Novel Gain-of-function Mutations of Platelet Glycoprotein Ibα by Valine Mutagenesis in the Cys209–Cys248 Disulfide Loop-Reference-Cited by-同舟云学术

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Novel Gain-of-function Mutations of Platelet Glycoprotein Ibα by Valine Mutagenesis in the Cys209–Cys248 Disulfide Loop

Published:2000-09 Issue:36 Volume:275 Page:27663-27670
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Dong Jing-fei,Schade Alicia J.,Romo Gabriel M.,Andrews Robert K.,Gao Shan,McIntire Larry V.,López José A.

Publisher

American Society for Biochemistry & Molecular Biology (ASBMB)

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference42 articles.

1. Molecular mechanisms of platelet adhesion and activation

2. Structure and function of the glycoprotein Ib-IX-V complex

3. The platelet glycoprotein Ib???IX complex

4. Site-directed mutagenesis of a soluble recombinant fragment of platelet glycoprotein Ib alpha demonstrating negatively charged residues involved in von Willebrand factor binding

5. Tyrosine Sulfation of the Glycoprotein Ib-IX Complex: Identification of Sulfated Residues and Effect on Ligand Binding

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1. Physical Characteristics of von Willebrand Factor Binding with Platelet Glycoprotein Ibɑ Mutants at Residue 233 Causing Various Biological Functions;TH Open;2022-09-07

2. Gestational thrombocytopenia: a case–control study of over 3,500 pregnancies;British Journal of Haematology;2021-06-09

3. The N-terminal Flanking Region of the A1 Domain Regulates the Force-dependent Binding of von Willebrand Factor to Platelet Glycoprotein Ibα;Journal of Biological Chemistry;2013-11

4. Biodegradable nanoparticles mimicking platelet binding as a targeted and controlled drug delivery system;International Journal of Pharmaceutics;2012-02

5. A novel D235Y mutation in the GP1BA gene enhances platelet interaction with von Willebrand factor in an Iranian family with platelet-type von Willebrand disease;Thrombosis and Haemostasis;2012

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