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Search results 401 to 447 out of 447 for Mmp8

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0.019s

Type

Details

Score

Publication

10622708 | -

First Author:	Wang X
Year:	1999
Journal:	FEBS Lett
Title:	Expression, purification and characterization of recombinant mouse MT5-MMP protein products.
Volume:	462
Issue:	3
Pages:	261-6

•

Publication

11278606 | -

First Author:	Iida J
Year:	2001
Journal:	J Biol Chem
Title:	Melanoma chondroitin sulfate proteoglycan regulates matrix metalloproteinase-dependent human melanoma invasion into type I collagen.
Volume:	276
Issue:	22
Pages:	18786-94

•

Publication

14681236 | -

First Author:	Zhao H
Year:	2004
Journal:	J Biol Chem
Title:	Differential inhibition of membrane type 3 (MT3)-matrix metalloproteinase (MMP) and MT1-MMP by tissue inhibitor of metalloproteinase (TIMP)-2 and TIMP-3 rgulates pro-MMP-2 activation.
Volume:	279
Issue:	10
Pages:	8592-601

•

Publication

17616928 | -

First Author:	Walsh LA
Year:	2007
Journal:	Int J Dev Biol
Title:	Soluble membrane-type 3 matrix metalloprioteinase causes changes in gene expression and increased gelatinase activity during Xenopus laevis development.
Volume:	51
Issue:	5
Pages:	389-95

•

Publication

10559137 | -

First Author:	Fernandez-Patron C
Year:	1999
Journal:	Circ Res
Title:	Vascular matrix metalloproteinase-2 cleaves big endothelin-1 yielding a novel vasoconstrictor.
Volume:	85
Issue:	10
Pages:	906-11

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Publication

11029402 | -

First Author:	Fernandez-Patron C
Year:	2000
Journal:	Circ Res
Title:	Vascular matrix metalloproteinase-2-dependent cleavage of calcitonin gene-related peptide promotes vasoconstriction.
Volume:	87
Issue:	8
Pages:	670-6

•

Publication

16115940 | -

First Author:	Kim SK
Year:	2005
Journal:	Clin Cancer Res
Title:	PEX-producing human neural stem cells inhibit tumor growth in a mouse glioma model.
Volume:	11
Issue:	16
Pages:	5965-70

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Publication

9476898 | -

First Author:	Brooks PC
Year:	1998
Journal:	Cell
Title:	Disruption of angiogenesis by PEX, a noncatalytic metalloproteinase fragment with integrin binding activity.
Volume:	92
Issue:	3
Pages:	391-400

•

Publication

22262494 | -

First Author:	Host L
Year:	2012
Journal:	Int J Cancer
Title:	The proteolytic activity of MT4-MMP is required for its pro-angiogenic and pro-metastatic promoting effects.
Volume:	131
Issue:	7
Pages:	1537-48

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Publication

18286233 | -

First Author:	Sohail A
Year:	2008
Journal:	Cancer Metastasis Rev
Title:	MT4-(MMP17) and MT6-MMP (MMP25), A unique set of membrane-anchored matrix metalloproteinases: properties and expression in cancer.
Volume:	27
Issue:	2
Pages:	289-302

•

Protein Domain

IPR028723 | MMP24

Type:

Family

Description:

Matrix metalloproteinases (MMPs) are zinc-dependent and calcium-dependent proteases that cleave within a polypeptide (endopeptidases). They degrade most components of the extracellular matrix (such as growth factors, their binding proteins, and other bioactive molecules, as well as binding sites for cell-surface molecules) and some non-extracellular-matrix molecules []. Two categories of MMPs can be recognised based on their cellular localisation: soluble vs. membrane-bound. The soluble MMPs are divided into the collagenases (MMP1, MMP8 and MMP13), gelatinases (MMP2 and MMP9), stromelysins (MMP3, MMP12) and those yet to be classified. The membrane-bound MMPs include MT1, 2, 3, 4, 5 and their hallmark is the presence of plasma membrane anchoring domains []. MMPs are highly expressed in various cancers, both by tumour cells and in surrounding stromal cells such as macrophages []. Matrix metalloproteinase-24 (MMP24; MEROPS identifier M10.023), or membrane-type matrix metalloproteinase 5 (MT5), activates progelatinase A (also known as MMP-2), which is involved in diverse functions such as remodelling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture []. MMP24 may play an important role in extracellular matrix remodelling events in the brain and during embryonic development [].

