Localization of Mutations Leading to Altered Cell Shape and Anion Transport in the Crystal Structure of the Cytoplasmic Domain of Band 3
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Hematology,Molecular Biology,Molecular Medicine
Reference19 articles.
1. Red blood cell membrane disorders;Tse;Br. J. Haematol.,1999
2. The molecular basis of disorders of the red cell membrane;McMullin;J. Clin. Pathol.,1999
3. Hematologically important mutations: Band 3 and protein 4.2 variants in hereditary spherocytosis;Gallagher;Blood Cells Mol. Dis.,1997
4. 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
5. 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
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3. Band 3, the human red cell chloride/bicarbonate anion exchanger (AE1, SLC4A1), in a structural context;Biochimica et Biophysica Acta (BBA) - Biomembranes;2016-07
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