Functional Characterization of Integrin α6β4 Adhesion Interactions Using Soluble Integrin Constructs Reveals the Involvement of Different Functional Domains in the β4 Subunit-Reference-Cited by-同舟云学术

Functional Characterization of Integrin α6β4 Adhesion Interactions Using Soluble Integrin Constructs Reveals the Involvement of Different Functional Domains in the β4 Subunit

Published:2008-01 Issue:4 Volume:15 Page:317-331
ISSN:1541-9061
Container-title:Cell Communication & Adhesion
language:en
Short-container-title:Cell Communication & Adhesion

Author:

Chen Ling Ling,Gabarra Veronica,Cho Samuel,Browning Beth,Cao Xianjun,Huet Heather,Cheung Anne,Morena Ron,Ramirez Miriam,Shields Michael,Blake Pepinsky R.,McLachlan Karen

Publisher

Informa UK Limited

Subject

Cell Biology,Clinical Biochemistry,General Medicine

Link

http://www.tandfonline.com/doi/pdf/10.1080/15419060802428356

Reference49 articles.

1. Analysis of fibronectin receptor function with monoclonal antibodies: roles in cell adhesion, migration, matrix assembly, and cytoskeletal organization.

2. β4Integrin Is a Transforming Molecule that Unleashes Met Tyrosine Kinase Tumorigenesis

3. β4 integrin activates a Shp2–Src signaling pathway that sustains HGF-induced anchorage-independent growth

4. Ligand-dependent and -independent integrin focal contact localization: the role of the alpha chain cytoplasmic domain.

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