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Information on EC 3.4.24.B12 - ADAMTS5 endopeptidase
for references in articles please use BRENDA:EC3.4.24.B12
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preliminary BRENDA-supplied EC number
EC Tree 3 Hydrolases
3.4 Acting on peptide bonds (peptidases)
3.4.24 Metalloendopeptidases
3.4.24.B12 ADAMTS5 endopeptidase
The enzyme appears in viruses and cellular organisms
- 3.4.24.B12
- cartilage
- osteoarthritis
- chondrocytes
-
articular
- metalloproteinase
- collagen
- joint
-
disintegrin
- degeneration
- adamts-4
- tnf
- proteoglycans
- knee
-
intervertebral
-
degener
- synovial
- cox-2
- mmp-1
-
col2a1
- pulposus
- meniscus
- interleukin-1
-
intra-articular
- versican
-
disintegrin-like
- timp-3
-
temporomandibular
-
subchondral
-
safranin
-
cruciate
-
matrix-degrading
-
neoepitope
-
chondroprotective
-
chondrogenic
- brevican
- medicine
-
mankin
-
surgically-induced
-
oa-like
-
collagen-ii
-
meniscectomy
-
anti-catabolic
-
cartilage-degrading
-
interglobular
-
dmm-induced
-
condylar
-
oa-related
-
oa-associated
- osteophyte
-
motifs-4
-
osteoarthritis-like
showSynonyms
adamts-5, adamts5, aggrecanase-2, adam-ts5, aggrecanase 2, aggrecanase-, adamts11, agg-2, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
a disintegrin and metalloproteinase with thrombospondin motifs 5
a disintegrin and metalloproteinase with thrombospondin motifs-5
a disintegrin and metalloproteinase with thrombospondin type 1 motifs, member 5
-
a disintegrin and metalloproteinase with thrombospondin type I motifs-5
-
A disintegrin-like and metalloproteinase with thrombospondin type-1 motifs-5
-
a disintegrin-like and metalloproteinase with thrombospondin-1 motifs 5
-
ADAM-TS 5
ADAM-TS11
ADAM-TS5
ADAMTS-5
ADAMTS-5-2
ADAMTS-5 which lacks the C-terminal cysteine-rich spacer and thrombospondin domains
ADAMTS5
ADMP-2
aggrecanase-2
implantin
M12.225
a disintegrin and metalloproteinase with thrombospondin motifs 5
-
-
ADAMTS-5
-
-
ADAMTS-5
a disintegrin and metalloproteinase with thrombospondin motifs-5
ADAMTS-5
a disintegrin and metalloproteinase with thrombospondin motifs-5
ADAMTS5
-
-
aggrecanase-2
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
proteolytic degradation of proteins
-
-
-
-
proteolytic degradation of proteins
strict specificity for cleavage between glutamic acid and uncharged aliphatic amino acids in the core proteins of large aggregating proteoglycans
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis
endoproteolytic cleavage of specific Glu-Xaa bonds within the core protein of aggrecan
hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY
405150-12-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
aggrecan + H2O
7 aggregan fragment
Substrates: several cleavage sites are determined
Products: product determination, overview
Products: product determination, overview
?
C6-(Gly-Pro-Hyp-Pro-Hyp-Gly)2-Gly-Pro-Hyp-Gly-Thr-Lys(Mca)-Gly-Glu-Leu-Glu-Gly-Arg-Gly-Thr-Lys(Dnp)-Gly-Ile-Ser-(Gly-Pro-Hyp-Pro-Hyp-Gly)2-Gly-Pro-Hyp-NH2 + H2O
?
-
Substrates: -
Products: -
Products: -
?
complement C3 + H2O
?
Substrates: multiple kidney proteins are affected by ADAMTS5. Specific proteolysis of complement C3 and fibronectin associated with IgA on immune complexes
Products: -
Products: -
?
FAM-AELQGRPISIAK-TAMRA + H2O
?
-
Substrates: activity measured using a quenched fluorescent substrate
Products: -
Products: -
?
fibromodulin + H2O
29000 Da fibromodulin fragment + ?
-
Substrates: very low activity
Products: -
Products: -
?
inter-alpha-inhibitor heavy chain-2 + H2O
?
Substrates: the major cleavage site is in the C terminus of heavy chain HC2
Products: -
Products: -
?
K(6FAM)-DVQEFRGVTAVIRC(Qsy9)-KGK + H2O
K-(6FAM)-DVQE + FRGVTAVIRC(Qsy9)-KGK
-
Substrates: -
Products: -
Products: -
?
K-[6FAM]-DVQEFRGVTAVIRC-[Qsy9]-KGK + H2O
K-[6FAM]-DVQE + FRGVTAVIRC-[Qsy9]-KGK
Substrates: -
Products: -
Products: -
?
kidney matrix + H2O
?
Substrates: multiple kidney proteins are affected by ADAMTS5. Specific proteolysis of complement C3 and fibronectin associated with IgA on immune complexes
Products: -
Products: -
?
Lys(7-methoxycoumarin-4-yl)-Lys-Gln-Glu-Phe-Arg-Gly-Gln-Thr-Lys(Dnp)-NH2 + H2O
?
-
Substrates: -
Products: -
Products: -
?
Lys(carboxyfluorescein)-Asp-Val-Gln-Glu-Phe-Arg-Gly-Val-Thr-Ala-Val-Ile-Arg-Lys(tetramethylrhodamine)-Lys-Gly-Lys-NH2 + H2O
?
-
Substrates: -
Products: -
Products: -
?
matrilin-2 + H2O
?
Substrates: -
Products: substrate contains two putative cleavage sites. The first site is located between residues D851 and L852 in the middle of the domain and the second at the boundary with the coiled-coil domain at the C-terminus. Deletion of the entire unique domain eliminates the proteolysis of matrilin-2. The first cleavage site is present in all matrilin-2 oligomers, the second cleavage site becomes apparent only in the matrilin-2 hetero-oligomers with matrilin-1 or matrilin-3
Products: substrate contains two putative cleavage sites. The first site is located between residues D851 and L852 in the middle of the domain and the second at the boundary with the coiled-coil domain at the C-terminus. Deletion of the entire unique domain eliminates the proteolysis of matrilin-2. The first cleavage site is present in all matrilin-2 oligomers, the second cleavage site becomes apparent only in the matrilin-2 hetero-oligomers with matrilin-1 or matrilin-3
?
matrilin-4 + H2O
?
-
Substrates: matrilin-4 is specifically cleaved by ADAMTS-5
Products: -
Products: -
?
o-aminobenzoyl-TESESRGAIY-N-3-[2,4-dinitrophenyl]-L-2,3-diaminopropionyl-KK-NH2 + H2O
o-aminobenzoyl-TESE + SRGAIY-N-3-[2,4-dinitrophenyl]-L-2,3-diaminopropionyl-KK-NH2
Substrates: -
Products: -
Products: -
?
o-aminobenzoyl-Thr-Glu-Ser-Glu-Ser-Arg-Gly-Ala-Ile-Tyr-(N-3-[2,4-dinitrophenyl]-L-2,3-diaminopropionyl)-Lys-Lys-NH2 + H2O
o-aminobenzoyl-Thr-Glu-Ser-Glu + Ser-Arg-Gly-Ala-Ile-Tyr-(N-3-[2,4-dinitrophenyl]-L-2,3-diaminopropionyl)-Lys-Lys-NH2
VQTVTWPDMELPLPRNITEGEARGSVILTVKPIFEVSPSPLKG + H2O
?
-
Substrates: 43mer peptide substrate
Products: -
Products: -
?
aggrecan + H2O
2 aggrecan fragment
-
Substrates: cleavage site is Glu373-Ala374
Products: -
Products: -
?
aggrecan + H2O
2 aggrecan fragment
-
Substrates: cleavage site is Glu373-Ala374, reaction is relevant to cartilage degeneration in inflammatory joint diseases
Products: -
Products: -
?
aggrecan + H2O
?
Substrates: substrate from cartilage, N-terminal cleavage sites between glutamate and small uncharged aliphatic amino acids in nonglycosylated regions of the aggregan core protein: the interglobular domain E373-A, and within the chondroitinsulfate 2 attachment region E1666-G, E1771-A, and E1871-L
Products: -
Products: -
?
aggrecan + H2O
?
Substrates: enzyme may play a role in cartilage breakdown
Products: -
Products: -
?
aggrecan + H2O
?
-
Substrates: cleavage site is Glu373-Ala374, other cleavage sites are Glu1545-Gly1546, Glu1819-Ala1820, and Glu1919-Leu1920
Products: -
Products: -
?
aggrecan + H2O
?
-
Substrates: substrate from cartilage, extensive digestion, N-terminal cleavage sites between glutamate and small uncharged aliphatic amino acids in nonglycosylated regions of the aggregan core protein: the interglobular domain E373-A, and between chondroitin sulfate attachment sites 1 and 2 E1480-G
Products: -
Products: -
?
aggrecan + H2O
?
-
Substrates: enzyme may play a role in cartilage breakdown
Products: -
Products: -
?
aggrecan + H2O
?
-
Substrates: ADAMTS-5 is able to cleave aggrecan core protein about 1,000 times more effectively than ADAMTS-4
Products: -
Products: -
?
aggrecan + H2O
?
-
Substrates: 2 microg, 90 min, reaction stopped by addition of 21 mM EDTA
Products: -
Products: -
?
aggrecan + H2O
?
-
Substrates: aggrecan cleavage by a disintegrin and metalloproteinase with a thrombospondin type 1 motif, member 5 (ADAMTS-5) is crucial for the breakdown of cartilage matrix during osteoarthritis, a degenerative joint disease that leads to the progressive destruction of articular structures
Products: -
Products: -
?
aggrecan + H2O
?
Substrates: ADAMTS-4 and ADAMTS-5 are the proteases responsible for the endogenous aggrecanase activity observed in IL-1beta stimulated bovine cartilage
Products: -
Products: -
?
aggrecan + H2O
?
Substrates: cleavage at the Glu373-Ala374 site of aggrecan is measured
Products: -
Products: -
?
aggrecan + H2O
?
-
Substrates: recombinant bovine aggrecan mutated at amino acids N-terminal or C-terminal to the interglobular domain cleavage site. Identification of multiple conserved amino acids within regions N- and C-terminal to the site of scission that may influence enzyme-substrate recognition, and may interact with exosites on ADAMTS-5. The S377Q mutant is extremely resistant to cleavage at Glu373-Ala374 by ADAMTS-5. Cleavage of S377T with ADAMTS-5 is also significantly inhibited compared to wild-type. The other P4'-mutant digests are similar to wild-type. Gln or Thr at the P4' position are inhibitory to ADAMTS-5 cleavage
Products: -
Products: -
?
aggrecan + H2O
?
-
Substrates: ADAMTS5 is the most active aggrecanase compared to ADAMTS4 and is responsible for the generation of an oncostatin M-specific degradation pattern in the CS-2 region. ADAMTS5 has the ability to cleave at the oncostatin M-specific site adjacent to the aggrecan G3 region (Glu373-Ala374 bond). Truncation of the C-terminal TS domain or Sp domain does not affect the ability of the enzyme to cleave at this site
Products: -
Products: -
?
aggrecan-interglobular domain + H2O
?
-
Substrates: cleavage site Glu373-Ala374 in aggrecaninterglobular domain
Products: -
Products: -
?
aggrecan-interglobular domain + H2O
?
-
Substrates: an aggrecan peptide with the N-terminal sequence ARGSVIL is released and quantified
Products: -
Products: -
?
brevican + H2O
?
-
Substrates: assay at 37°C, 3 h, 25 nM recombinant ADAMTS
Products: -
Products: -
?
Fibronectin + H2O
?
Substrates: multiple kidney proteins are affected by ADAMTS5. Specific proteolysis of complement C3 and fibronectin associated with IgA on immune complexes
Products: -
Products: -
?
o-aminobenzoyl-Thr-Glu-Ser-Glu-Ser-Arg-Gly-Ala-Ile-Tyr-(N-3-[2,4-dinitrophenyl]-L-2,3-diaminopropionyl)-Lys-Lys-NH2 + H2O
o-aminobenzoyl-Thr-Glu-Ser-Glu + Ser-Arg-Gly-Ala-Ile-Tyr-(N-3-[2,4-dinitrophenyl]-L-2,3-diaminopropionyl)-Lys-Lys-NH2
-
Substrates: recombinant ADAMTS-5 cleaves this substrate more readily than ADAMTS-4 in vitro
Products: -
Products: -
?
o-aminobenzoyl-Thr-Glu-Ser-Glu-Ser-Arg-Gly-Ala-Ile-Tyr-(N-3-[2,4-dinitrophenyl]-L-2,3-diaminopropionyl)-Lys-Lys-NH2 + H2O
o-aminobenzoyl-Thr-Glu-Ser-Glu + Ser-Arg-Gly-Ala-Ile-Tyr-(N-3-[2,4-dinitrophenyl]-L-2,3-diaminopropionyl)-Lys-Lys-NH2
Substrates: -
Products: -
Products: -
?
proteins + H2O
peptides
Substrates: strict specificity for cleavage between glutamic acid and uncharged aliphatic amino acids in the core proteins of large aggregating proteoglycans
Products: -
Products: -
?
versican + H2O
?
Substrates: expression of Adamts5 during neuromuscular development and in smooth muscle cells coincides with the broadly distributed proteoglycan versican, an ADAMTS5 substrate
Products: -
Products: -
?
versican + H2O
?
-
Substrates: cleaves versican at Glu441-Ala442 within the glycosaminoglycan beta region of versican V1
Products: -
Products: -
?
additional information
?
-
Substrates: interaction with sulfated glucosaminglycan may be very important for the localization and activity of the enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: interaction with sulfated glucosaminglycan may be very important for the localization and activity of the enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: interaction with sulfated glucosaminglycan may be very important for the localization and activity of the enzymew
Products: -
Products: -
?
additional information
?
-
-
Substrates: deglycosylated aggrecan is a poor substrate
Products: -
Products: -
?
additional information
?
-
Substrates: recombinant protein substrate based on the IGD (interglobular domain) of aggrecan, gst-IGD-flag
Products: -
Products: -
?
additional information
?
-
-
Substrates: recombinant protein substrate based on the IGD (interglobular domain) of aggrecan, gst-IGD-flag
Products: -
Products: -
?
additional information
?
-
-
Substrates: ADAMTS-5 shows proteolytic activity by second TS domain and little by catalytic domain alone and exhibits 1000fold greater strength of proteolytic activities as compared to ADAMTS-4
Products: -
Products: -
?
additional information
?
-
Substrates: development of rapidly cleaved and highly selective ADAMTS-5 Förster resonance energy-transfer (FRET) peptide substrates through in silico docking and combinatorial chemistry
Products: -
Products: -
-
additional information
?
-
Substrates: autocatalytic conversion of ADAMTS-5. ADAMTS-5 does not generate appreciable levels of lumican fragment
Products: -
Products: -
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
aggrecan + H2O
2 aggrecan fragment
-
Substrates: cleavage site is Glu373-Ala374, reaction is relevant to cartilage degeneration in inflammatory joint diseases
Products: -
Products: -
?
inter-alpha-inhibitor heavy chain-2 + H2O
?
Substrates: the major cleavage site is in the C terminus of heavy chain HC2
Products: -
Products: -
?
aggrecan + H2O
?
Substrates: enzyme may play a role in cartilage breakdown
Products: -
Products: -
?
aggrecan + H2O
?
-
Substrates: enzyme may play a role in cartilage breakdown
Products: -
Products: -
?
aggrecan + H2O
?
-
Substrates: aggrecan cleavage by a disintegrin and metalloproteinase with a thrombospondin type 1 motif, member 5 (ADAMTS-5) is crucial for the breakdown of cartilage matrix during osteoarthritis, a degenerative joint disease that leads to the progressive destruction of articular structures
Products: -
Products: -
?
aggrecan + H2O
?
Substrates: ADAMTS-4 and ADAMTS-5 are the proteases responsible for the endogenous aggrecanase activity observed in IL-1beta stimulated bovine cartilage
Products: -
Products: -
?
versican + H2O
?
