Substrate-dependent reversal of anion transport site orientation in the human red blood cell anion-exchange protein, AE1
Author:
Publisher
Proceedings of the National Academy of Sciences
Subject
Multidisciplinary
Reference15 articles.
1. Stoichiometry of a half-turnover of band 3, the chloride transport protein of human erythrocytes.
2. Pre-steady state transport by erythrocyte band 3 protein: uphill countertransport induced by the impermeant inhibitor H2DIDS
3. Asymmetry in the mechanism for anion exchange in human red blood cell membranes. Evidence for reciprocating sites that react with one transported anion at a time.
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2. Cell physiology and molecular mechanism of anion transport by erythrocyte band 3/AE1;American Journal of Physiology-Cell Physiology;2021-12-01
3. Identification of multiple substrate binding sites in SLC4 transporters in the outward-facing conformation: Insights into the transport mechanism;Journal of Biological Chemistry;2021-01
4. Fractal Dimension of Erythrocyte Membranes: A Highly Useful Precursor for Rapid Morphological Assay;Annals of Biomedical Engineering;2018-05-23
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