The integrin alpha IIb-beta 3, platelet glycoprotein IIb-IIIa, can form a functionally active heterodimer complex without the cysteine-rich repeats of the beta 3 subunit.-Reference-Cited by-同舟云学术

The integrin alpha IIb-beta 3, platelet glycoprotein IIb-IIIa, can form a functionally active heterodimer complex without the cysteine-rich repeats of the beta 3 subunit.

Published:1994-03 Issue:12 Volume:269 Page:8754-8761
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Wippler J.,Kouns W.C.,Schlaeger E.J.,Kuhn H.,Hadvary P.,Steiner B.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference69 articles.

1. Integrins: Versatility, modulation, and signaling in cell adhesion

2. Structure of the platelet membrane glycoprotein IIb. Homology to the alpha subunits of the vitronectin and fibronectin membrane receptors.

3. Evidence That Platelet Glycoprotein Ilia Has a Large Disulfidebonded Loop That Is Susceptible to Proteolytic Cleavage

4. Assignment of disulphide bonds in human platelet GPIIIa. A disulphide pattern for the β-subunits of the integrin family

5. Protein sequence of endothelial glycoprotein IIIa derived from a cDNA clone. Identity with platelet glycoprotein IIIa and similarity to “integrin”.

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