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Information on EC 3.4.24.B4 - matrix metalloproteinase-13 and Organism(s) Mus musculus and UniProt Accession P33435
for references in articles please use BRENDA:EC3.4.24.B4preliminary BRENDA-supplied EC number
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EC Tree
3.4.24.B4 matrix metalloproteinase-13Specify your search results
Word Map
- 3.4.24.B4
- cartilage
- chondrocytes
- osteoarthritis
- metalloproteinases
- joint
-
articular
- aggrecan
- degeneration
- mmp-2
- tnf
- knee
- timp-1
- arthritis
- synovial
- interleukin-1
- proteoglycans
-
degener
- cox-2
- osteoblast
- adamts-5
- ligament
-
intra-articular
- collagenases
-
col2a1
- thrombospondin
- pulposus
- runx2
-
cruciate
-
zymography
-
chondrogenic
- gelatinase
- meniscus
-
intervertebral
-
subchondral
-
disintegrin
-
endochondral
-
safranin
- synoviocytes
-
collagenolytic
-
matrix-degrading
-
chondroprotective
-
ossification
-
temporomandibular
- mt1-mmp
-
chondrogenesis
- medicine
- stromelysin-1
- diagnostics
-
cartilage-specific
-
condylar
- analysis
- osteophyte
- drug development
- aggrecanase
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-13, mmp13, collagenase-3, matrix metalloproteinase-13, matrix metalloproteinase 13, collagenase 3, mmp13a, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
MMP13
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CAS REGISTRY NUMBER
COMMENTARY
175449-82-8
-
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
Y(NO2)GGPAGLYEK(Abz)G + H2O
Y(NO2)GGPAG + LYEK(Abz)G
FRET substrate, cleavage rate is 0.468 nmoles/second
-
-
?
Y(NO2)GPLGMRGLK(Abz)G + H2O
Y(NO2)GPLG + MRGLK(Abz)G
FRET substrate, cleavage rate is 0.006 nmoles/second
-
-
?
Collagen type I + H2O
?
-
Interstitial fibers of collagen type I in the plaque can be degraded by MMP13 specifically. MMP13 is capable of degrading collagen type I in the upstream atherosclerotic lesions
-
-
?
additional information
?
-
-
stimulates bradykinin-induced tyrosine phosphorylation and activation of epidermal growth factor receptor
-
-
?
additional information
?
-
-
MMP-13 degrades intact collagen and participates in situations where rapid and effective remodeling of collagenous extracellular matrix is required
-
-
?
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 type I + H2O
?
-
Interstitial fibers of collagen type I in the plaque can be degraded by MMP13 specifically. MMP13 is capable of degrading collagen type I in the upstream atherosclerotic lesions
-
-
?
additional information
?
-
-
MMP-13 degrades intact collagen and participates in situations where rapid and effective remodeling of collagenous extracellular matrix is required
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
His201, His211, and His 205 are involved in metal ion binding, geometry from crystal structure
Ca2+
Zn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
hydroxamate inhibitor RS-113456
a diphenyl ether sulfon compound, complexing of the enzyme via His205 and Glu202
-
AG1296
-
a platelet-derived growth factor receptor inhibitor, shows several physiological effects, overview
BB94
-
a broadspectrum MMP inhibitor, significantly inhibits keratinocyte migration
N-hydroxy-1-(4-methoxyphenyl)sulfonyl-4-(4-biphenylcarbonyl)piperazine-2-carboxamide
-
-
N-[[(4,5-dihydro-5-thioxo-1,3,4-thiadiazol-2-yl)amino]carbonyl]-L-phenylalanine
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the prodomain of MMP13 determines autoactivation of MMP13 and intracellular degradation of MMP13
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
myoblast cell line, expression of enzyme and tissue inhibitor of matrix metalloproteinase, TIMP-1, is regulated by Wnt signaling combined with bone morphogenic protein BMP-2 in osteoblastic differentiation
-
scar-associated macrophages are a major source of hepatic matrix metalloproteinase-13
-
MMP-13 expression in the tissues around in vivo developing oral sulcus at E11, 12, and 13, immunohistochemic analysis
-
MMP-13 expression is negligible in the normal unwounded skin at day 0, but it increases on days 1 to 7 upon wounding, diminishes on day 14 and disappears on day 28
-
induced tumors, stromal MMP13 is associated with vascular endothelial growth factor receptor-2 on endothelial cells in invasive areas. Tumour invasion was downregulated in Mmp13-/- animals. Kinetics of angiogenesis and tumour growth in surface transplants, overview
additional information
-
MMP13 is expressed by hypertrophic chondrocytes and osteoblasts in the fracture callus
additional information
-
expression analysis of MMP13 in healthy and wounded skin, overview
additional information
-
MMP-13 mRNA abundance is greatly enhanced in Hdac4-deficient mice compared with wild-type or heterozygous littermates. MMP-13 staining in the tibiae of knockout mice is strongly detected in late hypertrophic chondrocytes and bone regions compared with wild-type or heterozygous mice
additional information
-
Mmp13 is expressed in mouse choroidal neovascular lesions induced by laser burn
additional information
