{"doi":"10.1074/jbc.m309826200","title":"Altered Structure and Anion Transport Properties of Band 3 (AE1, SLC4A1) in Human Red Cells Lacking Glycophorin A","abstract":null,"journal":"Journal of Biological Chemistry","year":2004,"id":684792,"datarank":0.5709993734655481,"base_score":3.8066624897703196,"endowment":3.8066624897703196,"self_citation_contribution":0.5709993734655481,"citation_network_contribution":0.0,"self_endowment_contribution":0.5709993734655481,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":44,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1789083,"name":"Rui-jun Pan","orcid":null,"position":1,"is_corresponding":false},{"id":1789084,"name":"Diane L. Cope","orcid":null,"position":2,"is_corresponding":false},{"id":754341,"name":"Makoto Uchikawa","orcid":null,"position":3,"is_corresponding":false},{"id":1789085,"name":"Robert B. Gunn","orcid":null,"position":4,"is_corresponding":false},{"id":1789086,"name":"Richard J. Cherry","orcid":null,"position":5,"is_corresponding":false},{"id":1789087,"name":"Michael J.A. Tanner","orcid":null,"position":6,"is_corresponding":false},{"id":1789081,"name":"Lesley J. Bruce","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Altered Structure and Anion Transport Properties of Band 3 (AE1, SLC4A1) in Human Red Cells Lacking Glycophorin A","abstract":"We have studied the properties of band 3 in different glycophorin A (GPA)-deficient red cells. These red cells lack either both GPA and glycophorin B (GPB) (M(k)M(k) cells) or GPA (En(a-) cells) or contain a hybrid of GPA and GPB (MiV cells). Sulfate transport was reduced in all three red cell types to approximately 60% of that in normal control red cells as a result of an increased apparent K(m) for sulfate. Transport of the monovalent anions iodide and chloride was also reduced. The reduced iodide transport resulted from a reduction in the V(max) for iodide transport. The anion transport site was investigated by measuring iodide fluorescence quenching of eosin-5-maleimide (EMA)-labeled band 3. The GPA-deficient cells had a normal K(d) for iodide binding, in agreement with the unchanged K(m) found in transport studies. However, the apparent diffusion quenching constant (K(q)) was increased, and the fluorescence polarization of band 3-bound EMA decreased in the variant cells, suggesting increased flexibility of the protein in the region of the EMA-binding site. This increased flexibility is probably associated with the decrease in V(max) observed for iodide transport. Our results suggest that band 3 in the red cell can take up two different structures: one with high anion transport activity when GPA is present and one with lower anion transport activity when GPA is absent.","is_dataset_classified":null,"base_score":3.8066624897703196,"endowment":3.8066624897703196,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"14604989","pmcid":null,"openalex_id":"https://openalex.org/W2091933512","authors":[],"funders":[{"funder_name":"NHLBI NIH HHS","grant_id":"HL-66173","title":null}],"total_grants":1,"fwci":1.0697,"citation_percentile":0.75862069,"influential_citations":0,"citation_trend":[{"year":2013,"count":2},{"year":2014,"count":2},{"year":2015,"count":3},{"year":2016,"count":2},{"year":2018,"count":2},{"year":2020,"count":1},{"year":2021,"count":2},{"year":2022,"count":6},{"year":2023,"count":1},{"year":2024,"count":1},{"year":2025,"count":1}],"oa_status":"hybrid","license":"cc-by-nc-nd","oa_locations":[{"url":"https://doi.org/10.1074/jbc.m309826200","host_type":"journal"},{"url":"https://doi.org/10.1074/jbc.m309826200","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S002192581852603X?httpAccept=text/xml","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S002192581852603X?httpAccept=text/plain","host_type":"publisher"},{"url":"https://syndication.highwire.org/content/doi/10.1074/jbc.M309826200","host_type":"publisher"},{"url":"https://pubmed.ncbi.nlm.nih.gov/14604989","host_type":"repository"},{"url":"https://research-information.bris.ac.uk/en/publications/dae221ef-19d2-4330-9cc2-6f8fa21d1730","host_type":"repository"},{"url":"https://hdl.handle.net/1983/dae221ef-19d2-4330-9cc2-6f8fa21d1730","host_type":"repository"}],"fields_of_study":["Erythrocyte Function and Pathophysiology","Pancreatic function and diabetes","Amino Acid Enzymes and Metabolism","Anion Exchange Protein 1, Erythrocyte","Erythrocytes","Glycophorins","Humans","Ion Transport","Mutation","Protein Binding","Structure-Activity Relationship"],"mesh_terms":["Anion Exchange Protein 1, Erythrocyte","Erythrocytes","Glycophorins","Humans","Mutation","Protein Binding","Structure-Activity Relationship","Ion Transport"],"keywords":["Glycophorin","Band 3","Ion","Chemistry","Biophysics","Biochemistry","Biology","Erythrocyte membrane"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Clean water and sanitation"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-18T15:03:20.588225Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}