enzyme L67Y FheCL1
2.75
benzyloxycarbonyl-L-Leu-L-Arg-4-methylcoumarinyl-7-amide
mutant enzyme L205A FheCL1
4.35
benzyloxycarbonyl-L-Leu-L-Arg-4-methylcoumarinyl-7-amide
wild-type enzyme FheCL1
8.16
benzyloxycarbonyl-L-Phel-L-Arg-4-methylcoumarinyl-7-amide
mutant enzyme L67Y FheCL1
19.21
benzyloxycarbonyl-L-Phel-L-Arg-4-methylcoumarinyl-7-amide
mutant enzyme L205A FheCL1
24.18
benzyloxycarbonyl-L-Phel-L-Arg-4-methylcoumarinyl-7-amide
wild-type enzyme FheCL1
48.41
benzyloxycarbonyl-L-Pro-L-Arg-4-methylcoumarinyl-7-amide
mutant enzyme L205A FheCL1
137
benzyloxycarbonyl-L-Pro-L-Arg-4-methylcoumarinyl-7-amide
mutant enzyme L67Y FheCL1
191.2
benzyloxycarbonyl-L-Pro-L-Arg-4-methylcoumarinyl-7-amide
wild-type enzyme FheCL1
0.0036
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin
37°C, pH 7.3
0.0044
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin
37°C, pH 5.5
0.003
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
37°C, pH 7.3
0.0147
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
-
pH 7.0, 37°C
0.0242
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
37°C, pH 5.5
0.1819
benzyloxycarbonyl-Pro-Arg-7-amido-4-methylcoumarin
37°C, pH 7.3
0.1912
benzyloxycarbonyl-Pro-Arg-7-amido-4-methylcoumarin
37°C, pH 5.5
10.43
tert-butoxycarbonyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide
wild-type enzyme FheCL1
11.13
tert-butoxycarbonyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide
mutant enzyme L67Y FheCL1
21.57
tert-butoxycarbonyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide
mutant enzyme L205A FheCL1
0.026
tosyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide
-
pH 7.0, 37°C, cathepsin L1
6.96
tosyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide
mutant enzyme L67Y FheCL1
10.02
tosyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide
wild-type enzyme FheCL1
20.35
tosyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide
mutant enzyme L205A FheCL1
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0.03
benzoyl-Phe-Val-Arg-4-methylcoumarinyl-7-amide
-
pH 7.0, 37°C, cathepsin L1
0.03
benzoyl-Phe-Val-Arg-7-amido-4-methylcoumarin
-
pH 7.0, 37°C
0.04
benzyloxycarbonyl-Arg-4-methylcoumarinyl-7-amide
-
pH 7.0, 37°C, cathepsin L1
0.04
benzyloxycarbonyl-Arg-7-amido-4-methylcoumarin
-
pH 7.0, 37°C
0.002
benzyloxycarbonyl-Arg-Arg-4-methylcoumarinyl-7-amide
-
pH 7.0, 37°C, cathepsin L1
0.002
benzyloxycarbonyl-Arg-Arg-7-amido-4-methylcoumarin
-
pH 7.0, 37°C
1.73 - 36.52
benzyloxycarbonyl-L-Leu-L-Arg-4-methylcoumarinyl-7-amide
3.58 - 29.6
benzyloxycarbonyl-L-Phe-L-Arg-4-methylcoumarinyl-7-amide
0.122 - 1.03
benzyloxycarbonyl-L-Pro-L-Arg-4-methylcoumarinyl-7-amide
11 - 36.5
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin
1.08
benzyloxycarbonyl-Phe-Arg-4-methylcoumarinyl-7-amide
-
pH 7.0, 37°C, cathepsin L1
1.08 - 24.7
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
1 - 1.7
benzyloxycarbonyl-Pro-Arg-7-amido-4-methylcoumarin
0.02
H-Leu-Val-Tyr-4-methylcoumarinyl-7-amide
-
pH 7.0, 37°C, cathepsin L1
0.02
H-Leu-Val-Tyr-7-amido-4-methylcoumarin
-
pH 7.0, 37°C
0.05
succinyl-Ala-Phe-Lys-4-methylcoumarinyl-7-amide
-
pH 7.0, 37°C, cathepsin L1
0.05
succinyl-Ala-Phe-Lys-7-amido-4-methylcoumarin
-
pH 7.0, 37°C
0.01
succinyl-Leu-Leu-Val-Tyr-4-methylcoumarinyl-7-amide
-
pH 7.0, 37°C, cathepsin L1
0.01
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
-
pH 7.0, 37°C
