Thrombin-dependent MMP-2 activity is regulated by heparan sulfate. - Wikidata - wikimedia - TriplyDB

Thrombin-dependent MMP-2 activity is regulated by heparan sulfate.

Thrombin-dependent MMP-2 activity is regulated by heparan sulfate.

http://www.wikidata.org/entity/Q34438694

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Increased permeability of blood-brain barrier is mediated by serine protease during Cryptococcus meningitis Heparinoids activate a protease, secreted by mucosa and tumors, via tethering supplemented by allostery.Dimerization of matrix metalloproteinase-2 (MMP-2): functional implication in MMP-2 activation Prevention of preterm birth: harnessing science to address the global epidemic.Actions of thrombin in the interstitium.Identification of High-Risk Plaques by MRI and Fluorescence Imaging in a Rabbit Model of Atherothrombosis.Thrombin stimulates VSMC proliferation through an EGFR-dependent pathway: involvement of MMP-2.

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Thrombin-dependent MMP-2 activity is regulated by heparan sulfate.

http://www.wikidata.org/entity/Q34438694

description

2010 nî lūn-bûn

@nan

2010 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

Thrombin-dependent MMP-2 activity is regulated by heparan sulfate.

@ast

Thrombin-dependent MMP-2 activity is regulated by heparan sulfate.

@en

Thrombin-dependent MMP-2 activity is regulated by heparan sulfate.

@nl

type

label

Thrombin-dependent MMP-2 activity is regulated by heparan sulfate.

@ast

Thrombin-dependent MMP-2 activity is regulated by heparan sulfate.

@en

Thrombin-dependent MMP-2 activity is regulated by heparan sulfate.

@nl

prefLabel

Thrombin-dependent MMP-2 activity is regulated by heparan sulfate.

@ast

Thrombin-dependent MMP-2 activity is regulated by heparan sulfate.

@en

Thrombin-dependent MMP-2 activity is regulated by heparan sulfate.

@nl

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JBC.M110.171595

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Journal of Biological Chemistry

P1476

Thrombin-dependent MMP-2 activity is regulated by heparan sulfate.

@en

P2093

Bon-Hun Koo

http://www.w3.org/2001/XMLSchema#string

Doo-Sik Kim

http://www.w3.org/2001/XMLSchema#string

Jung Ho Han

http://www.w3.org/2001/XMLSchema#string

Young Il Yeom

http://www.w3.org/2001/XMLSchema#string

P2860

Suppression of membrane-type 1 matrix metalloproteinase (MMP)-mediated MMP-2 activation and tumor invasion by testican 3 and its splicing variant gene product, N-Tes

Matrix metalloproteinases: old dogs with new tricks

Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed

Activation of pro-(matrix metalloproteinase-2) (pro-MMP-2) by thrombin is membrane-type-MMP-dependent in human umbilical vein endothelial cells and generates a distinct 63 kDa active species

The membrane-anchored MMP inhibitor RECK is a key regulator of extracellular matrix integrity and angiogenesis

Heparan sulfate proteoglycans as extracellular docking molecules for matrilysin (matrix metalloproteinase 7)

Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease

Human progelatinase A can be activated by matrilysin

Activation of type IV procollagenases by human tumor-associated trypsin-2

The TIMP2 membrane type 1 metalloproteinase "receptor" regulates the concentration and efficient activation of progelatinase A. A kinetic study

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41270-41279

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scholarly article

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10.1074/JBC.M110.171595

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53

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285

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2010-11-01T00:00:00Z

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21041295

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3009852

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