-
MMP13 is upregulated at the breast tumor-bone interface, gene expression profiling, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
neuropathy is reversed upon injection of MMP13 inhibitor into obese mice on a high-fat/high sugar diet
metabolism
physiological function
additional information
metabolism
-
the activation of MMP-13 expression by T3 is in a competitive balance with the regulation of osteocalcin expression, overview
metabolism
-
the prodomain of MMP13 determines autoactivation of MMP13 and intracellular degradation of MMP13
physiological function
-
functional role of MMP13 in tumor-induced osteolysis, MMP-13 regulates mammary tumor-induced osteolysis by activating MMP9 and transforming growth factor-beta signaling at the tumor-bone interface
physiological function
-
inhibition of MMP-13 reduces resorptive activity of the cells indicating that MMP-13 likely plays an important role in bone giant cell tumor. Mesenchymal stromal cells and the multinucleated giant cells cell-cell cooperation involves giant cell-derived cytokine up-regulation of MMP-13 in the stromal cells, which in turn assists the giant cells in bone resorption
physiological function
-
MMP-13 is a matrix metalloproteinase that is important for bone development and remodelling
physiological function
-
MMP-13 participate in the bone-remodeling mechanism involving the platelet-derived growth factor receptor
physiological function
-
MMP13 affects the keratinocyte migration in the skin, overview. Connective tissue growth factor, CTGF, blocks angiogenic activity of vascular epithelial growth factor, VEGF, by complex formation, and MMP13 re-activates VEGF activity through selective cleavage of CTGF in the complex
physiological function
-
MMP13 catalyzes the degradation of extracellular matrix components in the growth plate and at the same time cleaves and releases biologically active molecules stored in the extracellular matrix, such as the vascular endothelial growth factor A. In mice, ablation of Mmp9, Mmp13, or both Mmp9 and Mmp13 causes severe distortion of the metaphyseal growth plate
physiological function
-
MMP13 has an essential role in highly malignant and invasive growth in skin squamous cell carcinoma. Lack of host MMP13 strongly impairs implanted tumour growth of malignant skin squamous cell carcinoma cells, leading to small, mostly avascular cysts. MMP13 is essential for maintenance of angiogenesis and for invasion
physiological function
-
the MMP-13 knockout phenotype, which is due to an inability of chondrocytes to exit the growth plate, resolves completely by 12 weeks of age, suggesting that other (collagen degrading) proteases can at least partially functionally substitute for MMP13 in this developmental role
physiological function
-
MMP13 mediates cell proliferation in melanocytes and melanoma cells. Growth stimuli are mediated via MMP13 in melanocytes and melanoma
additional information
-
ALK1 and Alk5 are involved in MMP-13 activity regulation, age-related shift in ALK1/ALK5 ratio in murine cartilage. A change in balance between ALK5 and ALK1 receptors in chondrocytes causes changes in MMP-13 expression, thereby causing an osteoarthritis-like phenotype
additional information
-
angiotensin II promotes a stable fibrotic phenotype by inducing severe intra-plaque hemorrhages, characterized by increased degradation of interstitial collagen I via an MMP13 or MMP8-mediated mechanism, overview
additional information
-
cartilage structural damage in osteoarthritis in mice is dependent on MMP13 activity
additional information
-
down-regulation of MMP13, Birc2, or Birc3 results in reduced tumor growth when transplanted into immunodeficient recipient mice, high MMP13 expression enhances osteosarcoma cell survival
additional information
-
kinetics of MMP13 mRNA expression and tumor-induced osteolysis
additional information
-
potential role of MMP13 in choroidal angiogenesis in a murine model of laser-induced ocular neovascularisation. Deficiency of Mmp13 impaires choroidal neovascularization formation which is fully restored by wild-type bone marrow engraftment and partially rescued by several injections of wild-type mesenchymal stem cells. Mmp13 deficiency not only affects vessel recruitment, but also impairs their maturation through pericyte coverage
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). POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
-
the prodomain of MMP13 determines autoactivation of MMP13 and intracellular degradation of MMP13
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme complexed with a hydroxamate inhibitor, hanging-drop vapour diffusion method, 17 mg/ml protein in 10 mM HEPES, pH 7.5, with ammonium sufate to saturation, 18°C, 60 days, X-ray diffraction structure determination at 2.0 A resolution, and analysis
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
enzyme-null mice show profound defects in growth plate cartilage with markedly increased hyperthrophic domains and delay in indochondrial ossification and formation and vascularization of primary ossification centers. Cartilaginous growth plate abnormalities persist in adult animals and phenocopy defects observed in human hereditary chondrodysplasis