Substrates: expression of Adamts5 during neuromuscular development and in smooth muscle cells coincides with the broadly distributed proteoglycan versican, an ADAMTS5 substrate
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1R,2R,3S)-1-([[5-(4-chloro-1H-pyrazol-1-yl)thiophen-2-yl]sulfonyl]amino)-2,3-dimethylcyclopropanecarboxylate
-
-
(1R,2S)-1-([(4'-chlorobiphenyl-4-yl)sulfonyl][2-[4-(methoxycarbonyl)-1H-imidazol-1-yl]ethyl]amino)-2-phenylcyclopropanecarboxylate
-
-
(1R,2S)-1-([(4'-chlorobiphenyl-4-yl)sulfonyl][2-[4-(methoxycarbonyl)-1H-imidazol-1-yl]ethyl]amino)-2-phenylcyclopropanecarboxylic acid
-
(1R,2S)-1-([(4'-chlorobiphenyl-4-yl)sulfonyl][2-[5-(methoxycarbonyl)-1H-imidazol-1-yl]ethyl]amino)-2-phenylcyclopropanecarboxylic acid
-
(1R,2S)-1-([[4'-(acetylamino)biphenyl-4-yl]sulfonyl][2-(2-oxopyrrolidin-1-yl)ethyl]amino)-2-phenylcyclopropanecarboxylic acid
-
(1R,2S)-1-([[4'-(dimethylamino)biphenyl-4-yl]sulfonyl][2-(2-oxopyrrolidin-1-yl)ethyl]amino)-2-phenylcyclopropanecarboxylic acid
-
(1R,2S)-1-([[4-(4-chlorophenyl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl][2-(2-oxopyrrolidin-1-yl)ethyl]amino)-2-phenylcyclopropanecarboxylic acid
-
(1R,2S)-1-([[6-(4-chlorophenyl)pyridin-3-yl]sulfonyl][2-(2-oxopyrrolidin-1-yl)ethyl]amino)-2-phenylcyclopropanecarboxylic acid
-
(1R,2S)-1-[[(4'-chlorobiphenyl-4-yl)sulfonyl](2-pyridin-2-ylethyl)amino]-2-phenylcyclopropanecarboxylic acid
-
(1R,2S)-1-[[(4'-chlorobiphenyl-4-yl)sulfonyl](2-pyridin-3-ylethyl)amino]-2-phenylcyclopropanecarboxylate
-
(1R,2S)-1-[[(4'-chlorobiphenyl-4-yl)sulfonyl](2-pyridin-4-ylethyl)amino]-2-phenylcyclopropanecarboxylic acid
-
(1R,2S)-1-[[(4'-chlorobiphenyl-4-yl)sulfonyl]amino]-2-phenylcyclopropanecarboxylate
-
-
(1R,2S)-1-[[(4'-chlorobiphenyl-4-yl)sulfonyl][2-(1H-1,2,3-triazol-1-yl)ethyl]amino]-2-phenylcyclopropanecarboxylate
-
(1R,2S)-1-[[(4'-chlorobiphenyl-4-yl)sulfonyl][2-(1H-1,2,4-triazol-1-yl)ethyl]amino]-2-phenylcyclopropanecarboxylic acid
-
(1R,2S)-1-[[(4'-chlorobiphenyl-4-yl)sulfonyl][2-(1H-imidazol-1-yl)ethyl]amino]-2-phenylcyclopropanecarboxylic acid
-
(1R,2S)-1-[[(4'-chlorobiphenyl-4-yl)sulfonyl][2-(1H-tetrazol-1-yl)ethyl]amino]-2-phenylcyclopropanecarboxylic acid
-
(1R,2S)-1-[[(4'-chlorobiphenyl-4-yl)sulfonyl][2-(2,5-dioxopyrrolidin-1-yl)ethyl]amino]-2-phenylcyclopropanecarboxylic acid
-
(1R,2S)-1-[[(4'-chlorobiphenyl-4-yl)sulfonyl][2-(2-oxo-1,3-oxazinan-3-yl)ethyl]amino]-2-phenylcyclopropanecarboxylate
-
(1R,2S)-1-[[(4'-chlorobiphenyl-4-yl)sulfonyl][2-(2-oxo-1,3-oxazolidin-3-yl)ethyl]amino]-2-phenylcyclopropanecarboxylic acid
-
(1R,2S)-1-[[(4'-chlorobiphenyl-4-yl)sulfonyl][2-(2-oxopiperidin-1-yl)ethyl]amino]-2-phenylcyclopropanecarboxylic acid
-
(1R,2S)-1-[[(4'-chlorobiphenyl-4-yl)sulfonyl][2-(2-oxopyrrolidin-1-yl)ethyl]amino]-2-phenylcyclopropanecarboxylic acid
-
(1R,2S)-1-[[(4'-chlorobiphenyl-4-yl)sulfonyl][2-(2H-1,2,3-triazol-2-yl)ethyl]amino]-2-phenylcyclopropanecarboxylate
-
(1R,2S)-1-[[(4'-chlorobiphenyl-4-yl)sulfonyl][2-(3-methoxy-2-oxopyridin-1(2H)-yl)ethyl]amino]-2-phenylcyclopropanecarboxylate
-
(1R,2S)-1-[[(4'-chlorobiphenyl-4-yl)sulfonyl][2-(4H-1,2,4-triazol-4-yl)ethyl]amino]-2-phenylcyclopropanecarboxylic acid
-
(1R,2S)-1-[[(4'-chlorobiphenyl-4-yl)sulfonyl][2-(7H-purin-7-yl)ethyl]amino]-2-phenylcyclopropanecarboxylic acid
-
(1R,2S)-1-[[(4'-chlorobiphenyl-4-yl)sulfonyl][2-(9H-purin-9-yl)ethyl]amino]-2-phenylcyclopropanecarboxylic acid
-
(1S)-1-([[5-(4-chloro-1H-pyrazol-1-yl)thiophen-2-yl]sulfonyl]amino)-2,2-dimethylcyclopropanecarboxylate
-
0.001 mM, 19.6% inhibition
(1S,2R)-1-([(4'-chlorobiphenyl-4-yl)sulfonyl][2-[4-(methoxycarbonyl)-1H-imidazol-1-yl]ethyl]amino)-2-phenylcyclopropanecarboxylate
-
0.0003 mM, 18% inhibition
(1S,2R)-1-([[5-(2-chlorophenyl)thiophen-2-yl]sulfonyl]amino)-2-phenylcyclopropanecarboxylate
-
0.001 mM, 48% inhibition
(1S,2R)-1-([[5-(3-chlorophenyl)thiophen-2-yl]sulfonyl]amino)-2-phenylcyclopropanecarboxylate
-
-
(1S,2R)-1-([[5-(4-chloro-1H-pyrazol-1-yl)thiophen-2-yl]sulfonyl]amino)-2-(propan-2-yl)cyclopropanecarboxylate
-
-
(1S,2R)-1-([[5-(4-chloro-1H-pyrazol-1-yl)thiophen-2-yl]sulfonyl]amino)-2-cyclohexylcyclopropanecarboxylate
-
-
(1S,2R)-1-([[5-(4-chloro-1H-pyrazol-1-yl)thiophen-2-yl]sulfonyl]amino)-2-methyl-2-phenylcyclopropanecarboxylate
-
-
(1S,2R)-1-([[5-(4-chloro-1H-pyrazol-1-yl)thiophen-2-yl]sulfonyl]amino)-2-phenylcyclopropanecarboxylate
-
-
(1S,2R)-1-([[5-(4-chlorophenyl)thiophen-2-yl]sulfonyl]amino)-2-methyl-2-phenylcyclopropanecarboxylate
-
-
(1S,2R)-1-([[5-(4-chlorophenyl)thiophen-2-yl]sulfonyl]amino)-2-phenylcyclopropanecarboxylate
-
-
(1S,2R)-1-([[5-(5-chloropyridin-2-yl)thiophen-2-yl]sulfonyl]amino)-2-phenylcyclopropanecarboxylate
-
-
(1S,2R)-1-[[(4'-chlorobiphenyl-4-yl)sulfonyl]amino]-2-phenylcyclopropanecarboxylate
-
-
(1S,2R,3R)-1-([[5-(4-chloro-1H-pyrazol-1-yl)thiophen-2-yl]sulfonyl]amino)-2-methyl-3-phenylcyclopropanecarboxylate
-
-
(1S,2R,3R)-1-([[5-(4-chlorophenyl)thiophen-2-yl]sulfonyl]amino)-2-methyl-3-phenylcyclopropanecarboxylate
-
-
(1S,2S)-1-([[5-(4-chloro-1H-pyrazol-1-yl)thiophen-2-yl]sulfonyl]amino)-2-methylcyclopropanecarboxylate
-
0.001 mM, 3.5% inhibition
(1S,2S)-2-benzyl-1-([[5-(4-chloro-1H-pyrazol-1-yl)thiophen-2-yl]sulfonyl]amino)cyclopropanecarboxylate
-
0.001 mM, 25% inhibition
(1S,2S,3R)-1-([[5-(4-chlorophenyl)thiophen-2-yl]sulfonyl]amino)-2-methyl-3-phenylcyclopropanecarboxylate
-
-
(2R)-2-[4-(1,3-benzodioxol-5-yl)benzyl]-N4-hydroxy-N1-[(1S,2R)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]butanediamide
nanomolar inhibitor of both ADAMTS-5
(2R)-N4-hydroxy-2-(3-hydroxybenzyl)-N1-[(1S,2R)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]butanediamide
(2R,5R)-1-([4-[(2,4-dichlorobenzyl)oxy]phenyl]sulfonyl)-N,5-dihydroxy-3,3-dimethylpiperidine-2-carboxamide
-
-
(2S,3R)-2-[(cyclopropylmethyl)amino]-N1-hydroxy-N4-[(1S,2R)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]-3-methylbutanediamide
the reduced pattern of H-bond interactions is suitable for the flexible environment of ADAMTS4 and ADAMTS5 since it enables the inhibitor to re-optimize its interaction pattern step-by-step, following the loop motion. The conformational flexibility observed for the S1' loop of ADAMTS4 and ADAMTS5 seems to be correlated to the motion of the TS-domain
(3R)-N2-(cyclopropylmethyl)-N1-hydroxy-3-(3-hydroxybenzyl)-N4-[(1S,2R)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]-L-aspartamide
-
(5E)-2-thioxo-5-([3-[3-(trifluoromethyl)phenoxy]phenyl]methylidene)-1,3-thiazolidin-4-one
-
-
(5E)-3-benzyl-5-[[3,4-bis(benzyloxy)phenyl]methylidene]-2-thioxo-1,3-thiazolidin-4-one
-
-
(5E)-5-([3-methoxy-4-[(4-methoxybenzyl)oxy]phenyl]methylidene)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5E)-5-([4-[(4-chlorobenzyl)oxy]-3-methoxyphenyl]methylidene)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5E)-5-[[3,4-bis(benzyloxy)phenyl]methylidene]-2-thioxo-1,3-thiazolidin-4-one
-
-
(5E)-5-[[3,4-bis(benzyloxy)phenyl]methylidene]-3-(2-phenylethyl)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5E)-5-[[3,4-bis(benzyloxy)phenyl]methylidene]-3-ethyl-2-thioxo-1,3-thiazolidin-4-one
-
-
(5E)-5-[[3,4-bis(benzyloxy)phenyl]methylidene]-3-methyl-2-thioxo-1,3-thiazolidin-4-one
-
-
(5E)-5-[[3,4-bis(benzyloxy)phenyl]methylidene]-3-phenyl-2-thioxo-1,3-thiazolidin-4-one
-
-
(5E)-5-[[3,5-bis(benzyloxy)phenyl]methylidene]-2-thioxo-1,3-thiazolidin-4-one
-
-
(5E)-5-[[3-(3,4-dichlorophenoxy)phenyl]methylidene]-2-thioxo-1,3-thiazolidin-4-one
-
-
(5E)-5-[[3-(3,5-dichlorophenoxy)phenyl]methylidene]-2-thioxo-1,3-thiazolidin-4-one
-
-
(5E)-5-[[3-(4-chlorophenoxy)phenyl]methylidene]-2-thioxo-1,3-thiazolidin-4-one
-
-
(5E)-5-[[3-(4-methoxyphenoxy)phenyl]methylidene]-2-thioxo-1,3-thiazolidin-4-one
-
-
(5E)-5-[[3-(4-methylphenoxy)phenyl]methylidene]-2-thioxo-1,3-thiazolidin-4-one
-
-
(5E)-5-[[3-(4-tert-butylphenoxy)phenyl]methylidene]-2-thioxo-1,3-thiazolidin-4-one
-
-
(5E)-5-[[4-(benzyloxy)-3-methoxyphenyl]methylidene]-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-[[3-(3,4-dichlorophenoxy)phenyl]methylidene]-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-[[3-(3,5-dichlorophenoxy)phenyl]methylidene]-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-[[3-(3,5-dichlorophenoxy)phenyl]methylidene]-2-thioxoimidazolidin-4-one
-
-
(5Z)-5-[[3-(4-chlorophenoxy)phenyl]methylidene]-1-methyl-2-thioxoimidazolidin-4-one
-
-
(5Z)-5-[[3-(4-tert-butylphenoxy)phenyl]methylidene]-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-[[3-(4-tert-butylphenoxy)phenyl]methylidene]-2-thioxoimidazolidin-4-one
-
-
(E)-2-((1H-benzo[d]imidazol-2-yl)methylene)-5-propylthiazolidin-4-one
potent small-molecule ADAMTS-5 inhibitor with good permeability
(R)-2-(4'-((4-(4-fluorobenzoyl)phenoxy)methyl)biphenyl-4-ylsulfonamido)-3-methylbutanoic acid
-
-
(R)-2-(4'-((4-(cyclohexanecarbonyl)phenoxy)methyl)biphenyl-4-ylsulfonamido)-3-methylbutanoic acid
-
-
(R)-2-(4'-((4-isobutyrylphenoxy)methyl)biphenyl-4-ylsulfonamido)-3-methylbutanoic acid
-
-
(R)-3-methyl-2-(4'-((5-oxo-5,6,7,8-tetrahydronaphthalen-2-yloxy)methyl)biphenyl-4-ylsulfonamido)butanoic acid
-
-
(S)-2-dimethylamino-N-hydroxy-3,3-dimethyl-4-[(4-phenoxyphenyl)-sulfonyl]-butanamide
-
SC81956, potent inhibitor of ADAMTS-5
1-benzyl-4-((4-(4-chlorophenoxy) phenyl)-sulfonyl)-N-hydroxypiperidine-4-carboxamide
multi-MMP inhibitor
2-(4-acetylphenoxy)-N-[(5-chloro-8-hydroxyquinolin-7-yl)(3-nitrophenyl)methyl]acetamide
-
2-(benzyloxy)-N-[(5-chloro-8-hydroxyquinolin-7-yl)(3-fluorophenyl)methyl]acetamide
-
2-(benzyloxy)-N-[(5-chloro-8-hydroxyquinolin-7-yl)(4-methylphenyl)methyl]acetamide
-
2-[(5E)-5-[[3,4-bis(benzyloxy)phenyl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]-3-methylbutanoic acid
-
-
2-[(5E)-5-[[3,4-bis(benzyloxy)phenyl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
-
-
2-[(5Z)-5-[[3-(3,4-dichlorophenoxy)phenyl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]-3-methylbutanoic acid
-
-
2-[(5Z)-5-[[3-(3,4-dichlorophenoxy)phenyl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
-
-
2-[4-(acetylamino)phenoxy]-N-[(5-chloro-8-hydroxyquinolin-7-yl)(2-chlorophenyl)methyl]acetamide
-
2-[4-(acetylamino)phenoxy]-N-[(5-chloro-8-hydroxyquinolin-7-yl)(3-fluorophenyl)methyl]acetamide
-
2-[4-(acetylamino)phenoxy]-N-[(5-chloro-8-hydroxyquinolin-7-yl)(4-methoxyphenyl)methyl]acetamide
-
2-[4-(benzyloxy)phenyl]-2,3-dihydro-1-oxo-1H-pyrrolo[3,4-c]quinoline-4-carboxylate
-
the inhibitor is unable to discriminate between ADAMTS-5 and ADAMTS-4
2-[4-(benzyloxy)phenyl]-2,3-dihydro-N-hydroxy-1-oxo-1Hpyrrolo[3,4-c]quinoline-4-carboxamide
-
-
2-[4-(benzyloxy)phenyl]-3-oxoisoindoline-4-carboxylic acid
-
does not inhibit ADAMTS-4
2-[4-(benzyloxy)phenyl]-N-hydroxy-3-oxoisoindoline-4-carboxamide
-
does not inhibit ADAMTS-4
3-[(5E)-5-[[3,4-bis(benzyloxy)phenyl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-
-
3-[2-[(Z)-(4-oxo-1,3-thiazolidin-2-ylidene)methyl]-4-(pyridin-2-yl)-1,3-thiazol-5-yl]propanoic acid
inhibits the spontaneous aggrecan degradation in IL-1-stimulated bovine cartilage, shows good selectivity over other metalloproteases; inhibits the spontaneous aggrecan degradation in IL-1-stimulated bovine cartilage, shows good selectivity over other metalloproteases
4-[(4-oxo-2-thioxo-1,3-thiazolidin-5-yl)methyl]-3-phenyl-5-(2-pyrimidin-1(6H)-ylpiperazin-1-yl)-1H-pyrazole-1-carbonitrile
-
-
4-[(4-oxo-2-thioxo-1,3-thiazolidin-5-yl)methyl]-5-(2-pyrimidin-1(6H)-ylpiperazin-1-yl)-3-(trifluoromethyl)-1H-pyrazole-1-carbonitrile
-
-
5-([1,3-diphenyl-5-[(thiophen-2-ylmethyl)sulfanyl]-1H-pyrazol-4-yl]methyl)-2-thioxo-1,3-thiazolidin-4-one
-
-
5-([1-methyl-5-[(2H-thiopyran-2-ylmethyl)sulfanyl]-3-(2,2,2-trifluoroethyl)-1H-pyrazol-4-yl]methyl)-2-thioxo-1,3-thiazolidin-4-one
-
40% inhibition at 0.02 mM
5-([1-methyl-5-[(4-methylphenyl)sulfanyl]-3-phenyl-1H-pyrazol-4-yl]methyl)-2-thioxo-1,3-thiazolidin-4-one
-
-
5-([1-phenyl-5-[2-(tetrahydrothiophen-2-yl)ethoxy]-3-(trifluoromethyl)-1H-pyrazol-4-yl]methyl)-2-thioxo-1,3-thiazolidin-4-one
-
-
5-([5-[(2-chlorobenzyl)sulfanyl]-1-methyl-3-(2,2,2-trifluoroethyl)-1H-pyrazol-4-yl]methyl)-2-thioxo-1,3-thiazolidin-4-one
-
-
5-([5-[(4-chlorobenzyl)sulfanyl]-1-methyl-3-(2,2,2-trifluoroethyl)-1H-pyrazol-4-yl]methyl)-2-thioxo-1,3-thiazolidin-4-one
-
-
5-([5-[(4-chlorobenzyl)sulfanyl]-1-phenyl-3-(2,2,2-trifluoroethyl)-1H-pyrazol-4-yl]methyl)-2-thioxo-1,3-thiazolidin-4-one
-
-
5-([5-[(4-chlorophenyl)sulfanyl]-1-methyl-3-(2,2,2-trifluoroethyl)-1H-pyrazol-4-yl]methyl)-2-thioxo-1,3-thiazolidin-4-one
-
47% inhibition at 0.02 mM
5-([5-[(4-methoxybenzyl)sulfanyl]-1-methyl-3-(2,2,2-trifluoroethyl)-1H-pyrazol-4-yl]methyl)-2-thioxo-1,3-thiazolidin-4-one
-
53% inhibition at 0.02 mM
5-([5-[(4-tert-butylbenzyl)sulfanyl]-1-methyl-3-(2,2,2-trifluoroethyl)-1H-pyrazol-4-yl]methyl)-2-thioxo-1,3-thiazolidin-4-one
-
-
5-([5-[(furan-2-ylmethyl)sulfanyl]-1,3-diphenyl-1H-pyrazol-4-yl]methyl)-2-thioxo-1,3-thiazolidin-4-one
-
-
5-([5-[(furan-2-ylmethyl)sulfanyl]-1-methyl-3-phenyl-1H-pyrazol-4-yl]methyl)-2-thioxo-1,3-thiazolidin-4-one
-
-
5-([5-[(furan-2-ylmethyl)sulfanyl]-1-phenyl-3-(trifluoromethyl)-1H-pyrazol-4-yl]methyl)-2-thioxo-1,3-thiazolidin-4-one
-
42% inhibition at 0.02 mM
5-([5-[2-(4-chlorophenyl)ethoxy]-1-phenyl-3-(trifluoromethyl)-1H-pyrazol-4-yl]methyl)-2-thioxo-1,3-thiazolidin-4-one
-
-
5-([5-[2-(4-fluorophenyl)ethoxy]-1-phenyl-3-(trifluoromethyl)-1H-pyrazol-4-yl]methyl)-2-thioxo-1,3-thiazolidin-4-one
-
-
5-([5-[2-(4-methoxyphenyl)ethoxy]-1-phenyl-3-(trifluoromethyl)-1H-pyrazol-4-yl]methyl)-2-thioxo-1,3-thiazolidin-4-one
