Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Targeted disruption of the murine erythroid band 3 gene results in spherocytosis and severe haemolytic anaemia despite a normal membrane skeleton.

Nature genetics - 1 Oct 1996

Southgate C D, Chishti A H, Mitchell B, Yi S J, Palek J

Abstract excerpt

Band 3 is the most abundant integral protein of the red blood cell membrane. It performs two critical biological functions: maintaining ionic homeostasis, by transporting Cl- and HCO3-ions, and providing mechanical stability to the erythroid membrane. Erythroid band 3 (AE1) is one of three anion exchangers that are encoded by separate genes. The AE1 gene is transcribed by two promoters: the upstream promoter...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Alleles
Share to Cell Membrane
Share to Genes

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Homozygote

Share to Kidney

Share to Membrane Proteins

Share to Mice, Mutant Strains

Source

Identifiers

PMID: 8841202
DOI: 10.1038/ng1096-227

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Targeted disruption of the murine erythroid band 3 gene results in spherocytosis and severe haemolytic anaemia despite a normal membrane skeleton.PMID 8841202Read ↗

The structure and function of band 3 (AE1): Recent developments (Review)Semantic proximity Read ↗

The N-terminal 11 amino acids of human erythrocyte band 3 are critical for aldolase binding and protein phosphorylation: implications for band 3 function.Semantic proximity Read ↗

The cytoskeletal binding domain of band 3 is required for multiprotein complex formation and retention during erythropoiesis.Semantic proximity Read ↗

Erythroid band 3 variants and disease.Semantic proximity Read ↗

The interactome of the N-terminus of band 3 regulates red blood cell metabolism and storage qualitySemantic proximity Read ↗

Band 3 Courcouronnes (Ser667Phe): a trafficking mutant differentially rescued by wild-type band 3 and glycophorin A.Semantic proximity Read ↗

Band 3 function and dysfunction in a structural context.Semantic proximity Read ↗

Band 3 and its alterations in health and disease.Semantic proximity Read ↗

Molecular Defect of the Band 3 Protein in Southeast Asian OvalocytosisSemantic proximity Read ↗

The structure of the human red blood cell anion exchanger (EPB3, AE1, band 3) geneSemantic proximity Read ↗

Defective anion transport and marked spherocytosis with membrane instability caused by hereditary total deficiency of red cell band 3 in cattle due to a nonsense mutation.Semantic proximity Read ↗

The major integral proteins of the human red cell.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.