Rh-RhAG/Ankyrin-R, a New Interaction Site between the Membrane Bilayer and the Red Cell Skeleton, Is Impaired by Rhnull-associated Mutation-Reference-Cited by-同舟云学术

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Rh-RhAG/Ankyrin-R, a New Interaction Site between the Membrane Bilayer and the Red Cell Skeleton, Is Impaired by Rhnull-associated Mutation

Published:2003-07 Issue:28 Volume:278 Page:25526-25533
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Nicolas Virginie,Le Van Kim Caroline,Gane Pierre,Birkenmeier Connie,Cartron Jean-Pierre,Colin Yves,Mouro-Chanteloup Isabelle

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference44 articles.

1. Selective solubilization of proteins and phospholipids from red blood cell membranes by nonionic detergents

2. Blood: Principles and Practice of Hematology;Lux,1995

3. Molecular Basis of Red Cell Membrane Disorders

4. Mapping of a palmitoylatable band 3-binding domain of human erythrocyte membrane protein 4.2

5. Regulation of Protein 4.1R, p55, and Glycophorin C Ternary Complex in Human Erythrocyte Membrane

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1. Molecular dynamics of the human RhD and RhAG blood group proteins;Frontiers in Chemistry;2024-03-19

2. Uso de la biología computacional para comparar las estructuras terciarias teóricas de las formas más comunes de RHCE y RHD;Revista Mexicana de Medicina Transfusional;2024

3. Use of computational biology to compare the theoretical tertiary structures of the most common forms of RhCE and RhD;Vox Sanguinis;2023-08-09

4. Erythrocyte membrane integrity and protein activity in high-fat diet fed male Wistar rats;Nutrire;2022-11-02

5. Pleiotropic Ankyrins: Scaffolds for Ion Channels and Transporters;Channels;2022-09-08

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