-
31% inhibition at 0.02 mM
5-([5-[4-(4-chlorophenyl)piperazin-1-yl]-1-methyl-3-(2,2,2-trifluoroethyl)-1H-pyrazol-4-yl]methyl)-2-thioxo-1,3-thiazolidin-4-one
-
-
5-([5-[4-(4-chlorophenyl)piperazin-1-yl]-1-phenyl-3-(2,2,2-trifluoroethyl)-1H-pyrazol-4-yl]methyl)-2-thioxo-1,3-thiazolidin-4-one
-
-
5-[(4-chlorobenzyl)sulfanyl]-4-[(4-oxo-2-thioxo-1,3-thiazolidin-5-yl)methyl]-3-(2,2,2-trifluoroethyl)-1H-pyrazole-1-carbonitrile
-
-
5-[(furan-2-ylmethyl)sulfanyl]-4-[(4-oxo-2-thioxo-1,3-thiazolidin-5-yl)methyl]-3-phenyl-1H-pyrazole-1-carbonitrile
-
-
5-[[1-methyl-5-(phenylsulfanyl)-3-(2,2,2-trifluoroethyl)-1H-pyrazol-4-yl]methylen]-2-thioxo-1,3-thiazolidin-4-one
-
28% inhibition at 0.02 mM
5-[[5-(4-methylpiperazin-1-yl)-1,3-diphenyl-1H-pyrazol-4-yl]methyl]-2-thioxo-1,3-thiazolidin-4-one
-
-
5-[[5-(4-methylpiperazin-1-yl)-1-phenyl-3-(trifluoromethyl)-1H-pyrazol-4-yl]methyl]-2-thioxo-1,3-thiazolidin-4-one
-
45% inhibition at 0.02 mM
5-[[5-(benzylsulfanyl)-1-methyl-3-(2,2,2-trifluoroethyl)-1H-pyrazol-4-yl]methyl]-2-thioxo-1,3-thiazolidin-4-one
-
44% inhibition at 0.02 mM
5-[[5-(benzylsulfanyl)-1-phenyl-3-(trifluoromethyl)-1H-pyrazol-4-yl]methyl]-2-thioxo-1,3-thiazolidin-4-one
-
-
aggrecanase inhibitor BB-16
-
prevents aggrecan degradation in osteoarthritic cartilage
BB-16
-
(2S,5R,6S)-3-Aza-4-oxo-10-oxa-5-hexyl-2-(methylcarboxamido)-10-paracyclophane-6-N-hydroxycarboxamide
calcium pentosan polysulfate
chemically sulfated xylopyranose from beechwood. Multifaceted exosite inhibitor, protects cartilage against aggrecan degradation. Inhibitor interacts with the noncatalytic spacer domain of isoform ADAMTS-4 and the cysteine-rich domain of ADAMTS-5, blocking activity against their natural substrate aggrecan with inhibitory concentration 50 values of 10-40 nM but only weakly inhibiting hydrolysis of a nonglycosylated recombinant protein substrate. calcium pentosan polysulfate increases cartilage levels of tissue inhibitor of metalloproteinases TIMP-3, an endogenous inhibitor of ADAMTS-4 and -5
-
catechin gallate esters
from green tea Camellia sinensis, strong inhibition, independent of Zn2+, reversible
-
N-benzyl-N-[(4'-chlorobiphenyl-4-yl)sulfonyl]-D-phenylalanine
30% inhibition at 0.01 mM
N-hydroxy-4-(4-(4-(trifluoromethyl)-phenoxy)phenylsulfonyl)-tetrahydro-2H-pyran-4-carboxamide
nanomolar inhibitor of both ADAMTS-5
N-hydroxy-4-([4-[4-(trifluoromethyl)phenoxy]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
-
-
N-terminal domain of tissue inhibitor of metalloproteinases-3
-
all isoforms of ADAMTS-5 are effectively inhibited. Inhibited more strongly by N-terminal domain of tissue inhibitor of metalloproteinases-3 than by full-length tissue inhibitor of metalloproteinases-3
-
N-terminal inhibitory domain of tissue inhibitor of metalloproteinases 3
N-terminal mutants of N-TIMP-3 (tissue inhibitor of metalloproteinases 3) that have lost their matrix metalloproteinaseP-inhibitory activities (N-TIMP-3(T2G) and [-1A]N-TIMP-3), retain their ability to inhibit ADAMTS-4 and ADAMTS-5. The [-2A]N-TIMP-3 mutant also retains strong affinity with ADAMTS-5, but has a lower affinity for ADAMTS-4 and ADAM17
-
N-[(1R)-1-(dihydroxymethyl)-2-methylpropyl]-4'-{[4-(2-methylpropanoyl)phenoxy]methyl}biphenyl-4-sulfonamide
-
-
N-[(2-chlorophenyl)(8-hydroxy-5-methylquinolin-7-yl)methyl]-2-phenoxyacetamide
-
N-[(2-chlorophenyl)(8-hydroxy-5-nitroquinolin-7-yl)methyl]-2-phenoxyacetamide
-
N-[(4'-chlorobiphenyl-4-yl)sulfonyl]-N-(cyclohexylmethyl)-D-phenylalanine
22% inhibition at 0.01 mM
N-[(4'-chlorobiphenyl-4-yl)sulfonyl]-N-(cyclopropylmethyl)-D-phenylalanine
46% inhibition at 0.01 mM
N-[(5-bromo-8-hydroxyquinolin-7-yl)(2-chlorophenyl)methyl]-2-phenoxyacetamide
-
N-[(5-bromo-8-hydroxyquinolin-7-yl)(3-nitrophenyl)methyl]-2-phenoxyacetamide
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)(2-chlorophenyl)methyl]-2-phenoxyacetamide
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)(2-chlorophenyl)methyl]-2-[3-(dimethylamino)phenoxy]acetamide
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)(2-chlorophenyl)methyl]-N2-(4-chloro-3-methylphenyl)glycinamide
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)(2-chlorophenyl)methyl]-N2-methyl-N2-phenylglycinamide
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)(2-cyanophenyl)methyl]-2-phenoxyacetamide
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)(2-fluorophenyl)methyl]-2-phenoxyacetamide
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)(2-methylphenyl)methyl]-2-phenoxyacetamide
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)(2-nitrophenyl)methyl]-2-phenoxyacetamide
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)(3-fluorophenyl)methyl]-2-phenoxyacetamide
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)(3-fluorophenyl)methyl]-2-[3-(dimethylamino)phenoxy]acetamide
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)(3-fluorophenyl)methyl]-N2-(4-chloro-3-methylphenyl)glycinamide
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)(3-fluorophenyl)methyl]-N2-methyl-N2-phenylglycinamide
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)(3-nitrophenyl)methyl]-2-(pyridin-3-yloxy)acetamide
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)(3-nitrophenyl)methyl]-2-phenoxyacetamide
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)(3-nitrophenyl)methyl]-N2-(4-chloro-3-methylphenyl)glycinamide
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)(3-nitrophenyl)methyl]-N2-methyl-N2-phenylglycinamide
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)(4-chlorophenyl)methyl]-2-phenoxyacetamide
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)(4-methoxyphenyl)methyl]-2-(4-methoxyphenoxy)acetamide
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)(4-methoxyphenyl)methyl]-2-(4-methylphenoxy)acetamide
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)(4-methoxyphenyl)methyl]-2-(pyridin-3-yloxy)acetamide
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)(4-methoxyphenyl)methyl]-2-phenoxyacetamide
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)(4-methoxyphenyl)methyl]-2-[3-(dimethylamino)phenoxy]acetamide
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)(4-methylphenyl)methyl]-2-phenoxyacetamide
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)(4-methylphenyl)methyl]-N2-(4-chloro-3-methylphenyl)glycinamide
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)(4-methylphenyl)methyl]-N2-(4-cyanophenyl)glycinamide
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)(4-methylphenyl)methyl]-N2-methyl-N2-phenylglycinamide
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)(4-methylphenyl)methyl]-N2-[3-(dimethylamino)phenyl]glycinamide
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)(4-nitrophenyl)methyl]-2-phenoxyacetamide
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)(phenyl)methyl]-2-(4-chlorophenoxy)acetamide
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)(phenyl)methyl]-2-(4-methylphenoxy)acetamide
-
N-[(5-chloro-8-hydroxyquinolin-7-yl)[2-(trifluoromethyl)phenyl]methyl]-2-phenoxyacetamide
-
N-[(8-hydroxy-5-methylquinolin-7-yl)(3-nitrophenyl)methyl]-2-phenoxyacetamide
-
N-[[(4S)-4-(1-methylimidazol-2-yl)-2,5-dioxo-imidazolidin-4-yl]methyl]-5-(trifluoromethyl)benzofuran-2-carboxamide
-
inhibitor has excellent selectivity over other zinc metalloproteases such as TACE, MMP2, MMP3, MMP13, and MMP14
N2-(4-acetylphenyl)-N-[(5-chloro-8-hydroxyquinolin-7-yl)(3-nitrophenyl)methyl]glycinamide
-
N2-(4-acetylphenyl)-N-[(5-chloro-8-hydroxyquinolin-7-yl)(4-methylphenyl)methyl]glycinamide
-
N2-benzyl-N-[(5-chloro-8-hydroxyquinolin-7-yl)(2-chlorophenyl)methyl]-N2-methylglycinamide
-
N2-benzyl-N-[(5-chloro-8-hydroxyquinolin-7-yl)(2-chlorophenyl)methyl]glycinamide
-
N2-benzyl-N-[(5-chloro-8-hydroxyquinolin-7-yl)(3-fluorophenyl)methyl]-N2-methylglycinamide
-
N2-benzyl-N-[(5-chloro-8-hydroxyquinolin-7-yl)(3-fluorophenyl)methyl]glycinamide
-
N2-benzyl-N-[(5-chloro-8-hydroxyquinolin-7-yl)(3-nitrophenyl)methyl]-N2-methylglycinamide
-
N2-benzyl-N-[(5-chloro-8-hydroxyquinolin-7-yl)(4-methylphenyl)methyl]-N2-methylglycinamide
-
N2-benzyl-N-[(5-chloro-8-hydroxyquinolin-7-yl)(4-methylphenyl)methyl]glycinamide
-
N2-[4-(acetylamino)phenyl]-N-[(5-chloro-8-hydroxyquinolin-7-yl)(3-nitrophenyl)methyl]glycinamide
-
[(5E)-5-[[3,4-bis(benzyloxy)phenyl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl](phenyl)acetic acid
-
-
[(5E)-5-[[3,4-bis(benzyloxy)phenyl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-
-
[(5Z)-5-[[3-(3,4-dichlorophenoxy)phenyl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl](phenyl)acetic acid
-
-
[(5Z)-5-[[3-(3,4-dichlorophenoxy)phenyl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-
-
(2R)-N4-hydroxy-2-(3-hydroxybenzyl)-N1-[(1S,2R)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]butanediamide
-
(2R)-N4-hydroxy-2-(3-hydroxybenzyl)-N1-[(1S,2R)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]butanediamide
the reduced pattern of H-bond interactions is suitable for the flexible environment of ADAMTS4 and ADAMTS5 since it enables the inhibitor to re-optimize its interaction pattern step-by-step, following the loop motion. The conformational flexibility observed for the S1' loop of ADAMTS4 and ADAMTS5 seems to be correlated to the motion of the TS-domain
alpha2-Macroglobulin
-
after 10 min 100% and 68% inhibition at concentrations of 2.5 and 7.5 nM, respectively, similar results when using 25 and 75 nM
-
TIMP-3
-
recombinant human inhibitor protein from Escherichia coli, i.e. tissue inhibitor of metalloproteinases, strong inhibitor with regulatory function
-
tissue inhibitor of metalloproteinases-3
-
all isoforms of ADAMTS-5 are effectively inhibited. Inhibited more strongly by N-terminal domain of tissue inhibitor of metalloproteinases-3 than by full-length tissue inhibitor of metalloproteinases-3
-
additional information
-
no inhibition by matrix metalloprotease inhibitor XS309
-
additional information
-
[3S-[3R*,2-[2R*,2-(R*,S*)]-hexahydro-2-(2-[2-(hydroxyamino)-1-methyl-2-oxyethyl])-4-methyl-1-oxypentyl]-N-methyl]-3-pyridazinecarboxamide, i.e.XS309 is inactive at less than 0.01 mM in blocking ADAMTS-5
-
additional information
-
not inhibited by N-TIMP-1 or TIMP-2; the general proteolytic activitiy of ADAMTS-5 as measured with carboxymethylated transferrin is unaffected by concentrations up to 1 M NaCl
-
additional information
-
substrate specificity of ADAMTS-5 against recombinant aggrecan, aggrecan mutants S377Q and S377T lead to aggrecan cleavage inhibition
-
additional information
design and development for potent and selective inhibitors of ADAMTS-4 and ADAMTS-5
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
interleukin-1beta
-
increased transcription in the presence of interleukin-1beta
-
tissue necrosis factor alpha
-
increased transcription in the presence of tissue necrosis factor alpha
-
interleukin-1alpha
-
increased transcription in the presence of interleukin-1alpha
-
interleukin-1alpha
-
increased transcription in the presence of interleukin-1alpha
-
interleukin-1alpha
-
increased transcription in the presence of interleukin-1alpha
-
additional information
-
ADAMTS5 expression is not stimulated by interleukin-1, tumor necrosis factor alpha, oncostatin M or transforming growth factor beta
-
additional information
-
higher enzyme expression in degenerated intervertebral discs
-
additional information
-
higher expression level in metastatic foci compared with corresponding primary tumor
-
additional information
-
syndecan-4 controls the activation of ADAMTS-5 through direct interaction with the protease and through regulating mitogen-activated protein kinase (MAPK)-dependent synthesis of matrix metalloproteinase-3 (MMP-3). Syndecan-4 is crucial in regulating Mmp-3 expression by activating ERK1/2 and by targeting ADAMTS-5 to the cell surface of chondrocytes
-
additional information
-
little effect from interleukin-1alpha and retinoate on aggrecanase activity
-
additional information
-
ADAMTS5 expression is not stimulated by interleukin-1, tumor necrosis factor alpha, oncostatin M or transforming growth factor beta
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1252
o-aminobenzoyl-TESESRGAIY-N-3-[2,4-dinitrophenyl]-L-2,3-diaminopropionyl-KK-NH2
37°C, pH 7.5
-
0.076
o-aminobenzoyl-Thr-Glu-Ser-Glu-Ser-Arg-Gly-Ala-Ile-Tyr-(N-3-[2,4-dinitrophenyl]-L-2,3-diaminopropionyl)-Lys-Lys-NH2
pH 7.5, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.61
o-aminobenzoyl-TESESRGAIY-N-3-[2,4-dinitrophenyl]-L-2,3-diaminopropionyl-KK-NH2
37°C, pH 7.5
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
29.1
o-aminobenzoyl-TESESRGAIY-N-3-[2,4-dinitrophenyl]-L-2,3-diaminopropionyl-KK-NH2
37°C, pH 7.5
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000093
(2R)-N4-hydroxy-2-(3-hydroxybenzyl)-N1-[(1S,2R)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]butanediamide
or above, pH not specified in the publication, temperature not specified in the publication
0.000017
(2S,3R)-2-[(cyclopropylmethyl)amino]-N1-hydroxy-N4-[(1S,2R)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]-3-methylbutanediamide
or above, pH not specified in the publication, temperature not specified in the publication
0.000106
marimastat
pH not specified in the publication, temperature not specified in the publication
0.0012
(E)-4-[2-(3,5-dihydroxyphenyl)ethenyl]1,2-benzenediol
-
