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(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Ala-S-[(4-methoxyphenyl)methyl]Cys-Trp-Ala-Arg-N3-(2,4-dinitrophenyl)-L-2,3-diamino propionylamide + H2O
(7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Ala + S-[(4-methoxyphenyl)methyl]Cys-Trp-Ala-Arg-N3-(2,4-dinitrophenyl)-L-2,3-diamino propionylamide
-
-
-
?
aggrecan + H2O
?
-
28 kDa N-terminal domain, cartilage proteoglycan encapsulated in polyacrylamide beads
-
?
alpha1-antitrypsin inhibitor + H2O
?
-
-
-
?
alpha1-protease inhibitor + H2O
?
carboxymethylated transferrin + H2O
?
-
28 kDa N-terminal domain
-
?
dansyl-Ala-Ala-Ala-S-(phenylmethyl)cysteine-Trp-Ala-Arg-NH2 + H2O
dansyl-Ala-Ala-Ala + S-(phenylmethyl)cysteine-Trp-Ala-Arg-NH2
-
-
-
?
dansyl-Pro-Leu-Ala-(2S)-2-aminoheptanoyl-Trp-Ala-Arg-NH2 + H2O
dansyl-Pro-Leu-Ala + (2S)-2-aminoheptanoyl-Trp-Ala-Arg-NH2
-
-
-
?
dansyl-Pro-Leu-Ala-(2S)-2-aminooctanoyl-Trp-Ala-Arg-NH2 + H2O
dansyl-Pro-Leu-Ala + (2S)-2-aminooctanoyl-Trp-Ala-Arg-NH2
-
-
-
?
dansyl-Pro-Leu-Ala-(5-phenyl)Nva-Trp-Ala-Arg-NH2 + H2O
dansyl-Pro-Leu-Ala + (5-phenyl)Nva-Trp-Ala-Arg-NH2
-
-
-
?
dansyl-Pro-Leu-Ala-Leu-Trp-Ala-Arg-NH2 + H2O
?
dansyl-Pro-Leu-Ala-Met-Trp-Ala-Arg-NH2 + H2O
?
dansyl-Pro-Leu-Ala-Nle-Trp-Ala-Arg-NH2 + H2O
?
-
-
-
?
dansyl-Pro-Leu-Ala-Phe-Trp-Ala-Arg-NH2 + H2O
?
-
-
-
?
dansyl-Pro-Leu-Ala-S-(phenylmethyl)Cys-Trp-Ala-Arg-NH2 + H2O
dansyl-Pro-Leu-Ala + S-(phenylmethyl)Cys-Trp-Ala-Arg-NH2
-
-
-
?
dansyl-Pro-Leu-Ala-S-p-methoxybenzylcysteine-Trp-Ala-Arg-NH2 + H2O
?
-
wild-type and mutants Q215R and Q215L, mutant Q215Y shows no activity with this substrate
-
?
dansyl-Pro-Leu-Ala-S-[(4-methoxyphenyl)methyl]Cys-Trp-Ala-Arg-NH2 + H2O
dansyl-Pro-Leu-Ala + S-[(4-methoxyphenyl)methyl]Cys-Trp-Ala-Arg-NH2
dansyl-Pro-Leu-Ala-S-[(4-methoxyphenyl)methyl]Ser-Trp-Ala-Arg-NH2 + H2O
dansyl-Pro-Leu-Ala + S-[(4-methoxyphenyl)methyl]Ser-Trp-Ala-Arg-NH2
-
-
-
?
dansyl-Pro-Leu-Phe-S-(phenylmethyl)Cys-Trp-Ala-Arg-NH2 + H2O
dansyl-Pro-Leu-Phe + S-(phenylmethyl)Cys-Trp-Ala-Arg-NH2
-
-
-
?
Fibronectin + H2O
?
-
28 kDa N-terminal domain
-
?
GAAGAMFLEA + H2O
GAAGA + MFLEA
-
-
-
?
GGAANLVRGG + H2O
GGAAN + LVRGG
-
-
-
?
GGPLALWARGG + H2O
GGPLA + LWARGG
-
-
-
?
GGPLGLYAGG + H2O
GGPLG + LYAGG
-
-
-
?
GGQPRGVWGG + H2O
GGQPRG + VWGG
-
-
-
?
GGTDAWLSGG + H2O
GGTDA + WLSGG
-
-
-
?
GGYAELRMGG + H2O
GGYAE + LRMGG
-
best substrate
-
?
Human alpha1-proteinase inhibitor + H2O
?
-
preferred cleavage site: (A)/(G/A)(A)(M)(F/A)(L) (P3-P3') inability of Xenopus alpha1-proteinase inhibitor to be cleaved
-
-
?
insulin-like growth factor-binding protein-1 + H2O
2 peptides of 16 and 9 kDa MW
-
specific for, cleavage site is the His140-Val141 bond
-
?
laminin receptor precursor + H2O
?
additional information
?
-
alpha1-protease inhibitor + H2O
?
-
-
-
?
alpha1-protease inhibitor + H2O
?
-
-
-
?
alpha1-protease inhibitor + H2O
?
-
-
-
?
alpha1-protease inhibitor + H2O
?
-
wild-type enzyme and mutants Q215L, Q215R and Q215Y
-
?
casein + H2O
?
-
-
-
?
casein + H2O
?
-
only recombinant processed enzyme mutant A235P lacking the N-terminal prodomain and 175 amino acid residues of the C-terminus
-
?
casein + H2O
?
-
28 kDa N-terminal domain
-
?
casein + H2O
?
-
only recombinant processed enzyme lacking the N-terminal prodomain and 175 amino acid residues of the C-terminus
-
?
collagen type IV + H2O
?