•

Protein Domain

IPR028726 | MMP17

Type:

Family

Description:

Matrix metalloproteinases (MMPs) are zinc-dependent and calcium-dependent proteases that cleave within a polypeptide (endopeptidases). They degrade most components of the extracellular matrix (such as growth factors, their binding proteins, and other bioactive molecules, as well as binding sites for cell-surface molecules) and some non-extracellular-matrix molecules []. Two categories of MMPs can be recognised based on their cellular localisation: soluble vs. membrane-bound. The soluble MMPs are divided into the collagenases (MMP1, MMP8 and MMP13), gelatinases (MMP2 and MMP9), stromelysins (MMP3, MMP12) and those yet to be classified. The membrane-bound MMPs include MT1, 2, 3, 4, 5 and their hallmark is the presence of plasma membrane anchoring domains []. MMPs are highly expressed in various cancers, both by tumour cells and in surrounding stromal cells such as macrophages []. Matrix metalloproteinase-17 (MMP17; MEROPS identifier M10.017) or membrane-type matrix metalloproteinase 4 degrades various components of the extracellular matrix, such as fibrin. It may be involved in the activation of membrane-bound precursors of growth factors or inflammatory mediators, such as tumour necrosis factor-alpha []. It may also be involved in tumour progression [, ].

•

Protein Domain

IPR028708 | 72kDa_collagenase

Type:

Family

Description:

Matrix metalloproteinases (MMPs) are zinc-dependent and calcium-dependent proteases that cleave within a polypeptide (endopeptidases). They degrade most components of the extracellular matrix (such as growth factors, their binding proteins, and other bioactive molecules, as well as binding sites for cell-surface molecules) and some non-extracellular-matrix molecules []. Two categories of MMPs can be recognised based on their cellular localisation: soluble vs. membrane-bound. The soluble MMPs are divided into the collagenases (MMP1, MMP8 and MMP13), gelatinases (MMP2 and MMP9), stromelysins (MMP3, MMP12) and those yet to be classified. The membrane-bound MMPs include MT1, 2, 3, 4, 5 and their hallmark is the presence of plasma membrane anchoring domains []. MMPs are highly expressed in various cancers, both by tumour cells and in surrounding stromal cells such as macrophages []. 72kDa type IV collagenase, also known as 72kDa gelatinase or matrix metalloproteinase-2 (MMP2; MEROPS identifier M10.003), is a ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumour invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction [, ]. PEX, a naturally occurring fragment of human MMP2, acts as an inhibitor of cell proliferation, migration, and angiogenesis [, ].

•

Protein Domain

IPR028697 | MMP16

Type:

Family

Description:

Matrix metalloproteinases (MMPs) are zinc-dependent and calcium-dependent proteases that cleave within a polypeptide (endopeptidases). They degrade most components of the extracellular matrix (such as growth factors, their binding proteins, and other bioactive molecules, as well as binding sites for cell-surface molecules) and some non-extracellular-matrix molecules []. Two categories of MMPs can be recognised based on their cellular localisation: soluble vs. membrane-bound. The soluble MMPs are divided into the collagenases (MMP1, MMP8 and MMP13), gelatinases (MMP2 and MMP9), stromelysins (MMP3, MMP12) and those yet to be classified. The membrane-bound MMPs include MT1, 2, 3, 4, 5 and their hallmark is the presence of plasma membrane anchoring domains []. MMPs are highly expressed in various cancers, both by tumour cells and in surrounding stromal cells such as macrophages []. Matrix metalloproteinase-16 (MMP16; MEROPS identifier M10.016), also called MT3-MMP, degrades various components of the extracellular matrix, such as collagen type III and fibronectin. It has no effect on type I, II, IV and V collagen. However, upon interaction with CSPG4, it may be involved in degradation and invasion of type I collagen by melanoma cells []. MMP-16 can not only directly degrade some matrix molecules, but can also activate pro-MMP-2 (gelatinase A), one of the most important MMPs in tissue remodelling and cell migration [, ].