7.9
t-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
-
pH 7.0, 37°C
0.02
t-butyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin
-
pH 7.0, 37°C
0.2 - 0.93
tert-butoxycarbonyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide
7.9
tert-butyloxycarbonyl-Val-Leu-Lys-4-methylcoumarinyl-7-amide
-
pH 7.0, 37°C, cathepsin L1
0.02
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumarinyl-7-amide
-
pH 7.0, 37°C, cathepsin L1
0.03 - 0.36
tosyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide
0.03
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin
-
pH 7.0, 37°C
0.03
tosyl-Gly-Pro-Lys-4-methylcoumarinyl-7-amide
-
pH 7.0, 37°C, cathepsin L1
0.03
tosyl-Gly-Pro-Lys-7-amido-4-methylcoumarin
-
pH 7.0, 37°C
1.73
benzyloxycarbonyl-L-Leu-L-Arg-4-methylcoumarinyl-7-amide
mutant enzyme L67Y FheCL1
9.15
benzyloxycarbonyl-L-Leu-L-Arg-4-methylcoumarinyl-7-amide
mutant enzyme L205A FheCL1
36.52
benzyloxycarbonyl-L-Leu-L-Arg-4-methylcoumarinyl-7-amide
wild-type enzyme FheCL1
3.58
benzyloxycarbonyl-L-Phe-L-Arg-4-methylcoumarinyl-7-amide
mutant enzyme L67YFheCL1
24.69
benzyloxycarbonyl-L-Phe-L-Arg-4-methylcoumarinyl-7-amide
wild-type enzyme, FheCL1
29.6
benzyloxycarbonyl-L-Phe-L-Arg-4-methylcoumarinyl-7-amide
mutant enzyme L205A FheCL1
0.122
benzyloxycarbonyl-L-Pro-L-Arg-4-methylcoumarinyl-7-amide
mutant enzyme L205A FheCL1
0.62
benzyloxycarbonyl-L-Pro-L-Arg-4-methylcoumarinyl-7-amide
mutant enzyme L67Y FheCL1
1.03
benzyloxycarbonyl-L-Pro-L-Arg-4-methylcoumarinyl-7-amide
wild-type enzyme FheCL1
11
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin
37°C, pH 7.3
36.5
benzyloxycarbonyl-Leu-Arg-7-amido-4-methylcoumarin
37°C, pH 5.5
1.08
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
-
pH 7.0, 37°C
2
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
37°C, pH 7.3
24.7
benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin
37°C, pH 5.5
1
benzyloxycarbonyl-Pro-Arg-7-amido-4-methylcoumarin
37°C, pH 5.5
1.7
benzyloxycarbonyl-Pro-Arg-7-amido-4-methylcoumarin
37°C, pH 7.3
0.2
tert-butoxycarbonyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide
mutant enzyme L205A FheCL1
0.48
tert-butoxycarbonyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide
wild-type enzyme FheCL1
0.93
tert-butoxycarbonyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide
mutant enzyme L67Y FheCL1
0.03
tosyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide
-
pH 7.0, 37°C, cathepsin L1
0.113
tosyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide
mutant enzyme L205A FheCL1
0.26
tosyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide
mutant enzyme L67Y FheCL1
0.36
tosyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide
wild-type enzyme FheCL1
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0.003
Benzyloxycarbonyl-Phe-Ala-CHN2
Fasciola hepatica
-
in 0.1 M sodium acetate, at 37°C, pH not specified in the publication
0.0044
N-2,3,4,5,6-pentafluorobenzoyl-L-leucyl-glycine nitrile
Fasciola hepatica
-
in 0.1 M sodium acetate, at 37°C, pH not specified in the publication
0.0034
N-2,3,4,5-tetrafluorobenzoyl-L-leucyl-glycine nitrile
Fasciola hepatica
-
in 0.1 M sodium acetate, at 37°C, pH not specified in the publication
0.0041
N-2,3,4-trifluorobenzoyl-L-leucyl-glycine nitrile
Fasciola hepatica
-
in 0.1 M sodium acetate, at 37°C, pH not specified in the publication
0.006
N-2,3,6-trifluorobenzoyl-L-leucyl-glycine nitrile
