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

An irregularity in the transmembrane domain helix correlates with the rate of insulin receptor internalization.

Biochemistry - 29 Nov 1994

Li S C, Deber C M, Shoelson S E

Abstract excerpt

Internalization of insulin and its receptor via receptor-mediated endocytosis is an important step in insulin-induced signal transduction. To investigate the structural determinants underlying the enhanced internalization rate observed for the insulin receptor transmembrane mutant Gly933-Pro934-->Ala-Ala (GP-->AA), we have designed and chemically synthesized two peptides, IR(TM)-GP and IR-(TM)-AA, corresponding...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Cell Membrane
Share to Kinetics

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

Share to Molecular Sequence Data

Share to Molecular Weight

Share to Mutation

Share to Structure-Activity Relationship

Share to Temperature

Source

Identifiers

PMID: 7947843
DOI: 10.1021/bi00251a047

Genes

SDS

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

An irregularity in the transmembrane domain helix correlates with the rate of insulin receptor internalization.PMID 7947843Read ↗

An arginine to cysteine(252) mutation in insulin receptors from a patient with severe insulin resistance inhibits receptor internalisation but preserves signalling events.Semantic proximity Read ↗

The insulin receptor juxtamembrane region contains two independent tyrosine/beta-turn internalization signals.Semantic proximity Read ↗

Structural Dynamics of Insulin Receptor and Transmembrane Signaling.Semantic proximity Read ↗

Probing the mechanism of insulin fibril formation with insulin mutants.Semantic proximity Read ↗

Cys860 in the extracellular domain of insulin receptor beta-subunit is critical for internalization and signal transduction.Semantic proximity Read ↗

A beta-turn endocytic code is required for optimal internalization of the growth hormone receptor but not for alpha-adaptin association.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 ↗

Molecular Dynamics Simulations of Insulin: Elucidating the Conformational Changes that Enable Its Binding.Semantic proximity Read ↗

Substitution of the insulin receptor transmembrane domain with that of glycophorin A inhibits insulin action.Semantic proximity Read ↗

All-atom structural models of insulin binding to the insulin receptor in the presence of a tandem hormone-binding element.Semantic proximity Read ↗

Mutation of Arg55/56 to Leu55/Ala56 in insulin-like growth factor-I results in two forms different in disulfide structure and native conformation but similar under reverse-phase conditions.Semantic proximity Read ↗

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

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