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Article

Regulation of the Raf-1 kinase domain by phosphorylation and 14-3-3 association.

The Biochemical journal - 1 Oct 2000

Yip-Schneider M T, Miao W, Lin A, Barnard D S, Tzivion G, Marshall M S

Abstract excerpt

The Raf-1 kinase domain is kept in an inactive state by the N-terminal regulatory domain. Activation of the kinase domain occurs following release from the N-terminal repression and possible catalytic upregulation. To distinguish the regulatory mechanisms that directly influence the catalytic activity of the enzyme from those which act through the inhibitory domain, the catalytic domain of Raf-1 (CR3) was...

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Identifiers

PMID: 10998357
DOI: 10.1042/0264-6021:3510151
PMCID: PMC1221345

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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.

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