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

Insulin receptor structural requirements for the formation of a ternary complex with IRS-1 and PI 3-kinase.

Molecular and cellular endocrinology - 18 Sept 1996

Wilden P A, Rovira I, Broadway D E

Abstract excerpt

Insulin receptor substrate-1 (IRS-1) is a major substrate of the insulin receptor tyrosine kinase and is an intermediate in insulin signaling. Phosphotyrosyl-IRS-1 binds to other signaling proteins including phosphatidylinositol 3-kinase (PI 3-kinase). We examined the role of three insulin receptor tyrosine autophosphorylation domains in association of the receptor with IRS-1. Our data support the idea that...

Read the complete abstract on PubMed

Topics

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

Share to Binding Sites
Share to CHO Cells
Share to Cricetinae

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

Share to Gene Expression

Share to Mutation

Share to Phosphorylation

Share to Structure-Activity Relationship

Share to Transfection

Source

Identifiers

PMID: 8902843
DOI: 10.1016/0303-7207(96)03872-5

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

Insulin receptor structural requirements for the formation of a ternary complex with IRS-1 and PI 3-kinase.PMID 8902843Read ↗

Insulin stimulation of phosphatidylinositol 3-kinase activity maps to insulin receptor regions required for endogenous substrate phosphorylation.Semantic proximity Read ↗

Interaction of insulin receptor substrate 3 with insulin receptor, insulin receptor-related receptor, insulin-like growth factor-1 receptor, and downstream signaling proteins.Semantic proximity Read ↗

Structural and biochemical characterization of the KRLB region in insulin receptor substrate-2.Semantic proximity Read ↗

Interaction of the molecular weight 85K regulatory subunit of the phosphatidylinositol 3-kinase with the insulin receptor and the insulin-like growth factor-1 (IGF- I) receptor: comparative study using the yeast two-hybrid system.Semantic proximity Read ↗

14-3-3 proteins interact with the insulin-like growth factor receptor but not the insulin receptor.Semantic proximity Read ↗

Serine phosphorylation proximal to its phosphotyrosine binding domain inhibits insulin receptor substrate 1 function and promotes insulin resistance.Semantic proximity Read ↗

Substitution of glutamic acid for alanine 1135 in the putative "catalytic loop" of the tyrosine kinase domain of the human insulin receptor. A mutation that impairs proteolytic processing into subunits and inhibits receptor tyrosine kinase activity.Semantic proximity Read ↗

Decreased phosphorylation of mutant insulin receptor by protein kinase C and protein kinase A.Semantic proximity Read ↗

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

High-affinity insulin binding: insulin interacts with two receptor ligand binding sites.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 ↗

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 ↗

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