Fasciola hepatica
-
in 0.1 M sodium acetate, at 37°C, pH not specified in the publication
0.0034
N-2,3-difluorobenzoyl-L-leucyl-glycine nitrile
Fasciola hepatica
-
in 0.1 M sodium acetate, at 37°C, pH not specified in the publication
0.0045
N-2,4,5-trifluorobenzoyl-L-leucyl-glycine nitrile
Fasciola hepatica
-
in 0.1 M sodium acetate, at 37°C, pH not specified in the publication
0.0055
N-2,4-difluorobenzoyl-L-leucyl-glycine nitrile
Fasciola hepatica
-
in 0.1 M sodium acetate, at 37°C, pH not specified in the publication
0.0031
N-2,5-difluorobenzoyl-L-leucyl-glycine nitrile
Fasciola hepatica
-
in 0.1 M sodium acetate, at 37°C, pH not specified in the publication
0.0037
N-2,6-difluorobenzoyl-L-leucyl-glycine nitrile
Fasciola hepatica
-
in 0.1 M sodium acetate, at 37°C, pH not specified in the publication
0.1
N-2-fluorobenzoyl-L-alanine-beta-alanine nitrile
Fasciola hepatica
-
IC50 above 0.1 mM, in 0.1 M sodium acetate, at 37°C, pH not specified in the publication
0.0876
N-2-fluorobenzoyl-L-alanine-glycine nitrile
Fasciola hepatica
-
in 0.1 M sodium acetate, at 37°C, pH not specified in the publication
0.0294
N-2-fluorobenzoyl-L-leucine-beta-alanine benzyl ester
Fasciola hepatica
-
in 0.1 M sodium acetate, at 37°C, pH not specified in the publication
0.0243
N-2-fluorobenzoyl-L-leucine-beta-alanine nitrile
Fasciola hepatica
-
in 0.1 M sodium acetate, at 37°C, pH not specified in the publication
0.0153
N-2-fluorobenzoyl-L-leucine-gamma-aminobutyric acid benzyl ester
Fasciola hepatica
-
in 0.1 M sodium acetate, at 37°C, pH not specified in the publication
0.1
N-2-fluorobenzoyl-L-leucyl-glycine benzyl ester
Fasciola hepatica
-
IC50 above 0.1 mM, in 0.1 M sodium acetate, at 37°C, pH not specified in the publication
0.003
N-2-fluorobenzoyl-L-leucyl-glycine nitrile
Fasciola hepatica
-
in 0.1 M sodium acetate, at 37°C, pH not specified in the publication
0.0041
N-2-trifluoromethylbenzoyl-L-leucyl-glycine nitrile
Fasciola hepatica
-
in 0.1 M sodium acetate, at 37°C, pH not specified in the publication
0.0034
N-3,4,5-trifluorobenzoyl-L-leucyl-glycine nitrile
Fasciola hepatica
-
in 0.1 M sodium acetate, at 37°C, pH not specified in the publication
0.0031
N-3,4-difluorobenzoyl-L-leucyl-glycine nitrile
Fasciola hepatica
-
in 0.1 M sodium acetate, at 37°C, pH not specified in the publication
0.003
N-3,5-difluorobenzoyl-L-leucyl-glycine nitrile
Fasciola hepatica
-
in 0.1 M sodium acetate, at 37°C, pH not specified in the publication
0.0248
N-3-fluorobenzoyl-L-leucine-beta-alanine benzyl ester
Fasciola hepatica
-
in 0.1 M sodium acetate, at 37°C, pH not specified in the publication
0.0401
N-3-fluorobenzoyl-L-leucine-gamma-aminobutyric acid benzyl ester
Fasciola hepatica
-
in 0.1 M sodium acetate, at 37°C, pH not specified in the publication
0.1
N-3-fluorobenzoyl-L-leucyl-glycine benzyl ester
Fasciola hepatica
-
IC50 above 0.1 mM, in 0.1 M sodium acetate, at 37°C, pH not specified in the publication
0.0031
N-3-fluorobenzoyl-L-leucyl-glycine nitrile
Fasciola hepatica
-
in 0.1 M sodium acetate, at 37°C, pH not specified in the publication
0.0091
N-3-trifluoromethylbenzoyl-L-leucyl-glycine nitrile
Fasciola hepatica
-
in 0.1 M sodium acetate, at 37°C, pH not specified in the publication
0.0623
N-4-fluorobenzoyl-L-leucine-beta-alanine benzyl ester
Fasciola hepatica
-
in 0.1 M sodium acetate, at 37°C, pH not specified in the publication
