ArticleProceedings of the National Academy of Sciences of the United States of America1989
Cloning and characterization of band 3, the human erythrocyte anion-exchange protein (AE1).
Article in Proceedings of the National Academy of Sciences of the United States of America, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers, 1 of them a synthesis that pooled it.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
60 citing papers in PubMed, 1 synthesis or guideline pooled it, 305 citations in OpenAlex.
- A novel variant of SLC4A1 for hereditary spherocytosis in a Chinese family: a case report and systematic review.BMC medical genomics · 2022Pooled it
- The structural insight into the functional modulation of human anion exchanger 3.Nature communications · 2024Article
- Organization and Dynamics of the Red Blood Cell Band 3 Anion Exchanger SLC4A1: Insights From Molecular Dynamics Simulations.Frontiers in physiology · 2022Review
- Cell physiology and molecular mechanism of anion transport by erythrocyte band 3/AE1.American journal of physiology. Cell physiology · 2021Review
- Article
- Genes encoding putative bicarbonate transporters as a missing molecular link between molt and mineralization in crustaceans.Scientific reports · 2021Article
- Moonlighting Proteins in the Fuzzy Logic of Cellular Metabolism.Molecules (Basel, Switzerland) · 2020Review
- Natural Antioxidants Beneficial Effects on Anion Exchange through Band 3 Protein in Human Erythrocytes.Antioxidants (Basel, Switzerland) · 2019Review
- Molecular Simulations of Intact Anion Exchanger 1 Reveal Specific Domain and Lipid Interactions.Biophysical journal · 2019Article
- Interaction of the human erythrocyte Band 3 anion exchanger 1 (AE1, SLC4A1) with lipids and glycophorin A: Molecular organization of the Wright (Wr) blood group antigen.PLoS computational biology · 2018Article
- Chloride Influx of Anion Exchanger 2 Was Modulated by Calcium-Dependent Spinophilin in Submandibular Glands.Frontiers in physiology · 2018Article
- [Clinical features of hereditary distal renal tubular acidosis and SLC4A1 gene mutation].Zhongguo dang dai er ke za zhi = Chinese journal of contemporary pediatrics · 2017Article
- Structure of Bor1 supports an elevator transport mechanism for SLC4 anion exchangers.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Membrane perturbations induced by the interactions of zinc ions with band 3 in human erythrocytes.Biochemistry and biophysics reports · 2015Article
- Structure and Function of SLC4 Family [Formula: see text] Transporters.Frontiers in physiology · 2015Article
- Human erythrocyte band 3 functions as a receptor for the sialic acid-independent invasion of Plasmodium falciparum. Role of the RhopH3-MSP1 complex.Biochimica et biophysica acta · 2014Article
- Cloning expeditions: risky but rewarding.Molecular and cellular biology · 2013Article
- Lipid bilayer and cytoskeletal interactions in a red blood cell.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Basolateral chloride loading by the anion exchanger type 2: role in fluid secretion by the human airway epithelial cell line Calu-3.The Journal of physiology · 2012Article
- A novel SLC4A1 variant in an autosomal dominant distal renal tubular acidosis family with a severe phenotype.Endocrine · 2010Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The human erythrocyte anion-exchange protein (band 3 or AE1) was cloned from a fetal liver cDNA library. Three overlapping clones, encompassing 3637 nucleotides, were analyzed in detail. These encode a 911-amino acid protein (Mr 101,791) and detect a single 4.7-kilobase species in human reticulocyte RNA. The corresponding gene is located on chromosome 17. The protein is similar in structure to other anion exchangers and is divided into three regions: a hydrophilic, cytoplasmic domain that interacts with a variety of membrane and cytoplasmic proteins (residues 1-403); a hydrophobic, transmembrane domain that forms the anion antiporter (residues 404-882); and an acidic, C-terminal domain of unknown function (residues 883-911). The N-terminal domain contains several conserved sections (e.g., residues 57-86, 102-164, 219-347, and 375-403), some of which may contribute to binding sites for ankyrin, protein 4.1, or protein 4.2. The membrane domain is highly conserved with the exception of a single segment (residues 543-567) that contains several sites for cleavage of the protein by extracellular proteases. Based on hydropathy analyses and the wealth of available topographical and functional data, a model is proposed in which the protein crosses the membrane 14 times.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.