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Article

Structural analysis of the mechanism of phosphorylation of a critical autoregulatory tyrosine residue in FGFR1 kinase domain.

Genes to cells : devoted to molecular & cellular mechanisms - 1 Oct 2015

Kobashigawa Yoshihiro, Amano Shinjiro, Yokogawa Mariko, Kumeta Hiroyuki, Morioka Hiroshi, Inouye Masayori, Schlessinger Joseph, Inagaki Fuyuhiko

Abstract excerpt

Receptor and nonreceptor tyrosine kinases are enzymes that play important roles in regulating signal transduction pathways in a variety of normal cellular process and in many pathological conditions. Ordered phosphorylation is required for receptor tyrosine kinase (RTK) activation, a process mediated by transient dimer formation of the kinase domains. This process is triggered by the tyrosine phosphorylation in...

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Source

Identifiers

PMID: 26300540
DOI: 10.1111/gtc.12277

Genes

FGFR1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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