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

Protein 4.2: a complex linker.

Blood cells, molecules & diseases - 1 Jan 2000

Satchwell Timothy J, Shoemark Debbie K, Sessions Richard B, Toye Ashley M

Abstract excerpt

The peripheral membrane protein, protein 4.2, is one of the most abundant protein components of the erythrocyte membrane. Protein 4.2 has an important role in red cell membrane structure, its absence due to natural mutations in humans or gene knockout in mice has a detrimental effect on membrane stability and results in hereditary spherocytosis. It is known to be a point of connection between the band 3 complex...

Read the complete abstract on PubMed

Topics

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

Share to Blood Proteins
Share to Cell Shape
Share to Cytoskeleton

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

Share to Erythrocyte Membrane

Share to Protein Interaction Mapping

Share to Protein Processing, Post-Translational

Share to Spherocytosis, Hereditary

Share to Transglutaminases

Source

Identifiers

PMID: 19269200
DOI: 10.1016/j.bcmd.2009.01.005

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

Protein 4.2: a complex linker.PMID 19269200Read ↗

Investigating the key membrane protein changes during in vitro erythropoiesis of protein 4.2 (-) cells (mutations Chartres 1 and 2).Semantic proximity Read ↗

Protein 4.2 Komatsu (D175Y) associated with the lack of interaction with ankyrin in human red blood cells.Semantic proximity Read ↗

Protein-4.2 association with band 3 (AE1, SLCA4) in Xenopus oocytes: effects of three natural protein-4.2 mutations associated with hemolytic anemia.Semantic proximity Read ↗

Band 4.2 abnormalities in human red cells.Semantic proximity Read ↗

Red cell membrane protein band 4.2: phenotypic, genetic and electron microscopic aspects.Semantic proximity Read ↗

Structure, dynamics and assembly of the ankyrin complex on human red blood cell membraneSemantic proximity Read ↗

Absence of CD47 in protein 4.2-deficient hereditary spherocytosis in man: an interaction between the Rh complex and the band 3 complexSemantic proximity Read ↗

Protein 4.2 is critical to CD47-membrane skeleton attachment in human red cells.Semantic proximity Read ↗

Band 3 Tuscaloosa: Pro327----Arg327 substitution in the cytoplasmic domain of erythrocyte band 3 protein associated with spherocytic hemolytic anemia and partial deficiency of protein 4.2.Semantic proximity Read ↗

Structure, function, and molecular genetics of erythroid membrane skeletal protein 4.1 in normal and abnormal red blood cells.Semantic proximity Read ↗

Truncated (2/2) hemoglobin: Unconventional structures and functional roles in vivo and in human pathogenesisSemantic proximity Read ↗

Hereditary elliptocytosis due to both qualitative and quantitative defects in membrane skeletal protein 4.1.Semantic proximity Read ↗

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