additional information
-
generation of MMP13 and MMP13/MMP9 knockout mice, that all show delayed wound closure compared to wild-type mice. The rate of re-epithelialization is significantly delayed in MMP-9 KO and MMP-13 KO mice and remarkably delayed in MMP-9/13 double KO mice, phenotype, overview
additional information
-
identification of mutations in MMP13 as the molecular basis of metaphyseal anadysplasia, MAD, overview. Recessive MAD is caused by homozygous loss of function of either MMP9 or MMP13, whereas dominant MAD is associated with missense mutations in the prodomain of MMP13 that determine autoactivation of MMP13 and intracellular degradation of both MMP13 and MMP9, resulting in a double enzymatic deficiency
additional information
-
knockdown of MMP13 expression at the tumor-bone interface leads to significant reduction in bone destruction and in the number of activated osteoclasts at the tumor-bone interface
additional information
-
MMP13 knockout mice are viable, healthy, and grossly normal. The absence of MMP13, however, delays the endochondral ossification process of skeletal development, knockout phenotype, overview. The mutant mice show hypertrophic chondrocytes within the articular cartilage of trabecular bone that is due to impaired remodeling of the extracellular matrix, and they show reduced apoptosis of the hypertrophic chondrocytes. Tibial cartilage erosion does not progress with time in MMP13 knockout mice
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
matrix metalloproteinase gene MMP13 and the antiapoptotic genes Birc2, cIAP1, and Birc3, cIAP2, form an amplicon located on chromosome 9A1, and show elevated expression in osteosarcomas
-
reverse transcription-PCR expression analysis of MMP13 in wild-type and mutant mice, overview
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
MMP13 is a direct target of osteoblast-specific transcription factor Osx in osteoblasts. Calvaria obtained from Osx-null embryos display dramatic reductions in MMP13 expression compared to wild-type calvaria. Stable overexpression of Osx stimulates MMP13 expression in C2C12 mesenchymal cells. Inhibition of Osx expression by siRNA leads to downregulation of MMP13 expression. Osx directly activates a 1 kb fragment of the MMP13 promoter in a dose-dependent manner
1,25-dihydroxy vitamin D3, 1,25D3, and T3 hormones induce MMP-13 expression in osteoblasts and are important for enzyme regulation in bone. The activation of MMP-13 expression by T3 is in a competitive balance with the regulation of osteocalcin expression, overview. PKA inhibitor HA1004 stimulates 1,25D3 activation of MMP-13 expression and reduces the stimulation by T3
-
BMP-2 siRNA induces a 60% increase in the expression of MMP-13 protein and a marked increase in the staining intensity for MMP-13 in the epithelial region of the BMP-2 siRNA treated mandibles
-
HDAC4 represses MMP-13 transcription in osteoblastic cells, and parathyroid hormone controls this repression
-
keratinocytes transfected with siRNA for MMP-13 exhibit downregulation of mRNA and protein expression of the MMP
-
mechanical strain induction of MMP-13 by high mechanical forces, with receptor of platelet-derived growth factor receptor alpha, PDGFR-alpha, as a potential mechanoreceptor in the MMP-13 induction, inhibited by platelet-derived growth factor receptor inhibitor AG1296, overview. The receptor performs autophosphorylation under mechanical stress
-
MMP13 expression is transiently induced by wounding, MMP-13 expression is negligible in the normal unwounded skin at day 0, but it increases on days 1 to 7 upon wounding, diminishes on day 14 and disappears on day 28
-
transfection of chondrocytes with adenovirus overexpressing constitutive active ALK1 increased MMP-13 expression, while small interfering RNA against ALK1 decreases MMP-13 expression to nondetectable levels
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
in a collagen-induced arthritis model, MMP-12 and MMP-13 activity probes based on derived from substrates Y(NO2)GPLG-LEEAK(Abz)G-NH2 and Y(NO2)GPAG-LYEK(Abz)G-NH2, respectively, discriminate between the activities of the 2 enzymes. In the disease model, MMP13 activity probe activation increases gradually after disease onset and correlates with disease severity over a longer period of 15 days
medicine
medicine
-
cartilaginous growth plate abnormalities result from enzyme deficiency in mice phenocopy defects observed in human hereditary chondrodysplasis
medicine
-
expression of enzyme and tissue inhibitor of matrix metalloproteinase, TIMP-1, is regulated by Wnt signaling combined with bone morphogenic protein BMP-2 in osteoblastic differentiation
medicine
-
MMP13 is a potential therapeutic target for breast cancer bone metastasis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Botos, I.; Meyer, E.; Swanson, S.M.; Lemaitre, V.; Eeckhout, Y.; Meyer, E.F.