pH 7.5, 37°C, substrate: C6-(Gly-Pro-Hyp-Pro-Hyp-Gly)2-Gly-Pro-Hyp-Gly-Thr-Lys(7-methoxycoumarin-4-yl)-Gly-GluLeuGluGly-ArgGly-Thr-Lys(Dnp)-Gly-Ile-Ser-(Gly-Pro-Hyp-Pro-Hyp-Gly)2-Gly-Pro-Hyp-NH2
0.0111
(E)-4-[2-(3,5-dihydroxyphenyl)ethenyl]1,2-benzenediol
-
pH 7.5, 37°C, substrate: pH 7.5, 37°C, substrate: Lys(7-methoxycoumarin-4-yl)-Lys-Gln-Glu-Phe-Arg-Gly-Gln-Thr-Lys(Dnp)-NH2
0.00013
N-terminal domain of tissue inhibitor of metalloproteinases-3
-
pH 7.5, 37°C, isoenzyme ADAMTS5-1
-
0.00029
N-terminal domain of tissue inhibitor of metalloproteinases-3
-
pH 7.5, 37°C, isoenzyme ADAMTS5-3
-
0.00035
N-terminal domain of tissue inhibitor of metalloproteinases-3
-
pH 7.5, 37°C, isoenzyme ADAMTS5-2
-
0.0004
N-terminal domain of tissue inhibitor of metalloproteinases-3
-
pH 7.5, 37°C, isoenzyme ADAMTS5-4
-
0.00101
N-terminal domain of tissue inhibitor of metalloproteinases-3
-
pH 7.5, 37°C, isoenzyme ADAMTS5-5
-
0.00363
pyrogallol
-
pH 7.5, 37°C, substrate: C6-(Gly-Pro-Hyp-Pro-Hyp-Gly)2-Gly-Pro-Hyp-Gly-Thr-Lys(7-methoxycoumarin-4-yl)-Gly-GluLeuGluGly-ArgGly-Thr-Lys(Dnp)-Gly-Ile-Ser-(Gly-Pro-Hyp-Pro-Hyp-Gly)2-Gly-Pro-Hyp-NH2
0.037
pyrogallol
-
pH 7.5, 37°C, substrate: Lys(7-methoxycoumarin-4-yl)-Lys-Gln-Glu-Phe-Arg-Gly-Gln-Thr-Lys(Dnp)-NH2
0.00063
tissue inhibitor of metalloproteinases-3
-
pH 7.5, 37°C, isoenzyme ADAMTS5-1
-
0.00072
tissue inhibitor of metalloproteinases-3
-
pH 7.5, 37°C, isoenzyme ADAMTS5-2
-
0.001
tissue inhibitor of metalloproteinases-3
-
pH 7.5, 37°C, isoenzyme ADAMTS5-3
-
0.00113
tissue inhibitor of metalloproteinases-3
-
pH 7.5, 37°C, isoenzyme ADAMTS5-4
-
0.00117
tissue inhibitor of metalloproteinases-3
-
pH 7.5, 37°C, isoenzyme ADAMTS5-5
-
additional information
additional information
Ki(app) of N-terminal alanine-extension mutants and of position [-1] mutants of N-terminal inhibitory domain of tissue inhibitor of metalloproteinases 3
-
additional information
additional information
-
Ki(app) of N-terminal alanine-extension mutants and of position [-1] mutants of N-terminal inhibitory domain of tissue inhibitor of metalloproteinases 3
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0008
(1R,2R,3S)-1-([[5-(4-chloro-1H-pyrazol-1-yl)thiophen-2-yl]sulfonyl]amino)-2,3-dimethylcyclopropanecarboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.000073
(1R,2S)-1-([(4'-chlorobiphenyl-4-yl)sulfonyl][2-[4-(methoxycarbonyl)-1H-imidazol-1-yl]ethyl]amino)-2-phenylcyclopropanecarboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.00007
(1R,2S)-1-([(4'-chlorobiphenyl-4-yl)sulfonyl][2-[4-(methoxycarbonyl)-1H-imidazol-1-yl]ethyl]amino)-2-phenylcyclopropanecarboxylic acid
Homo sapiens
-
0.0002
(1R,2S)-1-([(4'-chlorobiphenyl-4-yl)sulfonyl][2-[5-(methoxycarbonyl)-1H-imidazol-1-yl]ethyl]amino)-2-phenylcyclopropanecarboxylic acid
Homo sapiens
-
0.0045
(1R,2S)-1-([[4'-(acetylamino)biphenyl-4-yl]sulfonyl][2-(2-oxopyrrolidin-1-yl)ethyl]amino)-2-phenylcyclopropanecarboxylic acid
Homo sapiens
-
0.0066
(1R,2S)-1-([[4'-(dimethylamino)biphenyl-4-yl]sulfonyl][2-(2-oxopyrrolidin-1-yl)ethyl]amino)-2-phenylcyclopropanecarboxylic acid
Homo sapiens
-
0.00088
(1R,2S)-1-([[4-(4-chlorophenyl)-3,6-dihydropyridin-1(2H)-yl]sulfonyl][2-(2-oxopyrrolidin-1-yl)ethyl]amino)-2-phenylcyclopropanecarboxylic acid
Homo sapiens
-
0.0011
(1R,2S)-1-([[6-(4-chlorophenyl)pyridin-3-yl]sulfonyl][2-(2-oxopyrrolidin-1-yl)ethyl]amino)-2-phenylcyclopropanecarboxylic acid
Homo sapiens
-
0.00082
(1R,2S)-1-[[(4'-chlorobiphenyl-4-yl)sulfonyl](2-pyridin-2-ylethyl)amino]-2-phenylcyclopropanecarboxylic acid
Homo sapiens
-
0.00029
(1R,2S)-1-[[(4'-chlorobiphenyl-4-yl)sulfonyl](2-pyridin-3-ylethyl)amino]-2-phenylcyclopropanecarboxylate
Homo sapiens
-
0.00075
(1R,2S)-1-[[(4'-chlorobiphenyl-4-yl)sulfonyl](2-pyridin-4-ylethyl)amino]-2-phenylcyclopropanecarboxylic acid
Homo sapiens
-
0.00027
(1R,2S)-1-[[(4'-chlorobiphenyl-4-yl)sulfonyl][2-(1H-1,2,3-triazol-1-yl)ethyl]amino]-2-phenylcyclopropanecarboxylate
Homo sapiens
-
0.00018
(1R,2S)-1-[[(4'-chlorobiphenyl-4-yl)sulfonyl][2-(1H-1,2,4-triazol-1-yl)ethyl]amino]-2-phenylcyclopropanecarboxylic acid
Homo sapiens
-
0.0002
(1R,2S)-1-[[(4'-chlorobiphenyl-4-yl)sulfonyl][2-(1H-imidazol-1-yl)ethyl]amino]-2-phenylcyclopropanecarboxylic acid
Homo sapiens
-
0.00027
(1R,2S)-1-[[(4'-chlorobiphenyl-4-yl)sulfonyl][2-(1H-tetrazol-1-yl)ethyl]amino]-2-phenylcyclopropanecarboxylic acid
Homo sapiens
-
0.0001
(1R,2S)-1-[[(4'-chlorobiphenyl-4-yl)sulfonyl][2-(2,5-dioxopyrrolidin-1-yl)ethyl]amino]-2-phenylcyclopropanecarboxylic acid
Homo sapiens
-
0.00018
(1R,2S)-1-[[(4'-chlorobiphenyl-4-yl)sulfonyl][2-(2-oxo-1,3-oxazinan-3-yl)ethyl]amino]-2-phenylcyclopropanecarboxylate
Homo sapiens
-
0.00022
(1R,2S)-1-[[(4'-chlorobiphenyl-4-yl)sulfonyl][2-(2-oxo-1,3-oxazolidin-3-yl)ethyl]amino]-2-phenylcyclopropanecarboxylic acid
Homo sapiens
-
0.00021
(1R,2S)-1-[[(4'-chlorobiphenyl-4-yl)sulfonyl][2-(2-oxopiperidin-1-yl)ethyl]amino]-2-phenylcyclopropanecarboxylic acid
Homo sapiens
-
0.0002
(1R,2S)-1-[[(4'-chlorobiphenyl-4-yl)sulfonyl][2-(2-oxopyrrolidin-1-yl)ethyl]amino]-2-phenylcyclopropanecarboxylic acid
Homo sapiens
-
0.00026
(1R,2S)-1-[[(4'-chlorobiphenyl-4-yl)sulfonyl][2-(2H-1,2,3-triazol-2-yl)ethyl]amino]-2-phenylcyclopropanecarboxylate
Homo sapiens
-
0.00078
(1R,2S)-1-[[(4'-chlorobiphenyl-4-yl)sulfonyl][2-(3-methoxy-2-oxopyridin-1(2H)-yl)ethyl]amino]-2-phenylcyclopropanecarboxylate
Homo sapiens
-
0.00019
(1R,2S)-1-[[(4'-chlorobiphenyl-4-yl)sulfonyl][2-(4H-1,2,4-triazol-4-yl)ethyl]amino]-2-phenylcyclopropanecarboxylic acid
Homo sapiens
-
0.000071
(1R,2S)-1-[[(4'-chlorobiphenyl-4-yl)sulfonyl][2-(7H-purin-7-yl)ethyl]amino]-2-phenylcyclopropanecarboxylic acid
Homo sapiens
-
0.00017
(1R,2S)-1-[[(4'-chlorobiphenyl-4-yl)sulfonyl][2-(9H-purin-9-yl)ethyl]amino]-2-phenylcyclopropanecarboxylic acid
Homo sapiens
-
0.00021
(1S,2R)-1-([(4'-chlorobiphenyl-4-yl)sulfonyl][2-[4-(methoxycarbonyl)-1H-imidazol-1-yl]ethyl]amino)-2-phenylcyclopropanecarboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.000094
(1S,2R)-1-([[5-(3-chlorophenyl)thiophen-2-yl]sulfonyl]amino)-2-phenylcyclopropanecarboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.00077
(1S,2R)-1-([[5-(4-chloro-1H-pyrazol-1-yl)thiophen-2-yl]sulfonyl]amino)-2-(propan-2-yl)cyclopropanecarboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.00036
(1S,2R)-1-([[5-(4-chloro-1H-pyrazol-1-yl)thiophen-2-yl]sulfonyl]amino)-2-cyclohexylcyclopropanecarboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.000032
(1S,2R)-1-([[5-(4-chloro-1H-pyrazol-1-yl)thiophen-2-yl]sulfonyl]amino)-2-methyl-2-phenylcyclopropanecarboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.00008
(1S,2R)-1-([[5-(4-chloro-1H-pyrazol-1-yl)thiophen-2-yl]sulfonyl]amino)-2-phenylcyclopropanecarboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.00001
(1S,2R)-1-([[5-(4-chlorophenyl)thiophen-2-yl]sulfonyl]amino)-2-methyl-2-phenylcyclopropanecarboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.00006
(1S,2R)-1-([[5-(4-chlorophenyl)thiophen-2-yl]sulfonyl]amino)-2-phenylcyclopropanecarboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.0001
(1S,2R)-1-([[5-(5-chloropyridin-2-yl)thiophen-2-yl]sulfonyl]amino)-2-phenylcyclopropanecarboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.000084
(1S,2R)-1-[[(4'-chlorobiphenyl-4-yl)sulfonyl]amino]-2-phenylcyclopropanecarboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.0000074
(1S,2R,3R)-1-([[5-(4-chloro-1H-pyrazol-1-yl)thiophen-2-yl]sulfonyl]amino)-2-methyl-3-phenylcyclopropanecarboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.000021
(1S,2R,3R)-1-([[5-(4-chlorophenyl)thiophen-2-yl]sulfonyl]amino)-2-methyl-3-phenylcyclopropanecarboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.00012
(1S,2S,3R)-1-([[5-(4-chlorophenyl)thiophen-2-yl]sulfonyl]amino)-2-methyl-3-phenylcyclopropanecarboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.000129
(2R)-2-[4-(1,3-benzodioxol-5-yl)benzyl]-N4-hydroxy-N1-[(1S,2R)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]butanediamide
Homo sapiens
pH and temperature not specified in the publication
0.000093
(2R)-N4-hydroxy-2-(3-hydroxybenzyl)-N1-[(1S,2R)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]butanediamide
Homo sapiens
pH 7.5, 37°C
0.0000014
(2R,5R)-1-([4-[(2,4-dichlorobenzyl)oxy]phenyl]sulfonyl)-N,5-dihydroxy-3,3-dimethylpiperidine-2-carboxamide
Homo sapiens
-
37°C, pH and temperature not specified in the publication
0.000017
(3R)-N2-(cyclopropylmethyl)-N1-hydroxy-3-(3-hydroxybenzyl)-N4-[(1S,2R)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]-L-aspartamide
Homo sapiens
pH 7.5, 37°C
0.0053
(5E)-2-thioxo-5-([3-[3-(trifluoromethyl)phenoxy]phenyl]methylidene)-1,3-thiazolidin-4-one
Homo sapiens
-
-
0.067
(5E)-3-benzyl-5-[[3,4-bis(benzyloxy)phenyl]methylidene]-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
IC50 above 0.067 mM
0.0116
(5E)-5-([3-methoxy-4-[(4-methoxybenzyl)oxy]phenyl]methylidene)-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
-
0.0035
(5E)-5-([4-[(4-chlorobenzyl)oxy]-3-methoxyphenyl]methylidene)-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
-
0.022
(5E)-5-[(3-phenoxyphenyl)methylidene]-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
IC50 above 0.022 mM
0.0018
(5E)-5-[[3,4-bis(benzyloxy)phenyl]methylidene]-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
-
0.067
(5E)-5-[[3,4-bis(benzyloxy)phenyl]methylidene]-3-(2-phenylethyl)-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
IC50 above 0.067 mM
0.067
(5E)-5-[[3,4-bis(benzyloxy)phenyl]methylidene]-3-ethyl-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
IC50 above 0.067 mM
0.067
(5E)-5-[[3,4-bis(benzyloxy)phenyl]methylidene]-3-methyl-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
IC50 above 0.067 mM
0.067
(5E)-5-[[3,4-bis(benzyloxy)phenyl]methylidene]-3-phenyl-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
IC50 above 0.067 mM
0.0014
(5E)-5-[[3,5-bis(benzyloxy)phenyl]methylidene]-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
-
0.0032
(5E)-5-[[3-(3,4-dichlorophenoxy)phenyl]methylidene]-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
-
0.0025
(5E)-5-[[3-(3,5-dichlorophenoxy)phenyl]methylidene]-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
-
0.0049 - 0.022
(5E)-5-[[3-(4-chlorophenoxy)phenyl]methylidene]-2-thioxo-1,3-thiazolidin-4-one
0.0162
(5E)-5-[[3-(4-methoxyphenoxy)phenyl]methylidene]-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
-
0.0148
(5E)-5-[[3-(4-methylphenoxy)phenyl]methylidene]-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
-
0.0017
(5E)-5-[[3-(4-tert-butylphenoxy)phenyl]methylidene]-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
-
0.0201
(5E)-5-[[3-(benzyloxy)phenyl]methylidene]-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
-
0.022
(5E)-5-[[4-(benzyloxy)-3-methoxyphenyl]methylidene]-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
IC50 above 0.022 mM
0.01
(5Z)-5-[[3-(3,4-dichlorophenoxy)phenyl]methylidene]-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
-
0.0092
(5Z)-5-[[3-(3,5-dichlorophenoxy)phenyl]methylidene]-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
-
0.067
(5Z)-5-[[3-(3,5-dichlorophenoxy)phenyl]methylidene]-2-thioxoimidazolidin-4-one
Homo sapiens
-
IC50 above 0.067 mM
0.022
(5Z)-5-[[3-(4-chlorophenoxy)phenyl]methylidene]-1-methyl-2-thioxoimidazolidin-4-one
Homo sapiens
-
IC50 above 0.022 mM
0.067
(5Z)-5-[[3-(4-chlorophenoxy)phenyl]methylidene]-2-thioxoimidazolidin-4-one
Homo sapiens
-
IC50 above 0.067 mM
0.0068
(5Z)-5-[[3-(4-tert-butylphenoxy)phenyl]methylidene]-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
-
0.067
(5Z)-5-[[3-(4-tert-butylphenoxy)phenyl]methylidene]-2-thioxoimidazolidin-4-one
Homo sapiens
-
IC50 above 0.067 mM
0.0026
(R)-2-(4'-((4-(cyclohexanecarbonyl)phenoxy)methyl)biphenyl-4-ylsulfonamido)-3-methylbutanoic acid
Mus musculus
-
-
0.0084
(R)-2-(4'-((4-isobutyrylphenoxy)methyl)biphenyl-4-ylsulfonamido)-3-methylbutanoic acid
Mus musculus
-
-
0.0066
(R)-3-methyl-2-(4'-((5-oxo-5,6,7,8-tetrahydronaphthalen-2-yloxy)methyl)biphenyl-4-ylsulfonamido)butanoic acid
Mus musculus
-
-
0.00042
1-benzyl-4-((4-(4-chlorophenoxy) phenyl)-sulfonyl)-N-hydroxypiperidine-4-carboxamide
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.00233
2-(4-acetylphenoxy)-N-[(5-chloro-8-hydroxyquinolin-7-yl)(3-nitrophenyl)methyl]acetamide
Homo sapiens
-
0.00083
2-(benzyloxy)-N-[(5-chloro-8-hydroxyquinolin-7-yl)(3-fluorophenyl)methyl]acetamide
Homo sapiens
-
0.0007
2-(benzyloxy)-N-[(5-chloro-8-hydroxyquinolin-7-yl)(4-methylphenyl)methyl]acetamide
Homo sapiens
-
0.0011
2-[(5E)-5-[[3,4-bis(benzyloxy)phenyl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]-3-methylbutanoic acid
Homo sapiens
-
-
0.0013
2-[(5E)-5-[[3,4-bis(benzyloxy)phenyl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
Homo sapiens
-
-
0.0018
2-[(5Z)-5-[[3-(3,4-dichlorophenoxy)phenyl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]-3-methylbutanoic acid
Homo sapiens
-
-
0.0016
2-[(5Z)-5-[[3-(3,4-dichlorophenoxy)phenyl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
Homo sapiens
-
-
0.00234
2-[4-(acetylamino)phenoxy]-N-[(5-chloro-8-hydroxyquinolin-7-yl)(2-chlorophenyl)methyl]acetamide
Homo sapiens
-
0.00133
2-[4-(acetylamino)phenoxy]-N-[(5-chloro-8-hydroxyquinolin-7-yl)(3-fluorophenyl)methyl]acetamide
Homo sapiens
-
0.00339
2-[4-(acetylamino)phenoxy]-N-[(5-chloro-8-hydroxyquinolin-7-yl)(4-methoxyphenyl)methyl]acetamide
Homo sapiens
-
0.012
2-[4-(benzyloxy)phenyl]-2,3-dihydro-1-oxo-1H-pyrrolo[3,4-c]quinoline-4-carboxylate