•

Publication

32552811 | J:291900

First Author:	Wang Q
Year:	2020
Journal:	Respir Res
Title:	E-cigarette-induced pulmonary inflammation and dysregulated repair are mediated by nAChR α7 receptor: role of nAChR α7 in SARS-CoV-2 Covid-19 ACE2 receptor regulation.
Volume:	21
Issue:	1
Pages:	154

•

Publication

25910275 | J:235104

First Author:	Dadson K
Year:	2015
Journal:	PLoS One
Title:	Temporal and Molecular Analyses of Cardiac Extracellular Matrix Remodeling following Pressure Overload in Adiponectin Deficient Mice.
Volume:	10
Issue:	4
Pages:	e0121049

•

Publication

34403447 | J:357121

First Author:	Koyuncu D
Year:	2021
Journal:	PLoS Pathog
Title:	CXCL1: A new diagnostic biomarker for human tuberculosis discovered using Diversity Outbred mice.
Volume:	17
Issue:	8
Pages:	e1009773

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Protein

Q91ZS5

Organism:	Mus musculus/domesticus
Length:	56
Fragment?:	true

•

Protein

A2A5K8

Organism:	Mus musculus/domesticus
Length:	67
Fragment?:	true

•

Publication

1480034 | -

First Author:	Tschesche H
Year:	1992
Journal:	Matrix Suppl
Title:	Latent collagenase and gelatinase from human neutrophils and their activation.
Volume:	1

Pages:	245-55

•

Publication

17709402 | -

First Author:	Van Lint P
Year:	2007
Journal:	J Leukoc Biol
Title:	Chemokine and cytokine processing by matrix metalloproteinases and its effect on leukocyte migration and inflammation.
Volume:	82
Issue:	6
Pages:	1375-81

•

Publication

22496659 | J:195392

First Author:	Bradley LM
Year:	2012
Journal:	PLoS Pathog
Title:	Matrix metalloprotease 9 mediates neutrophil migration into the airways in response to influenza virus-induced toll-like receptor signaling.
Volume:	8
Issue:	4
Pages:	e1002641

•

Publication

12814943 | -

First Author:	Ortega N
Year:	2003
Journal:	Ann N Y Acad Sci
Title:	How proteases regulate bone morphogenesis.
Volume:	995

Pages:	109-16

•

Publication

22410640 | -

First Author:	Ben-David D
Year:	2012
Journal:	Inflamm Res
Title:	The involvement of oxidants and NF-κB in cytokine-induced MMP-9 synthesis by bone marrow-derived osteoprogenitor cells.
Volume:	61
Issue:	7
Pages:	673-88

•

Publication

15883642 | -

First Author:	Alvarez J
Year:	2005
Journal:	J Bone Miner Res
Title:	Expression patterns of matrix metalloproteinases and vascular endothelial growth factor during epiphyseal ossification.
Volume:	20
Issue:	6
Pages:	1011-21

•

Publication

22326910 | -

First Author:	Dziembowska M
Year:	2012
Journal:	Int J Biochem Cell Biol
Title:	MMP9: a novel function in synaptic plasticity.
Volume:	44
Issue:	5
Pages:	709-13

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Publication

12879005 | -

First Author:	Takino T
Year:	2003
Journal:	Oncogene
Title:	Cleavage of metastasis suppressor gene product KiSS-1 protein/metastin by matrix metalloproteinases.
Volume:	22
Issue:	30
Pages:	4617-26