Structure of recombinant mouse collagenase-3 (MMP-13)
J. Mol. Biol.
292
837-844
1999
Mus musculus (P33435), Mus musculus
Nakashima, A.; Tamura, M.
Regulation of matrix metalloproteinase-13 and tissue inhibitor of matrix metalloproteinase-1 gene expression by WNT3A and bone morphogenetic protein-2 in osteoblastic differentiation
Front. Biosci.
11
1667-1678
2006
Mus musculus
Inada, M.; Wang, Y.; Byrne, M.H.; Rahman, M.U.; Miyaura, C.; Lopez-Otin, C.; Krane, S.M.
Critical roles for collagenase-3 (Mmp13) in development of growth plate cartilage and in endochondral ossification
Proc. Natl. Acad. Sci. USA
101
17192-17197
2004
Mus musculus
Fallowfield, J.A.; Mizuno, M.; Kendall, T.J.; Constandinou, C.M.; Benyon, R.C.; Duffield, J.S.; Iredale, J.P.
Scar-associated macrophages are a major source of hepatic matrix metalloproteinase-13 and facilitate the resolution of murine hepatic fibrosis
J. Immunol.
178
5288-5295
2007
Mus musculus
Mukhin, Y.V.; Gooz, M.; Raymond, J.R.; Garnovskaya, M.N.
Collagenase-2 and -3 mediate epidermal growth factor receptor transactivation by bradykinin B2 receptor in kidney cells
J. Pharmacol. Exp. Ther.
318
1033-1043
2006
Mus musculus
Behonick, D.J.; Xing, Z.; Lieu, S.; Buckley, J.M.; Lotz, J.C.; Marcucio, R.S.; Werb, Z.; Miclau, T.; Colnot, C.
Role of matrix metalloproteinase 13 in both endochondral and intramembranous ossification during skeletal regeneration
PLoS ONE
2
e1150
2007
Mus musculus
Lausch, E.; Keppler, R.; Hilbert, K.; Cormier-Daire, V.; Nikkel, S.; Nishimura, G.; Unger, S.; Spranger, J.; Superti-Furga, A.; Zabel, B.
Mutations in MMP9 and MMP13 determine the mode of inheritance and the clinical spectrum of metaphyseal anadysplasia
Am. J. Hum. Genet.
85
168-178
2009
Mus musculus, Homo sapiens (P45452), Homo sapiens
Hattori, N.; Mochizuki, S.; Kishi, K.; Nakajima, T.; Takaishi, H.; DArmiento, J.; Okada, Y.
MMP-13 plays a role in keratinocyte migration, angiogenesis, and contraction in mouse skin wound healing
Am. J. Pathol.
175
533-546
2009
Mus musculus
Fukui, T.; Suga, T.; Iida, R.H.; Morito, M.; Luan, X.; Diekwisch, T.G.; Nakamura, Y.; Yamane, A.
BMP-2 regulates the formation of oral sulcus in mouse tongue by altering the balance between TIMP-1 and MMP-13
Anat. Rec. (Hoboken)
293
1408-1415
2010
Mus musculus
Cheng, C.; Tempel, D.; van Haperen, R.; van Damme, L.; Alguer, M.; Krams, R.; de Crom, R.
Activation of MMP8 and MMP13 by angiotensin II correlates to severe intra-plaque hemorrhages and collagen breakdown in atherosclerotic lesions with a vulnerable phenotype
Atherosclerosis
204
26-33
2009
Mus musculus
Ma, O.; Cai, W.W.; Zender, L.; Dayaram, T.; Shen, J.; Herron, A.J.; Lowe, S.W.; Man, T.K.; Lau, C.C.; Donehower, L.A.
MMP13, Birc2 (cIAP1), and Birc3 (cIAP2), amplified on chromosome 9, collaborate with p53 deficiency in mouse osteosarcoma progression
Cancer Res.
69
2559-2567
2009
Homo sapiens, Mus musculus
Nannuru, K.C.; Futakuchi, M.; Varney, M.L.; Vincent, T.M.; Marcusson, E.G.; Singh, R.K.
