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Article

Characterization of the activation domain of the Rad53 checkpoint kinase.

Cell cycle (Georgetown, Tex.) - 15 Feb 2008

Fiorani Simona, Mimun Guendalina, Caleca Laura, Piccini Daniele, Pellicioli Achille

Abstract excerpt

Rad53 protein, the yeast orthologue of the human checkpoint kinase Chk2, presents two highly conserved phosphorylatable threonine residues (T354 and T358) in the activation domain, whose phosphorylation is critical to allow the activation of the kinase. In this study we found that Rad53 protein variants in which alanine and/or aspartate replace the threonine residues 354 and/or 358 do not retain kinase activity...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 18287812
DOI: 10.4161/cc.7.4.5323

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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