-
only recombinant processed enzyme mutant A235P lacking the N-terminal prodomain and 175 amino acid residues of the C-terminus
-
?
collagen type IV + H2O
?
-
only recombinant processed enzyme lacking the N-terminal prodomain and 175 amino acid residues of the C-terminus
-
?
collagen type IV + H2O
?
-
only unfolded collagen, 28 kDa N-terminal domain
-
?
collagen VI + H2O
?
-
MMP11 cleaves the native alpha3 chain of collagen VI, which is an adipocyte-related extracellular matrix component. Extracellular proteolytic processing of this chain is required for correct collagen VI folding. MMP11-deficient fat tissue is less cohesive and exhibits collagen VI alteration, dramatic adipocyte plasma and basement membrane abnormalities and lipid leakage. MMP11 is thus required for correct collagen VI folding and therefore for fat tissue cohesion and adipocyte function. The native alpha3 chain of collagen VI constitutes a specific MMP11 substrate. This MMP11 collagenolytic activity is functional in fat tissue ontogenesis as well as during cancer invasive steps
-
-
?
collagen VI + H2O
?
-
MMP11 cleaves the native alpha3 chain of collagen VI, which is an adipocyte-related extracellular matrix component. Extracellular proteolytic processing of this chain is required for correct collagen VI folding. MMP11-deficient fat tissue is less cohesive and exhibits collagen VI alteration, dramatic adipocyte plasma and basement membrane abnormalities and lipid leakage. MMP11 is thus required for correct collagen VI folding and therefore for fat tissue cohesion and adipocyte function. The native alpha3 chain of collagen VI constitutes a specific MMP11 substrate. This MMP11 collagenolytic activity is functional in fat tissue ontogenesis as well as during cancer invasive steps
-
-
?
dansyl-Pro-Leu-Ala-Leu-Trp-Ala-Arg-NH2 + H2O
?
-
-
-
?
dansyl-Pro-Leu-Ala-Leu-Trp-Ala-Arg-NH2 + H2O
?
-
wild-type enzyme and mutants Q215L, Q215R and Q215Y
-
?
dansyl-Pro-Leu-Ala-Met-Trp-Ala-Arg-NH2 + H2O
?
-
-
-
-
?
dansyl-Pro-Leu-Ala-Met-Trp-Ala-Arg-NH2 + H2O
?
-
-
-
?
dansyl-Pro-Leu-Ala-S-[(4-methoxyphenyl)methyl]Cys-Trp-Ala-Arg-NH2 + H2O
dansyl-Pro-Leu-Ala + S-[(4-methoxyphenyl)methyl]Cys-Trp-Ala-Arg-NH2
-
-
-
-
?
dansyl-Pro-Leu-Ala-S-[(4-methoxyphenyl)methyl]Cys-Trp-Ala-Arg-NH2 + H2O
dansyl-Pro-Leu-Ala + S-[(4-methoxyphenyl)methyl]Cys-Trp-Ala-Arg-NH2
-
-
-
?
Gelatin + H2O
?
-
-
-
?
Gelatin + H2O
?
-
28 kDa N-terminal domain, low activity
-
?
Laminin + H2O
?
-
only recombinant processed enzyme mutant A235P lacking the N-terminal prodomain and 175 amino acid residues of the C-terminus
-
?
Laminin + H2O
?
-
28 kDa N-terminal domain
-
?
Laminin + H2O
?
-
only recombinant processed enzyme lacking the N-terminal prodomain and 175 amino acid residues of the C-terminus
-
?
laminin receptor precursor + H2O
?
-
-
-
-
?
laminin receptor precursor + H2O
?
-
-
-
-
?
laminin receptor precursor + H2O
?
-
laminin receptor precursor is a likely in vivo substrate of stromelysin-3. Its cleavage may alter cell-extracellular matrix interaction, thus playing a role in mediating the effects of stromelysin-3 on cell fate and behavior observed during development and pathogenesis. Human laminin receptor precursor is cleaved by stromelysin-3 at the same two sites as in Xenopus laminin receptor precursor, yielding two N-terminal fragments of sizes identical to the corresponding Xenopus laminin receptor precursor fragments due to amino acid insertion in the C-terminus part of Xenopus laminin receptor precursor
-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
?
protein + H2O
peptides
-
substrate specificity, enzyme prefers 2 consensus sequences: 1. A(A/Q)(N/A)_(L/Y)(T/V/M/R)(R/K) and 2. G(G/A)E_LR, with _ marking the cleavage sites, enzyme also cleaves peptides containing Ala in position 3, Ala in position 1, and Leu/Tyr in position 1', peptides with proline in position 3 are poor substrates
-
?
protein + H2O
peptides
-
enzyme is involved in both physiological and pathological tissue remodeling processes, including those associated with cancer progression
-
?
protein + H2O
peptides
-
enzyme plays a role in tumor progression and wound healing
-
?
protein + H2O
peptides
-
the enzyme promotes and modulates tumor progression
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
?
protein + H2O
peptides
-
-
?
protein + H2O
peptides
-
substrate specificity
-
?
protein + H2O
peptides
-
enzyme is involved in both physiological and pathological tissue remodeling processes, including those associated with cancer progression
-
?
protein + H2O
peptides
-
the enzyme promotes and modulates tumor progression
-
?
protein + H2O
peptides
-
-
?
additional information
?
-
-
enzyme shows mild caseinolytic activity
-
-
?
additional information
?
-
enzyme shows mild caseinolytic activity
-
-
?
additional information
?