0.0216
N-4-fluorobenzoyl-L-leucine-beta-alanine nitrile
Fasciola hepatica
-
in 0.1 M sodium acetate, at 37°C, pH not specified in the publication
0.0193
N-4-fluorobenzoyl-L-leucine-gamma-aminobutyric acid benzyl ester
Fasciola hepatica
-
in 0.1 M sodium acetate, at 37°C, pH not specified in the publication
0.0434
N-4-fluorobenzoyl-L-leucyl-glycine benzyl ester
Fasciola hepatica
-
in 0.1 M sodium acetate, at 37°C, pH not specified in the publication
0.0028
N-4-fluorobenzoyl-L-leucyl-glycine nitrile
Fasciola hepatica
-
in 0.1 M sodium acetate, at 37°C, pH not specified in the publication
0.0032
N-4-trifluoromethylbenzoyl-L-leucyl-glycine nitrile
Fasciola hepatica
-
in 0.1 M sodium acetate, at 37°C, pH not specified in the publication
0.01
N-benzoyl-L-leucyl-glycine
Fasciola hepatica
-
in 0.1 M sodium acetate, at 37°C, pH not specified in the publication
0.011
N-cinnamoyl-L-leucyl-glycine nitrile
Fasciola hepatica
-
in 0.1 M sodium acetate, at 37°C, pH not specified in the publication
0.1
N-pentafluorobenzoyl-L-alanine-beta-alanine nitrile
Fasciola hepatica
-
IC50 above 0.1 mM, in 0.1 M sodium acetate, at 37°C, pH not specified in the publication
0.0683
N-pentafluorobenzoyl-L-alanine-glycine nitrile
Fasciola hepatica
-
in 0.1 M sodium acetate, at 37°C, pH not specified in the publication
0.0577
N-pentafluorobenzoyl-L-leucine-beta-alanine benzyl ester
Fasciola hepatica
-
in 0.1 M sodium acetate, at 37°C, pH not specified in the publication
0.0214
N-pentafluorobenzoyl-L-leucine-gamma-aminobutyric acid benzyl ester
Fasciola hepatica
-
in 0.1 M sodium acetate, at 37°C, pH not specified in the publication
0.0395
N-pentafluorobenzoyl-L-leucyl-glycine benzyl ester
Fasciola hepatica
-
in 0.1 M sodium acetate, at 37°C, pH not specified in the publication
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agriculture
-
screening of cathepsin L1/cathepsin L2 mimotopes and use of an M13 phage random 12-mers peptide library to evaluate their immunogenicity in sheep. Immunization of sheep with clones showing positive reactivity to rabbit cathepsin L1/L2 antiserum results in decrease in worm burdens after challenge. A significant reduction in worm size and burden is observed for those sheep immunized with clone 1. Animals receiving clone 20, show a significant reduction in egg output. Immunization induces a reduction of egg viability ranging from 58% to 82%. Vaccinated animals produce clone-specific antibodies which are boosted after challenge with metacercariae of Fasciola hepatica
agriculture
-
vaccination of rats with recombinant zymogen and subsequent challenge with fasciola hepatica metercercariae. Vaccination results in significantly smaller and fewer flukes than in controls
diagnostics
a monoclonal antibody (MoAb) against recombinant Fasciola gigantica cathepsin L1H (rFgCatL1H) is produced by hybridoma technique using spleen cells from BALB/c mice immunized with recombinant proFgCatL1H (rproFgCatL1H). This MoAb is an immunoglobulin (Ig)G1 with kappa light chain isotype. The MoAb reacts specifically with rproFgCatL1H, the native FgCatL1H at a molecular weight (MW) 38-48 kDa in the extract of whole body (WB) of metacercariae and newly excysted juvenile (NEJ) and cross-reacted with rFgCatL1 and native FgCatLs at MW 25 to 28 kDa in WB of 2- and 4-week-old juveniles, adult, and adult excretory-secretory (ES) fractions by immunoblotting and indirect ELISA. It does not cross-react with antigens in WB fractions from other parasites. FgCatL1H and its MoAb may be used for immunodiagnosis of both early and late fasciolosis in ruminants and humans
