Localization of matrix metalloproteinase MMP-2 to the surface of invasive cells by interaction with integrin alpha v beta 3. (Q34733220)

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16 October 2019

title

Localization of matrix metalloproteinase MMP-2 to the surface of invasive cells by interaction with integrin alpha v beta 3 (English)

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16 October 2019

2

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William G Stetler-Stevenson

16 October 2019

6

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16 October 2019

author name string

P C Brooks

1

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16 October 2019

L C Sanders

3

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16 October 2019

T L von Schalscha

4

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16 October 2019

R T Aimes

5

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16 October 2019

J P Quigley

7

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16 October 2019

D A Cheresh

8

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16 October 2019

publication date

1 May 1996

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16 October 2019

language of work or name

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16 October 2019

volume

85

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16 October 2019

issue

5

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16 October 2019

page(s)

683-693

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Cloning of a 72 kDa matrix metalloproteinase (gelatinase) from chicken embryo fibroblasts using gene family PCR: expression of the gelatinase increases upon malignant transformation

16 October 2019

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Proteolytic remodeling of extracellular matrix

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Urokinase and urokinase receptor: a paracrine/autocrine system regulating cell migration and invasiveness

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Subtractive immunization yields monoclonal antibodies that specifically inhibit metastasis

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Requirement of vascular integrin alpha v beta 3 for angiogenesis

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Integrin alpha v beta 3 antagonists promote tumor regression by inducing apoptosis of angiogenic blood vessels

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Antiintegrin alpha v beta 3 blocks human breast cancer growth and angiogenesis in human skin

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The C-terminal region of membrane type matrix metalloproteinase is a functional transmembrane domain required for pro-gelatinase A activation

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Prevention of metastasis by inhibition of the urokinase receptor

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Affinity of integrins for damaged extracellular matrix: alpha v beta 3 binds to denatured collagen type I through RGD sites

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Vitronectin and its receptors

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Requirement of the NPXY motif in the integrin beta 3 subunit cytoplasmic tail for melanoma cell migration in vitro and in vivo.

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Definition of Two Angiogenic Pathways by Distinct alpha(v) Integrins

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Glioblastoma expression of vitronectin and the alpha v beta 3 integrin. Adhesion mechanism for transformed glial cells

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Integrins: versatility, modulation, and signaling in cell adhesion

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Stability analysis of latent and active 72-kDa type IV collagenase: the role of tissue inhibitor of metalloproteinases-2 (TIMP-2).

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7 January 2021

Structural biochemistry and activation of matrix metalloproteases

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Expression of adhesion-related membrane components in adherent versus nonadherent hamster melanoma cells

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7 January 2021

Tumor cell adhesion to the extracellular matrix and signal transduction mechanisms implicated in tumor cell motility, invasion and metastasis

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7 January 2021

Cancer metastasis and angiogenesis: An imbalance of positive and negative regulation

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Biology and biochemistry of proteinases in tumor invasion.

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Integrin alpha v beta 3 rescues melanoma cells from apoptosis in three-dimensional dermal collagen

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A metalloproteinase inhibitor as an inhibitor of neovascularization

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The C-terminal domain of 72 kDa gelatinase A is not required for catalysis, but is essential for membrane activation and modulates interactions with tissue inhibitors of metalloproteinases

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7 January 2021

Co-culture of human breast adenocarcinoma MCF-7 cells and human dermal fibroblasts enhances the production of matrix metalloproteinases 1, 2 and 3 in fibroblasts

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7 January 2021

Modulation of bovine microvascular endothelial cell proteolytic properties by inhibitors of angiogenesis

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7 January 2021

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7 January 2021

A matrix metalloproteinase expressed on the surface of invasive tumour cells

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7 January 2021

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7 January 2021

Tissue inhibitor of metalloproteinases-2 inhibits the activation of 72 kDa progelatinase by fibroblast membranes

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7 January 2021

Integrins alpha v beta 3 and alpha v beta 5 contribute to cell attachment to vitronectin but differentially distribute on the cell surface

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7 January 2021

The precursor region of a protein active in sperm-egg fusion contains a metalloprotease and a disintegrin domain: structural, functional, and evolutionary implications

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7 January 2021

ADAM, a novel family of membrane proteins containing A Disintegrin And Metalloprotease domain: multipotential functions in cell-cell and cell-matrix interactions

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Identifiers

DOI

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16 October 2019

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