-
the recombinant peptide exhibits both caseinolytic and gelatinase activities without requiring activation by 4-aminophenylmercuric acetate
-
-
?
additional information
?
-
-
the recombinant peptide exhibits both caseinolytic and gelatinase activities without requiring activation by 4-aminophenylmercuric acetate
-
-
?
additional information
?
-
-
no activity with casein or gelatin
-
?
additional information
?
-
-
wild-type enzyme does not cleave extracellular matrix proteins such as collagen, laminin, fibronectin, and elastin
-
?
additional information
?
-
-
adipocytes/pre-adipocytes and MMP-11 participate in a highly complex vicious cycle to support tumor progression, and this process is orchestrated by cancer cells. First, both invasive cancer cells and resting adipocytes/pre-adipocytes do not express MMP-11. When a cancer cell meets an adipocyte/pre-adipocyte, their cross-talk/interaction induces the expression/secretion of MMP-11 by the adipocyte/pre-adipocyte. MMP-11 negatively regulates adipogenesis, leading to a decrease in adipocyte differentiation and accumulation/maintenance of MMP-11-expressing fibroblast like cells. These latter cells then act on adjacent invasive cancer cells to favor their survival and potentiate this vicious cycle
-
-
?
additional information
?
-
-
enzyme can activate the activity of trypsin-activated interstitial collagenase, no activation of prostromelysin-1, progelatinase A, progelatinase B, no activity with collagen type I
-
?
additional information
?
-
-
no efficient cleavage of matrixin substrate Mca-Pro-Leu-Ala-Leu-Dpa-Ala-Arg-NH2
-
?
additional information
?
-
-
MMPs belong to a family of over 20 neutral endopeptidases that are collectively able to cleave all extracellular matrix components as well as many non-extracellular matrix proteins. The stromelysins, MMP-3, MMP-10 and MMP-11, have a domain arrangement similar to that of collagenases, but they do not cleave interstitial collagens
-
-
?
additional information
?
-
-
the enzyme regulates cell fate and tissue morphogenesis through direct or indirect remodeling of extracellular matrix
-
-
?
additional information
?
-
-
stromelysin-3 expression, in the absence of thyroid hormone, causes significant muscle cell death in the tail of premetamorphic transgenic tadpoles. On the other hand, only relatively low levels of epidermal cell death are induced by precocious thyroid hormone expression in the tail
-
-
?
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cephalosporin EK2900
-
-
-
matrix metalloprotease inhibitor TIMP-2
-
matrix metalloproteinase inhibitor AG3340
-
broad spectrum inhibitor
matrix metalloproteinase inhibitor BB-94
-
-
matrix metalloproteinase inhibitor TIMP-1
-
complete inhibition, human
-
matrix metalloproteinase inhibitor TIMP-2
-
-
-
N-alpha-(2-[[(1-[[(4,6-dichloro-1H-indol-2-yl)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-5-phenylpentanoyl)-L-tryptophanamide
-
N-alpha-(2-[[(1-[[(6,8-dichloro-2-oxo-2H-chromen-3-yl)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-5-phenylpentanoyl)-L-tryptophanamide
-
N-alpha-(2-[[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-4-methylpentanoyl)-L-tryptophanamide
-
N-alpha-(2-[[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-4-naphthalen-2-ylbutanoyl)-L-tryptophanamide
-
N-alpha-(2-[[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-4-phenylbutanoyl)-L-tryptophanamide
-
N-alpha-(2-[[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-5-phenylpentanoyl)-D-tryptophanamide
1% residual activity at 0.002 mM
N-alpha-(2-[[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-5-phenylpentanoyl)-L-tryptophanamide
RXP03
N-alpha-(2-[[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-6-phenylhexanoyl)-L-tryptophanamide
-
N-alpha-(2-[[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]tetradecanoyl)-L-tryptophanamide
-
N-alpha-(2-[[(1-[[(benzyloxy)carbonyl]amino]ethyl)(hydroxy)phosphoryl]methyl]-4-phenylbutanoyl)-L-tryptophanamide
-
N-alpha-(2-[[(1-[[(benzyloxy)carbonyl]amino]ethyl)(hydroxy)phosphoryl]methyl]-5-phenylpentanoyl)-L-tryptophanamide
-
N-alpha-(2-[[(1-[[3-(benzyloxy)propanoyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-5-phenylpentanoyl)-L-tryptophanamide
-
N-alpha-(2-[[(1-[[N-(3-chlorophenyl)-b-alanyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-5-phenylpentanoyl)-L-tryptophanamide
-
N-alpha-(2-[[(1-[[N-(5-chloro-2-hydroxyphenyl)-b-alanyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-5-phenylpentanoyl)-L-tryptophanamide
-
N-alpha-(3-[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]-2-[[(4-methoxybenzyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[(cyclohexylsulfanyl)methyl]propanoyl)-L-tryptophanamide
-
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[(decylsulfanyl)methyl]propanoyl)-L-tryptophanamide
-
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[(naphthalen-2-ylsulfanyl)methyl]propanoyl)-L-tryptophanamide
-
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(2-ethoxy-2-oxoethyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(2-methoxy-2-oxoethyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(2-methylpropyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(2-phenylethyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(3-ethoxy-3-oxopropyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(3-methoxy-3-oxopropyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(3-methoxyphenyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(3-methylbutyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(4-chlorobenzyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(4-methoxybenzyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(furan-2-ylmethyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
