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

Structural basis by which a recessive mutation in the alpha-subunit of the insulin receptor affects insulin binding.

The Journal of biological chemistry - 27 May 1994

Taouis M, Levy-Toledano R, Roach P, Taylor S I, Gorden P

Abstract excerpt

Recently, a mutation substituting Leu for Ser323 in the alpha-subunit of the human insulin receptor has been identified in an insulin-resistant patient. The Leu323 mutation leads to a severe impairment in insulin binding without significantly altering the processing or cell surface expression of the receptor. In order to study how alpha beta half-receptors interact to form the insulin-binding site, we...

Read the complete abstract on PubMed

Topics

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

Share to 3T3 Cells
Share to Genes, Recessive
Share to Insulin

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

Share to Mutation

Share to Phosphoproteins

Share to Phosphorylation

Share to Serine

Source

Identifiers

PMID: 8195122

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

Structural basis by which a recessive mutation in the alpha-subunit of the insulin receptor affects insulin binding.PMID 8195122Read ↗

Investigation of the mechanism of the dominant negative effect of mutations in the tyrosine kinase domain of the insulin receptor.Semantic proximity Read ↗

Two mutations in a conserved structural motif in the insulin receptor inhibit normal folding and intracellular transport of the receptor.Semantic proximity Read ↗

A mutation in the extracellular domain of the insulin receptor impairs the ability of insulin to stimulate receptor autophosphorylation.Semantic proximity Read ↗

Functional properties of a naturally occurring Trp1200----Ser1200 mutation of the insulin receptor.Semantic proximity Read ↗

Molecular biology of insulin resistance.Semantic proximity Read ↗

A mutation in the insulin receptor that impairs proreceptor processing but not insulin binding.Semantic proximity Read ↗

A naturally occurring mutation of insulin receptor alanine 1134 impairs tyrosine kinase function and is associated with dominantly inherited insulin resistance.Semantic proximity Read ↗

Hybrid insulin receptors. Molecular mechanisms of negative-dominant mutations in receptor-mediated insulin resistance.Semantic proximity Read ↗

Insulin/IGF-1 hybrid receptors: implications for the dominant-negative phenotype in syndromes of insulin resistance.Semantic proximity Read ↗

An in-frame insertion in exon 3 and a nonsense mutation in exon 2 of the insulin receptor gene associated with severe insulin resistance in a patient with Rabson-Mendenhall syndrome.Semantic proximity Read ↗

Substitution of isoleucine for methionine at position 1153 in the beta-subunit of the human insulin receptor. A mutation that impairs receptor tyrosine kinase activity, receptor endocytosis, and insulin action.Semantic proximity Read ↗

Evidence supporting a passive role for the insulin receptor transmembrane domain in insulin-dependent signal transduction.Semantic proximity Read ↗

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