Homo sapiens
-
37°C, pH and temperature not specified in the publication
0.00095
2-[4-(benzyloxy)phenyl]-2,3-dihydro-N-hydroxy-1-oxo-1Hpyrrolo[3,4-c]quinoline-4-carboxamide
Homo sapiens
-
37°C, pH and temperature not specified in the publication
0.0053
3-[(5E)-5-[[3,4-bis(benzyloxy)phenyl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
Homo sapiens
-
-
0.00023 - 0.023
3-[2-[(Z)-(4-oxo-1,3-thiazolidin-2-ylidene)methyl]-4-(pyridin-2-yl)-1,3-thiazol-5-yl]propanoic acid
0.008
4-[(4-oxo-2-thioxo-1,3-thiazolidin-5-yl)methyl]-3-phenyl-5-(2-pyrimidin-1(6H)-ylpiperazin-1-yl)-1H-pyrazole-1-carbonitrile
Homo sapiens
-
-
0.0117
4-[(4-oxo-2-thioxo-1,3-thiazolidin-5-yl)methyl]-5-(2-pyrimidin-1(6H)-ylpiperazin-1-yl)-3-(trifluoromethyl)-1H-pyrazole-1-carbonitrile
Homo sapiens
-
-
0.0037
5-([1,3-diphenyl-5-[(thiophen-2-ylmethyl)sulfanyl]-1H-pyrazol-4-yl]methyl)-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
-
0.0083
5-([1-methyl-5-[(4-methylphenyl)sulfanyl]-3-phenyl-1H-pyrazol-4-yl]methyl)-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
-
0.0091
5-([1-phenyl-5-[2-(tetrahydrothiophen-2-yl)ethoxy]-3-(trifluoromethyl)-1H-pyrazol-4-yl]methyl)-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
-
0.0232
5-([5-[(2-chlorobenzyl)sulfanyl]-1-methyl-3-(2,2,2-trifluoroethyl)-1H-pyrazol-4-yl]methyl)-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
-
0.0011
5-([5-[(4-chlorobenzyl)sulfanyl]-1-methyl-3-(2,2,2-trifluoroethyl)-1H-pyrazol-4-yl]methyl)-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
-
0.0025
5-([5-[(4-chlorobenzyl)sulfanyl]-1-phenyl-3-(2,2,2-trifluoroethyl)-1H-pyrazol-4-yl]methyl)-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
-
0.0022
5-([5-[(4-tert-butylbenzyl)sulfanyl]-1-methyl-3-(2,2,2-trifluoroethyl)-1H-pyrazol-4-yl]methyl)-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
-
0.0067
5-([5-[(furan-2-ylmethyl)sulfanyl]-1,3-diphenyl-1H-pyrazol-4-yl]methyl)-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
-
0.0141
5-([5-[(furan-2-ylmethyl)sulfanyl]-1-methyl-3-phenyl-1H-pyrazol-4-yl]methyl)-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
-
0.0042
5-([5-[2-(4-chlorophenyl)ethoxy]-1-phenyl-3-(trifluoromethyl)-1H-pyrazol-4-yl]methyl)-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
-
0.0071
5-([5-[2-(4-fluorophenyl)ethoxy]-1-phenyl-3-(trifluoromethyl)-1H-pyrazol-4-yl]methyl)-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
-
0.009
5-([5-[4-(4-chlorophenyl)piperazin-1-yl]-1-methyl-3-(2,2,2-trifluoroethyl)-1H-pyrazol-4-yl]methyl)-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
-
0.0021
5-([5-[4-(4-chlorophenyl)piperazin-1-yl]-1-phenyl-3-(2,2,2-trifluoroethyl)-1H-pyrazol-4-yl]methyl)-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
-
0.0042
5-[(4-chlorobenzyl)sulfanyl]-4-[(4-oxo-2-thioxo-1,3-thiazolidin-5-yl)methyl]-3-(2,2,2-trifluoroethyl)-1H-pyrazole-1-carbonitrile
Homo sapiens
-
-
0.0046
5-[(furan-2-ylmethyl)sulfanyl]-4-[(4-oxo-2-thioxo-1,3-thiazolidin-5-yl)methyl]-3-phenyl-1H-pyrazole-1-carbonitrile
Homo sapiens
-
-
0.0046
5-[[5-(4-methylpiperazin-1-yl)-1,3-diphenyl-1H-pyrazol-4-yl]methyl]-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
-
0.0169
5-[[5-(benzylsulfanyl)-1-phenyl-3-(trifluoromethyl)-1H-pyrazol-4-yl]methyl]-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
-
0.129
N-hydroxy-4-(4-(4-(trifluoromethyl)-phenoxy)phenylsulfonyl)-tetrahydro-2H-pyran-4-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.00029
N-hydroxy-4-([4-[4-(trifluoromethyl)phenoxy]phenyl]sulfonyl)tetrahydro-2H-pyran-4-carboxamide
Homo sapiens
-
in 100 mM Tris-HCl, 100 mM NaCl, 0.01 mM CaCl2, 0.05% Brij, pH 7.5
0.00242
N-[(2-chlorophenyl)(8-hydroxy-5-methylquinolin-7-yl)methyl]-2-phenoxyacetamide
Homo sapiens
-
0.00094
N-[(2-chlorophenyl)(8-hydroxy-5-nitroquinolin-7-yl)methyl]-2-phenoxyacetamide
Homo sapiens
-
0.00083
N-[(5-bromo-8-hydroxyquinolin-7-yl)(2-chlorophenyl)methyl]-2-phenoxyacetamide
Homo sapiens
-
0.00062
N-[(5-bromo-8-hydroxyquinolin-7-yl)(3-nitrophenyl)methyl]-2-phenoxyacetamide
Homo sapiens
-
0.00035
N-[(5-chloro-8-hydroxyquinolin-7-yl)(2-chlorophenyl)methyl]-2-phenoxyacetamide
Homo sapiens
sub-micromol ADAMTS-5 potency and good selectivity over the related metalloproteases ADAMTS-4 (aggrecanase-1), MMP-13, and MMP-12
0.00172
N-[(5-chloro-8-hydroxyquinolin-7-yl)(2-chlorophenyl)methyl]-2-[3-(dimethylamino)phenoxy]acetamide
Homo sapiens
-
0.00148
N-[(5-chloro-8-hydroxyquinolin-7-yl)(2-chlorophenyl)methyl]-N2-(4-chloro-3-methylphenyl)glycinamide
Homo sapiens
-
0.00099
N-[(5-chloro-8-hydroxyquinolin-7-yl)(2-chlorophenyl)methyl]-N2-methyl-N2-phenylglycinamide
Homo sapiens
-
0.00232
N-[(5-chloro-8-hydroxyquinolin-7-yl)(2-cyanophenyl)methyl]-2-phenoxyacetamide
Homo sapiens
-
0.00122
N-[(5-chloro-8-hydroxyquinolin-7-yl)(2-fluorophenyl)methyl]-2-phenoxyacetamide
Homo sapiens
-
0.00185
N-[(5-chloro-8-hydroxyquinolin-7-yl)(2-methylphenyl)methyl]-2-phenoxyacetamide
Homo sapiens
-
0.00121
N-[(5-chloro-8-hydroxyquinolin-7-yl)(2-nitrophenyl)methyl]-2-phenoxyacetamide
Homo sapiens
-
0.00062
N-[(5-chloro-8-hydroxyquinolin-7-yl)(3-fluorophenyl)methyl]-2-phenoxyacetamide
Homo sapiens
-
0.00337
N-[(5-chloro-8-hydroxyquinolin-7-yl)(3-fluorophenyl)methyl]-2-[3-(dimethylamino)phenoxy]acetamide
Homo sapiens
-
0.00143
N-[(5-chloro-8-hydroxyquinolin-7-yl)(3-fluorophenyl)methyl]-N2-(4-chloro-3-methylphenyl)glycinamide
Homo sapiens
-
0.00125
N-[(5-chloro-8-hydroxyquinolin-7-yl)(3-fluorophenyl)methyl]-N2-methyl-N2-phenylglycinamide
Homo sapiens
-
0.00166
N-[(5-chloro-8-hydroxyquinolin-7-yl)(3-nitrophenyl)methyl]-2-(pyridin-3-yloxy)acetamide
Homo sapiens
-
0.00049
N-[(5-chloro-8-hydroxyquinolin-7-yl)(3-nitrophenyl)methyl]-2-phenoxyacetamide
Homo sapiens
sub-micromol ADAMTS-5 potency and good selectivity over the related metalloproteases ADAMTS-4 (aggrecanase-1), MMP-13, and MMP-12
0.00119
N-[(5-chloro-8-hydroxyquinolin-7-yl)(3-nitrophenyl)methyl]-N2-(4-chloro-3-methylphenyl)glycinamide
Homo sapiens
-
0.00056
N-[(5-chloro-8-hydroxyquinolin-7-yl)(3-nitrophenyl)methyl]-N2-methyl-N2-phenylglycinamide
Homo sapiens
sub-micromol ADAMTS-5 potency and good selectivity over the related metalloproteases ADAMTS-4 (aggrecanase-1), MMP-13, and MMP-12. Good balance of potent ADAMTS-5 inhibition, moderate CYP3A4 inhibition and good rat liver microsome stability
0.00083
N-[(5-chloro-8-hydroxyquinolin-7-yl)(4-chlorophenyl)methyl]-2-phenoxyacetamide
Homo sapiens
-
0.00094
N-[(5-chloro-8-hydroxyquinolin-7-yl)(4-methoxyphenyl)methyl]-2-(4-methoxyphenoxy)acetamide
Homo sapiens
sub-micromol ADAMTS-5 potency and good selectivity over the related metalloproteases ADAMTS-4 (aggrecanase-1), MMP-13, and MMP-12
0.00077
N-[(5-chloro-8-hydroxyquinolin-7-yl)(4-methoxyphenyl)methyl]-2-(4-methylphenoxy)acetamide
Homo sapiens
-
0.00298
N-[(5-chloro-8-hydroxyquinolin-7-yl)(4-methoxyphenyl)methyl]-2-(pyridin-3-yloxy)acetamide
Homo sapiens
-
0.00135
N-[(5-chloro-8-hydroxyquinolin-7-yl)(4-methoxyphenyl)methyl]-2-phenoxyacetamide
Homo sapiens
-
0.00167
N-[(5-chloro-8-hydroxyquinolin-7-yl)(4-methoxyphenyl)methyl]-2-[3-(dimethylamino)phenoxy]acetamide
Homo sapiens
-
0.00076
N-[(5-chloro-8-hydroxyquinolin-7-yl)(4-methylphenyl)methyl]-2-phenoxyacetamide
Homo sapiens
-
0.00158
N-[(5-chloro-8-hydroxyquinolin-7-yl)(4-methylphenyl)methyl]-N2-(4-chloro-3-methylphenyl)glycinamide
Homo sapiens
-
0.00101
N-[(5-chloro-8-hydroxyquinolin-7-yl)(4-methylphenyl)methyl]-N2-(4-cyanophenyl)glycinamide
Homo sapiens
-
0.00078
N-[(5-chloro-8-hydroxyquinolin-7-yl)(4-methylphenyl)methyl]-N2-methyl-N2-phenylglycinamide
Homo sapiens
-
0.00193
N-[(5-chloro-8-hydroxyquinolin-7-yl)(4-methylphenyl)methyl]-N2-[3-(dimethylamino)phenyl]glycinamide
Homo sapiens
-
0.00046
N-[(5-chloro-8-hydroxyquinolin-7-yl)(4-nitrophenyl)methyl]-2-phenoxyacetamide
Homo sapiens
-
0.00102
N-[(5-chloro-8-hydroxyquinolin-7-yl)(phenyl)methyl]-2-(4-chlorophenoxy)acetamide
Homo sapiens
-
0.0019
N-[(5-chloro-8-hydroxyquinolin-7-yl)(phenyl)methyl]-2-(4-methylphenoxy)acetamide
Homo sapiens
-
0.00078
N-[(5-chloro-8-hydroxyquinolin-7-yl)(phenyl)methyl]-2-phenoxyacetamide
Homo sapiens
-
0.00083
N-[(5-chloro-8-hydroxyquinolin-7-yl)[2-(trifluoromethyl)phenyl]methyl]-2-phenoxyacetamide
Homo sapiens
-
0.00484
N-[(5-fluoro-8-hydroxyquinolin-7-yl)(phenyl)methyl]-2-phenoxyacetamide
Homo sapiens
-
0.00132
N-[(8-hydroxy-5-methylquinolin-7-yl)(3-nitrophenyl)methyl]-2-phenoxyacetamide
Homo sapiens
-
0.00135
N-[(8-hydroxy-5-nitroquinolin-7-yl)(phenyl)methyl]-2-phenoxyacetamide
Homo sapiens
-
0.000004 - 0.000035
N-[[(4S)-4-(1-methylimidazol-2-yl)-2,5-dioxo-imidazolidin-4-yl]methyl]-5-(trifluoromethyl)benzofuran-2-carboxamide
0.00107
N2-(4-acetylphenyl)-N-[(5-chloro-8-hydroxyquinolin-7-yl)(3-nitrophenyl)methyl]glycinamide
Homo sapiens
-
0.00113
N2-(4-acetylphenyl)-N-[(5-chloro-8-hydroxyquinolin-7-yl)(4-methylphenyl)methyl]glycinamide
Homo sapiens
-
0.0011
N2-(biphenyl-4-ylcarbonyl)-N-(2-phenylpropan-2-yl)-L-alpha-glutamine
Homo sapiens
-
37°C, pH and temperature not specified in the publication
0.00131
N2-benzyl-N-[(5-chloro-8-hydroxyquinolin-7-yl)(2-chlorophenyl)methyl]-N2-methylglycinamide
Homo sapiens
-
0.00189
N2-benzyl-N-[(5-chloro-8-hydroxyquinolin-7-yl)(2-chlorophenyl)methyl]glycinamide
Homo sapiens
-
0.00144
N2-benzyl-N-[(5-chloro-8-hydroxyquinolin-7-yl)(3-fluorophenyl)methyl]-N2-methylglycinamide
Homo sapiens
-
0.00172
N2-benzyl-N-[(5-chloro-8-hydroxyquinolin-7-yl)(3-fluorophenyl)methyl]glycinamide
Homo sapiens
-
0.00082
N2-benzyl-N-[(5-chloro-8-hydroxyquinolin-7-yl)(3-nitrophenyl)methyl]-N2-methylglycinamide
Homo sapiens
-
0.00128
N2-benzyl-N-[(5-chloro-8-hydroxyquinolin-7-yl)(4-methylphenyl)methyl]-N2-methylglycinamide
Homo sapiens
-
0.00183
N2-benzyl-N-[(5-chloro-8-hydroxyquinolin-7-yl)(4-methylphenyl)methyl]glycinamide
Homo sapiens
-
0.00277
N2-[4-(acetylamino)phenyl]-N-[(5-chloro-8-hydroxyquinolin-7-yl)(3-nitrophenyl)methyl]glycinamide
Homo sapiens
-
0.0000038
TIMP-3
Homo sapiens
-
in 100 mM Tris-HCl, 100 mM NaCl, 0.01 mM CaCl2, 0.05% Brij, pH 7.5
-
0.0009
[(5E)-5-[[3,4-bis(benzyloxy)phenyl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl](phenyl)acetic acid
Homo sapiens
-
-
0.0067
[(5E)-5-[[3,4-bis(benzyloxy)phenyl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
Homo sapiens
-
-
0.0013
[(5Z)-5-[[3-(3,4-dichlorophenoxy)phenyl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl](phenyl)acetic acid
Homo sapiens
-
-
0.0111
[(5Z)-5-[[3-(3,4-dichlorophenoxy)phenyl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
Homo sapiens
-
-
0.0049
(5E)-5-[[3-(4-chlorophenoxy)phenyl]methylidene]-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
-
0.022
(5E)-5-[[3-(4-chlorophenoxy)phenyl]methylidene]-2-thioxo-1,3-thiazolidin-4-one
Homo sapiens
-
IC50 above 0.022 mM
0.00017
(E)-2-((1H-benzo[d]imidazol-2-yl)methylene)-5-propylthiazolidin-4-one
Homo sapiens
pH 7.5, 37°C
0.021
(E)-2-((1H-benzo[d]imidazol-2-yl)methylene)-5-propylthiazolidin-4-one
Homo sapiens
pH 7.5, 37°C
0.00023
3-[2-[(Z)-(4-oxo-1,3-thiazolidin-2-ylidene)methyl]-4-(pyridin-2-yl)-1,3-thiazol-5-yl]propanoic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.023
3-[2-[(Z)-(4-oxo-1,3-thiazolidin-2-ylidene)methyl]-4-(pyridin-2-yl)-1,3-thiazol-5-yl]propanoic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.000004
N-[[(4S)-4-(1-methylimidazol-2-yl)-2,5-dioxo-imidazolidin-4-yl]methyl]-5-(trifluoromethyl)benzofuran-2-carboxamide
Homo sapiens
-
pH 7.5, 22°C
0.000035
N-[[(4S)-4-(1-methylimidazol-2-yl)-2,5-dioxo-imidazolidin-4-yl]methyl]-5-(trifluoromethyl)benzofuran-2-carboxamide
Homo sapiens
-
pH 7.5, 22°C, presence of 50% rat plasma
additional information
2-[4-(benzyloxy)phenyl]-3-oxoisoindoline-4-carboxylic acid
Homo sapiens
-
IC25-value: 0.0075 mM, 37°C, pH and temperature not specified in the publication, plateau inhibition at about 50%
additional information
2-[4-(benzyloxy)phenyl]-N-hydroxy-3-oxoisoindoline-4-carboxamide
Homo sapiens
-
IC25-value: 0.0025 mM, 37°C, pH and temperature not specified in the publication, plateau inhibition at about 50%
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
constitutive Adamts5 expression in adult tissue
brenda
constitutive Adamts5 expression in adult tissue
brenda
in the kidney, constitutive Adamts5 expression in adult tissue
brenda
expressed by interstitial inflammatory cells in IgA nephropathy
brenda
expressed by interstitial inflammatory cells in IgA nephropathy
brenda
-
ADAMTS-5 is the main aggrecanase in laryngeal squamous cell carcinoma
brenda
-
ADAMTS-4, EC 3.4.24.82, is the highest expressed aggrecanase in normal larynx
brenda
lining the peritoneal, pericardial and pleural cavities, constitutive Adamts5 expression in adult tissue
brenda
of the peripheral and autonomic nervous system, constitutive Adamts5 expression in adult tissue
brenda
in bronchi and pancreatic ducts, constitutive Adamts5 expression in adult tissue. Expression of Adamts5 during neuromuscular development and in smooth muscle cells coincides with the broadly distributed proteoglycan versican, an ADAMTS5 substrate
brenda
embryonic expression is scarce prior to 11.5 days of gestation (E11.5) and noted only in the floor plate of the developing brain at E9.5. After E11.5 there is continued expression in brain, especially in the choroid plexus, peripheral nerves, dorsal root ganglia, cranial nerve ganglia, spinal and cranial nerves, and neural plexuses of the gut. In addition to nerves, developing limbs have Adamts5 expression in skeletal muscle (from E13.5), tendons (from E16.5), and inter-digital mesenchyme of the developing autopod (E13.515.5)
