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(2R)-2-(biphenyl-4-ylsulfonyl)-3-(1H-indol-2-yl)propanoic acid
-
IC50: 0.0028 mM
(2R)-2-(biphenyl-4-ylsulfonyl)-3-phenylpropanoic acid
-
IC50: 0.0043 mM
(2R)-2-(biphenyl-4-ylsulfonyl)pentanedioic acid
-
IC50: 0.0011 mM
(2R)-2-(biphenyl-4-ylsulfonyl)propanoic acid
-
IC50: 0.0055 mM
(2R)-2-([[3'-(acetylamino)biphenyl-4-yl]sulfonyl]amino)-3-methylbutanoic acid
-
-
(2R)-2-([[3'-(aminomethyl)biphenyl-4-yl]sulfonyl]amino)-3-methylbutanoic acid
-
-
(2R)-2-([[3'-(hydroxymethyl)biphenyl-4-yl]sulfonyl]amino)-3-methylbutanoic acid
-
-
(2R)-2-([[4'-(acetylamino)biphenyl-4-yl]sulfonyl]amino)-3-methylbutanoic acid
-
-
(2R)-2-([[4'-(carbamoyloxy)biphenyl-4-yl]sulfonyl]amino)-3-methylbutanoic acid
-
-
(2R)-2-([[4'-(hydroxymethyl)biphenyl-4-yl]sulfonyl]amino)-3-methylbutanoic acid
-
-
(2R)-2-[(biphenyl-4-ylsulfonyl)amino]-3-methylbutanoic acid
-
-
(2R)-2-[[(3'-carbamoylbiphenyl-4-yl)sulfonyl]amino]-3-methylbutanoic acid
-
-
(2R)-2-[[(3'-cyanobiphenyl-4-yl)sulfonyl]amino]-3-methylbutanoic acid
-
-
(2R)-2-[[(3'-hydroxybiphenyl-4-yl)sulfonyl]amino]-3-methylbutanoic acid
-
-
(2R)-2-[[(4'-hydroxybiphenyl-4-yl)sulfonyl]amino]-3-methylbutanoic acid
-
-
(2R)-3-methyl-2-[([4'-[(methylcarbamoyl)oxy]biphenyl-4-yl]sulfonyl)amino]butanoic acid
-
-
(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
-
-
(2R,5R)-1-([4-[(5-fluoro-2-methylbenzyl)oxy]phenyl]sulfonyl)-N,5-dihydroxypiperidine-2-carboxamide
-
IC50: 145 nM
(2R,5R)-N,5-dihydroxy-1-([4-[(2,4-dichlorobenzyl)oxy]phenyl]sulfonyl)piperidine-2-carboxamide
-
IC50: 2.1 nM
(2R,5R)-N,5-dihydroxy-1-([4-[(2-bromobenzyl)oxy]phenyl]sulfonyl)piperidine-2-carboxamide
-
IC50: 16 nM
(2R,5R)-N,5-dihydroxy-1-([4-[(2-chloro-4-fluorobenzyl)oxy]phenyl]sulfonyl)piperidine-2-carboxamide
-
IC50: 0.5 nM
(2R,5R)-N,5-dihydroxy-1-([4-[(2-ethylbenzyl)oxy]phenyl]sulfonyl)piperidine-2-carboxamide
-
IC50: 67 nM
(2R,5R)-N,5-dihydroxy-1-([4-[(2-isopropylbenzyl)oxy]phenyl]sulfonyl)piperidine-2-carboxamide
-
78% inhibition of enzyme activity at 500 nM
(2R,5R)-N,5-dihydroxy-1-([4-[(2-methyl-3-fluorobenzyl)oxy]phenyl]sulfonyl)piperidine-2-carboxamide
-
IC50: 3.9 nM
(2R,5R)-N,5-dihydroxy-1-([4-[(2-methyl-4-fluorobenzyl)oxy]phenyl]sulfonyl)piperidine-2-carboxamide
-
IC50: 2.7 nM
(2R,5R)-N,5-dihydroxy-1-([4-[(2-methyl-5-fluorobenzyl)oxy]phenyl]sulfonyl)piperidine-2-carboxamide
-
IC50: 40 nM
(2R,5R)-N,5-dihydroxy-1-([4-[(2-methylbenzyl)oxy]phenyl]sulfonyl)piperidine-2-carboxamide
-
IC50: 38 nM
(2R,5R)-N,5-dihydroxy-1-([4-[(3-bromobenzyl)oxy]phenyl]sulfonyl)piperidine-2-carboxamide
-
57% inhibition of enzyme activity at 500 nM
(2R,5R)-N,5-dihydroxy-1-([4-[(3-methylbenzyl)oxy]phenyl]sulfonyl)piperidine-2-carboxamide
-
IC50: 100 nM
(2R,5R)-N,5-dihydroxy-1-([4-[(3-methylisothiazol-4-yl)methoxy]phenyl]sulfonyl)piperidine-2-carboxamide
-
76% inhibition of enzyme activity at 500 nM
(2R,5R)-N,5-dihydroxy-1-([4-[(4-bromobenzyl)oxy]phenyl]sulfonyl)piperidine-2-carboxamide
-
IC50: 100 nM
(2R,5R)-N,5-dihydroxy-1-([4-[(4-methylbenzyl)oxy]phenyl]sulfonyl)piperidine-2-carboxamide
-
19% inhibition of enzyme activity at 500 nM
(2R,5R)-N,5-dihydroxy-1-([4-[(4-methylisothiazol-5-yl)methoxy]phenyl]sulfonyl)piperidine-2-carboxamide
-
55% inhibition of enzyme activity at 500 nM
(2R,5R)-N,5-dihydroxy-1-[[4-(2-chloropyridin-4-ylmethoxy)phenyl]sulfonyl]piperidine-2-carboxamide
-
IC50: 18 nM
(2R,5R)-N,5-dihydroxy-1-[[4-(2-methylpyridin-3-ylmethoxy)phenyl]sulfonyl]piperidine-2-carboxamide
-
IC50: 91 nM
(2R,5R)-N,5-dihydroxy-1-[[4-(isoquinolin-4-ylmethoxy)phenyl]sulfonyl]piperidine-2-carboxamide
-
IC50: 100 nM
(2R,5R)-N,5-dihydroxy-1-[[4-(quinolin-4-ylmethoxy)phenyl]sulfonyl]piperidine-2-carboxamide
-
IC50: 15 nM
(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-optimizing 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
-
-
(E)-4-[2-(3,5-dihydroxyphenyl)ethenyl]1,2-benzenediol
-
i.e. piceatannol
(R)-2-(3-fluoro-4'-((5-oxo-5,6,7,8-tetrahydronaphthalen-2-yloxy)methyl)biphenyl-4-ylsulfonamido)-3-methylbutanoic acid
-
(R)-2-(4'-((2,8-bis(trifluoromethyl)quinolin-4-yloxy)methyl)biphenyl-4-ylsulfonamido)-3-methylbutanoic acid
-
(R)-2-(4'-((3-(dimethylamino)phenoxy)methyl)biphenyl-4-ylsulfonamido)-3-methylbutanoic acid
-
(R)-2-(4'-((3-acetylphenoxy)methyl)biphenyl-4-ylsulfonamido)-3-methylbutanoic acid
-
(R)-2-(4'-((3-benzoylphenoxy)methyl)biphenyl-4-ylsulfonamido)-3-methylbutanoic acid
-
(R)-2-(4'-((3-fluorophenoxy)methyl)biphenyl-4-ylsulfonamido)-3-methylbutanoic acid
-
(R)-2-(4'-((3-hydroxyphenoxy)methyl)biphenyl-4-ylsulfonamido)-3-methylbutanoic acid
-
(R)-2-(4'-((3-methoxyphenoxy)methyl)biphenyl-4-ylsulfonamido)-3-methylbutanoic acid
-
(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-(tert-butoxycarbonylamino)phenoxy)methyl)biphenyl-4-ylsulfonamido)-3-methylbutanoic acid
-
(R)-2-(4'-((4-acetylphenoxy)methyl)biphenyl-4-ylsulfonamido)-3-methylbutanoic acid
-
(R)-2-(4'-((4-fluorophenoxy)methyl)biphenyl-4-ylsulfonamido)-3-methylbutanoic acid
-
(R)-2-(4'-((4-isobutyrylphenoxy)methyl)biphenyl-4-ylsulfonamido)-3-methylbutanoic acid
-
(R)-2-(4'-((4-methoxyphenoxy)methyl)biphenyl-4-ylsulfonamido)-3-methylbutanoic acid
-
(R)-3-methyl-2-(4'-((3-methylquinolin-2-yloxy)methyl)biphenyl-4-ylsulfonamido)butanoic acid
-
(R)-3-methyl-2-(4'-((4-(6-methylpyridin-2-yloxy)phenoxy)methyl)biphenyl-4-ylsulfonamido)butanoic acid
-
(R)-3-methyl-2-(4'-((4-(morpholine-4-carbonyl)phenoxy)methyl)biphenyl-4-ylsulfonamido)butanoic acid
-
(R)-3-methyl-2-(4'-((4-(morpholinomethyl)phenoxy)methyl)biphenyl-4-ylsulfonamido)butanoic acid
-
(R)-3-methyl-2-(4'-((4-(pyridin-2-yloxy)phenoxy)methyl)biphenyl-4-ylsulfonamido)butanoic acid
-
(R)-3-methyl-2-(4'-((4-(pyrrolidine-1-carbonyl)phenoxy)methyl)biphenyl-4-ylsulfonamido)butanoic acid
-
(R)-3-methyl-2-(4'-((4-phenoxyphenoxy)methyl)biphenyl-4-ylsulfonamido)butanoic acid
