Recognition of the N-terminal modules of thrombospondin-1 and thrombospondin-2 by alpha6beta1 integrin. (Q44543826)

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6 November 2019

title

Recognition of the N-terminal modules of thrombospondin-1 and thrombospondin-2 by alpha6beta1 integrin (English)

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6 November 2019

7

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6 November 2019

Peter Yurchenco

4

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6 November 2019

author name string

Maria J Calzada

1

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6 November 2019

John M Sipes

2

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6 November 2019

Henry C Krutzsch

3

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6 November 2019

Douglas S Annis

5

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6 November 2019

Deane F Mosher

6

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6 November 2019

language of work or name

English

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publication date

8 August 2003

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Journal of Biological Chemistry

6 November 2019

published in

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6 November 2019

volume

278

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6 November 2019

issue

42

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6 November 2019

page(s)

40679-40687

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Integrins: bidirectional, allosteric signaling machines

6 November 2019

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Cell attachment to thrombospondin: the role of ARG-GLY-ASP, calcium, and integrin receptors

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Pro-adhesive and chemotactic activities of thrombospondin-1 for breast carcinoma cells are mediated by alpha3beta1 integrin and regulated by insulin-like growth factor-1 and CD98

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Interactions of thrombospondins with alpha4beta1 integrin and CD47 differentially modulate T cell behavior

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CD36 mediates the In vitro inhibitory effects of thrombospondin-1 on endothelial cells

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Physical characterization of the procollagen module of human thrombospondin 1 expressed in insect cells.

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Merging extracellular domains: fold prediction for laminin G-like and amino-terminal thrombospondin-like modules based on homology to pentraxins

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The alpha 1/beta 1 and alpha 6/beta 1 integrin heterodimers mediate cell attachment to distinct sites on laminin

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Integrin recognition of different cell-binding fragments of laminin (P1, E3, E8) and evidence that alpha 6 beta 1 but not alpha 6 beta 4 functions as a major receptor for fragment E8

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Specificities of heparin-binding sites from the amino-terminus and type 1 repeats of thrombospondin-1.

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Platelet thrombospondin modulates endothelial cell adhesion, motility, and growth: a potential angiogenesis regulatory factor.

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Multiple beta 1 chain integrins are receptors for invasin, a protein that promotes bacterial penetration into mammalian cells

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Mouse egg integrin alpha 6 beta 1 functions as a sperm receptor.

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Identifiers

DOI

10.1074/JBC.M302014200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12909644%20AND%20SRC:MED&resulttype=core&format=json

6 November 2019

1 reference