N-alpha-[(2R)-3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-([[2-(1-methylethyl)phenyl]sulfanyl]methyl)propanoyl]-L-tryptophanamide
-
N-alpha-[(2R)-3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-([[2-(trifluoromethoxy)phenyl]sulfanyl]methyl)propanoyl]-L-tryptophanamide
-
N-alpha-[(2R)-3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-([[3-(trifluoromethoxy)biphenyl-4-yl]sulfanyl]methyl)propanoyl]-L-tryptophanamide
-
N-alpha-[(2R)-3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-([[4-bromo-2-(trifluoromethoxy)phenyl]sulfanyl]methyl)propanoyl]-L-tryptophanamide
-
N-alpha-[(2R)-3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[(phenylsulfanyl)methyl]propanoyl]-L-tryptophanamide
-
N-alpha-[(2R)-3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(2,4-di-tert-butylphenyl)sulfanyl]methyl]propanoyl]-L-tryptophanamide
-
N-alpha-[(2R)-3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(2,5-dimethoxyphenyl)sulfanyl]methyl]propanoyl]-L-tryptophanamide
-
N-alpha-[(2R)-3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(2-bromophenyl)sulfanyl]methyl]propanoyl]-L-tryptophanamide
-
N-alpha-[(2R)-3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(2-ethylphenyl)sulfanyl]methyl]propanoyl]-L-tryptophanamide
-
N-alpha-[(2R)-3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(2-methoxyphenyl)sulfanyl]methyl]propanoyl]-L-tryptophanamide
-
N-alpha-[2-([[1-(acetylamino)-2-phenylethyl](hydroxy)phosphoryl]methyl)-5-phenylpentanoyl]-L-tryptophanamide
-
N-alpha-[2-([[1-([N-[(benzyloxy)carbonyl]-D-alanyl]amino)-2-phenylethyl](hydroxy)phosphoryl]methyl)-5-phenylpentanoyl]-L-tryptophanamide
-
N-alpha-[2-([[1-([N-[(benzyloxy)carbonyl]-D-leucyl]amino)-2-phenylethyl](hydroxy)phosphoryl]methyl)-5-phenylpentanoyl]-L-tryptophanamide
-
N-alpha-[2-([[1-[[(benzyloxy)carbonyl]amino]-2-(3-bromophenyl)ethyl](hydroxy)phosphoryl]methyl)-5-phenylpentanoyl]-L-tryptophanamide
-
N-alpha-[2-benzyl-3-[(1-[[(benzyloxy)carbonyl]amino]ethyl)(hydroxy)phosphoryl]propanoyl]-L-tryptophanamide
-
N-alpha-[2-[(hydroxy[1-[(1H-indol-2-ylcarbonyl)amino]-2-phenylethyl]phosphoryl)methyl]-5-phenylpentanoyl]-L-tryptophanamide
-
N-alpha-[2-[(hydroxy[2-phenyl-1-[(N-phenyl-b-alanyl)amino]ethyl]phosphoryl)methyl]-5-phenylpentanoyl]-L-tryptophanamide
-
N-alpha-[2-[(hydroxy[2-phenyl-1-[(quinolin-2-ylcarbonyl)amino]ethyl]phosphoryl)methyl]-5-phenylpentanoyl]-L-tryptophanamide
-
N-alpha-[3-(benzyloxy)-2-[[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]propanoyl]-L-tryptophanamide
-
N-alpha-[3-(benzyloxy)-2-[[(1-[[(benzyloxy)carbonyl]amino]ethyl)(hydroxy)phosphoryl]methyl]propanoyl]-L-tryptophanamide
-
N-alpha-[3-[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]-2-(naphthalen-2-ylmethyl)propanoyl]-L-tryptophanamide
-
N-alpha-[3-[(1-[[(benzyloxy)carbonyl]amino]ethyl)(hydroxy)phosphoryl]-2-methylpropanoyl]-L-tryptophanamide
-
N-alpha-[3-[(1-[[(benzyloxy)carbonyl]amino]ethyl)(hydroxy)phosphoryl]-2-[(benzylsulfanyl)methyl]propanoyl]-L-tryptophanamide
-
N2-(2-[[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-5-phenylpentanoyl)-3-[(3,5-dinitrophenyl)amino]-L-alaninamide
-
N2-(2-[[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-5-phenylpentanoyl)-L-alaninamide
20% residual activity at 0.002 mM
phenylmethylsulfonyl fluoride
-
slight inhibition
TIMP-1
tissue inhibitor of metalloproteinases
-
1,10-phenanthroline
-
1,10-phenanthroline
-
complete inhibition
EDTA
-
EDTA
-
complete inhibition
matrix metalloprotease inhibitor TIMP-2
-
-
-
matrix metalloprotease inhibitor TIMP-2
-
-
-
phosphinic inhibitor
-
-
phosphinic inhibitor
inhibitor binding mechanism
-
additional information
-
no inhibition by aprotinin
-
additional information
-
no inhibition by phosphoramidon and L-3-caroxy-2,3-trans-epoxypropionyl-leucylamido-(4-guanidino)butane, i.e. E-64
-
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0.000006
matrix metalloproteinase inhibitor AG3340
-
pH 7.6, 37°C
0.0000009
N-alpha-(2-[[(1-[[(4,6-dichloro-1H-indol-2-yl)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-5-phenylpentanoyl)-L-tryptophanamide
-
0.000005
N-alpha-(2-[[(1-[[(6,8-dichloro-2-oxo-2H-chromen-3-yl)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-5-phenylpentanoyl)-L-tryptophanamide
-
0.000022
N-alpha-(2-[[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-4-methylpentanoyl)-L-tryptophanamide
-
0.000015
N-alpha-(2-[[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-4-naphthalen-2-ylbutanoyl)-L-tryptophanamide
-
0.000009
N-alpha-(2-[[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-4-phenylbutanoyl)-L-tryptophanamide
-
0.000005
N-alpha-(2-[[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-5-phenylpentanoyl)-L-tryptophanamide
-
0.000033
N-alpha-(2-[[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-6-phenylhexanoyl)-L-tryptophanamide
-
0.000034
N-alpha-(2-[[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]tetradecanoyl)-L-tryptophanamide
-
0.000051
N-alpha-(2-[[(1-[[(benzyloxy)carbonyl]amino]ethyl)(hydroxy)phosphoryl]methyl]-4-phenylbutanoyl)-L-tryptophanamide
-
0.0001
N-alpha-(2-[[(1-[[(benzyloxy)carbonyl]amino]ethyl)(hydroxy)phosphoryl]methyl]-5-phenylpentanoyl)-L-tryptophanamide
-
0.000005
N-alpha-(2-[[(1-[[3-(benzyloxy)propanoyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-5-phenylpentanoyl)-L-tryptophanamide
-
0.000004
N-alpha-(2-[[(1-[[N-(3-chlorophenyl)-b-alanyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-5-phenylpentanoyl)-L-tryptophanamide
-
0.00001
