Protein 4.2 interaction with hereditary spherocytosis mutants of the cytoplasmic domain of human anion exchanger 1
Author:
Affiliation:
1. Department of Biochemistry, University of Toronto, Toronto, ON, Canada, M5S 1A8
2. Department of Medicine, University of Toronto, Toronto, ON, Canada, M5S 1A8
Abstract
Publisher
Portland Press Ltd.
Subject
Cell Biology,Molecular Biology,Biochemistry
Link
https://portlandpress.com/biochemj/article-pdf/433/2/313/664257/bj4330313.pdf
Reference46 articles.
1. Disorders of the red cell membrane;Lux,1995
2. Structure and function of the red blood cell anion transport protein;Jennings;Annu. Rev. Biophys. Biophys. Chem.,1989
3. Human erythrocyte protein 42 deficiency associated with hemolytic anemia and a homozygous 40glutamic acid→lysine substitution in the cytoplasmic domain of band 3 (band 3 Montefiore);Rybicki;Blood,1993
4. Homozygous missense mutation (band 3 Fukuoka: G130R): a mild form of hereditary spherocytosis with near-normal band 3 content and minimal changes of membrane ultrastructure despite moderate protein 4.2 deficiency;Inoue;Br. J. Haematol.,1998
5. Band 3 Tuscaloosa: Pro327→Arg327 substitution in the cytoplasmic domain of erythrocyte band 3 protein associated with spherocytic hemolytic anemia and partial deficiency of protein 4.2;Jarolim;Blood,1992
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