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

Structure and stability of hereditary spherocytosis mutants of the cytosolic domain of the erythrocyte anion exchanger 1 protein.

Biochemistry - 24 Jan 2006

Bustos Susan P, Reithmeier Reinhart A F

Abstract excerpt

Anion exchanger 1 (AE1, Band 3) is the predominant membrane protein of erythrocytes. Its 52 kDa C-terminal domain functions as a chloride-bicarbonate exchanger, while its 43 kDa N-terminal cytosolic domain (cdb3) anchors the cytoskeleton to the membrane. Several proteins bind to cdb3, including protein 4.2, a cytoskeletal protein. Three mutations in cdb3 are associated with hereditary spherocytosis (HS) and...

Read the complete abstract on PubMed

Topics

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

Share to Anion Exchange Protein 1, Erythrocyte
Share to Circular Dichroism

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cytoplasm

Share to Hydrogen-Ion Concentration

Share to Protein Denaturation

Share to Protein Structure, Tertiary

Share to Spherocytosis, Hereditary

Share to Trypsin

Source

Identifiers

PMID: 16411779
DOI: 10.1021/bi051692c

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structure and stability of hereditary spherocytosis mutants of the cytosolic domain of the erythrocyte anion exchanger 1 protein.PMID 16411779Read ↗

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

Band 3, the human red cell chloride/bicarbonate anion exchanger (AE1, SLC4A1), in a structural context.Semantic proximity Read ↗

Protein 4.2 interaction with hereditary spherocytosis mutants of the cytoplasmic domain of human anion exchanger 1.Semantic proximity Read ↗

Structure of the cytoplasmic domain of erythrocyte band 3 hereditary spherocytosis variant P327R: band 3 Tuscaloosa.Semantic proximity Read ↗

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

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

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

Structure, function, and trafficking of SLC4 and SLC26 anion transporters.Semantic proximity Read ↗

[Molecular mechanism of hereditary spherocytosis].Semantic proximity Read ↗

Localization of mutations leading to altered cell shape and anion transport in the crystal structure of the cytoplasmic domain of band 3.Semantic proximity Read ↗

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