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

A domain of the insulin receptor required for endocytosis in rat fibroblasts.

The Journal of biological chemistry - 15 Jun 1990

Thies R S, Webster N J, McClain D A

Abstract excerpt

To study the mechanism and role of ligand-dependent endocytosis, we have engineered a mutant insulin receptor that retains its insulin binding and insulin-stimulated tyrosine kinase activities but does not exhibit ligand-induced internalization. The mutant has a deletion of the 16th exon which encodes 22 amino acids (residues 944-965) on the cytoplasmic side of the transmembrane region of the receptor...

Read the complete abstract on PubMed

Topics

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

Share to Base Sequence
Share to Cell Line
Share to Chromosome Deletion

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

Share to Kinetics

Share to Molecular Sequence Data

Share to Mutation

Share to Phosphorylation

Share to Transfection

Source

Identifiers

PMID: 2161833

Genes

NAPA

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

A domain of the insulin receptor required for endocytosis in rat fibroblasts.PMID 2161833Read ↗

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

Different ligand affinities of the two human insulin receptor splice variants are reflected in parallel changes in sensitivity for insulin action.Semantic proximity Read ↗

Receptor-mediated internalization of insulin requires a 12-amino acid sequence in the juxtamembrane region of the insulin receptor beta-subunit.Semantic proximity Read ↗

Postbinding characterization of five naturally occurring mutations in the human insulin receptor gene: impaired insulin-stimulated c-jun expression and thymidine incorporation despite normal receptor autophosphorylation.Semantic proximity Read ↗

Mutational analysis of the N-linked glycosylation sites of the human insulin receptor.Semantic proximity Read ↗

Insulin inhibition of protein degradation in cells expressing wild-type and mutant insulin receptors.Semantic proximity Read ↗

Characterization of an insulin receptor mutant lacking the subunit processing site.Semantic proximity Read ↗

Immunoglobulin heavy chain-binding protein binds to misfolded mutant insulin receptors with mutations in the extracellular domain.Semantic proximity Read ↗

Deletion analysis of the human insulin receptor ectodomain reveals independently folded soluble subdomains and insulin binding by a monomeric alpha-subunit.Semantic proximity Read ↗

Insulin receptors internalize by a rapid, saturable pathway requiring receptor autophosphorylation and an intact juxtamembrane region.Semantic proximity Read ↗

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

Transmembrane domain interactions are necessary for negative cooperativity of the insulin receptor.Semantic proximity Read ↗

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