•

Protein Domain

IPR028688 | MMP9

Type:

Family

Description:

Matrix metalloproteinases (MMPs) are zinc-dependent and calcium-dependent proteases that cleave within a polypeptide (endopeptidases). They degrade most components of the extracellular matrix (such as growth factors, their binding proteins, and other bioactive molecules, as well as binding sites for cell-surface molecules) and some non-extracellular-matrix molecules []. Two categories of MMPs can be recognised based on their cellular localisation: soluble vs. membrane-bound. The soluble MMPs are divided into the collagenases (MMP1, MMP8 and MMP13), gelatinases (MMP2 and MMP9), stromelysins (MMP3, MMP12) and those yet to be classified. The membrane-bound MMPs include MT1, 2, 3, 4, 5 and their hallmark is the presence of plasma membrane anchoring domains []. MMPs are highly expressed in various cancers, both by tumour cells and in surrounding stromal cells such as macrophages []. This entry represents matrix metalloproteinase-9 (MMP9, also known as gelatinase B), which is involved in matrix remodelling during the normal processes of embryogenesis, tissue remodelling and development []. It is released extracellularly in a pro-form with the enzymatic site covered by a propeptide that has to be cleaved off to reveal the activity. MMP9 can cleave gelatin types I and V and collagen types IV and V []. It plays an essential role in local proteolysis of the extracellular matrix and in leukocyte migration [, ]. MMP9 is one of the key regulators for remodelling skeletal tissues [], and could play a role in bone osteoclastic resorption triggered by inflammatory processes [, ]. MMP9 also has a role in synaptic plasticity []. MMP9 cleaves the metastasis suppressor gene product KiSS1 [].

•

Protein

Q6GXA5

Organism:	Mus musculus/domesticus
Length:	111
Fragment?:	true

•

Protein

Q6GX95

Organism:	Mus musculus/domesticus
Length:	78
Fragment?:	true

•

Protein

Q6GXA2

Organism:	Mus musculus/domesticus
Length:	68
Fragment?:	true

•

Protein

Q6GX96

Organism:	Mus musculus/domesticus
Length:	103
Fragment?:	true

•

Protein

A0A1B0GS88

Organism:	Mus musculus/domesticus
Length:	126
Fragment?:	true

•

Protein

Q8BSA6

Organism:	Mus musculus/domesticus
Length:	161
Fragment?:	true

•

Protein

B1AVG8

Organism:	Mus musculus/domesticus
Length:	127
Fragment?:	true

•

Protein

B1AVH0

Organism:	Mus musculus/domesticus
Length:	174
Fragment?:	true

•

Protein

Q9R0S3

Organism:	Mus musculus/domesticus
Length:	578
Fragment?:	false

•

Protein

Q9R0S2

Organism:	Mus musculus/domesticus
Length:	618
Fragment?:	false

•

Protein

O54732

Organism:	Mus musculus/domesticus
Length:	657
Fragment?:	false

•

Protein

P33434

Organism:	Mus musculus/domesticus
Length:	662
Fragment?:	false

•

Protein

P41245

Organism:	Mus musculus/domesticus
Length:	730
Fragment?:	false

•

Protein

Q9WTR0

Organism:	Mus musculus/domesticus
Length:	607
Fragment?:	false

•

Protein

Q3UQ52

Organism:	Mus musculus/domesticus
Length:	730
Fragment?:	false

•

Protein

Q3UG07

Organism:	Mus musculus/domesticus
Length:	662
Fragment?:	false

•

Protein

V9GXD8

Organism:	Mus musculus/domesticus
Length:	415
Fragment?:	false

•

Protein

Q3TTU7

Organism:	Mus musculus/domesticus
Length:	730
Fragment?:	false

•

Protein

Q2M4J5

Organism:	Mus musculus/domesticus
Length:	730
Fragment?:	false

•

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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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