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
ADAMTS5-/- mice have significantly less cartilage damage than wild-type after induction of osteoarthritis through surgical instability
malfunction
-
ADAMTS-5 deficient mice do not develop mechanical allodynia associated with osteoarthritis following medial meniscal destabilization
malfunction
-
ADAMTS5 deficient mice have reduced versican proteolysis, increased pericellular matrix, altered cell shape, enhanced alpha-smooth muscle actin expression and increased contractility within three dimensional collagen gels
malfunction
-
ADAMTS-5 knockout mice express no major phenotypical abnormalities, but show a significant reduction in the severity of surgically induced osteoarthritis in the ADAMTS-5 in contrast to the ADAMTS-4 knockout groups
malfunction
influenza virus infection of enzyme-deficient mice results in delayed virus clearance, compromised T cell migration and immunity and accumulation of versican. Enzyme-deficient mice exhibit increased weight loss and delayed influenza virus clearance following infection
malfunction
enzyme-deficient mice develop less subcutaneous and gonadal white adipose tissue as compared to their wild type littermates. Enhanced browning of white adipose tissue and improved insulin sensitivity are seen in enzyme-knockout mice upon cold exposure
malfunction
insufficiency of enzyme expression in Sertoli cells may have an important role in the etiology of male infertility
malfunction
loss of Adamts5 caused a reduction of Bglap expressing osteoblasts throughout mandibular condylar development and in young adult mice. The protease Mmp13, that is involved in mineralization and is expressed by hypertrophic chondrocytes and osteoblasts, was reduced in the mandibular condyle of Adamts5 deficient mice
physiological function
-
key metalloprotease mediating cartilage destruction in arthritis
physiological function
-
both long and short forms of the procollagen C-proteinase enhancers netrin-like (PCPE-1 NTR) domain show no inhibition, at micromolar concentrations, of several members of the metzincin superfamily, including matrix metalloproteinase-2, bone morphogenetic protein-1, and different ADAMTS-2, ADAMTS-4 or ADAMTS-5
physiological function
-
aggrecan cleavage by a disintegrin and metalloproteinase with a thrombospondin type 1 motif, member 5 (ADAMTS-5) is crucial for the breakdown of cartilage matrix during osteoarthritis, a degenerative joint disease that leads to the progressive destruction of articular structures
physiological function
-
ADAMTS5 maintains optimal versican content and pericellular matrix volume by continually trimming versican in hyaluronan-versican aggregates
physiological function
-
ADAMTS-5 contributes to the structural damage of cartilage that characterizes human osteoarthritis
physiological function
-
in the growth plate ADAMTS-5 has a physiological function in the intracellular processing of matrilins and potentially of other extracellular matrix proteins
physiological function
-
disruptive changes in chondrocyte-matrix interactions by hyaluran oligosaccharides induce matrix degradation and elevate aggrecanases ADAMTS4, ADAMTS5 via the activation of the NF-kappaB signaling pathway
physiological function
-
overexpression of full-length ADAMTS5 suppresses B16 melanoma growth in mice. The reduced tumor growth is correlated with diminished tumor angiogenesis, together with reduced tumor cell proliferation and increased tumor cell apoptosis. Catalytically active ADAMTS5 proteolytic fragment also suppresses angiogenesis in vitro. The catalytic activity of ADAMTS5 is dispensable for its anti-tumorigenic function. ADAMTS5 inhibits B16 tumorigenesis through its TSR1 by suppressing tumor angiogenesis
physiological function
-
ADAMTS-5 is markedly reduced in atherosclerotic aortas of apolipoprotein E-null mice. The reduction of ADAMTS-5 is accompanied by accumulation of biglycan and versican, the major lipoprotein-binding proteoglycans, in atherosclerosis. ADAMTS-5 activity induced the release of ADAMTS-specific versican and aggrecan fragments as well as biglycan and link protein from the aortic wall. Fibroblast growth factor 2 inhibits ADAMTS-5 expression in isolated aortic smooth muscle cells and blocked the spontaneous release of ADAMTS-generated versican and aggrecan fragments from aortic explants. In aortas of ADAMTS-5-deficient mice, ADAMTS-specific versican neoepitopes are not detectable. Biglycan levels are increased. ADAMTS-5 proteolytic activity reduces the low density lipoprotein binding ability of biglycan and releases low density lipoprotein from human aortic lesions
physiological function
-
the enzyme also plays an important non-enzymatic role in regulating the Sonic Hedgehog pathway during embryogenesis that impacts on muscle development
physiological function
the enzyme is a critical regulator of virus-specific T cell immunity. Its enzymatic activity plays a key role in the development of influenza-specific immunity. The enzyme cleaves large proteoglycans such as aggrecan, leading to the destruction of cartilage and osteoarthritis
physiological function
the enzyme is a principal mediator of aggrecan loss in osteoarthritis
physiological function
ADAMTS5 promotes permeability of the blood-brain barrier during Treponema pallidum subspecies pallidum invading the central nervous system. Treponema pallidum subspecies pallidum promotes the expression of ADAMTS5 through IL-1beta in hCMEC/D3 cells
physiological function
ADAMTS-5 is a matrix-degrading protease. It cleaves inter-alpha-inhibitor and releases active heavy chain 2 (HC2) in synovial fluids from arthritic patients. ADAMTS-5 cleavage of HC2 could alter the physiological and mechanical properties of the extracellular matrix and contribute to the progression of arthritis
physiological function
endothelial secretion of ADAMTS5 and cleavage of versican is a downstream mechanisms of cerebral cavernous malformation pathogenesis and provides a basis for the participation of wild-type endothelial cells in lesion formation
physiological function
the enzyme is involved in the maintenance of cartilage extracellular matrix
physiological function
ADAMTS5 is required for normal trabeculated bone development in the mandibular condyle
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ATS5_BOVIN
207
0
22576
Swiss-Prot
other Location (Reliability: 2)
ATS1_HUMAN
967
0
105358
Swiss-Prot
Mitochondrion (Reliability: 3)
ATS5_HUMAN
930
0
101718
Swiss-Prot
other Location (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60000
64000
x * 64000, C-terminally processed recombinant mature enzyme, SDS-PAGE
74000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
proteolytic modification
recombinant enzyme is also processed in insect cells
proteolytic modification
-
synthesized as a zymogen, proADAMTS5. The propeptide excision mechanism is a major regulatory step. proADAMTS5 is processed by proprotein convertases, specifically furin and PC7, but not PC6B. proADAMTS5 processing occurs after Arg261. Cleaved ADAMTS5 propeptide and mature ADAMTS5 are found exclusively in the conditioned medium. Extracellular ADAMTS5 processing is supported by activation of proADAMTS5 added exogenously to HEK-293 cells stably expressing furin
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ADAMTS-5 catalytic domain in complex with inhibitor, vapor diffusion method, using 30% (w/v) PEG 3350 and 0.1 M Tris pH 8.5, at 22°C
in complex with batimastat, vapour diffusion method at 18°C using 10% PEG 8K, 0.2 M ammonium sulfate, and 0.1M MES (pH 6.5) as a precipitate
-
molecular dynamics simulations and multiway explorative data analysis on ADAMTS4 complexed with Marimastat and two cis-1(S)2(R)-amino-2-indanol ligands, and comparison with proteases MMP13, ADAMTS5. Determinant characteristics for ligand binding and selectivity among the three enzymes are to be found in the different protein conformation flexibility
sitting drop method, crystal structure of the catalytic domain of ADAMTS-5 in complex with marimastat, (2R)-N4-hydroxy-2-(3-hydroxybenzyl)-N1-[(1S,2R)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]butanediamide or (3R)-N2-(cyclopropylmethyl)-N1-hydroxy-3-(3-hydroxybenzyl)-N4-[(1S,2R)-2-hydroxy-2,3-dihydro-1H-inden-1-yl]-L-aspartamide
vapour diffusion method with 25% (v/v) polyethylene glycol 3350, 200 mM ammonium acetate, 100 mM Tris, pH 8.5
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E411A
-
active site mutant, presents similar tumor suppression activity as wild-type enzyme
E411Q
full length ADAMTS-5 active site mutant generated by point mutation
additional information
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
anti-FLAG M2-agarose column chromatography, Macro-Prep 25 S resin chromatography, and
-
M2-agarose column chromatography, Macro-Prep S resin column chromatography, and Sephacryl S-200 gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
correction of point mutations G577S and Q579R by overlap extension PCR, subcloning from FLAG-tagged construct in the baculovirus, cloning and expression of His-FLAG-tagged wild-type enzyme and mutants in insect cells via baculovirus infection
expressed in CHO cells
expression in Drosophila S2 cells
expression of a recombinant interglobular domain of human aggrecan, residues 330YTGED to HLPGG458 tagged with glutathione S-transferase and FLAG, in Escherichia coli
expression of FLAG-tagged enzyme in Spodoptera frugiperda Sf9 cells via baculovirus infection, secretion of recombinant protein to the medium
-
the catalytic domain of ADAMTS-5 comprising amino acids S263 to I480 preceded by a Met-Ala sequence and incorporating the single point mutation L282K is expressed in Escherichia coli
the first thrombospondin type 1 repeat is expressed in Escherichia coli strain BL21DE3
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ADAMTS-5 expression is not regulated by interleukin-1 and tumor necrosis factor-alpha
-
ADAMTS5 and endothelial glycocalyx components notably increase in the cerebrospinal fluid of HIV-negative neurosyphilis patients
Adamts5 mRNA is superinduced in Fgf2/ mice compared with Fgf2+/+ (fibroblast growth factor 2) mice 2 weeks following surgical destabilization of the medial meniscus
-
disruption of chondrocyte hyaluran receptor CD44-hyaluran interactions with hyaluran oligosaccharides induces the transcription of endopeptidases ADAMTS-4 and ADAMTS-5 in a time- and dose-dependent manner
-
fibroblast growth factor 2 inhibits ADAMTS-5 expression in isolated aortic smooth muscle cells and blocks the spontaneous release of ADAMTS-generated versican and aggrecan fragments from aortic explants
-
interleukin-1beta+OSM and tumor necrosis factor alpha+ OSM treatments induces a 17fold and 13fold increase in ADAMTS5 gene expression. Relatively little modulation in ADAMTS5 expression is observed in the presence of interleukin-1beta, tumor necrosis factor alpha or OSM alone
-
the enzyme is expressed 2.1fold less in Sertoli cells of individuals with nonobstructive azoospermia than those of control individuals with obstructive azoospermia
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
in 50 mM HEPES, pH 8.0, 2 mM oxidized glutathione, 50 mM arginine, 10 mM CaCl2, 0.2 mM ZnCl2, and 1% protease inhibitors, at room temperature
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
medicine
additional information
-
neurite extension mediated by the MAP kinase pathway, increased number of primary and secondary neurites
diagnostics
ADAMTS-5 activity could thus be used as a potential clinical biomarker for human osteoarthritis
medicine
-
the first thrombospondin type 1 repeat domain of ADAMTS5, unlike the second, has anti-angiogenic activities, ADAMTS5 is therefore an anti-angiogenic peptide and may serve as a prototype for future development into anti-cancer drugs
medicine
-
stop progression of cartilage degradation in osteoarthritis by prevention of aggrecan cleavage via inhibition of aggrecanase
medicine
design and development for potent and selective inhibitors of ADAMTS-4 and ADAMTS-5, which may be required for chronic osteoarthritis therapy
medicine
-
ADAMTS5 is a biomarker for prediction of response to Infliximab in patients with rheumatoid arthritis
medicine
-
a single injection of ADAMTS5 siRNA induces the suppression of degradation in nucleus pulposus tissues
medicine
-
overexpression of full-length ADAMTS5 suppresses B16 melanoma growth in mice. The reduced tumor growth is correlated with diminished tumor angiogenesis, together with reduced tumor cell proliferation and increased tumor cell apoptosis
medicine
-
ADAMTS-5 is the main aggrecanase in laryngeal squamous cell carcinoma presenting a stage-related increase up to stage III (8fold higher expression compared to normal), and thereafter decreased in stage IV. ADAMTS-5 is highly expressed by carcinoma cells. Within the cancerous and their corresponding macroscopically normal laryngeal tissues, an altered distribution and organization of multiple molecular forms (latent, activated and fragmented forms) of the enzymes is found
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Boeckmann, B.; Bairoch, A.; Apweiler, R.; Blatter, M.C.; Estreicher, A.; Gasteiger, E.; Martin M.J.; Michoud, K.; O'Donovan, C.; Phan, I.; Pilbout, S.; Schneider, M.