N-alpha-(2-[[(1-[[N-(5-chloro-2-hydroxyphenyl)-b-alanyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-5-phenylpentanoyl)-L-tryptophanamide
-
0.000002
N-alpha-(3-[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]-2-[[(4-methoxybenzyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
0.00026
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[(cyclohexylsulfanyl)methyl]propanoyl)-L-tryptophanamide
-
0.00005
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[(decylsulfanyl)methyl]propanoyl)-L-tryptophanamide
-
0.000026
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[(naphthalen-2-ylsulfanyl)methyl]propanoyl)-L-tryptophanamide
-
0.00053
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(2-ethoxy-2-oxoethyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
0.0003
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(2-methoxy-2-oxoethyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
0.000165
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(2-methylpropyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
0.00008
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(2-phenylethyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
0.000275
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(3-ethoxy-3-oxopropyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
0.00038
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(3-methoxy-3-oxopropyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
0.000066
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(3-methoxyphenyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
0.000165
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(3-methylbutyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
0.000017
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(4-chlorobenzyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
0.000002
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(4-methoxybenzyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
0.000033
N-alpha-(3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(furan-2-ylmethyl)sulfanyl]methyl]propanoyl)-L-tryptophanamide
-
0.0003
N-alpha-[(2R)-3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-([[2-(1-methylethyl)phenyl]sulfanyl]methyl)propanoyl]-L-tryptophanamide
-
0.000413
N-alpha-[(2R)-3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-([[2-(trifluoromethoxy)phenyl]sulfanyl]methyl)propanoyl]-L-tryptophanamide
-
0.000615
N-alpha-[(2R)-3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-([[3-(trifluoromethoxy)biphenyl-4-yl]sulfanyl]methyl)propanoyl]-L-tryptophanamide
-
0.00033
N-alpha-[(2R)-3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-([[4-bromo-2-(trifluoromethoxy)phenyl]sulfanyl]methyl)propanoyl]-L-tryptophanamide
-
0.00001
N-alpha-[(2R)-3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[(phenylsulfanyl)methyl]propanoyl]-L-tryptophanamide
-
0.000077
N-alpha-[(2R)-3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(2,4-di-tert-butylphenyl)sulfanyl]methyl]propanoyl]-L-tryptophanamide
-
0.00043
N-alpha-[(2R)-3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(2,5-dimethoxyphenyl)sulfanyl]methyl]propanoyl]-L-tryptophanamide
-
0.000113
N-alpha-[(2R)-3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(2-bromophenyl)sulfanyl]methyl]propanoyl]-L-tryptophanamide
-
0.00027
N-alpha-[(2R)-3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(2-ethylphenyl)sulfanyl]methyl]propanoyl]-L-tryptophanamide
-
0.00023
N-alpha-[(2R)-3-[[(1S)-1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl](hydroxy)phosphoryl]-2-[[(2-methoxyphenyl)sulfanyl]methyl]propanoyl]-L-tryptophanamide
-
0.00002
N-alpha-[2-([[1-(acetylamino)-2-phenylethyl](hydroxy)phosphoryl]methyl)-5-phenylpentanoyl]-L-tryptophanamide
-
0.000008
N-alpha-[2-([[1-([N-[(benzyloxy)carbonyl]-D-alanyl]amino)-2-phenylethyl](hydroxy)phosphoryl]methyl)-5-phenylpentanoyl]-L-tryptophanamide
-
0.000006
N-alpha-[2-([[1-([N-[(benzyloxy)carbonyl]-D-leucyl]amino)-2-phenylethyl](hydroxy)phosphoryl]methyl)-5-phenylpentanoyl]-L-tryptophanamide
-
0.000005
N-alpha-[2-([[1-[[(benzyloxy)carbonyl]amino]-2-(3-bromophenyl)ethyl](hydroxy)phosphoryl]methyl)-5-phenylpentanoyl]-L-tryptophanamide
-
0.00035
N-alpha-[2-benzyl-3-[(1-[[(benzyloxy)carbonyl]amino]ethyl)(hydroxy)phosphoryl]propanoyl]-L-tryptophanamide
-
0.0000015
N-alpha-[2-[(hydroxy[1-[(1H-indol-2-ylcarbonyl)amino]-2-phenylethyl]phosphoryl)methyl]-5-phenylpentanoyl]-L-tryptophanamide
-
0.000015
N-alpha-[2-[(hydroxy[2-phenyl-1-[(N-phenyl-b-alanyl)amino]ethyl]phosphoryl)methyl]-5-phenylpentanoyl]-L-tryptophanamide
-
0.0000042
N-alpha-[2-[(hydroxy[2-phenyl-1-[(quinolin-2-ylcarbonyl)amino]ethyl]phosphoryl)methyl]-5-phenylpentanoyl]-L-tryptophanamide
-
0.000016
N-alpha-[3-(benzyloxy)-2-[[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]propanoyl]-L-tryptophanamide
-
0.000175
N-alpha-[3-(benzyloxy)-2-[[(1-[[(benzyloxy)carbonyl]amino]ethyl)(hydroxy)phosphoryl]methyl]propanoyl]-L-tryptophanamide
-
0.000074
N-alpha-[3-[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]-2-(naphthalen-2-ylmethyl)propanoyl]-L-tryptophanamide
-
0.0027
N-alpha-[3-[(1-[[(benzyloxy)carbonyl]amino]ethyl)(hydroxy)phosphoryl]-2-methylpropanoyl]-L-tryptophanamide
-
0.000036
N-alpha-[3-[(1-[[(benzyloxy)carbonyl]amino]ethyl)(hydroxy)phosphoryl]-2-[(benzylsulfanyl)methyl]propanoyl]-L-tryptophanamide
-
0.000027
N2-(2-[[(1-[[(benzyloxy)carbonyl]amino]-2-phenylethyl)(hydroxy)phosphoryl]methyl]-5-phenylpentanoyl)-3-[(3,5-dinitrophenyl)amino]-L-alaninamide
-
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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 (P24347), Xenopus laevis (Q11005)
brenda
Gall, A.L.; Ruff, M.; Moras, D.