Matrix metalloproteinase (MMP)-13 regulates mammary tumor-induced osteolysis by activating MMP9 and transforming growth factor-beta signaling at the tumor-bone interface
Cancer Res.
70
3494-3504
2010
Mus musculus
Lederle, W.; Hartenstein, B.; Meides, A.; Kunzelmann, H.; Werb, Z.; Angel, P.; Mueller, M.M.
MMP13 as a stromal mediator in controlling persistent angiogenesis in skin carcinoma
Carcinogenesis
31
1175-1184
2010
Mus musculus
Lecomte, J.; Louis, K.; Detry, B.; Blacher, S.; Lambert, V.; Bekaert, S.; Munaut, C.; Paupert, J.; Blaise, P.; Foidart, J.M.; Rakic, J.M.; Krane, S.M.; Noel, A.
Bone marrow-derived mesenchymal cells and MMP13 contribute to experimental choroidal neovascularization
Cell. Mol. Life Sci.
68
677-686
2011
Homo sapiens (P45452), Homo sapiens, Mus musculus, Mus musculus C57BL/6
Varga, F.; Rumpler, M.; Spitzer, S.; Karlic, H.; Klaushofer, K.
Osteocalcin attenuates T3- and increases vitamin D3-induced expression of MMP-13 in mouse osteoblasts
Endocr. J.
56
441-450
2009
Mus musculus
Mak, I.W.; Seidlitz, E.P.; Cowan, R.W.; Turcotte, R.E.; Popovic, S.; Wu, W.C.; Singh, G.; Ghert, M.
Evidence for the role of matrix metalloproteinase-13 in bone resorption by giant cell tumor of bone
Hum. Pathol.
41
1320-1329
2010
Homo sapiens, Mus musculus
Yang, C.M.; Hsieh, H.L.; Yao, C.C.; Hsiao, L.D.; Tseng, C.P.; Wu, C.B.
Protein kinase C-delta transactivates platelet-derived growth factor receptor-alpha in mechanical strain-induced collagenase 3 (matrix metalloproteinase-13) expression by osteoblast-like cells
J. Biol. Chem.
284
26040-26050
2009
Mus musculus
Shimizu, E.; Selvamurugan, N.; Westendorf, J.J.; Olson, E.N.; Partridge, N.C.
HDAC4 represses matrix metalloproteinase-13 transcription in osteoblastic cells, and parathyroid hormone controls this repression
J. Biol. Chem.
285
9616-9626
2010
Mus musculus, Rattus norvegicus
Blaney Davidson, E.N.; Remst, D.F.; Vitters, E.L.; van Beuningen, H.M.; Blom, A.B.; Goumans, M.J.; van den Berg, W.B.; van der Kraan, P.M.
Increase in ALK1/ALK5 ratio as a cause for elevated MMP-13 expression in osteoarthritis in humans and mice
J. Immunol.
182
7937-7945
2009
Homo sapiens, Mus musculus
Li, J.J.; Johnson, A.R.
Selective MMP13 inhibitors
Med. Res. Rev.
31
863-894
2011
Homo sapiens, Mus musculus, Rattus norvegicus
Meierjohann, S.; Hufnagel, A.; Wende, E.; Kleinschmidt, M.A.; Wolf, K.; Friedl, P.; Gaubatz, S.; Schartl, M.
MMP13 mediates cell cycle progression in melanocytes and melanoma cells: in vitro studies of migration and proliferation
Mol. Cancer
9
201
2010
Homo sapiens, Mus musculus
Lim, N.; Meinjohanns, E.; Bou-Gharios, G.; Gompels, L.; Nuti, E.; Rossello, A.; Devel, L.; Dive, V.; Meldal, M.; Nagase, H.
In vivo imaging of matrix metalloproteinase 12 and matrix metalloproteinase 13 activities in the mouse model of collagen-induced arthritis
Arthritis Rheumatol.
66
589-598
2014
Mus musculus (P33435), Mus musculus
Zhang, C.; Tang, W.; Li, Y.
Matrix metalloproteinase 13 (MMP13) is a direct target of osteoblast-specific transcription factor osterix (Osx) in osteoblasts
PLoS ONE
7
e50525
2012
Mus musculus (P33435)
Waldron, A.L.; Schroder, P.A.; Bourgon, K.L.; Bolduc, J.K.; Miller, J.L.; Pellegrini, A.D.; Dubois, A.L.; Blaszkiewicz, M.; Townsend, K.L.; Rieger, S.
Oxidative stress-dependent MMP-13 activity underlies glucose neurotoxicity
J. Diabetes Complicat.
32
249-257
2018
Danio rerio, Mus musculus (P33435)
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