-
(R)-3-methyl-2-(4'-((5-(trifluoromethyl)pyridin-2-yloxy)methyl)biphenyl-4-ylsulfonamido)butanoic acid
-
(R)-3-methyl-2-(4'-((5-oxo-5,6,7,8-tetrahydronaphthalen-2-yloxy)methyl)-3-(trifluoromethoxy)biphenyl-4-ylsulfonamido)butanoic acid
-
(R)-3-methyl-2-(4'-((5-oxo-5,6,7,8-tetrahydronaphthalen-2-yloxy)methyl)-3-(trifluoromethyl)biphenyl-4-ylsulfonamido)butanoic acid
-
(R)-3-methyl-2-(4'-((5-oxo-5,6,7,8-tetrahydronaphthalen-2-yloxy)methyl)biphenyl-4-ylsulfonamido)butanoic acid
-
(R)-3-methyl-2-(4'-((quinolin-2-yloxy)methyl)biphenyl-4-ylsulfonamido)butanoic acid
-
2-deoxyfluoroglucose
-
0.01 mM
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-1H-pyrrolo[3,4-c]quinoline-4-carboxamide
-
-
3-[(biphenyl-4-ylsulfonyl)amino]-4-methylpentanoic acid
-
IC50: 0.1 mM
3-[[(4'-[[(1R)-1-carboxy-2-methylpropyl]sulfamoyl]biphenyl-4-yl)oxy]methyl]benzoic acid
-
-
acetyl-DVQEFRGVTAVIRNH2
-
-
acetyl-HNEFRQRETYMVF-NH2
-
-
actinonin
-
0.01 mg/ml, 61% inhibition
alpha2-Macroglobulin
-
-
-
antibody 237-53
antibody 237-53 almost completely blocks the activity of the enzyme in a molar ratio of 1:5 (enzyme:antibody)
-
BB94
-
0.000524 mM, 85% inhibition, hydroxamate-based matrix metalloproteinase inhibitor
C-terminal 40-kDa fibronectin fragment
-
wild type enzyme IC50: 170 nM, complete inhibition at 750 nM
-
calcium pentosan polysulfate
-
no impact on gene expression, but directly inhibit the aggrecanase activity
-
chondroitin 6-sulfate
-
-
CT-1746
-
0.000048 mM, 50% inhibition, hydroxamate-based matrix metalloproteinase inhibitor
doxycycline
-
dose-dependently inhibits the activity of rhADAMTS4 in vitro
DPC
-
non-peptidomimetric hydroxamate matrix metalloproteinase inhibitor, IC50: 10 nM
EGTA
-
5 mM, complete inhibition
GGWGPWGPWGD
peptide representing the N-terminal region of the aggrecane TPS-1 motif containign the GAG binding motif, 0.017 mM, 50% inhibition
GGWGPWGPWGDCSRTCGGG
peptide containing both the GAG and CD36 binding motifs of aggrecan, 0.003 mM, 50% inhibition
hyaluronan
-
hyaluronan 800 kDA and 2700 kDa decreased IL1alpha-induced expression of aggrecanase-1 decreased
interleukin-1beta
lower mRNA level of aggrecan
-
Janus kinase 2 inhibitor
-
10 g/ml
-
Janus kinase 3 inhibitor
-
30 g/ml
-
LY294002
-
0.01 mM, reduces ADAMTS-4 expression
minocycline
-
dose-dependently inhibits the activity of rhADAMTS4 in vitro
N-(biphenyl-3-ylsulfonyl)-D-valine
-
IC50: 0.1 mM
N-(biphenyl-4-ylsulfonyl)-D-valine
-
IC50: 0.003 mM
N-(biphenyl-4-ylsulfonyl)-L-valine
-
IC50: 0.1 mM
N-(biphenyl-4-ylsulfonyl)-N-(pyridin-3-ylmethyl)-D-valine
-
IC50: 0.012 mM
N-(biphenyl-4-ylsulfonyl)-N-methyl-D-valine
-
IC50: 0.0016 mM
N-([3'-[(acetylamino)methyl]biphenyl-4-yl]sulfonyl)-D-valine
-
-
N-([4'-[(1-benzofuran-2-ylcarbonyl)amino]biphenyl-4-yl]sulfonyl)-D-valine
-
IC50: 0.0075 mM
N-([4'-[(1-benzofuran-2-ylcarbonyl)oxy]biphenyl-4-yl]sulfonyl)-D-valine
-
IC50: 0.00035 mM
N-([4'-[(2-cyanobenzyl)oxy]biphenyl-4-yl]sulfonyl)-D-valine
-
-
N-([4'-[(2-methylpyridin-4-yl)methoxy]biphenyl-4-yl]sulfonyl)-D-valine
-
-
N-([4'-[(2-methylquinolin-4-yl)methoxy]biphenyl-4-yl]sulfonyl)-D-valine
-
-
N-([4'-[(3-bromobenzyl)oxy]biphenyl-4-yl]sulfonyl)-D-valine
-
-
N-([4'-[(3-chlorobenzyl)oxy]biphenyl-4-yl]sulfonyl)-D-valine
-
-
N-([4'-[(3-cyanobenzyl)oxy]biphenyl-4-yl]sulfonyl)-D-valine
-
-
N-([4'-[(3-fluorobenzyl)oxy]biphenyl-4-yl]sulfonyl)-D-valine
-
-
N-([4'-[(3-hydroxybenzyl)oxy]biphenyl-4-yl]sulfonyl)-D-valine
-
-
N-([4'-[(3-nitrobenzyl)oxy]biphenyl-4-yl]sulfonyl)-D-valine
-
-
N-([4'-[(4-cyanobenzyl)oxy]biphenyl-4-yl]sulfonyl)-D-valine
-
-
N-([4'-[(benzoylamino)methyl]biphenyl-4-yl]sulfonyl)-D-valine
-
-
N-([4'-[(benzylcarbamoyl)oxy]biphenyl-4-yl]sulfonyl)-D-valine
-
-
N-([4'-[(furan-2-yloxy)carbonyl]biphenyl-4-yl]sulfonyl)-D-valine
-
IC50: 0.0116 mM
N-([4'-[(phenylcarbamoyl)oxy]biphenyl-4-yl]sulfonyl)-D-valine
-
-
N-([4'-[(phenylsulfonyl)oxy]biphenyl-4-yl]sulfonyl)-D-valine
-
-
N-([4'-[(Z)-2-(1-benzofuran-2-yl)ethenyl]biphenyl-4-yl]sulfonyl)-D-valine
-
IC50: 0.0004 mM
N-([4'-[2-(1-benzofuran-2-yl)-2-oxoethyl]biphenyl-4-yl]sulfonyl)-D-valine
-
IC50: 0.0038 mM
N-terminal domain of tissue inhibitor of metalloproteinases-3
-
all isoforms of ADAMTS-4 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 metalloproteinase P-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-[(2'-aminobiphenyl-4-yl)sulfonyl]-D-valine
-
IC50: 0.05 mM
N-[(2'-hydroxybiphenyl-4-yl)sulfonyl]-D-valine
-
IC50: 0.02 mM
N-[(2-aminobiphenyl-4-yl)sulfonyl]-D-valine
-
IC50: 0.03 mM
N-[(3'-hydroxybiphenyl-4-yl)sulfonyl]-D-valine
-
IC50: 0.009 mM
N-[(4'-hydroxybiphenyl-4-yl)sulfonyl]-D-valine
-
IC50: 0.0046 mM
N-[(4'-phenoxybiphenyl-4-yl)sulfonyl]-D-valine
-
-
N-[(4'-[1-[3-(trifluoromethyl)phenyl]ethoxy]biphenyl-4-yl)sulfonyl]-D-valine
-
-
N-[(4'-[[(3-methyl-1-benzofuran-2-yl)carbonyl]oxy]biphenyl-4-yl)sulfonyl]-D-valine
-
IC50: 0.000086 mM
N-[(4'-[[(3-methyl-1-benzofuran-2-yl)oxy]methyl]biphenyl-4-yl)sulfonyl]-D-valine
-
IC50: 0.0007 mM
N-[(4'-[[2-(trifluoromethyl)benzyl]oxy]biphenyl-4-yl)sulfonyl]-D-valine
-
-
N-[(4'-[[2-(trifluoromethyl)pyridin-4-yl]methoxy]biphenyl-4-yl)sulfonyl]-D-valine
-
-
N-[(4'-[[3-(methoxycarbonyl)benzyl]oxy]biphenyl-4-yl)sulfonyl]-D-valine
-
-
N-[(4'-[[3-(trifluoromethyl)benzyl]oxy]biphenyl-4-yl)sulfonyl]-D-valine
-
-
N-[(4'-[[4-(trifluoromethyl)benzyl]oxy]biphenyl-4-yl)sulfonyl]-D-valine
-
-
N-[(4'-[[6-(trifluoromethyl)pyridin-2-yl]methoxy]biphenyl-4-yl)sulfonyl]-D-valine
-
-
N-[(4'-[[acetyl(methyl)amino]methyl]biphenyl-4-yl)sulfonyl]-D-valine
-
-
N-[[(4R)-4-cyclopropyl-2,5-dioxoimidazolidin-4-yl]methyl]-5-(trifluoromethyl)-1-benzofuran-2-carboxamide
-
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
N-[[4'-(1-benzofuran-2-ylmethoxy)biphenyl-4-yl]sulfonyl]-D-valine
-
IC50: 0.0014 mM
N-[[4'-(benzyloxy)biphenyl-4-yl]sulfonyl]-D-valine
-
-