diagnostics
analysis of the diagnostic values of the three different clades of cathepsin Ls, FhCL1, FhCL2, and FhCL5, from adult flukes in an ELISA, test of sera from sheep and cattle naturally infected with Fasciola hepatica, of cross-reactive antibodies, overview. For sheep sera, the sensitivity is 100% for the three rFhpCLs, while for cattle sera, the highest sensitivity is obtained using rFhpCL2 (97%), being equal for both rFhpCL1 and rFhpCL5 (87.9%), after adjusting cut-offs for maximum specificity
diagnostics
design and synthesis of a new peptide derived from Fasciola gigantica cathepsin L1 with potential application in serodiagnosis of fascioliasis via ELISA, overview. Cathepsin L1 as antigen for serodiagnosis of animal fasciolosis
diagnostics
design and synthesis of a new peptide derived from Fasciola gigantica cathepsin L1 with potential application in serodiagnosis of fascioliasis via ELISA, overview. Cathepsin L1 as antigen for serodiagnosis of animal fasciolosis
diagnostics
recombinant proFgCatL1H protein expressed from Pichia pastoris is mixed with Freund's adjuvants and used to subcutaneously immunize mice, the mice are then challenged with metacercariae of Fasciola gigantica. The percentage of worm protection in the rproFgCatL1H-vaccinated mice compared to the non-immunized and adjuvant control mice are approximately 62.7% and 66.1%, respectively. Anti-rproFgCatL1H antisera collected from vaccinated mice react specifically with rproFgCatL1H and other cathepsin L isoforms of Fasciola gigantica, but the antibodies do not crossreact with antigens from other trematode and nematode parasites, including Eurytrema pancreaticum, Opisthorchis viverrini, Fischoederius cobboldi, Cotylophoron cotylophorum, Gigantocotyle explanatum, Paramphistomum cervi, and Setarialabiato papillosa
medicine
-
potential in the development of first generation liver fluke vaccines. Vaccine trials in both sheep and cattle with purified native FheCL1 and FheCL2 show that the enzymes can induce protection, ranging from 33-79%, to experimental challenge with metacercariae of Fasciola hepatica, and very potent anti-embryonation/hatch rate effects that would block parasite transmission
medicine
-
diagnostic ability to detect human IgG antibodies against Fasciola gigantica cathepsin L1 by peptide-based ELISA, serodiagnosis of human fascioliasis, which is rapid, cheap and easy to produce
medicine
the cathepsin L1 gene may be used for DNA vaccination, recombinant protein derived from the gene can be used for serological diagnostics against Fasciola hepatica in Turkey
medicine
-
enteral vaccination of rats against Fasciola hepatica using recombinant cysteine proteinase (cathepsin L1). The mature CPFhW protein is the enzyme secreted by Fasciola hepatica with which the host organism has contact. This can explain why immunisation with this antigen resultes in best protection in challenged animals, especially in comparison to the immature form of the CPFhW protein. Substantial protection can be obtained when the antigen is given with food. Oral administration of the antigen does not lead to decreasing of the level of protection compared with intragastric administration