The dual role of CHAPS in the crystallization of stromelysin-3 catalytic domain
Acta Crystallogr. Sect. D
59
603-606
2003
Mus musculus (Q02853)
brenda
Holtz, B.; Cuniasse, P.; Boulay, A.; Kannan, R.; Mucha, A.; Beau, F.; Basset, P.; Dive, V.
Role of the S1' subsite glutamine 215 in activity and specificity of stromelysin-3 by site-directed mutagenesis
Biochemistry
38
12174-12179
1999
Mus musculus
brenda
Murphy, G.; Segain, J.P.; O'Shea, M.; Cockett, M.; Ioannou, C.; Lefebvre, O.; Chambon, P.; Basset, P.
The 28-kDa N-terminal domain of mouse stromelysin-3 has the general properties of a weak metalloproteinase
J. Biol. Chem.
268
15435-15441
1993
Mus musculus
brenda
Noel, A.; Santavicca, M.; Stoll, I.; L'Hoir, C.; Staub, A.; Murphy, G.; Rio, M.C.; Basset, P.
Identification of structural determinants controlling human and mouse stromelysin-3 proteolytic activities
J. Biol. Chem.
270
22866-22872
1995
Homo sapiens, Mus musculus
brenda
Manes, S.; Mira, E.; Barbacid, M.M.; Cipres, A.; Fernandez-Resa, P.; Buesa, J.M.; Merida, I.; Aracil, M.; Marquez, G.; Martinez, A.C.
Identification of insulin-like growth factor-binding protein-1 as a potential physiological substrate for human stromelysin-3
J. Biol. Chem.
272
25706-25712
1997
Homo sapiens
brenda
Mucha, A.; Cuniasse, P.; Kannan, R.; Beau, F.; Yiotakis, A.; Basset, P.; Dive, V.
Membrane type-1 matrix metalloprotease and stromelysin-3 cleave more efficiently synthetic substrates containing unusual amino acids in their P1' positions
J. Biol. Chem.
273
2763-2768
1998
Mus musculus
brenda
Pan, W.; Arnone, M.; Kendall, M.; Grafstrom, R.H.; Seitz, S.P.; Wasserman, Z.R.; Albright, C.F.
Identification of peptide substrates for human MMP-11 (stromelysin-3) using phage display
J. Biol. Chem.
278
27820-27827
2003
Homo sapiens
brenda
Gall, A.L.; Ruff, M.; Kannan, R.; Cuniasse, P.; Yiotakis, A.; Dive, V.; Rio, M.C.; Basset, P.; Moras, D.
Crystal structure of the stromelysin-3 (MMP-11) catalytic domain complexed with a phosphinic inhibitor mimicking the transition-state
J. Mol. Biol.
307
577-586
2001
Mus musculus (Q02853)
brenda
Noel, A.; Boulay, A.; Kebers, F.; Kannan, R.; Hajitou, A.; Calberg-Bacq, C.M.; Basset, P.; Rio, M.C.; Foidart, J.M.
Demonstration in vivo that stromelysin-3 functions through its proteolytic activity
Oncogene
19
1605-1612
2000
Homo sapiens, Mus musculus
brenda
Kannan, R.; Ruff, M.; Kochins, J.G.; Manly, S.P.; Stoll, I.; El Fahime, M.; Noel, A.; Foidart, J.M.; Rio, M.C.; Dive, V.; Basset, P.
Purification of active matrix metalloproteinase catalytic domains and its use for screening of specific stromelysin-3 inhibitors
Protein Expr. Purif.
16
76-83
1999
Mus musculus
brenda
Deng, H.; Guo, R.F.; Li, W.M.; Zhao, M.; Lu, Y.Y.
Matrix metalloproteinase 11 depletion inhibits cell proliferation in gastric cancer cells
Biochem. Biophys. Res. Commun.
326
274-281
2005
Homo sapiens
brenda
Selvey, S.; Haupt, L.M.; Thompson, E.W.; Matthaei, K.I.; Irving, M.G.; Griffiths, L.R.