N-[[4'-(cyclohexylmethoxy)biphenyl-4-yl]sulfonyl]-D-valine
-
-
N-[[4'-(naphthalen-1-ylmethoxy)biphenyl-4-yl]sulfonyl]-D-valine
-
-
N-[[4'-(naphthalen-2-ylmethoxy)biphenyl-4-yl]sulfonyl]-D-valine
-
-
N-[[4'-(pyridin-2-ylmethoxy)biphenyl-4-yl]sulfonyl]-D-valine
-
-
N-[[4'-(pyridin-3-ylmethoxy)biphenyl-4-yl]sulfonyl]-D-valine
-
-
N-[[4'-(pyridin-4-ylmethoxy)biphenyl-4-yl]sulfonyl]-D-valine
-
-
N-[[4'-(quinolin-2-ylmethoxy)biphenyl-4-yl]sulfonyl]-D-valine
-
-
N-[[4'-(quinolin-4-ylmethoxy)biphenyl-4-yl]sulfonyl]-D-valine
-
-
N2-(biphenyl-4-ylcarbonyl)-N-(2-phenylpropan-2-yl)-L-alpha-glutamine
-
-
NL-71-101
-
0.02 mM, reduces ADAMTS-4 expression
o-phenanthroline
-
1 mM, complete inhibition of aggrecanase 1 and 2
parthenolide
-
0.005 mM, reduces ADAMTS-4 expression
PD98059
inhibition of MAP kinase signaling pathway result in inhibition of neurite outgrowth induced by ADAMTS4
phosphatidylinositol 3-kinase
-
reduces ADAMTS-4 expression
-
tetracycline
-
dose-dependently inhibits the activity of rhADAMTS4 in vitro
tissue inhibitor of matrix metalloproteinases-3
-
TIMP-3
-
Tissue inhibitor of metalloproteinase-1
-
150 nM or 270 nM
-
tissue inhibitor of metalloproteinases 3
-
tissue inhibitor of metalloproteinases-3
-
Tripterygium wilfordii Hook F extract
-
-
-
triptolide
-
600 nM, PG490
U0126
inhibition of MAP kinase signaling pathway result in inhibition of neurite outgrowth induced by ADAMTS4
XS309
0.002185 mM, 50% inhibition
(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-optimizing 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
AG3340
-
0.00066 mM, 50% inhibition, hydroxamate-based matrix metalloproteinase inhibitor
AG3340
-
non-peptidomimetric hydroxamate matrix metalloproteinase inhibitor, IC50: 120 nM
BB-16
-
0.000548 mM, 50% inhibition
BB-16
-
0.1 mM, complete inhibition of aggrecanase 1 and 2
BB-16
-
peptidomimetric hydroxamate, synthetic inhibitor originally targeted for matrix metalloproteinases, IC50: 150 nM
BB-16
0.000159 mM, 50% inhibition
EDTA
-
5 mM, complete inhibition
EDTA
-
1 mM, complete inhibition of aggrecanase 1 and 2
fibronectin
-
IC50: 110 nM
-
fibronectin
-
wild type enzyme IC50: 110 nM, complete inhibition at 500 nM
-
heparin
-
-
heparin
-
0.1 mg/ml, selective inhibition of full-length ADAMTS-4
marimastat
-
IC50: 210 nM
SC81956
-
-
SC81956
-
demonstrates noncompetitive inhibition kinetics
SE206
-
0.000137 mM, 50% inhibition
SE206
-
0.1 mM, complete inhibition of aggrecanase 1 and 2
SE206
-
macrocyclic derivate of BB-16, IC50: 76 nM
SE206
0.000076 mM, 50% inhibition
tissue inhibitor of metalloproteinases 3
-
-
-
tissue inhibitor of metalloproteinases 3
-
-
-
tissue inhibitor of metalloproteinases 3
-
20 nM, complete inhibition
-
tissue inhibitor of metalloproteinases-3
-
TIMP-3
-
tissue inhibitor of metalloproteinases-3
-
all isoforms of ADAMTS-4 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 of ADAMTS4 deletion mutants including DELTASp (DELTAArg693-Lys837, lacking the spacer domain)
-
additional information
-
no inhibitory effect of alpha1-antitrypsin
-
additional information
-
ADAMTS-4 is not inhibited by 125 nM or less tissue inhibitor of metalloproteinase-1
-
additional information
-
substrate specificity of ADAMTS-4 against recombinant aggrecan, aggrecan mutants V356A-V361A-E362D, V361Q-E362K, D360H-V361Q-E362K, S377Q lead to aggrecan cleavage inhibition
-
additional information
-
lower expression level in majority of primary tumors
-
additional information
-
down-regulation of IL-1beta-induced ADAMTS-4 activation by Ras knockdown or inhibition of reactive oxygen species by antioxidants along with ablation of MyD88, IRAK1, or TRAF6; inducing effect of IL-1beta partially blocked by knockdown of adaptor proteins MyD88, IRAK1 or TRAF6
-
additional information
-
design of ADAMTS-4 inhibitors. No inhibition observed with the ADAMTS-5 inhibitors: 2-[4-(benzyloxy)phenyl]-3-oxoisoindoline-4-carboxylic acid or 2-[4-(benzyloxy)phenyl]-N-hydroxy-3-oxoisoindoline-4-carboxamide
-
additional information
-
design and development for potent and selective inhibitors of ADAMTS-4 and ADAMTS-5
-
additional information
-
no inhibition by tissue inhibitor of metalloproteinases 1 or tissue inhibitor of metalloproteinases 2 at 100 nM
-
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0.0028
(2R)-2-(biphenyl-4-ylsulfonyl)-3-(1H-indol-2-yl)propanoic acid
Rattus norvegicus
-
IC50: 0.0028 mM
0.0043
(2R)-2-(biphenyl-4-ylsulfonyl)-3-phenylpropanoic acid
Rattus norvegicus
-
IC50: 0.0043 mM
0.0011
(2R)-2-(biphenyl-4-ylsulfonyl)pentanedioic acid
Rattus norvegicus
-
IC50: 0.0011 mM
0.0055
(2R)-2-(biphenyl-4-ylsulfonyl)propanoic acid
Rattus norvegicus
-
IC50: 0.0055 mM
0.02
(2R)-2-([[3'-(acetylamino)biphenyl-4-yl]sulfonyl]amino)-3-methylbutanoic acid
Homo sapiens
-
IC50 around 0.02 mM, pH and temperature not specified in the publication
0.0072
(2R)-2-([[3'-(aminomethyl)biphenyl-4-yl]sulfonyl]amino)-3-methylbutanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0021
(2R)-2-([[3'-(hydroxymethyl)biphenyl-4-yl]sulfonyl]amino)-3-methylbutanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.1
(2R)-2-([[4'-(acetylamino)biphenyl-4-yl]sulfonyl]amino)-3-methylbutanoic acid
Homo sapiens
-
IC50 around 0.1 mM, pH and temperature not specified in the publication
0.00042 - 0.0041
(2R)-2-([[4'-(carbamoyloxy)biphenyl-4-yl]sulfonyl]amino)-3-methylbutanoic acid
0.015
(2R)-2-([[4'-(hydroxymethyl)biphenyl-4-yl]sulfonyl]amino)-3-methylbutanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.003
(2R)-2-[(biphenyl-4-ylsulfonyl)amino]-3-methylbutanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0084
(2R)-2-[[(3'-carbamoylbiphenyl-4-yl)sulfonyl]amino]-3-methylbutanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.04
(2R)-2-[[(3'-cyanobiphenyl-4-yl)sulfonyl]amino]-3-methylbutanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.009