medicine
-
cattle can be protected against a natural infection of Fasciola hepatica by vaccination with recombinant cathepsin L1
medicine
mice immunized with recombinant CL1 show a decrease of 21.8% in Schistosoma mansoni burden
medicine
-
recombinant cathepsin L1 is a vaccine for fasciolosis in goats
medicine
a leucine aminopeptidase-cathepsin L1 chimeric protein may be used as a diagnostic tool for detection of antibodies against Fasciola hepatica in bovine sera and as an immunogen to induce protection against bovine fasciolosis
medicine
a monoclonal antibody (MoAb) against recombinant Fasciola gigantica cathepsin L1H (rFgCatL1H) is produced by hybridoma technique using spleen cells from BALB/c mice immunized with recombinant proFgCatL1H (rproFgCatL1H). This MoAb is an immunoglobulin (Ig)G1 with kappa light chain isotype. The MoAb reacts specifically with rproFgCatL1H, the native FgCatL1H at a molecular weight (MW) 38-48 kDa in the extract of whole body (WB) of metacercariae and newly excysted juvenile (NEJ) and cross-reacted with rFgCatL1 and native FgCatLs at MW 25 to 28 kDa in WB of 2- and 4-week-old juveniles, adult, and adult excretory-secretory (ES) fractions by immunoblotting and indirect ELISA. It does not cross-react with antigens in WB fractions from other parasites. FgCatL1H and its MoAb may be used for immunodiagnosis of both early and late fasciolosis in ruminants and humans
medicine
recombinant proFgCatL1H protein expressed from Pichia pastoris is mixed with Freund's adjuvants and used to subcutaneously immunize mice, the mice are then challenged with metacercariae of Fasciola gigantica. The percentage of worm protection in the rproFgCatL1H-vaccinated mice compared to the non-immunized and adjuvant control mice are approximately 62.7% and 66.1%, respectively. The levels of IgG1 and IgG2a in the immune sera are shown to be strongly correlated with the numbers of worm recovery, and the correlation coefficient is higher for IgG1. The levels of serum aspartate amino-transferase and alanine transaminase are significantly lower in the sera of rproFgCatL1H-vaccinated mice than in the infected control mice indicating a lower degree of liver damage
medicine
vaccination of mice by subcutaneous injection with recombinant proFgCatL1 and recombinant mature FgCatL1 combined with Freund's adjuvant. Two weeks after the second boost, mice are infected with 15 metacercariae by the oral route. The level of protection of rproFgCatL1 and rmatFgCatL1 vaccines is estimated to be 39.1-41.7% and 44.9-47.2% when compared with non vaccinated-infected and adjuvant-infected controls, respectively. Antibodies in the immune sera of vaccinated mice are shown by immunoblotting to react with the native FgCatL1 in the extract of newly excysted juveniles (NEJ), 4-week-old juveniles, and the excretory-secretory products of 4 week-old juveniles. rFgCatL1 has a potential as a vaccine candidate against Fasciola gigantica in mice, and might also be effective in ruminants
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2007
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Fasciola hepatica (Q7JNQ9)
brenda
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37
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Fasciola hepatica (Q9GRW5), Fasciola hepatica
brenda