Stimulation of MMP-11 (stromelysin-3) expression in mouse fibroblasts by cytokines, collagen and co-culture with human breast cancer cell lines
BMC Cancer
4
40
2004
Mus musculus
brenda
Andarawewa, K.L.; Motrescu, E.R.; Chenard, M.P.; Gansmuller, A.; Stoll, I.; Tomasetto, C.; Rio, M.C.
Stromelysin-3 is a potent negative regulator of adipogenesis participating to cancer cell-adipocyte interaction/crosstalk at the tumor invasive front
Cancer Res.
65
10862-10871
2005
Homo sapiens
brenda
Amano, T.; Kwak, O.; Fu, L.; Marshak, A.; Shi, Y.B.
The matrix metalloproteinase stromelysin-3 cleaves laminin receptor at two distinct sites between the transmembrane domain and laminin binding sequence within the extracellular domain
Cell Res.
15
150-159
2005
Xenopus laevis
brenda
Odaka, C.; Izumiyama, S.
Expression of stromelysin-3 (matrix metalloproteinase-11) in macrophages of murine thymus following thymocyte apoptosis
Cell. Immunol.
235
21-28
2005
Mus musculus
brenda
Amano, T.; Fu, L.; Sahu, S.; Markey, M.; Shi, Y.B.
Substrate specificity of Xenopus matrix metalloproteinase stromelysin-3
Int. J. Mol. Med.
14
233-239
2004
Xenopus laevis
brenda
Fu, L.; Ishizuya-Oka, A.; Buchholz, D.R.; Amano, T.; Matsuda, H.; Shi, Y.B.
A causative role of stromelysin-3 in extracellular matrix remodeling and epithelial apoptosis during intestinal metamorphosis in Xenopus laevis
J. Biol. Chem.
280
27856-27865
2005
Xenopus laevis
brenda
Sharma, R.; Chattopadhyay, T.K.; Mathur, M.; Ralhan, R.
Prognostic significance of stromelysin-3 and tissue inhibitor of matrix metalloproteinase-2 in esophageal cancer
Oncology
67
300-309
2004
Homo sapiens
brenda
Kasper, G.; Reule, M.; Tschirschmann, M.; Dankert, N.; Stout-Weider, K.; Lauster, R.; Schrock, E.; Mennerich, D.; Duda, G.N.; Lehmann, K.E.
Stromelysin-3 over-expression enhances tumourigenesis in MCF-7 and MDA-MB-231 breast cancer cell lines: involvement of the IGF-1 signalling pathway
BMC Cancer
7
12
2007
Homo sapiens
brenda
Kim, H.J.; Lee, J.Y.; Kim, S.H.; Seo, Y.J.; Lee, J.H.; Park, J.K.; Kim, M.H.; Cinn, Y.W.; Cho, K.H.; Yoon, T.Y.
Stromelysin-3 expression in the differential diagnosis of dermatofibroma and dermatofibrosarcoma protuberans: comparison with factor XIIIa and CD34
Br. J. Dermatol.
157
319-324
2007
Homo sapiens
brenda
Jia, L.; Cao, J.; Wei, W.; Wang, S.; Zuo, Y.; Zhang, J.
CD147 depletion down-regulates matrix metalloproteinase-11, vascular endothelial growth factor-A expression and the lymphatic metastasis potential of murine hepatocarcinoma Hca-F cells
Int. J. Biochem. Cell Biol.
39
2135-2142
2007
Mus musculus
brenda
Fu, L.; Tomita, A.; Wang, H.; Buchholz, D.R.; Shi, Y.B.
Transcriptional regulation of the Xenopus laevis stromelysin-3 gene by thyroid hormone is mediated by a DNA element in the first intron
J. Biol. Chem.
281
16870-16878
2006
Xenopus laevis (Q71VB9), Xenopus laevis
brenda
Matziari, M.; Dive, V.; Yiotakis, A.
Matrix metalloproteinase 11 (MMP-11; stromelysin-3) and synthetic inhibitors
Med. Res. Rev.
27
528-552
2007
Mus musculus (Q02853)
brenda
Shi, Y.B.; Fu, L.; Hasebe, T.; Ishizuya-Oka, A.
Regulation of extracellular matrix remodeling and cell fate determination by matrix metalloproteinase stromelysin-3 during thyroid hormone-dependent post-embryonic development
Pharmacol. Ther.
116
391-400
2007
Xenopus laevis
brenda
Motrescu, E.R.; Rio, M.C.
Cancer cells, adipocytes and matrix metalloproteinase 11: a vicious tumor progression cycle
Biol. Chem.
389
1037-1041
2008
Homo sapiens
brenda
Yang, Y.H.; Deng, H.; Li, W.M.; Zhang, Q.Y.; Hu, X.T.; Xiao, B.; Zhu, H.H.; Geng, P.L.; Lu, Y.Y.
Identification of matrix metalloproteinase 11 as a predictive tumor marker in serum based on gene expression profiling
Clin. Cancer Res.
14
74-81
2008
Homo sapiens
brenda
Mathew, S.; Fu, L.; Fiorentino, M.; Matsuda, H.; Das, B.; Shi, Y.B.
Differential regulation of cell type specific apoptosis by stromelysin-3: A potential mechanism via the cleavage of the laminin receptor during tail resorption in Xenopus laevis
J. Biol. Chem.
284
18545-18556
2009
Xenopus laevis
brenda
Motrescu, E.R.; Blaise, S.; Etique, N.; Messaddeq, N.; Chenard, M.P.; Stoll, I.; Tomasetto, C.; Rio, M.C.
Matrix metalloproteinase-11/stromelysin-3 exhibits collagenolytic function against collagen VI under normal and malignant conditions
Oncogene
27
6347-6355
2008
Homo sapiens, Mus musculus
brenda
Lijnen, H.R.; Van Hoef, B.; Rodriguez, J.A.; Paramo, J.A.