(2R)-2-[[(3'-hydroxybiphenyl-4-yl)sulfonyl]amino]-3-methylbutanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0046
(2R)-2-[[(4'-hydroxybiphenyl-4-yl)sulfonyl]amino]-3-methylbutanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.05
(2R)-3-methyl-2-[([4'-[(methylcarbamoyl)oxy]biphenyl-4-yl]sulfonyl)amino]butanoic acid
Homo sapiens
-
IC50 around 0.05 mM, pH and temperature not specified in the publication
0.000065
(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
0.0000011
(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
0.000145
(2R,5R)-1-([4-[(5-fluoro-2-methylbenzyl)oxy]phenyl]sulfonyl)-N,5-dihydroxypiperidine-2-carboxamide
Homo sapiens
-
IC50: 145 nM
0.0000021
(2R,5R)-N,5-dihydroxy-1-([4-[(2,4-dichlorobenzyl)oxy]phenyl]sulfonyl)piperidine-2-carboxamide
Homo sapiens
-
IC50: 2.1 nM
0.000016
(2R,5R)-N,5-dihydroxy-1-([4-[(2-bromobenzyl)oxy]phenyl]sulfonyl)piperidine-2-carboxamide
Homo sapiens
-
IC50: 16 nM
0.0000005
(2R,5R)-N,5-dihydroxy-1-([4-[(2-chloro-4-fluorobenzyl)oxy]phenyl]sulfonyl)piperidine-2-carboxamide
Homo sapiens
-
IC50: 0.5 nM
0.000067
(2R,5R)-N,5-dihydroxy-1-([4-[(2-ethylbenzyl)oxy]phenyl]sulfonyl)piperidine-2-carboxamide
Homo sapiens
-
IC50: 67 nM
0.0000039
(2R,5R)-N,5-dihydroxy-1-([4-[(2-methyl-3-fluorobenzyl)oxy]phenyl]sulfonyl)piperidine-2-carboxamide
Homo sapiens
-
IC50: 3.9 nM
0.0000027
(2R,5R)-N,5-dihydroxy-1-([4-[(2-methyl-4-fluorobenzyl)oxy]phenyl]sulfonyl)piperidine-2-carboxamide
Homo sapiens
-
IC50: 2.7 nM
0.00004
(2R,5R)-N,5-dihydroxy-1-([4-[(2-methyl-5-fluorobenzyl)oxy]phenyl]sulfonyl)piperidine-2-carboxamide
Homo sapiens
-
IC50: 40 nM
0.000038
(2R,5R)-N,5-dihydroxy-1-([4-[(2-methylbenzyl)oxy]phenyl]sulfonyl)piperidine-2-carboxamide
Homo sapiens
-
IC50: 38 nM
0.0001
(2R,5R)-N,5-dihydroxy-1-([4-[(3-methylbenzyl)oxy]phenyl]sulfonyl)piperidine-2-carboxamide
Homo sapiens
-
IC50: 100 nM
0.0001
(2R,5R)-N,5-dihydroxy-1-([4-[(4-bromobenzyl)oxy]phenyl]sulfonyl)piperidine-2-carboxamide
Homo sapiens
-
IC50: 100 nM
0.000018
(2R,5R)-N,5-dihydroxy-1-[[4-(2-chloropyridin-4-ylmethoxy)phenyl]sulfonyl]piperidine-2-carboxamide
Homo sapiens
-
IC50: 18 nM
0.000091
(2R,5R)-N,5-dihydroxy-1-[[4-(2-methylpyridin-3-ylmethoxy)phenyl]sulfonyl]piperidine-2-carboxamide
Homo sapiens
-
IC50: 91 nM
0.0001
(2R,5R)-N,5-dihydroxy-1-[[4-(isoquinolin-4-ylmethoxy)phenyl]sulfonyl]piperidine-2-carboxamide
Homo sapiens
-
IC50: 100 nM
0.000015
(2R,5R)-N,5-dihydroxy-1-[[4-(quinolin-4-ylmethoxy)phenyl]sulfonyl]piperidine-2-carboxamide
Homo sapiens
-
IC50: 15 nM
0.000003
(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
0.00018
(R)-2-(3-fluoro-4'-((5-oxo-5,6,7,8-tetrahydronaphthalen-2-yloxy)methyl)biphenyl-4-ylsulfonamido)-3-methylbutanoic acid
Mus musculus
-
0.0002
(R)-2-(4'-((2,8-bis(trifluoromethyl)quinolin-4-yloxy)methyl)biphenyl-4-ylsulfonamido)-3-methylbutanoic acid
Mus musculus
-
0.0049
(R)-2-(4'-((3-(dimethylamino)phenoxy)methyl)biphenyl-4-ylsulfonamido)-3-methylbutanoic acid
Mus musculus
-
0.001
(R)-2-(4'-((3-acetylphenoxy)methyl)biphenyl-4-ylsulfonamido)-3-methylbutanoic acid
Mus musculus
-
0.00023
(R)-2-(4'-((3-benzoylphenoxy)methyl)biphenyl-4-ylsulfonamido)-3-methylbutanoic acid
Mus musculus
-
0.0012
(R)-2-(4'-((3-fluorophenoxy)methyl)biphenyl-4-ylsulfonamido)-3-methylbutanoic acid
Mus musculus
-
0.0011
(R)-2-(4'-((3-hydroxyphenoxy)methyl)biphenyl-4-ylsulfonamido)-3-methylbutanoic acid
Mus musculus
-
0.0018
(R)-2-(4'-((3-methoxyphenoxy)methyl)biphenyl-4-ylsulfonamido)-3-methylbutanoic acid
Mus musculus
-
0.00008
(R)-2-(4'-((4-(4-fluorobenzoyl)phenoxy)methyl)biphenyl-4-ylsulfonamido)-3-methylbutanoic acid
Mus musculus
-
0.00009
(R)-2-(4'-((4-(cyclohexanecarbonyl)phenoxy)methyl)biphenyl-4-ylsulfonamido)-3-methylbutanoic acid
Mus musculus
-
0.00059
(R)-2-(4'-((4-(tert-butoxycarbonylamino)phenoxy)methyl)biphenyl-4-ylsulfonamido)-3-methylbutanoic acid
Mus musculus
-
0.00043
(R)-2-(4'-((4-acetylphenoxy)methyl)biphenyl-4-ylsulfonamido)-3-methylbutanoic acid
Mus musculus
-
0.0017
(R)-2-(4'-((4-fluorophenoxy)methyl)biphenyl-4-ylsulfonamido)-3-methylbutanoic acid
Mus musculus
-
0.0001
(R)-2-(4'-((4-isobutyrylphenoxy)methyl)biphenyl-4-ylsulfonamido)-3-methylbutanoic acid
Mus musculus
-
0.0016
(R)-2-(4'-((4-methoxyphenoxy)methyl)biphenyl-4-ylsulfonamido)-3-methylbutanoic acid
Mus musculus
-
0.0002
(R)-3-methyl-2-(4'-((3-methylquinolin-2-yloxy)methyl)biphenyl-4-ylsulfonamido)butanoic acid
Mus musculus
-
0.00073
(R)-3-methyl-2-(4'-((4-(6-methylpyridin-2-yloxy)phenoxy)methyl)biphenyl-4-ylsulfonamido)butanoic acid
Mus musculus
-
0.0052
(R)-3-methyl-2-(4'-((4-(morpholine-4-carbonyl)phenoxy)methyl)biphenyl-4-ylsulfonamido)butanoic acid
Mus musculus
-
0.006
(R)-3-methyl-2-(4'-((4-(morpholinomethyl)phenoxy)methyl)biphenyl-4-ylsulfonamido)butanoic acid
Mus musculus
-
0.0009
(R)-3-methyl-2-(4'-((4-(pyridin-2-yloxy)phenoxy)methyl)biphenyl-4-ylsulfonamido)butanoic acid
Mus musculus
-
0.0019
(R)-3-methyl-2-(4'-((4-(pyrrolidine-1-carbonyl)phenoxy)methyl)biphenyl-4-ylsulfonamido)butanoic acid
Mus musculus
-
0.0004
(R)-3-methyl-2-(4'-((4-phenoxyphenoxy)methyl)biphenyl-4-ylsulfonamido)butanoic acid
Mus musculus
-
0.0008
(R)-3-methyl-2-(4'-((5-(trifluoromethyl)pyridin-2-yloxy)methyl)biphenyl-4-ylsulfonamido)butanoic acid
Mus musculus
-
0.02
(R)-3-methyl-2-(4'-((5-oxo-5,6,7,8-tetrahydronaphthalen-2-yloxy)methyl)-3-(trifluoromethoxy)biphenyl-4-ylsulfonamido)butanoic acid
Mus musculus
-
0.0032
(R)-3-methyl-2-(4'-((5-oxo-5,6,7,8-tetrahydronaphthalen-2-yloxy)methyl)-3-(trifluoromethyl)biphenyl-4-ylsulfonamido)butanoic acid
Mus musculus
-
0.00023
(R)-3-methyl-2-(4'-((5-oxo-5,6,7,8-tetrahydronaphthalen-2-yloxy)methyl)biphenyl-4-ylsulfonamido)butanoic acid
Mus musculus
-
0.0004
(R)-3-methyl-2-(4'-((quinolin-2-yloxy)methyl)biphenyl-4-ylsulfonamido)butanoic acid
Mus musculus