The SWISS-PROT protein knowledgebase and its supplement TrEMBL
Nucleic Acids Res.
31
365-370
2003
Homo sapiens (Q9UNA0), Mus musculus (Q9R001), Bos taurus (Q9TT92)
brenda
Vankemmelbeke, M.N.; Holen, I.; Wilson, A.G.; Ilic, M.Z.; Handley, C.J.; Kelner, G.S.; Clark, M.; Liu, C.; Maki, R.A.; Burnett, D.; Buttle, D.J.
Expression and activity of ADAMTS-5 in synovium
Eur. J. Biochem.
268
1259-1268
2001
Homo sapiens, Bos taurus (Q9TT92), Bos taurus
brenda
Vankemmelbeke, M.N.; Jones, G.C.; Fowles, C.; Ilic, M.Z.; Handley, C.J.; Day, A.J.; Knight, C.G.; Mort, J.S.; Buttle, D.J.
Selective inhibition of ADAMTS-1, -4 and -5 by catechin gallate esters
Eur. J. Biochem.
270
2394-2403
2003
Homo sapiens (Q9UNA0)
brenda
Tang, B.L.
ADAMTS: a novel family of extracellular matrix proteases
Int. J. Biochem. Cell Biol.
33
33-44
2001
Bos taurus
brenda
Kashiwagi, M.; Tortorella, M.; Nagase, H.; Brew, K.
TIMP-3 is a potent inhibitor of aggrecanase 1 (ADAM-TS4) and aggrecanase 2 (ADAM-TS5)
J. Biol. Chem.
276
12501-12504
2001
Homo sapiens
brenda
Malfait, A.M.; Liu, R.Q.; Ijiri, K.; Komiya, S.; Tortorella, M.D.
Inhibition of ADAM-TS4 and ADAM-TS5 prevents aggrecan degradation in osteoarthritic cartilage
J. Biol. Chem.
277
22201-22208
2002
Homo sapiens
brenda
Nakada, M.; Miyamori, H.; Kita, D.; Takahashi, T.; Yamashita, J.; Sato, H.; Miura, R.; Yamaguchi, Y.; Okada, Y.
Human glioblastomas overexpress ADAMTS-5 that degrades brevican
Acta Neuropathol.
110
239-246
2005
Homo sapiens (Q9UHI8), Homo sapiens
brenda
Zeng, W.; Corcoran, C.; Collins-Racie, L.A.; LaVallie, E.R.; Morris, E.A.; Flannery, C.R.
Glycosaminoglycan-binding properties and aggrecanase activities of truncated ADAMTSs: Comparative analyses with ADAMTS-5, -9, -16 and -18
Biochim. Biophys. Acta
1760
517-524
2006
Homo sapiens (Q9UNA0), Homo sapiens
brenda
Miguel, R.F.; Pollak, A.; Lubec, G.
Metalloproteinase ADAMTS-1 but not ADAMTS-5 is manifold overexpressed in neurodegenerative disorders as Down syndrome, Alzheimers and Picks disease
Brain Res. Mol. Brain Res.
133
1-5
2005
Homo sapiens (Q9UHI8), Homo sapiens
brenda
Held-Feindt, J.; Paredes, E.B.; Bloemer, U.; Seidenbecher, C.; Stark, A.M.; Mehdorn, H.M.; Mentlein, R.
Matrix-degrading proteases ADAMTS4 and ADAMTS5 (disintegrins and metalloproteinases with thrombospondin motifs 4 and 5) are expressed in human glioblastomas
Int. J. Cancer
118
55-61
2005
Homo sapiens
brenda
Tortorella, M.D.; Arner, E.C.; Hills, R.; Easton, A.; Korte-Sarfaty, J.; Fok, K.; Wittwer, A.J.; Liu, R.Q.; Malfait, A.M.
Alpha2-macroglobulin is a novel substrate for ADAMTS-4 and ADAMTS-5 and represents an endogenous inhibitor of these enzymes
J. Biol. Chem.
279
17554-17561
2004
Homo sapiens
brenda
Stanton, H.; Rogerson, F.M.; East, C.J.; Golub, S.B.; Lawlor, K.E.; Meeker, C.T.; Little, C.B.; Last, K.; Farmer, P.J.; Campbell, I.K.; Fourie, A.M.; Fosang, A.J.
ADAMTS5 is the major aggrecanase in mouse cartilage in vivo and in vitro
Nature
434
648-652
2005
Mus musculus
brenda
Song, R.H.; Tortorella, M.D.; Malfait, A.M.; Alston, J.T.; Yang, Z.; Arner, E.C.; Griggs, D.W.
Aggrecan degradation in human articular cartilage explants is mediated by both ADAMTS-4 and ADAMTS-5
Arthritis Rheum.
56
575-585
2007
Homo sapiens
brenda
Sharghi-Namini, S.; Fan, H.; Sulochana, K.N.; Potturi, P.; Xiang, W.; Chong, Y.S.; Wang, Z.; Yang, H.; Ge, R.
The first but not the second thrombospondin type 1 repeat of ADAMTS5 functions as an angiogenesis inhibitor
Biochem. Biophys. Res. Commun.
371
215-219
2008
Homo sapiens
brenda
Bursavich, M.G.; Gilbert, A.M.; Lombardi, S.; Georgiadis, K.E.; Reifenberg, E.; Flannery, C.R.; Morris, E.A.
Synthesis and evaluation of aryl thioxothiazolidinone inhibitors of ADAMTS-5 (Aggrecanase-2)
Bioorg. Med. Chem. Lett.
17
1185-1188
2007
Homo sapiens
brenda
Gilbert, A.M.; Bursavich, M.G.; Lombardi, S.; Georgiadis, K.E.; Reifenberg, E.; Flannery, C.R.; Morris, E.A.
5-((1H-pyrazol-4-yl)methylene)-2-thioxothiazolidin-4-one inhibitors of ADAMTS-5
Bioorg. Med. Chem. Lett.
17
1189-1192
2007
Homo sapiens
brenda
Bondeson, J.; Wainwright, S.; Hughes, C.; Caterson, B.
The regulation of the ADAMTS4 and ADAMTS5 aggrecanases in osteoarthritis: a review
Clin. Exp. Rheumatol.
26
139-145
2008
Homo sapiens, Mus musculus
brenda
Fosang, A.J.; Rogerson, F.M.; East, C.J.; Stanton, H.
ADAMTS-5: the story so far
Eur. Cell Mater.
15
11-26
2008
Homo sapiens, Mus musculus, Bos taurus
brenda
Gendron, C.; Kashiwagi, M.; Lim, N.H.; Enghild, J.J.; Thogersen, I.B.; Hughes, C.; Caterson, B.; Nagase, H.
Proteolytic activities of human ADAMTS-5: comparative studies with ADAMTS-4
J. Biol. Chem.
282
18294-18306
2007
Homo sapiens
brenda
Ilic, M.Z.; East, C.J.; Rogerson, F.M.; Fosang, A.J.; Handley, C.J.
Distinguishing aggrecan loss from aggrecan proteolysis in ADAMTS-4 and ADAMTS-5 single and double deficient mice
J. Biol. Chem.
282
37420-37428
2007
Mus musculus
brenda
Shieh, H.S.; Mathis, K.J.; Williams, J.M.; Hills, R.L.; Wiese, J.F.; Benson, T.E.; Kiefer, J.R.; Marino, M.H.; Carroll, J.N.; Leone, J.W.; Malfait, A.M.; Arner, E.C.; Tortorella, M.D.; Tomasselli, A.
High resolution crystal structure of the catalytic domain of ADAMTS-5 (aggrecanase-2)
J. Biol. Chem.
283
1501-1507
2008
Homo sapiens
brenda
Fushimi, K.; Troeberg, L.; Nakamura, H.; Lim, N.H.; Nagase, H.
Functional differences of the catalytic and non-catalytic domains in human ADAMTS-4 and ADAMTS-5 in aggrecanolytic activity
J. Biol. Chem.
283
6706-6716
2008
Homo sapiens
brenda
Mosyak, L.; Georgiadis, K.; Shane, T.; Svenson, K.; Hebert, T.; McDonagh, T.; Mackie, S.; Olland, S.; Lin, L.; Zhong, X.; Kriz, R.; Reifenberg, E.L.; Collins-Racie, L.A.; Corcoran, C.; Freeman, B.; Zollner, R.; Marvell, T.; Vera, M.; Sum, P.E.; Lavallie, E.R.; Stahl, M.; Somers, W.
Crystal structures of the two major aggrecan degrading enzymes, ADAMTS4 and ADAMTS5
Protein Sci.
17
16-21
2008
Homo sapiens
brenda
Gilbert, A.M.; Bursavich, M.G.; Lombardi, S.; Georgiadis, K.E.; Reifenberg, E.; Flannery, C.R.; Morris, E.A.
N-((8-hydroxy-5-substituted-quinolin-7-yl)(phenyl)methyl)-2-phenyloxy/amino-acetamide inhibitors of ADAMTS-5 (Aggrecanase-2)
Bioorg. Med. Chem. Lett.
18
6454-6457
2008
Homo sapiens (Q9UNA0)
brenda
Shiozaki, M.; Maeda, K.; Miura, T.; Ogoshi, Y.; Haas, J.; Fryer, A.M.; Laird, E.R.; Littmann, N.M.; Andrews, S.W.; Josey, J.A.; Mimura, T.; Shinozaki, Y.; Yoshiuchi, H.; Inaba, T.
Novel N-substituted 2-phenyl-1-sulfonylamino-cyclopropane carboxylates as selective ADAMTS-5 (aggrecanase-2) inhibitors
Bioorg. Med. Chem. Lett.
19
1575-1580
2009
Homo sapiens (Q9UNA0)
brenda
McCulloch, D.R.; Goff, C.L.; Bhatt, S.; Dixon, L.J.; Sandy, J.D.; Apte, S.S.
Adamts5, the gene encoding a proteoglycan-degrading metalloprotease, is expressed by specific cell lineages during mouse embryonic development and in adult tissues
Gene Expr. Patterns
9
314-323
2009
Mus musculus (Q9R001), Mus musculus
brenda
Wang, Z.H.; Yang, Z.Q.; He, X.J.; Wang, L.; Li, L.X.; Tu, J.B.
Effects of RNAi-mediated inhibition of aggrecanase-1 and aggrecanase-2 on rat costochondral chondrocytes in vitro
Acta Pharmacol. Sin.
29
1215-1226
2008
Rattus norvegicus (Q6TY19)
brenda
Rogerson, F.M.; Stanton, H.; East, C.J.; Golub, S.B.; Tutolo, L.; Farmer, P.J.; Fosang, A.J.
Evidence of a novel aggrecan-degrading activity in cartilage: Studies of mice deficient in both ADAMTS-4 and ADAMTS-5
Arthritis Rheum.
58
1664-1673
2008
Mus musculus (Q9R001), Mus musculus
brenda
Pockert, A.J.; Richardson, S.M.; Le Maitre, C.L.; Lyon, M.; Deakin, J.A.; Buttle, D.J.; Freemont, A.J.; Hoyland, J.A.
Modified expression of the ADAMTS enzymes and tissue inhibitor of metalloproteinases 3 during human intervertebral disc degeneration
Arthritis Rheum.
60
482-491
2009
Homo sapiens
brenda
Miwa, H.E.; Gerken, T.A.; Huynh, T.D.; Duesler, L.R.; Cotter, M.; Hering, T.M.
Conserved sequence in the aggrecan interglobular domain modulates cleavage by ADAMTS-4 and ADAMTS-5
Biochim. Biophys. Acta
1790
161-172
2009
Homo sapiens
brenda
Hopper, D.W.; Vera, M.D.; How, D.; Sabatini, J.; Xiang, J.S.; Ipek, M.; Thomason, J.; Hu, Y.; Feyfant, E.; Wang, Q.; Georgiadis, K.E.; Reifenberg, E.; Sheldon, R.T.; Keohan, C.C.; Majumdar, M.K.; Morris, E.A.; Skotnicki, J.; Sum, P.E.
Synthesis and biological evaluation of ((4-keto)-phenoxy)methyl biphenyl-4-sulfonamides: a class of potent aggrecanase-1 inhibitors
Bioorg. Med. Chem. Lett.
19
2487-2491
2009
Mus musculus
brenda
Hamel, M.G.; Ajmo, J.M.; Leonardo, C.C.; Zuo, F.; Sandy, J.D.; Gottschall, P.E.
Multimodal signaling by the ADAMTSs (a disintegrin and metalloproteinase with thrombospondin motifs) promotes neurite extension
Exp. Neurol.
210
428-440
2008
Homo sapiens
brenda
Troeberg, L.; Fushimi, K.; Khokha, R.; Emonard, H.; Ghosh, P.; Nagase, H.
Calcium pentosan polysulfate is a multifaceted exosite inhibitor of aggrecanases
FASEB J.
22
3515-3524
2008
Homo sapiens (Q9UNA0)
brenda
Takizawa, M.; Yatabe, T.; Okada, A.; Chijiiwa, M.; Mochizuki, S.; Ghosh, P.; Okada, Y.
Calcium pentosan polysulfate directly inhibits enzymatic activity of ADAMTS4 (aggrecanase-1) in osteoarthritic chondrocytes
FEBS Lett.