Stromelysin-2 (MMP-10) deficiency does not affect adipose tissue formation in a mouse model of nutritionally induced obesity
Biochem. Biophys. Res. Commun.
389
378-381
2009
Mus musculus
brenda
Mathew, S.; Fu, L.; Hasebe, T.; Ishizuya-Oka, A.; Shi, Y.B.
Tissue-dependent induction of apoptosis by matrix metalloproteinase stromelysin-3 during amphibian metamorphosis
Birth Defects Res. C Embryo Today
90
55-66
2010
Homo sapiens, Mus musculus, Xenopus laevis
brenda
Peruzzi, D.; Mori, F.; Conforti, A.; Lazzaro, D.; De Rinaldis, E.; Ciliberto, G.; La Monica, N.; Aurisicchio, L.
MMP11: a novel target antigen for cancer immunotherapy
Clin. Cancer Res.
15
4104-4113
2009
Homo sapiens, Mus musculus, Mus musculus BALB/c
brenda
Cheng, C.W.; Yu, J.C.; Wang, H.W.; Huang, C.S.; Shieh, J.C.; Fu, Y.P.; Chang, C.W.; Wu, P.E.; Shen, C.Y.
The clinical implications of MMP-11 and CK-20 expression in human breast cancer
Clin. Chim. Acta
411
234-241
2010
Homo sapiens
brenda
Zhao, Z.S.; Chu, Y.Q.; Ye, Z.Y.; Wang, Y.Y.; Tao, H.Q.
Overexpression of matrix metalloproteinase 11 in human gastric carcinoma and its clinicopathologic significance
Hum. Pathol.
41
686-696
2010
Homo sapiens
brenda
Brasse, D.; Mathelin, C.; Leroux, K.; Chenard, M.P.; Blaise, S.; Stoll, I.; Tomasetto, C.; Rio, M.C.
Matrix metalloproteinase 11/stromelysin-3 exerts both activator and repressor functions during the hematogenous metastatic process in mice
Int. J. Cancer
127
1347-1355
2010
Mus musculus, Mus musculus BALB/c
brenda
Ban, J.Y.; Kim, S.K.; Kang, S.W.; Yoon, K.L.; Chung, J.H.
Association between polymorphisms of matrix metalloproteinase 11 (MMP-11) and Kawasaki disease in the Korean population
Life Sci.
86
756-759
2010
Homo sapiens (P24347), Homo sapiens
brenda
Barrasa, J.I.; Olmo, N.; Santiago-Gomez, A.; Lecona, E.; Anglard, P.; Turnay, J.; Lizarbe, M.A.
Histone deacetylase inhibitors upregulate MMP11 gene expression through Sp1/Smad complexes in human colon adenocarcinoma cells
Biochim. Biophys. Acta
1823
570-581
2012
Homo sapiens
brenda
Takeuchi, T.; Adachi, Y.; Nagayama, T.; Furihata, M.
Matrix metalloproteinase-11 overexpressed in lobular carcinoma cells of the breast promotes anoikis resistance
Virchows Arch.
459
291-297
2011
Homo sapiens
brenda
Sunil Kumar, B.V.; Kumar, K.A.; Padmanath, K.; Sharma, B.; Kataria, M.
Heterologous expression and functional characterization of matrix metalloproteinase-11 from canine mammary tumor
Anim. Biotechnol.
24
31-43
2013
Canis lupus familiaris (D6R1X0), Canis lupus familiaris
brenda
Sahoo, S.; Kataria, M.; Maiti, S.
Isolation and characterization of stromelysin-3 (MMP-11) like protein from a case of mammary carcinoma in dog
Indian J. Anim. Res.
49
127-131
2014
Canis lupus familiaris, Canis lupus familiaris (D6R1X0)
-
brenda
Sunil Kumar, B.V.; Kataria, M.
Identification of matrix metalloproteinase-11 as a predictive canine mammary tumor marker based on gene expression profiling
Natl. Acad. Sci. Lett.
35
535-539
2012
Canis lupus familiaris (D6R1X0)
-
brenda
Tan, J.; Buache, E.; Alpy, F.; Daguenet, E.; Tomasetto, C.L.; Ren, G.S.; Rio, M.C.
Stromal matrix metalloproteinase-11 is involved in the mammary gland postnatal development
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Mus musculus (Q02853)
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Gonzalez de Vega, R.; Clases, D.; Fernandez-Sanchez, M.L.; Eiro, N.; Gonzalez, L.O.; Vizoso, F.J.; Doble, P.A.; Sanz-Medel, A.
MMP-11 as a biomarker for metastatic breast cancer by immunohistochemical-assisted imaging mass spectrometry
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Homo sapiens (P24347), Homo sapiens
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Paul, R.K.; Kumar, M.; Kataria, M.
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Gallus gallus (F1NBH2), Gallus gallus
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Homo sapiens (P24347), Homo sapiens
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Zhang, Z.; Dong, T.; Fu, Y.; Zhou, W.; Tian, X.; Chen, G.; Liu, S.
MMP-11 promotes papillary thyroid cell proliferation and invasion via the NF-kappaB pathway
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Homo sapiens (P24347)
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Hsin, C.H.; Chou, Y.E.; Yang, S.F.; Su, S.C.; Chuang, Y.T.; Lin, S.H.; Lin, C.W.
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Homo sapiens (P24347), Homo sapiens
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Laminin and matrix metalloproteinase 11 regulate fibronectin levels in the zebrafish myotendinous junction
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Danio rerio
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