-
0.015
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
0.00021
2-[4-(benzyloxy)phenyl]-2,3-dihydro-N-hydroxy-1-oxo-1H-pyrrolo[3,4-c]quinoline-4-carboxamide
Homo sapiens
-
37°C, pH and temperature not specified in the publication
0.1
3-[(biphenyl-4-ylsulfonyl)amino]-4-methylpentanoic acid
Rattus norvegicus
-
IC50: 0.1 mM
0.022
3-[[(4'-[[(1R)-1-carboxy-2-methylpropyl]sulfamoyl]biphenyl-4-yl)oxy]methyl]benzoic acid
Homo sapiens
-
IC50 around 0.022 mM, pH and temperature not specified in the publication
0.00012
AG3340
Bos taurus
-
non-peptidomimetric hydroxamate matrix metalloproteinase inhibitor, IC50: 120 nM
0.0000789
antibody 237-53
Homo sapiens
at pH and 37°C
-
0.00015
BB-16
Bos taurus
-
peptidomimetric hydroxamate, synthetic inhibitor originally targeted for matrix metalloproteinases, IC50: 150 nM
0.00017
C-terminal 40-kDa fibronectin fragment
Bos taurus
-
wild type enzyme IC50: 170 nM, complete inhibition at 750 nM
-
0.00001
DPC
Bos taurus
-
non-peptidomimetric hydroxamate matrix metalloproteinase inhibitor, IC50: 10 nM
0.000079 - 0.00021
marimastat
0.1
N-(biphenyl-3-ylsulfonyl)-D-valine
Rattus norvegicus
-
IC50: 0.1 mM
0.003
N-(biphenyl-4-ylsulfonyl)-D-valine
Rattus norvegicus
-
IC50: 0.003 mM
0.1
N-(biphenyl-4-ylsulfonyl)-L-valine
Rattus norvegicus
-
IC50: 0.1 mM
0.012
N-(biphenyl-4-ylsulfonyl)-N-(pyridin-3-ylmethyl)-D-valine
Rattus norvegicus
-
IC50: 0.012 mM
0.0016
N-(biphenyl-4-ylsulfonyl)-N-methyl-D-valine
Rattus norvegicus
-
IC50: 0.0016 mM
0.2
N-([3'-[(acetylamino)methyl]biphenyl-4-yl]sulfonyl)-D-valine
Homo sapiens
-
IC50 above 0.2 mM, pH and temperature not specified in the publication
0.0075
N-([4'-[(1-benzofuran-2-ylcarbonyl)amino]biphenyl-4-yl]sulfonyl)-D-valine
Rattus norvegicus
-
IC50: 0.0075 mM
0.00035
N-([4'-[(1-benzofuran-2-ylcarbonyl)oxy]biphenyl-4-yl]sulfonyl)-D-valine
Rattus norvegicus
-
IC50: 0.00035 mM
0.015
N-([4'-[(2-cyanobenzyl)oxy]biphenyl-4-yl]sulfonyl)-D-valine
Homo sapiens
-
pH and temperature not specified in the publication
0.0024
N-([4'-[(2-methylpyridin-4-yl)methoxy]biphenyl-4-yl]sulfonyl)-D-valine
Homo sapiens
-
pH and temperature not specified in the publication
0.0005
N-([4'-[(2-methylquinolin-4-yl)methoxy]biphenyl-4-yl]sulfonyl)-D-valine
Homo sapiens
-
pH and temperature not specified in the publication
0.00042
N-([4'-[(3-bromobenzyl)oxy]biphenyl-4-yl]sulfonyl)-D-valine
Homo sapiens
-
pH and temperature not specified in the publication
0.0004
N-([4'-[(3-chlorobenzyl)oxy]biphenyl-4-yl]sulfonyl)-D-valine
Homo sapiens
-
pH and temperature not specified in the publication
0.0008
N-([4'-[(3-cyanobenzyl)oxy]biphenyl-4-yl]sulfonyl)-D-valine
Homo sapiens
-
pH and temperature not specified in the publication
0.0026
N-([4'-[(3-fluorobenzyl)oxy]biphenyl-4-yl]sulfonyl)-D-valine
Homo sapiens
-
pH and temperature not specified in the publication
0.0037
N-([4'-[(3-hydroxybenzyl)oxy]biphenyl-4-yl]sulfonyl)-D-valine
Homo sapiens
-
pH and temperature not specified in the publication
0.00054
N-([4'-[(3-nitrobenzyl)oxy]biphenyl-4-yl]sulfonyl)-D-valine
Homo sapiens
-
pH and temperature not specified in the publication
0.0014
N-([4'-[(4-cyanobenzyl)oxy]biphenyl-4-yl]sulfonyl)-D-valine
Homo sapiens
-
pH and temperature not specified in the publication
0.1
N-([4'-[(benzoylamino)methyl]biphenyl-4-yl]sulfonyl)-D-valine
Homo sapiens
-
IC50 around 0.1 mM, pH and temperature not specified in the publication
0.025
N-([4'-[(benzylcarbamoyl)oxy]biphenyl-4-yl]sulfonyl)-D-valine
Homo sapiens
-
IC50 around 0.025 mM, pH and temperature not specified in the publication
0.0116
N-([4'-[(furan-2-yloxy)carbonyl]biphenyl-4-yl]sulfonyl)-D-valine
Rattus norvegicus
-
IC50: 0.0116 mM
0.0056
N-([4'-[(phenylcarbamoyl)oxy]biphenyl-4-yl]sulfonyl)-D-valine
Homo sapiens
-
pH and temperature not specified in the publication
0.0082
N-([4'-[(phenylsulfonyl)oxy]biphenyl-4-yl]sulfonyl)-D-valine
Homo sapiens
-
pH and temperature not specified in the publication
0.0004
N-([4'-[(Z)-2-(1-benzofuran-2-yl)ethenyl]biphenyl-4-yl]sulfonyl)-D-valine
Rattus norvegicus
-
IC50: 0.0004 mM
0.0038
N-([4'-[2-(1-benzofuran-2-yl)-2-oxoethyl]biphenyl-4-yl]sulfonyl)-D-valine
Rattus norvegicus
-
IC50: 0.0038 mM
0.05
N-[(2'-aminobiphenyl-4-yl)sulfonyl]-D-valine
Rattus norvegicus
-
IC50: 0.05 mM
0.02
N-[(2'-hydroxybiphenyl-4-yl)sulfonyl]-D-valine
Rattus norvegicus
-
IC50: 0.02 mM
0.03
N-[(2-aminobiphenyl-4-yl)sulfonyl]-D-valine
Rattus norvegicus
-
IC50: 0.03 mM
0.009
N-[(3'-hydroxybiphenyl-4-yl)sulfonyl]-D-valine
Rattus norvegicus
-
IC50: 0.009 mM
0.0046
N-[(4'-hydroxybiphenyl-4-yl)sulfonyl]-D-valine
Rattus norvegicus
-
IC50: 0.0046 mM
0.0132
N-[(4'-phenoxybiphenyl-4-yl)sulfonyl]-D-valine
Homo sapiens
-
pH and temperature not specified in the publication
0.0027
N-[(4'-[1-[3-(trifluoromethyl)phenyl]ethoxy]biphenyl-4-yl)sulfonyl]-D-valine
Homo sapiens
-
pH and temperature not specified in the publication
0.000086
N-[(4'-[[(3-methyl-1-benzofuran-2-yl)carbonyl]oxy]biphenyl-4-yl)sulfonyl]-D-valine
Rattus norvegicus
-
IC50: 0.000086 mM
0.0007
N-[(4'-[[(3-methyl-1-benzofuran-2-yl)oxy]methyl]biphenyl-4-yl)sulfonyl]-D-valine
Rattus norvegicus
-
IC50: 0.0007 mM
0.0091
N-[(4'-[[2-(trifluoromethyl)benzyl]oxy]biphenyl-4-yl)sulfonyl]-D-valine
Homo sapiens
-
pH and temperature not specified in the publication
0.0022
N-[(4'-[[2-(trifluoromethyl)pyridin-4-yl]methoxy]biphenyl-4-yl)sulfonyl]-D-valine
Homo sapiens
-
pH and temperature not specified in the publication
0.00076
N-[(4'-[[3-(methoxycarbonyl)benzyl]oxy]biphenyl-4-yl)sulfonyl]-D-valine
Homo sapiens
-
pH and temperature not specified in the publication
0.00031
N-[(4'-[[3-(trifluoromethyl)benzyl]oxy]biphenyl-4-yl)sulfonyl]-D-valine
Homo sapiens
-
pH and temperature not specified in the publication
0.0019
N-[(4'-[[4-(trifluoromethyl)benzyl]oxy]biphenyl-4-yl)sulfonyl]-D-valine
Homo sapiens
