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

Oncogenic activation of p59fyn tyrosine protein kinase by mutation of its carboxyl-terminal site of tyrosine phosphorylation, tyrosine 528.

The Journal of biological chemistry - 8 Apr 1994

Davidson D, Fournel M, Veillette A

Abstract excerpt

As a result of alternative splicing, the Src-related tyrosine protein kinase p59fyn consists of two distinct isoforms termed FynB and FynT. Whereas the first product accumulates principally in brain, the second is expressed in hemopoietic cells, especially in T-lymphocytes. There is increasing ev...

Topics

3T3 Cells
Animals
Catalysis
Cell Transformation, Neoplastic
Enzyme Activation
Mice
Mutation
Phenylalanine
Phosphorylation
Protein-Tyrosine Kinases
Proto-Oncogene Proteins
Proto-Oncogene Proteins c-fyn

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Tyrosine

Source

Identifiers

PMID: 8144681

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8144681-2026-08-30.1. 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.

0

discussions

0

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

Oncogenic activation of p59fyn tyrosine protein kinase by mutation of its carboxyl-terminal site of tyrosine phosphorylation, tyrosine 528.PMID 8144681Read ↗

Regulation of T cell receptor signaling by a src family protein-tyrosine kinase (p59fyn).Semantic proximity Read ↗

Structural elements that regulate pp59c-fyn catalytic activity, transforming potential, and ability to associate with polyomavirus middle-T antigen.Semantic proximity Read ↗

Activation of p56lck through mutation of a regulatory carboxy-terminal tyrosine residue requires intact sites of autophosphorylation and myristylation.Semantic proximity Read ↗

Regulation of the oncogenic activity of the cellular src protein requires the correct spacing between the kinase domain and the C-terminal phosphorylated tyrosine (Tyr-527).Semantic proximity Read ↗

Site-directed mutagenesis of the SH2- and SH3-coding domains of c-src produces varied phenotypes, including oncogenic activation of p60c-src.Semantic proximity Read ↗

T cells expressing receptors of different affinity for antigen ligands reveal a unique role for p59fyn in T cell development and optimal stimulation of T cells by antigen.Semantic proximity Read ↗

Acidic residues at the carboxyl terminus of p60c-src are required for regulation of tyrosine kinase activity and transformation.Semantic proximity Read ↗

Phosphorylation of tyrosine residues in the kinase domain and juxtamembrane region regulates the biological and catalytic activities of Eph receptors.Semantic proximity Read ↗

Phosphorylation of Src mutants at Tyr 527 in fibroblasts does not correlate with in vitro phosphorylation by CSK.Semantic proximity Read ↗

The amino-terminal region of pp60c-src has a modulatory role and contains multiple sites of tyrosine phosphorylation.Semantic proximity Read ↗

Phenotypic changes induced by wild type and variant c-src genes carrying C-terminal sequence alterations.Semantic proximity Read ↗

Rapid plasma membrane anchoring of newly synthesized p59fyn: selective requirement for NH2-terminal myristoylation and palmitoylation at cysteine-3.Semantic proximity Read ↗

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