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Information on EC 3.4.24.B3 - matrix metalloproteinase-11 and Organism(s) Mus musculus and UniProt Accession Q02853
for references in articles please use BRENDA:EC3.4.24.B3preliminary BRENDA-supplied EC number
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EC Tree
3.4.24.B3 matrix metalloproteinase-11Specify your search results
Word Map
- 3.4.24.B3
- metalloproteinases
- metastasis
- mmp-2
- timps
- gelatinase
-
microperoxidase-11
-
metamorphosis
- tadpole
- matrilysin
-
menstrual
- medicine
- stromelysin-2
-
microperoxidase
- collagenase-3
- pharmacology
- diagnostics
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
mmp-11, mmp11, stromelysin-3, mp-11, stromelysin 3, matrix metalloproteinase 11, matrix metalloproteinase-11, mmp-11 proteinase, mmp stromelysin-3, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
additional information
-
the enzyme belongs to the matrix metalloproteinase superfamily of Zn2+-dependent proteases
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CAS REGISTRY NUMBER
COMMENTARY
145267-01-2
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(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
-
?
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-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-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
-
-
-
?
alpha1-protease inhibitor + H2O
?
-
wild-type enzyme and mutants Q215L, Q215R and Q215Y
-
?
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 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
-
?
dansyl-Pro-Leu-Ala-Leu-Trp-Ala-Arg-NH2 + H2O
?
-
wild-type enzyme and mutants Q215L, Q215R and Q215Y
-
?
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
-
-
-
?
Laminin + H2O
?
-
only recombinant processed enzyme lacking the N-terminal prodomain and 175 amino acid residues of the C-terminus
-
?
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
-
?
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
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
-
-
?
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
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zinc
3 zinc atoms per enzyme molecule, metalloproteinase, the zinc binding site is catalytically active
Zn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
additional information
-
no inhibition by phosphoramidon and L-3-caroxy-2,3-trans-epoxypropionyl-leucylamido-(4-guanidino)butane, i.e. E-64
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CD47
-
extracellular matrix metalloproteinase inducer, CD147 depletion in Hca-F cells results in the significantly decreased expression of matrix metalloproteinase-11
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide
-
substrate specificity with synthetic substrates
0.0045
dansyl-Pro-Leu-Ala-S-[(4-methoxyphenyl)methyl]Cys-Trp-Ala-Arg-NH2
-
pH 6.8, 25°C, mutant Q215L
0.0052
dansyl-Pro-Leu-Ala-S-[(4-methoxyphenyl)methyl]Cys-Trp-Ala-Arg-NH2
-
pH 6.8, 25°C, wild-type enzyme
0.0064
dansyl-Pro-Leu-Ala-S-[(4-methoxyphenyl)methyl]Cys-Trp-Ala-Arg-NH2
-
pH 6.8, 25°C, mutant Q215R
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide
0.078
dansyl-Pro-Leu-Ala-S-[(4-methoxyphenyl)methyl]Cys-Trp-Ala-Arg-NH2
-
pH 6.8, 25°C, wild-type enzyme
0.083
dansyl-Pro-Leu-Ala-S-[(4-methoxyphenyl)methyl]Cys-Trp-Ala-Arg-NH2
-
pH 6.8, 25°C, mutant Q215L
0.65
dansyl-Pro-Leu-Ala-S-[(4-methoxyphenyl)methyl]Cys-Trp-Ala-Arg-NH2
-
pH 6.8, 25°C, mutant Q215R
additional information
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide
-
substrate specificity with synthetic substrates
additional information
additional information
-
substrate specificity with synthetic substrates
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
MMP-11 stimulation in mouse fibroblasts using cytokines, matrix constituents and HBC cell lines
-
expression of stromelysin-3 (matrix metalloproteinase-11) in macrophages of murine thymus following thymocyte apoptosis
-
upregulation of stromelysin-3 in the thymus following thymocyte apoptosis
additional information
-
MMP-11 expression in benign and malign tissues, detailed overview
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
the enzyme is required for optimal postnatal ductal morphogenesis and function of the mammary gland but does not influence the intrinsic organization of the mammary epithelium
malfunction
malfunction
-
MMP11-deficient mice develop higher numbers of metastases than wild-type mice
malfunction
-
role of MMP11 in cancer progression, MMP11 expression correlates with aggressive profile and invasiveness of different types of carcinoma
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28000
-
x * 28000, recombinant active N-terminal domain, SDS-PAGE, x * 58000, inactive recombinant enzyme expressed in Escherichia coli, SDS-PAGE
58000
-
x * 28000, recombinant active N-terminal domain, SDS-PAGE, x * 58000, inactive recombinant enzyme expressed in Escherichia coli, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
MMP-11 possesses a furin recognition motif RXKR, but it lacks the C-terminal transmembrane domain of MMPs
?