-
pH and temperature not specified in the publication
0.0047
N-[(4'-[[6-(trifluoromethyl)pyridin-2-yl]methoxy]biphenyl-4-yl)sulfonyl]-D-valine
Homo sapiens
-
pH and temperature not specified in the publication
0.2
N-[(4'-[[acetyl(methyl)amino]methyl]biphenyl-4-yl)sulfonyl]-D-valine
Homo sapiens
-
IC50 above 0.2 mM, pH and 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
0.0014
N-[[4'-(1-benzofuran-2-ylmethoxy)biphenyl-4-yl]sulfonyl]-D-valine
Rattus norvegicus
-
IC50: 0.0014 mM
0.0055
N-[[4'-(benzyloxy)biphenyl-4-yl]sulfonyl]-D-valine
Homo sapiens
-
pH and temperature not specified in the publication
0.075
N-[[4'-(cyclohexylmethoxy)biphenyl-4-yl]sulfonyl]-D-valine
Homo sapiens
-
IC50 above 0.075 mM, pH and temperature not specified in the publication
0.0014
N-[[4'-(naphthalen-1-ylmethoxy)biphenyl-4-yl]sulfonyl]-D-valine
Homo sapiens
-
pH and temperature not specified in the publication
0.0008
N-[[4'-(naphthalen-2-ylmethoxy)biphenyl-4-yl]sulfonyl]-D-valine
Homo sapiens
-
pH and temperature not specified in the publication
0.033
N-[[4'-(pyridin-2-ylmethoxy)biphenyl-4-yl]sulfonyl]-D-valine
Homo sapiens
-
pH and temperature not specified in the publication
0.03
N-[[4'-(pyridin-3-ylmethoxy)biphenyl-4-yl]sulfonyl]-D-valine
Homo sapiens
-
IC50 around 0.03 mM, pH and temperature not specified in the publication
0.0085
N-[[4'-(pyridin-4-ylmethoxy)biphenyl-4-yl]sulfonyl]-D-valine
Homo sapiens
-
pH and temperature not specified in the publication
0.0106
N-[[4'-(quinolin-2-ylmethoxy)biphenyl-4-yl]sulfonyl]-D-valine
Homo sapiens
-
pH and temperature not specified in the publication
0.001
N-[[4'-(quinolin-4-ylmethoxy)biphenyl-4-yl]sulfonyl]-D-valine
Homo sapiens
-
pH and temperature not specified in the publication
0.00021
N2-(biphenyl-4-ylcarbonyl)-N-(2-phenylpropan-2-yl)-L-alpha-glutamine
Homo sapiens
-
37°C, pH and temperature not specified in the publication
0.005
pyrogallol
Sus scrofa
-
pH 7.5, 37°C
0.000076
SE206
Bos taurus
-
macrocyclic derivate of BB-16, IC50: 76 nM
0.00042
(2R)-2-([[4'-(carbamoyloxy)biphenyl-4-yl]sulfonyl]amino)-3-methylbutanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0041
(2R)-2-([[4'-(carbamoyloxy)biphenyl-4-yl]sulfonyl]amino)-3-methylbutanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.00011
fibronectin
Bos taurus
-
IC50: 110 nM
-
0.00011
fibronectin
Bos taurus
-
wild type enzyme IC50: 110 nM, complete inhibition at 500 nM
-
0.000079
marimastat
Homo sapiens
-
pH 7.5, 37°C
0.00021
marimastat
Bos taurus
-
IC50: 210 nM
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Hughes, C.E.; Buttner, F.H.; Eidenmuller, B.; Caterson, B.; Bartnik, E.
Utilization of a recombinant substrate rAgg1 to study the biochemical properties of aggrecanase in cell culture systems
J. Biol. Chem.
272
20269-20274
1997
Bos taurus, Rattus norvegicus
brenda
Little, C.B.; Flannery, C.R.; Hughes, C.E.; Mort, J.S.; Roughley, P.J.; Dent, C.; Caterson, B.
Aggrecanase versus matrix metalloproteinases in the catabolism of the interglobular domain of aggrecan in vitro
Biochem. J.
344
61-68
1999
Bos taurus, Homo sapiens, Sus scrofa
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brenda
Sugimoto, K.; Takahashi, M.; Yamamoto, Y.; Shimada, K.; Tanzawa, K.
Identification of aggrecanase activity in medium of cartilage culture
J. Biochem.
126
449-455
1999
Bos taurus
brenda
Tortorella, M.D.; Burn, T.C.; Pratta, M.A.; Abbaszade, I.; Hollis, J.M.; Liu, R.; Rosenfeld, S.A.; Copeland, R.A.; Decicco, C.P.; Wynn, R.; Rockwell, A.; Yang, F.; Duke, J.L.; Solomon, K.; George, H.; Bruckner, R.; Nagase, H.; Itoh, Y.; Ellis, D.M.; Ross, H.; Wiswall, B.H.; Murphy, K.; Hillman, M.C., Jr.; Hollis, G.F.; Arner, E.C.; et al.
Purification and cloning of aggrecanase-1: a member of the ADAMTS family of proteins
Science
284
1664-1666
1999
Bos taurus, Homo sapiens (O75173)
brenda
Nakamura, H.; Fujii, Y.; Inoki, I.; Sugimoto, K.; Tanzawa, K.; Matsuki, H.; Miura, R.; Yamaguchi, Y.; Okada, Y.
Brevican is degraded by matrix metalloproteinases and aggrecanase-1 (ADAMTS4) at different sites
J. Biol. Chem.
275
38885-38890
2000
Homo sapiens (O75173)
brenda
Tortorella, M.D.; Pratta, M.; Liu, R.Q.; Austin, J.; Ross, O.H.; Abbaszade, I.; Burn, T.; Arner, E.
Sites of aggrecan cleavage by recombinant human aggrecanase-1 (ADAMTS-4)
J. Biol. Chem.
275
18566-18573
2000
Bos taurus, Homo sapiens (O75173), Homo sapiens
brenda
Tortorella, M.; Pratta, M.; Liu, R.Q.; Abbaszade, I.; Ross, H.; Burn, T.; Arner, E.
The thrombospondin motif of aggrecanase-1 (ADAMTS-4) is critical for aggrecan substrate recognition and cleavage
J. Biol. Chem.
275
25791-25797
2000
Homo sapiens (O75173), Homo sapiens
brenda
Satoh, K.; Suzuki, N.; Yokota, H.
ADAMTS-4 (a disintegrin and metalloproteinase with thrombospondin motifs) is transcriptionally induced in beta-amyloid treated rat astrocytes
Neurosci. Lett.
289
177-180
2000
Rattus norvegicus (Q9ESP7)
brenda
Sandy, J.D.; Westling, J.; Kenagy, R.D.; Iruela-Arispe, M.L.; Verscharen, C.; Rodriguez-Mazaneque, J.C.; Zimmermann, D.R.; Lemire, J.M.; Fischer, J.W.; Wight, T.N.; Clowes, A.W.
Versican V1 proteolysis in human aorta in vivo occurs at the Glu441-Ala442 bond, a site that is cleaved by recombinant ADAMTS-1 and ADAMTS-4
J. Biol. Chem.
276
13372-13378
2001
Homo sapiens, Homo sapiens (O75173)
brenda
Bluteau, G.; Conrozier, T.; Mathieu, P.; Vignon, E.; Herbage, D.; Mallein-Gerin, F.
Matrix metalloproteinase-1, -3, -13 and aggrecanase-1 and -2 are differentially expressed in experimental osteoarthritis
Biochim. Biophys. Acta
1526
147-158
2001
Oryctolagus cuniculus (Q9GLK6), Oryctolagus cuniculus (Q9GLK7), Oryctolagus cuniculus
brenda
Flannery, C.R.; Zeng, W.; Corcoran, C.; Collins-Racie, L.A.; Chockalingam, P.S.; Hebert, T.; Mackie, S.A.; McDonagh, T.; Crawford, T.K.; Tomkinson, K.N.; LaVallie, E.R.; Morris, E.A.
