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

Autophosphorylation mutants of the EGF-receptor signal through auxiliary mechanisms involving SH2 domain proteins.

Oncogene - 1 Dec 1994

Li N, Schlessinger J, Margolis B

Abstract excerpt

Many growth factors bind and activate receptors with intrinsic protein tyrosine kinase activity. Once activated these receptors undergo autophosphorylation allowing them to bind src homology 2 (SH2) domain proteins. We mutated or deleted all known autophosphorylation sites of the Epidermal Growth Factor-Receptor (EGF-receptor) and examined the effects of these mutations on gene expression, MAP kinase activation...

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 Enzyme Activation
Share to Membrane Proteins

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

Share to Molecular Sequence Data

Share to Mutation

Share to Oligodeoxyribonucleotides

Share to Phosphorylation

Source

Identifiers

PMID: 7970705

Genes

EGF

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

Autophosphorylation mutants of the EGF-receptor signal through auxiliary mechanisms involving SH2 domain proteins.PMID 7970705Read ↗

Epidermal growth factor receptor cytoplasmic domain mutations trigger ligand-independent transformation.Semantic proximity Read ↗

erbB-2 autophosphorylation is required for mitogenic action and high-affinity substrate coupling.Semantic proximity Read ↗

A dominant negative mutation suppresses the function of normal epidermal growth factor receptors by heterodimerization.Semantic proximity Read ↗

Anti-oncogenic activity of signalling-defective epidermal growth factor receptor mutants.Semantic proximity Read ↗

Oncogenic HRAS mutations cause prolonged PI3K signaling in response to epidermal growth factor in fibroblasts of patients with Costello syndrome.Semantic proximity Read ↗

Tyrosyl phosphorylation of Shp2 is required for normal ERK activation in response to some, but not all, growth factors.Semantic proximity Read ↗

Requirement for intrinsic protein tyrosine kinase in the immediate and late actions of the EGF receptor.Semantic proximity Read ↗

A differential requirement for the COOH-terminal region of the epidermal growth factor (EGF) receptor in amphiregulin and EGF mitogenic signaling.Semantic proximity Read ↗

Multiple autophosphorylation site mutations of the epidermal growth factor receptor. Analysis of kinase activity and endocytosis.Semantic proximity Read ↗

Noonan syndrome-associated SHP2/PTPN11 mutants cause EGF-dependent prolonged GAB1 binding and sustained ERK2/MAPK1 activation.Semantic proximity Read ↗

Extracellular domain mutations of the EGF receptor differentially modulate high-affinity and low-affinity responses to EGF receptor ligands.Semantic proximity Read ↗

Tissue-specific transformation by oncogenic mutants of epidermal growth factor receptor.Semantic proximity Read ↗

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