Effect of tyrosine mutations on the kinase activity and transforming potential of an oncogenic human insulin-like growth factor I receptor.

doi:10.1074/jbc.271.1.160

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

Back to search

Article

Effect of tyrosine mutations on the kinase activity and transforming potential of an oncogenic human insulin-like growth factor I receptor.

The Journal of biological chemistry - 5 Jan 1996

Jiang Y, Chan J L, Zong C S, Wang L H

Abstract excerpt

The tyrosines in the cytoplasmic domain of an oncogenic human insulin-like growth factor I receptor (gag-IGFR) were systematically mutated to phenylalanines to investigate the role of those tyrosines in the enzymatic and biological function of the gag-IGFR. Our results indicate that tyrosines 113...

Topics

Animals
Cell Transformation, Neoplastic
Chick Embryo
Humans
Insulin Receptor Substrate Proteins
Isoenzymes
Mutagenesis, Site-Directed
Mutation
Phenylalanine
Phosphatidylinositol 3-Kinases
Phospholipase C gamma

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Phosphoproteins

Phosphorylation

Phosphotransferases (Alcohol Group Acceptor)

Protein-Tyrosine Kinases

Receptor, IGF Type 1

Signal Transduction

Type C Phospholipases

Source

Open in PubMed

Identifiers

PMID: 8550552
DOI: 10.1074/jbc.271.1.160

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8550552-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Effect of tyrosine mutations on the kinase activity and transforming potential of an oncogenic human insulin-like growth factor I receptor.PMID 8550552Read ↗

Tumorigenic and mitogenic capacities are reduced in transfected fibroblasts expressing mutant insulin-like growth factor (IGF)-I receptors. The role of tyrosine residues 1250, 1251, and 1316 in the carboxy-terminus of the IGF-I receptor.Semantic proximity Read ↗

Analyzing structural differences between insulin receptor (IR) and IGF1R for designing small molecule allosteric inhibitors of IGF1R as novel anti-cancer agents.Semantic proximity Read ↗

Mitogenicity and transforming activity of the insulin-like growth factor-I receptor with mutations in the tyrosine kinase domain.Semantic proximity Read ↗

Hallmarks of cancer: The insulin-like growth factors perspectiveSemantic proximity Read ↗

Effect of mutations at serines 1280-1283 on the mitogenic and transforming activities of the insulin-like growth factor I receptor.Semantic proximity Read ↗

Mutational analysis of the mitogenic and transforming activities of the insulin-like growth factor I receptor.Semantic proximity Read ↗

Oncogenic fusion proteins adopt the insulin-like growth factor signaling pathwaySemantic proximity Read ↗

Cooperative regulation of the invasive and metastatic phenotypes by different domains of the type I insulin-like growth factor receptor beta subunit.Semantic proximity Read ↗

How IGF-1 activates its receptor.Semantic proximity Read ↗

The receptor for the type I insulin-like growth factor and its ligands regulate multiple cellular functions that impact on metastasis.Semantic proximity Read ↗

Functional characterization of a clinically significant variant of IGF1R (M1054I) - a critical residue involved in defining the binding of small molecules in the allosteric pocket of IGF1R.Semantic proximity Read ↗

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

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