Autocatalytic cleavage of ADAMTS-4 (aggrecanase-1) reveals multiple glycosaminoglycan-binding sites
J. Biol. Chem.
277
42775-42780
2002
Homo sapiens (O75173)
brenda
Westling, J.; Fosang, A.J.; Last, K.; Thompson, V.P.; Tomkinson, K.N.; Hebert, T.; McDonagh, T.; Collins-Racie, L.A.; LaVallie, E.R.; Morris, E.A.; Sandy, J.D.
ADAMTS4 cleaves at the aggrecanase site (Glu373-Ala374) and secondarily at the matrix metalloproteinase site (Asn341-Phe342) in the aggrecan interglobular domain
J. Biol. Chem.
277
16059-16066
2002
Homo sapiens, Homo sapiens (O75173)
brenda
Gao, G.; Westling, J.; Thompson, V.P.; Howell, T.D.; Gottschall, P.E.; Sandy, J.D.
Activation of the proteolytic activity of ADAMTS4 (aggrecanase-1) by C-terminal truncation
J. Biol. Chem.
277
11034-11041
2002
Homo sapiens, Homo sapiens (O75173), Sus scrofa
brenda
Tortorella, M.D.; Liu, R.Q.; Burn, T.; Newton, R.C.; Arner, E.
Characterization of human aggrecanase 2 (ADAM-TS5): substrate specificity studies and comparison with aggrecanase 1 (ADAM-TS4)
Matrix Biol.
21
499-511
2002
Homo sapiens, Homo sapiens (O75173)
brenda
Miller, J.A.; Liu, R.Q.; Davis, G.L.; Pratta, M.A.; Trzaskos, J.M.; Copeland, R.A.
A microplate assay specific for the enzyme aggrecanase
Anal. Biochem.
314
260-265
2003
Bos taurus
brenda
Tortorella, M.D.; Arner, E.C.; Hills, R.; Gormley, J.; Fok, K.; Pegg, L.; Munie, G.; Malfait, A.M.
ADAMTS-4 (aggrecanase-1): N-terminal activation mechanisms
Arch. Biochem. Biophys.
444
34-44
2005
Bos taurus
brenda
Chockalingam, P.S.; Zeng, W.; Morris, E.A.; Flannery, C.R.
Release of hyaluronan and hyaladherins (aggrecan G1 domain and link proteins) from articular cartilage exposed to ADAMTS-4 (aggrecanase 1) or ADAMTS-5 (aggrecanase 2)
Arthritis Rheum.
50
2839-2848
2004
Homo sapiens
brenda
Behera, A.K.; Hildebrand, E.; Szafranski, J.; Hung, H.H.; Grodzinsky, A.J.; Lafyatis, R.; Koch, A.E.; Kalish, R.; Perides, G.; Steere, A.C.; Hu, L.T.
Role of aggrecanase 1 in Lyme arthritis
Arthritis Rheum.
54
3319-3329
2006
Bos taurus, Homo sapiens, Mus musculus, Mus musculus C3H/HEN
brenda
Liacini, A.; Sylvester, J.; Zafarullah, M.
Triptolide suppresses proinflammatory cytokine-induced matrix metalloproteinase and aggrecanase-1 gene expression in chondrocytes
Biochem. Biophys. Res. Commun.
327
320-327
2005
Homo sapiens
brenda
Westling, J.; Gottschall, P.E.; Thompson, V.P.; Cockburn, A.; Perides, G.; Zimmermann, D.R.; Sandy, J.D.
ADAMTS4 (aggrecanase-1) cleaves human brain versican V2 at Glu405-Gln406 to generate glial hyaluronate binding protein
Biochem. J.
377
787-795
2004
Homo sapiens
brenda
Yoshida, K.; Suzuki, Y.; Saito, A.; Fukuda, K.; Hamanishi, C.; Munakata, H.
Aggrecanase-1 (ADAMTS-4) interacts with a1-antitrypsin
Biochim. Biophys. Acta
1725
152-159
2005
Homo sapiens
brenda
Miwa, H.E.; Gerken, T.A.; Huynh, T.D.; Flory, D.M.; Hering, T.M.
Mammalian expression of full-length bovine aggrecan and link protein: Formation of recombinant proteoglycan aggregates and analysis of proteolytic cleavage by ADAMTS-4 and MMP-13
Biochim. Biophys. Acta
1760
472-486
2006
Homo sapiens
brenda
Noe, M.C.; Natarajan, V.; Snow, S.L.; Mitchell, P.G.; Lopresti-Morrow, L.; Reeves, L.M.; Yocum, S.A.; Carty, T.J.; Barberia, J.A.; Sweeney, F.J.; Liras, J.L.; Vaughn, M.; Hardink, J.R.; Hawkins, J.M.; Tokar, C.
Discovery of 3,3-dimethyl-5-hydroxypipecolic hydroxamate-based inhibitors of aggrecanase and MMP-13
Bioorg. Med. Chem. Lett.
15
2808-2811
2005
Homo sapiens
brenda
Xiang, J.S.; Hu, Y.; Rush, T.S.; Thomason, J.R.; Ipek, M.; Sum, P.E.; Abrous, L.; Sabatini, J.J.; Georgiadis, K.; Reifenberg, E.; Majumdar, M.; Morris, E.A.; Tam, S.
Synthesis and biological evaluation of biphenylsulfonamide carboxylate aggrecanase-1 inhibitors
Bioorg. Med. Chem. Lett.
16
311-316
2006
Rattus norvegicus
brenda
Cross, A.K.; Haddock, G.; Stock, C.J.; Allan, S.; Surr, J.; Bunning, R.A.; Buttle, D.J.; Woodroofe, M.N.
ADAMTS-1 and -4 are up-regulated following transient middle cerebral artery occlusion in the rat and their expression is modulated by TNF in cultured astrocytes
Brain Res.
1088
19-30
2006
Homo sapiens, Rattus norvegicus
brenda
Liu, R.; Trzaskos, J.M.
Aggrecanase: The family and its inhibitors
Curr. Med. Chem. Anti-Inflamm. Anti-Allergy
4
251-264
2005
Bos taurus
-
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
Cross, A.K.; Haddock, G.; Surr, J.; Plumb, J.; Bunning, R.A.; Buttle, D.J.; Woodroofe, M.N.
Differential expression of ADAMTS-1, -4, -5 and TIMP-3 in rat spinal cord at different stages of acute experimental autoimmune encephalomyelitis
J. Autoimmun.
26
16-23
2006
Rattus norvegicus
brenda
Gao, G.; Plaas, A.; Thompson, V.P.; Jin, S.; Zuo, F.; Sandy, J.D.
ADAMTS4 (aggrecanase-1) activation on the cell surface involves C-terminal cleavage by glycosylphosphatidyl inositol-anchored membrane type 4-matrix metalloproteinase and binding of the activated proteinase to chondroitin sulfate and heparan sulfate on syndecan-1
J. Biol. Chem.
279
10042-10051
2004
Homo sapiens
brenda
Kashiwagi, M.; Enghild, J.J.; Gendron, C.; Hughes, C.; Caterson, B.; Itoh, Y.; Nagase, H.
Altered Proteolytic Activities of ADAMTS-4 Expressed by C-terminal Processing
J. Biol. Chem.
279
10109-10119
2004
Sus scrofa
brenda
Hashimoto, G.; Shimoda, M.; Okada, Y.
ADAMTS4 (aggrecanase-1) interaction with the C-terminal domain of fibronectin inhibits proteolysis of aggrecan
J. Biol. Chem.
279
32483-32491
2004
Bos taurus
brenda
Wainwright, S.D.; Bondeson, J.; Hughes, C.E.
An alternative spliced transcript of ADAMTS4 is present in human synovium from OA patients
Matrix Biol.
25
317-320
2006
Homo sapiens
brenda
Cross, N.A.; Chandrasekharan, S.; Jokonya, N.; Fowles, A.; Hamdy, F.C.; Buttle, D.J.; Eaton, C.L.
The expression and regulation of ADAMTS-1, -4, -5, -9, and -15, and TIMP-3 by TGFbeta1 in prostate cells: relevance to the accumulation of versican
Prostate
63
269-275
2005
Homo sapiens
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
Wagsaeter, D.; Bjoerk, H.; Zhu, C.; Bjoerkegren, J.; Valen, G.; Hamsten, A.; Eriksson, P.
ADAMTS-4 and -8 are inflammatory regulated enzymes expressed in macrophage-rich areas of human atherosclerotic plaques
Atherosclerosis
196
514-522
2008
Homo sapiens
brenda
Wittwer, A.J.; Hills, R.L.; Keith, R.H.; Munie, G.E.; Arner, E.C.; Anglin, C.P.; Malfait, A.M.; Tortorella, M.D.
Substrate-dependent inhibition kinetics of an active site-directed inhibitor of ADAMTS-4 (aggrecanase 1)
Biochemistry
46
6393-6401
2007
Mus musculus
brenda
El Mabrouk, M.; Sylvester, J.; Zafarullah, M.
