The linker between the D3 and A1 domains of vWF suppresses A1-GPIbα catch bonds by site-specific binding to the A1 domain-Reference-Cited by-同舟云学术

The linker between the D3 and A1 domains of vWF suppresses A1-GPIbα catch bonds by site-specific binding to the A1 domain

Published:2013-07-27 Issue:8 Volume:22 Page:1049-1059
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Tischer Alexander¹,Cruz Miguel A.²,Auton Matthew¹

Affiliation:

1. Division of Hematology, Departments of Internal Medicine and Biochemistry and Molecular Biology; Mayo Clinic; Rochester Minnesota

2. Department of Medicine; Cardiovascular Sciences and Thrombosis Research Section of the Baylor College of Medicine; Houston Texas

Funder

National Heart Lung and Blood Institute of the National Institutes of Health

Mary R. Gibson Foundation

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/pro.2294/fullpdf

Reference41 articles.

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3. Initiation of platelet adhesion by arrest onto fibrinogen or translocation on von Willebrand factor;Savage;Cell,1996

4. von Willebrand factor. A reduced and alkylated 52/48-kDa fragment beginning at amino acid residue 449 contains the domain interacting with platelet glycoprotein Ib;Fujimura;J Biol Chem,1986

5. A heparin-binding domain of human von Willebrand factor. Characterization and localization to a tryptic fragment extending from amino acid residue Val-449 to Lys-728;Fujimura;J Biol Chem,1987

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