582
2945-2949
2008
Homo sapiens
brenda
Demircan, K.; Gunduz, E.; Gunduz, M.; Beder, L.B.; Hirohata, S.; Nagatsuka, H.; Cengiz, B.; Cilek, M.Z.; Yamanaka, N.; Shimizu, K.; Ninomiya, Y.
Increased mRNA expression of ADAMTS metalloproteinases in metastatic foci of head and neck cancer
Head Neck
10
793-801
2009
Homo sapiens
brenda
Lee, J.H.; Fitzgerald, J.B.; DiMicco, M.A.; Cheng, D.M.; Flannery, C.R.; Sandy, J.D.; Plaas, A.H.; Grodzinsky, A.J.
Co-culture of mechanically injured cartilage with joint capsule tissue alters chondrocyte expression patterns and increases ADAMTS5 production
Arch. Biochem. Biophys.
489
118-126
2009
Bos taurus
brenda
Seki, S.; Asanuma-Abe, Y.; Masuda, K.; Kawaguchi, Y.; Asanuma, K.; Muehleman, C.; Iwai, A.; Kimura, T.
Effect of small interference RNA (siRNA) for ADAMTS5 on intervertebral disc degeneration in the rabbit anular needle-puncture model
Arthritis Res. Ther.
11
R166
2009
Oryctolagus cuniculus
brenda
Chia, S.L.; Sawaji, Y.; Burleigh, A.; McLean, C.; Inglis, J.; Saklatvala, J.; Vincent, T.
Fibroblast growth factor 2 is an intrinsic chondroprotective agent that suppresses ADAMTS-5 and delays cartilage degradation in murine osteoarthritis
Arthritis Rheum.
60
2019-2027
2009
Mus musculus
brenda
Willems, S.H.; Tape, C.J.; Stanley, P.L.; Taylor, N.A.; Mills, I.G.; Neal, D.E.; McCafferty, J.; Murphy, G.
Thiol isomerases negatively regulate the cellular shedding activity of ADAM17
Biochem. J.
428
439-450
2010
Homo sapiens
brenda
Lim, N.H.; Kashiwagi, M.; Visse, R.; Jones, J.; Enghild, J.J.; Brew, K.; Nagase, H.
Reactive-site mutants of N-TIMP-3 that selectively inhibit ADAMTS-4 and ADAMTS-5: biological and structural implications
Biochem. J.
431
113-122
2010
Homo sapiens (Q9UNA0), Homo sapiens
brenda
Shiozaki, M.; Imai, H.; Maeda, K.; Miura, T.; Yasue, K.; Suma, A.; Yokota, M.; Ogoshi, Y.; Haas, J.; Fryer, A.M.; Laird, E.R.; Littmann, N.M.; Andrews, S.W.; Josey, J.A.; Mimura, T.; Shinozaki, Y.; Yoshiuchi, H.; Inaba, T.
Synthesis and SAR of 2-phenyl-1-sulfonylaminocyclopropane carboxylates as ADAMTS-5 (aggrecanase-2) inhibitors
Bioorg. Med. Chem. Lett.
19
6213-6217
2009
Homo sapiens
brenda
Cudic, M.; Burstein, G.D.; Fields, G.B.; Lauer-Fields, J.
Analysis of flavonoid-based pharmacophores that inhibit aggrecanases (ADAMTS-4 and ADAMTS-5) and matrix metalloproteinases through the use of topologically constrained peptide substrates
Chem. Biol. Drug Des.
74
473-482
2009
Sus scrofa
brenda
Cappelli, A.; Nannicini, C.; Valenti, S.; Giuliani, G.; Anzini, M.; Mennuni, L.; Giordani, A.; Caselli, G.; Stasi, L.P.; Makovec, F.; Giorgi, G.; Vomero, S.
Design, synthesis, and preliminary biological evaluation of pyrrolo[3,4-c]quinolin-1-one and oxoisoindoline derivatives as aggrecanase inhibitors
ChemMedChem
5
739-748
2010
Homo sapiens
brenda
Longpre, J.; McCulloch, D.; Koo, B.; Alexander, J.; Apte, S.; Leduc, R.
Characterization of proADAMTS5 processing by proprotein convertases
Int. J. Biochem. Cell Biol.
41
1116-1126
2009
Homo sapiens
brenda
Tortorella, M.D.; Tomasselli, A.G.; Mathis, K.J.; Schnute, M.E.; Woodard, S.S.; Munie, G.; Williams, J.M.; Caspers, N.; Wittwer, A.J.; Malfait, A.M.; Shieh, H.S.
Structural and inhibition analysis reveals the mechanism of selectivity of a series of aggrecanase inhibitors
J. Biol. Chem.
284
24185-24191
2009
Homo sapiens (Q9UNA0)
brenda
Steinmeyer, J.; Kordelle, J.; Stuerz, H.
In vitro inhibition of aggrecanase activity by tetracyclines and proteoglycan loss from osteoarthritic human articular cartilage
J. Orthop. Res.
28
828-833
2010
Homo sapiens
brenda
Tsuzaka, K.; Itami, Y.; Takeuchi, T.; Shinozaki, N.; Morishita, T.
ADAMTS5 is a biomarker for prediction of response to infliximab in patients with rheumatoid arthritis
J. Rheumatol.
37
1454-1460
2010
Homo sapiens
brenda
Troeberg, L.; Fushimi, K.; Scilabra, S.D.; Nakamura, H.; Dive, V.; Thogersen, I.B.; Enghild, J.J.; Nagase, H.
The C-terminal domains of ADAMTS-4 and ADAMTS-5 promote association with N-TIMP-3
Matrix Biol.
28
463-469
2009
Homo sapiens
brenda
Echtermeyer, F.; Bertrand, J.; Dreier, R.; Meinecke, I.; Neugebauer, K.; Fuerst, M.; Lee, Y.J.; Song, Y.W.; Herzog, C.; Theilmeier, G.; Pap, T.
Syndecan-4 regulates ADAMTS-5 activation and cartilage breakdown in osteoarthritis
Nat. Med.
15
1072-1076
2009
Homo sapiens
brenda
Botter, S.; Glasson, S.; Hopkins, B.; Clockaerts, S.; Weinans, H.; van Leeuwen, J.; van Osch, G.
ADAMTS5-/- mice have less subchondral bone changes after induction of osteoarthritis through surgical instability: implications for a link between cartilage and subchondral bone changes
Osteoarthritis Cartilage
17
636-645
2009
Mus musculus
brenda
Malfait, A.M.; Ritchie, J.; Gil, A.S.; Austin, J.S.; Hartke, J.; Qin, W.; Tortorella, M.D.; Mogil, J.S.
ADAMTS-5 deficient mice do not develop mechanical allodynia associated with osteoarthritis following medial meniscal destabilization
Osteoarthritis Cartilage
18
572-580
2010
Mus musculus
brenda
Durigova, M.; Troeberg, L.; Nagase, H.; Roughley, P.J.; Mort, J.S.
Involvement of ADAMTS5 and hyaluronidase in aggrecan degradation and release from OSM-stimulated cartilage
Eur. Cell Mater.
21
31-45
2011
Homo sapiens
brenda
Hattori, N.; Carrino, D.A.; Lauer, M.E.; Vasanji, A.; Wylie, J.D.; Nelson, C.M.; Apte, S.S.
Pericellular versican regulates the fibroblast-myofibroblast transition: a role for ADAMTS5 protease-mediated proteolysis
J. Biol. Chem.
286
34298-34310
2011
Mus musculus
brenda
Verma, P.; Dalal, K.
ADAMTS-4 and ADAMTS-5: key enzymes in osteoarthritis
J. Cell. Biochem.
112
3507-3514
2011
Homo sapiens
brenda
Durigova, M.; Nagase, H.; Mort, J.S.; Roughley, P.J.
MMPs are less efficient than ADAMTS5 in cleaving aggrecan core protein
Matrix Biol.
30
145-153
2011
Homo sapiens
brenda
Groma, G.; Grskovic, I.; Schael, S.; Ehlen, H.W.; Wagener, R.; Fosang, A.; Aszodi, A.; Paulsson, M.; Brachvogel, B.; Zaucke, F.
Matrilin-4 is processed by ADAMTS-5 in late Golgi vesicles present in growth plate chondrocytes of defined differentiation state
Matrix Biol.
30
275-280
2011
Mus musculus
brenda
Shieh, H.S.; Tomasselli, A.G.; Mathis, K.J.; Schnute, M.E.; Woodard, S.S.; Caspers, N.; Williams, J.M.; Kiefer, J.R.; Munie, G.; Wittwer, A.; Malfait, A.M.; Tortorella, M.D.
Structure analysis reveals the flexibility of the ADAMTS-5 active site
Protein Sci.
20
735-744
2011
Homo sapiens (Q9UNA0)
brenda
Kumar, S.; Sharghi-Namini, S.; Rao, N.; Ge, R.
ADAMTS5 functions as an anti-angiogenic and anti-tumorigenic protein independent of its proteoglycanase activity
Am. J. Pathol.
181
1056-1068
2012
Homo sapiens
brenda
Ariyoshi, W.; Takahashi, N.; Hida, D.; Knudson, C.; Knudson, W.
Mechanisms involved in enhancement of the expression and function of aggrecanases by hyaluronan oligosaccharides
Arthritis Rheumatol.
64
187-197
2012
Bos taurus
brenda
Filou, S.; Stylianou, M.; Triantaphyllidou, I.E.; Papadas, T.; Mastronikolis, N.S.; Goumas, P.D.; Papachristou, D.J.; Ravazoula, P.; Skandalis, S.S.; Vynios, D.H.
Expression and distribution of aggrecanases in human larynx: ADAMTS-5/aggrecanase-2 is the main aggrecanase in laryngeal carcinoma
Biochimie
95
725-734
2013
Homo sapiens
brenda
Atobe, M.; Maekawara, N.; Ishiguro, N.; Sogame, S.; Suenaga, Y.; Kawanishi, M.; Suzuki, H.; Jinno, N.; Tanaka, E.; Miyoshi, S.
A series of thiazole derivatives bearing thiazolidin-4-one as non-competitive ADAMTS-5 (aggrecanase-2) inhibitors
Bioorg. Med. Chem. Lett.
23
2106-2110
2013
Homo sapiens, Homo sapiens (Q9UNA0)
brenda
Sogame, S.; Suenaga, Y.; Atobe, M.; Kawanishi, M.; Tanaka, E.; Miyoshi, S.
Discovery of a benzimidazole series of ADAMTS-5 (aggrecanase-2) inhibitors by scaffold hopping
Eur. J. Med. Chem.
71
250-258
2014
Homo sapiens (Q9UNA0)
brenda
Didangelos, A.; Mayr, U.; Monaco, C.; Mayr, M.
Novel role of ADAMTS-5 protein in proteoglycan turnover and lipoprotein retention in atherosclerosis
J. Biol. Chem.
287
19341-19345
2012
Mus musculus
brenda
Durham, T.; Klimkowski, V.; Rito, C.; Marimuthu, J.; Toth, J.; Liu, C.; Durbin, J.; Stout, S.; Adams, L.; Swearingen, C.; Lin, C.; Chambers, M.; Thirunavukkarasu, K.; Wiley, M.
Identification of potent and selective hydantoin inhibitors of aggrecanase-1 and aggrecanase-2 that are efficacious in both chemical and surgical models of osteoarthritis
J. Med. Chem.
57
10476-10485
2014
Homo sapiens
brenda
Filomia, F.; Saxena, P.; Durante, C.; De Rienzo, F.; Cocchi, M.; Menziani, M.
Computational insights into ADAMTS4, ADAMTS5 and MMP13 inhibitor selectivity
Mol. Inform.
31
421-430
2012
Homo sapiens (Q9UNA0)
-
brenda
Wang, Z.; Luo, J.; Iwamoto, S.; Chen, Q.
Matrilin-2 is proteolytically cleaved by ADAMTS-4 and ADAMTS-5
Molecules
19
8472-8487
2014
Homo sapiens (Q9UNA0), Homo sapiens
brenda
Apte, S.S.
Anti-ADAMTS5 monoclonal antibodies implications for aggrecanase inhibition in osteoarthritis
Biochem. J.
473
e1-e4
2016
Mus musculus (P59384), Mus musculus
brenda
Dancevic, C.M.; Gibert, Y.; Berger, J.; Smith, A.D.; Liongue, C.; Stupka, N.; Ward, A.C.; McCulloch, D.R.
The ADAMTS5 metzincin regulates zebrafish somite differentiation
Int. J. Mol. Sci.
19
E766
2018
Danio rerio
brenda
Fowkes, M.M.; Lim, N.H.
Purification and activity determination of ADAMTS-4 and ADAMTS-5 and their domain deleted mutants
Methods Mol. Biol.
2043
75-91
2020
Homo sapiens (Q9UNA0)
brenda
McMahon, M.; Ye, S.; Izzard, L.; Dlugolenski, D.; Tripp, R.A.; Bean, A.G.; McCulloch, D.R.; Stambas, J.
ADAMTS5 is a critical regulator of virus-specific T cell immunity
PLoS Biol.
14
e1002580
2016
Mus musculus (P59384)
brenda
Bauters, D.; Bedossa, P.; Lijnen, H.R.; Hemmeryckx, B.
Functional role of ADAMTS5 in adiposity and metabolic health
PLoS ONE
13
e0190595
2018
Mus musculus (P59384)
brenda
Aydos, O.S.; Yukselten, Y.; Ozkavukcu, S.; Sunguroglu, A.; Aydos, K.
ADAMTS1 and ADAMTS5 metalloproteases produced by Sertoli cells a potential diagnostic marker in azoospermia
Syst. Biol. Reprod. Med.
65
29-38
2019
Homo sapiens (Q8TE58), Homo sapiens
brenda
Chen, Z.; Du, F.; Zhang, R.; Wu, Q.; Lu, Z.; Zhang, R.L.; Wang, Q.
ADAMTS5 promotes permeability of the blood-brain barrier during Treponema pallidum subspecies pallidum invading the central nervous system
ACS Infect. Dis.
10
1222-1231
2024
Homo sapiens (Q9UNA0)
brenda
Shu, C.C.; Flannery, C.R.; Little, C.B.; Melrose, J.
Catabolism of fibromodulin in developmental rudiment and pathologic articular cartilage demonstrates novel roles for MMP-13 and ADAMTS-4 in C-terminal processing of SLRPs
Int. J. Mol. Sci.
20
579
2019
Mus musculus (Q9R001)
brenda
Scavenius, C.; Poulsen, E.C.; Thgersen, I.B.; Roebuck, M.; Frostick, S.; Bou-Gharios, G.; Yamamoto, K.; Deleuran, B.; Enghild, J.J.
Matrix-degrading protease ADAMTS-5 cleaves inter-alpha-inhibitor and releases active heavy chain 2 in synovial fluids from arthritic patients
J. Biol. Chem.
294
15495-15504
2019
Homo sapiens (Q9UNA0)
brenda
Hong, C.C.; Tang, A.T.; Detter, M.R.; Choi, J.P.; Wang, R.; Yang, X.; Guerrero, A.A.; Wittig, C.F.; Hobson, N.; Girard, R.; Lightle, R.; Moore, T.; Shenkar, R.; Polster, S.P.; Goddard, L.M.; Ren, A.A.; Leu, N.A.; Sterling, S.; Yang, J.; Li, L.; Chen, M.; Mericko-Ishizuka, P.; Dow, L.E.; Watanabe, H.; Schwaninger, M.; Min, W.; Marchuk, D. A.; Zheng, X.; Awad, I.A.; Kahn, M.L.
Cerebral cavernous malformations are driven by ADAMTS5 proteolysis of versican
J. Exp. Med.
217
e20200140
2020
Mus musculus (Q9R001)
brenda
Taylor, S.; Whitfield, M.; Barratt, J.; Didangelos, A.
The metalloproteinase ADAMTS5 is expressed by interstitial inflammatory cells in IgA nephropathy and is proteolytically active on the kidney matrix
J. Immunol.
205
2243-2254
2020
Homo sapiens (Q9UNA0)
brenda
Fowkes, M.M.; Troeberg, L.; Brennan, P.E.; Vincent, T.L.; Meldal, M.; Lim, N.H.
Development of selective ADAMTS-5 peptide substrates to monitor proteinase activity
J. Med. Chem.
66
3522-3539
2023
Homo sapiens (Q9UNA0)
brenda
Rogers-DeCotes, A.W.; Porto, S.C.; Dupuis, L.E.; Kern, C.B.
ADAMTS5 is required for normal trabeculated bone development in the mandibular condyle
Osteoarthritis Cartilage
29
547-557
2021
Mus musculus (Q9R001)
brenda
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