-
x * 28000, recombinant active N-terminal domain, SDS-PAGE, x * 58000, inactive recombinant enzyme expressed in Escherichia coli, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
-
formation of a processed and truncated mature form of MW 21 kDa
proteolytic modification
-
recombinant protein from mouse myeloma cells is cleaved and loses its propeptide and the majority of its C-terminal domain, recombinant enzyme can be cleaved by trypsin to a 51 kDa stil latent enzyme form
proteolytic modification
-
MMPs with a furin-recognition motif RXKR, such as ST3 and MT-MMPs, are activated intracellularly through a furin-dependent process
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
catalytic domain complexed with a phosphinic inhibitor mimicking the transition state, hanging drop method, 5 mg/ml protein in 0.05 M MES, pH 5.5, 0.5 M ammonium sulfate, 1% v/v trifluoroethanol, 4°C, a few months, X-ray diffraction structure determination at 2.6 A resolution and analysis
enzyme complexed with a phosphinic inhibitor, inhibitor to protein ratio is 2.2:1, in presence of detergent CHAPS, hanging drop method, 5 mg/ml protein in 0.05 M MES, pH 5.5, 0.5 M ammonium sulfate, 1% v/v trifluoroethanol, X-ray diffraction structure determination at 2.6 A resolution and analysis
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E220A
-
site-directed mutagenesis, exchange of a residue in the zinc-binding catalytic domain, inactive
P235A
-
site-directed mutagenesis, truncated mutant with this introduces point mutation shows reduced enzyme activity against laminin and collgen IV
Q215L
-
site-directed mutagenesis, exchange of the residue preceeding the catalytic zinc-binding site results in altered substrate specificity for the P1' position of substrates compared to the wild-type
Q215R
-
site-directed mutagenesis, exchange of the residue preceeding the catalytic zinc-binding site results in altered substrate specificity for the P1' position of substrates compared to the wild-type
Q215Y
-
site-directed mutagenesis, exchange of the residue preceeding the catalytic zinc-binding site results in altered substrate specificity for the P1' position of substrates compared to the wild-type
additional information
additional information
-
HLA-A2.1 transgenic mice are used to identify reactive epitopes as tools to assess immunogenicity in humans, MMP11 vaccine in 1,2-dimethylhydrazine-colon cancer model, overview
additional information
-
mice lacking any one particular MMP, including ST3, often show little or weak phenotype
additional information
-
MMP-11-/- mice kept on high fat diet show adipocyte hypertrophy in adipose tissues
additional information
-
MMP11-deficient mice develop higher numbers of metastases than wild-type mice
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant from Escherichia coli, addition of CHAPS, i.e. 3-[(3-cholamidopropyl)dimethylammonio]-1-propane sulfonate, to avoid protein aggregation, binding mechanism
recombinant catalytic domain expressed in Escherichia coli with a recovery of 7%
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of catalytic domain connected to the hemopexin-like domain in Escherichia coli BL21(DE3)
expression of an inactive enzyme in Escherichia coli BL21(DE3), expression of a functional enzyme in NSO mouse myeloma cell line
-
expression of truncated mutant lacking the N-terminal prodomain in Escherichia coli BL21(DE3), and the C-terminal part of the hemopexin-like domain, expression of wild-type enzyme in MFC7 cells
-
from NIH-3T3 cells, establishing of a chemically induced, MMP11-overexpressing colon cancer model, overview
-
overexpression of wild-type and mutant E220A in Escherichia coli, expression of wild-type and inactive enzyme in MCF7 carcinoma cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
stromelysin-3 is slightly downregulated in obese adipose tissue compared to non-obese adipose tissue
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
recombinant truncated enzyme is solubilized and refolded from inclusion bodies after expression in Escherichia coli
-
refolding of recombinant enzyme from inclusion bodies after overexpression in Escherichia coli
-
solubilization and refolding of recombinant catalytic enzyme domain from inclusion bodies after expression in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
MMP11 is a novel broadly expressed tumor associated antigen and a target candidate for cancer immunotherapy. Possible use of murine MMP11 as tumor-associated antigen for vaccination of human cancer patients. MMP11 vaccine induces cell-mediated and antibody immune response and exerts significant antitumoral protection in mice with colon cancer in prophylactic and therapeutic settings
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
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
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
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
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
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)
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
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
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
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
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
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)
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
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
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
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
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
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