Membrane type-1 matrix metalloproteinase (MT1-MMP) processing of pro-alphav integrin regulates cross-talk between alphavbeta3 and alpha2beta1 integrins in breast carcinoma cells (Q40620302)

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scientific article published on November 2003

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English	Membrane type-1 matrix metalloproteinase (MT1-MMP) processing of pro-alphav integrin regulates cross-talk between alphavbeta3 and alpha2beta1 integrins in breast carcinoma cells	scientific article published on November 2003

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scholarly article

1 reference

Europe PubMed Central

22 September 2017

Membrane type-1 matrix metalloproteinase (MT1-MMP) processing of pro-alphav integrin regulates cross-talk between alphavbeta3 and alpha2beta1 integrins in breast carcinoma cells (English)

1 reference

Europe PubMed Central

22 September 2017

breast carcinoma

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based on heuristic

inferred from title

4

1 reference

Europe PubMed Central

22 September 2017

author name string

Peter C Baciu

1

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Europe PubMed Central

22 September 2017

E Aisha Suleiman

2

1 reference

Europe PubMed Central

22 September 2017

Elena I Deryugina

3

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Europe PubMed Central

22 September 2017

language of work or name

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publication date

1 November 2003

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Europe PubMed Central

22 September 2017

Experimental Cell Research

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Europe PubMed Central

22 September 2017

291

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Europe PubMed Central

22 September 2017

1

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Europe PubMed Central

22 September 2017

167-175

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Europe PubMed Central

22 September 2017

Membrane type 1-matrix metalloproteinase is activated during migration of human endothelial cells and modulates endothelial motility and matrix remodeling

1 reference

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Matrix metalloproteinases regulate neovascularization by acting as pericellular fibrinolysins

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Matrix-directed regulation of pericellular proteolysis and tumor progression

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

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Cell surface binding and activation of gelatinase A induced by expression of membrane-type-1-matrix metalloproteinase (MT1-MMP)

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Cell surface binding of TIMP-2 and pro-MMP-2/TIMP-2 complex

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Membrane-type 1 matrix metalloprotease (MT1-MMP) enables invasive migration of glioma cells in central nervous system white matter

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An alternative processing of integrin alpha(v) subunit in tumor cells by membrane type-1 matrix metalloproteinase

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Matrix-dependent proteolysis of surface transglutaminase by membrane-type metalloproteinase regulates cancer cell adhesion and locomotion.

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Membrane-type 1 matrix metalloproteinase cleaves CD44 and promotes cell migration

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The hemopexin-like C-terminal domain of membrane type 1 matrix metalloproteinase regulates proteolysis of a multifunctional protein, gC1qR

1 reference

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Endoproteolytic processing of integrin pro-α subunits involves the redundant function of furin and proprotein convertase (PC) 5A, but not paired basic amino acid converting enzyme (PACE) 4, PC5B or PC7

1 reference

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Functional activation of integrin alpha V beta 3 in tumor cells expressing membrane-type 1 matrix metalloproteinase

1 reference

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Processing of integrin alpha(v) subunit by membrane type 1 matrix metalloproteinase stimulates migration of breast carcinoma cells on vitronectin and enhances tyrosine phosphorylation of focal adhesion kinase

1 reference

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Regulation of cell invasion and morphogenesis in a three-dimensional type I collagen matrix by membrane-type matrix metalloproteinases 1, 2, and 3.

1 reference

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Matrix metalloproteinases (MMPs) regulate fibrin-invasive activity via MT1-MMP-dependent and -independent processes

1 reference

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MT1-MMP initiates activation of pro-MMP-2 and integrin alphavbeta3 promotes maturation of MMP-2 in breast carcinoma cells

1 reference

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Trans-dominant inhibition of integrin function.

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Role of endoproteolytic processing in the adhesive and signaling functions of alphavbeta5 integrin

1 reference

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Identification of the cleavage sites in the alpha6A integrin subunit: structural requirements for cleavage and functional analysis of the uncleaved alpha6Abeta1 integrin

1 reference

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7 January 2021

Prinomastat, a hydroxamate inhibitor of matrix metalloproteinases, has a complex effect on migration of breast carcinoma cells

1 reference

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7 January 2021

Activated R-ras, Rac1, PI 3-kinase and PKCepsilon can each restore cell spreading inhibited by isolated integrin beta1 cytoplasmic domains

1 reference

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Single subunit chimeric integrins as mimics and inhibitors of endogenous integrin functions in receptor localization, cell spreading and migration, and matrix assembly

1 reference

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7 January 2021

Identifiers

10.1016/S0014-4827(03)00387-2

1 reference

Europe PubMed Central

22 September 2017

1 reference

Europe PubMed Central

22 September 2017

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