Towards the localization of the essential arginine residues in the band 3 protein of human red blood cell membranes
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
Reference26 articles.
1. Chemical modification of membrane proteins in relation to inhibition of anion exchange in human red blood cells
2. Inhibition of anion transport across red blood cells with 1,2-cyclohex-anedione
3. Anion transport in red blood cells and arginine-specific reagents
4. Anion transport in red blood cells and arginine-specific reagents. Interaction between the substrate-binding site and the binding site of arginine-specific reagents
5. New evidence for the essential role of arginine residues in anion transport across the red blood cell membrane
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1. Cell physiology and molecular mechanism of anion transport by erythrocyte band 3/AE1;American Journal of Physiology-Cell Physiology;2021-12-01
2. Band 3, the human red cell chloride/bicarbonate anion exchanger (AE1, SLC4A1), in a structural context;Biochimica et Biophysica Acta (BBA) - Biomembranes;2016-07
3. Ligation of Glycophorin A Generates Reactive Oxygen Species Leading to Decreased Red Blood Cell Function;PLOS ONE;2016-01-19
4. Structural Model of the Anion Exchanger 1 (SLC4A1) and Identification of Transmembrane Segments Forming the Transport Site;Journal of Biological Chemistry;2013-09
5. Modification of Amino/Amidino Groups in Proteins;Chemical Modification of Biological Polymers;2011-09-13
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