Biochemical characterization of the catalytic domain of membrane-type 4 matrix metalloproteinase. - Wikidata - wikimedia - TriplyDB

Biochemical characterization of the catalytic domain of membrane-type 4 matrix metalloproteinase.

Biochemical characterization of the catalytic domain of membrane-type 4 matrix metalloproteinase.

http://www.wikidata.org/entity/Q33878616

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Mmp17b is essential for proper neural crest cell migration in vivo Membrane type 4 matrix metalloproteinase (MMP17) has tumor necrosis factor-alpha convertase activity but does not activate pro-MMP2.Catalytic activities of membrane-type 6 matrix metalloproteinase (MMP25).Matrix metalloproteinase inhibitors: do they have a place in anticancer therapy?Membrane-type 4 matrix metalloproteinase (MT4-MMP) induces lung metastasis by alteration of primary breast tumour vascular architecture.Constraining specificity in the N-domain of tissue inhibitor of metalloproteinases-1; gelatinase-selective inhibitors.Leukocyte cell surface proteinases: regulation of expression, functions, and mechanisms of surface localization.MT4-(MMP17) and MT6-MMP (MMP25), A unique set of membrane-anchored matrix metalloproteinases: properties and expression in cancer Coordinate action of membrane-type matrix metalloproteinase-1 (MT1-MMP) and MMP-2 enhances pericellular proteolysis and invasion.New Strategies for the Next Generation of Matrix-Metalloproteinase Inhibitors: Selectively Targeting Membrane-Anchored MMPs with Therapeutic Antibodies.Secretion of gelatinases and activation of gelatinase A (MMP-2) by human rheumatoid synovial fibroblasts.Developmental expression of membrane type 4-matrix metalloproteinase (Mt4-mmp/Mmp17) in the mouse embryo

P2860

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P2860

Biochemical characterization of the catalytic domain of membrane-type 4 matrix metalloproteinase.

http://www.wikidata.org/entity/Q33878616

description

1999 nî lūn-bûn

@nan

1999 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

1999 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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1999年の論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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1999年论文

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name

Biochemical characterization o ...... pe 4 matrix metalloproteinase.

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Biochemical characterization o ...... pe 4 matrix metalloproteinase.

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Biological Chemistry

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Biochemical characterization o ...... pe 4 matrix metalloproteinase.

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P2093

Essers L

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Kolkenbrock H

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Ulbrich N

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Will H

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P2860

Identification of the second membrane-type matrix metalloproteinase (MT-MMP-2) gene from a human placenta cDNA library. MT-MMPs form a unique membrane-type subclass in the MMP family

A matrix metalloproteinase expressed on the surface of invasive tumour cells

cDNA sequence and mRNA tissue distribution of a novel human matrix metalloproteinase with a potential transmembrane segment

Cellular mechanisms for human procollagenase-3 (MMP-13) activation. Evidence that MT1-MMP (MMP-14) and gelatinase a (MMP-2) are able to generate active enzyme

Expression of three membrane-type matrix metalloproteinases (MT-MMPs) in rat vascular smooth muscle cells and characterization of MT3-MMPs with and without transmembrane domain

Human 72-kilodalton type IV collagenase forms a complex with a tissue inhibitor of metalloproteases designated TIMP-2

The activity of the tissue inhibitors of metalloproteinases is regulated by C-terminal domain interactions: a kinetic analysis of the inhibition of gelatinase A.

Synthetic substrates for vertebrate collagenase.

Assay of coagulation proteases using peptide chromogenic and fluorogenic substrates.

The complex between a tissue inhibitor of metalloproteinases (TIMP-2) and 72-kDa progelatinase is a metalloproteinase inhibitor.

P304

1103-1108

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scholarly article

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10.1515/BC.1999.137

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9

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380

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10543448

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