Signaling pathways implicated in oncostatin M-induced aggrecanase-1 and matrix metalloproteinase-13 expression in human articular chondrocytes
Biochim. Biophys. Acta
1773
309-320
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
Bos taurus, Homo sapiens, Mus musculus, Sus scrofa
brenda
Hills, R.; Mazzarella, R.; Fok, K.; Liu, M.; Nemirovskiy, O.; Leone, J.; Zack, M.D.; Arner, E.C.; Viswanathan, M.; Abujoub, A.; Muruganandam, A.; Sexton, D.J.; Bassill, G.J.; Sato, A.K.; Malfait, A.M.; Tortorella, M.D.
Identification of an ADAMTS-4 cleavage motif using phage display leads to the development of fluorogenic peptide substrates and reveals matrilin-3 as a novel substrate
J. Biol. Chem.
282
11101-11109
2007
Homo sapiens
brenda
Lauer-Fields, J.L.; Minond, D.; Sritharan, T.; Kashiwagi, M.; Nagase, H.; Fields, G.B.
Substrate conformation modulates aggrecanase (ADAMTS-4) affinity and sequence specificity. Suggestion of a common topological specificity for functionally diverse proteases
J. Biol. Chem.
282
142-150
2007
Homo sapiens
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
Wayne, G.J.; Deng, S.J.; Amour, A.; Borman, S.; Matico, R.; Carter, H.L.; Murphy, G.
TIMP-3 inhibition of ADAMTS-4 (aggrecanase-1) is modulated by interactions between aggrecan and the C-terminal domain of ADAMTS-4
J. Biol. Chem.
282
20991-20998
2007
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
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 (Q9ESP7)
brenda
Yatabe, T.; Mochizuki, S.; Takizawa, M.; Chijiiwa, M.; Okada, A.; Kimura, T.; Fujita, Y.; Matsumoto, H.; Toyama, Y.; Okada, Y.
Hyaluronan inhibits expression of ADAMTS4 (aggrecanase-1) in human osteoarthritic chondrocytes
Ann. Rheum. Dis.
68
1051-1058
2009
Homo sapiens
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
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 (Q8BNJ2)
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 (O75173)
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
Ahmad, R.; Sylvester, J.; Ahmad, M.; Zafarullah, M.
Adaptor proteins and Ras synergistically regulate IL-1-induced ADAMTS-4 expression in human chondrocytes
J. Immunol.
182
5081-5087
2009
Homo sapiens
brenda
Frank, J.E.; Thompson, V.P.; Brown, M.P.; Sandy, J.D.
Removal of O-linked and N-linked oligosaccharides is required for optimum detection of NITEGE neoepitope on ADAMTS4-digested fetal aggrecans: implications for specific N-linked glycan-dependent aggrecanolysis at Glu373-Ala374
Osteoarthritis Cartilage
17
777-781
2008
Homo sapiens (O75173), Homo sapiens
brenda
Cheung, K.S.; Hashimoto, K.; Yamada, N.; Roach, H.I.
Expression of ADAMTS-4 by chondrocytes in the surface zone of human osteoarthritic cartilage is regulated by epigenetic DNA de-methylation
Rheumatol. Int.
29
525-534
2009
Homo sapiens (O75173), Homo sapiens
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
brenda
Zha, Y.; Chen, Y.; Xu, F.; Li, T.; Zhao, C.; Cui, L.
ADAMTS4 level in patients with stable coronary artery disease and acute coronary syndromes
Biomed. Pharmacother.
64
160-164
2010
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
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
brenda
Weaver, M.S.; Workman, G.; Cardo-Vila, M.; Arap, W.; Pasqualini, R.; Sage, E.H.
Processing of the matricellular protein hevin in mouse brain is dependent on ADAMTS4
J. Biol. Chem.
285
5868-5877
2010
Mus musculus
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
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
Hu, Y.; Xing, L.; Thomason, J.R.; Xiang, J.; Ipek, M.; Guler, S.; Li, H.; Sabatini, J.; Chockalingam, P.; Reifenberg, E.; Sheldon, R.; Morris, E.A.; Georgiadis, K.E.; Tam, S.
Continued exploration of biphenylsulfonamide scaffold as a platform for aggrecanase-1 inhibition
Bioorg. Med. Chem. Lett.
21
6800-6803
2011
Homo sapiens
brenda
Hsu, Y.P.; Staton, C.A.; Cross, N.; Buttle, D.J.
Anti-angiogenic properties of ADAMTS-4 in vitro
Int. J. Exp. Pathol.
93
70-77
2012
Homo sapiens
brenda
Verma, P.; Dalal, K.
ADAMTS-4 and ADAMTS-5: key enzymes in osteoarthritis
J. Cell. Biochem.
112
3507-3514
2011
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 (O75173), Homo sapiens
brenda
Rao, N.; Ke, Z.; Liu, H.; Ho, C.; Kumar, S.; Xiang, W.; Zhu, Y.; Ge, R.
ADAMTS4 and its proteolytic fragments differentially affect melanoma growth and angiogenesis in mice
Int. J. Cancer
133
294-306
2013
Mus musculus (Q8BNJ2)
brenda
Obika, M.; Vernon, R.; Gooden, M.; Braun, K.; Chan, C.; Wight, T.
ADAMTS-4 and biglycan are expressed at high levels and co-localize to podosomes during endothelial cell tubulogenesis in vitro
J. Histochem. Cytochem.
62
34-49
2014
Homo sapiens (Q75173)
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 (O75173)
brenda
Tauchi, R.; Imagama, S.; Natori, T.; Ohgomori, T.; Muramoto, A.; Shinjo, R.; Matsuyama, Y.; Ishiguro, N.; Kadomatsu, K.
The endogenous proteoglycan-degrading enzyme ADAMTS-4 promotes functional recovery after spinal cord injury
J. Neuroinflammation
9
53
2012
Rattus norvegicus (Q9ESP7)
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 (O75173)
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 (O75173), Homo sapiens
brenda
Roberts, S.; Evans, H.; Wright, K.; van Niekerk, L.; Caterson, B.; Richardson, J.; Kumar, K.; Kuiper, J.
ADAMTS-4 activity in synovial fluid as a biomarker of inflammation and effusion
Osteoarthritis Cartilage
23
1622-1626
2015
Homo sapiens (O75173)
brenda
Walter, S.; Jumpertz, T.; Huettenrauch, M.; Ogorek, I.; Gerber, H.; Storck, S.E.; Zampar, S.; Dimitrov, M.; Lehmann, S.; Lepka, K.; Berndt, C.; Wiltfang, J.; Becker-Pauly, C.; Beher, D.; Pietrzik, C.U.; Fraering, P.C.; Wirths, O.; Weggen, S.
The metalloprotease ADAMTS4 generates N-truncated A?4-x species and marks oligodendrocytes as a source of amyloidogenic peptides in Alzheimers disease
Acta Neuropathol.
137
239-257
2019
Mus musculus (Q8BNJ2), Mus musculus
brenda
Shiraishi, A.; Mochizuki, S.; Miyakoshi, A.; Kojoh, K.; Okada, Y.
Development of human neutralizing antibody to ADAMTS4 (aggrecanase-1) and ADAMTS5 (aggrecanase-2)
Biochem. Biophys. Res. Commun.
469
62-69
2016
Homo sapiens (O75173), Homo sapiens
brenda
Durham, T.B.; Marimuthu, J.; Toth, J.L.; Liu, C.; Adams, L.; Mudra, D.R.; Swearingen, C.; Lin, C.; Chambers, M.G.; Thirunavukkarasu, K.; Wiley, M.R.
A highly selective hydantoin inhibitor of aggrecanase-1 and aggrecanase-2 with a low projected human dose
J. Med. Chem.
60
5933-5939
2017
Homo sapiens (O75173), Homo sapiens
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 (O75173)
brenda
Fontanil, T.; Alvarez-Teijeiro, S.; Villaronga, M.A.; Mohamedi, Y.; Solares, L.; Moncada-Pazos, A.; Vega, J.A.; Garcia-Suarez, O.; Perez-Basterrechea, M.; Garcia-Pedrero, J.M.; Obaya, A.J.; Cal, S.
Cleavage of fibulin-2 by the aggrecanases ADAMTS-4 and ADAMTS-5 contributes to the tumorigenic potential of breast cancer cells
Oncotarget
8
13716-13729
2017
Homo sapiens (O75173)
brenda
Ren, P.; Hughes, M.; Krishnamoorthy, S.; Zou, S.; Zhang, L.; Wu, D.; Zhang, C.; Curci, J.A.; Coselli, J.S.; Milewicz, D.M.; LeMaire, S.A.; Shen, Y.H.
Critical role of ADAMTS-4 in the development of sporadic aortic aneurysm and dissection in mice
Sci. Rep.
7
12351
2017
Mus musculus (Q8BNJ2), Mus musculus
brenda