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

Structural basis of Rad53 kinase activation by dimerization and activation segment exchange.

Cellular signalling - 1 Sept 2014

Wybenga-Groot Leanne E, Ho Cynthia S, Sweeney Frédéric D, Ceccarelli Derek F, McGlade C Jane, Durocher Daniel, Sicheri Frank

Abstract excerpt

The protein kinase Rad53 is a key regulator of the DNA damage checkpoint in budding yeast. Its human ortholog, CHEK2, is mutated in familial breast cancer and mediates apoptosis in response to genotoxic stress. Autophosphorylation of Rad53 at residue Thr354 located in the kinase activation segment is essential for Rad53 activation. In this study, we assessed the requirement of kinase domain dimerization and the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cell Cycle Proteins
Share to Checkpoint Kinase 2

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

Share to Crystallography, X-Ray

Share to Dimerization

Share to Enzyme Activation

Share to Phosphorylation

Share to Saccharomyces cerevisiae Proteins

Share to Ultracentrifugation

Source

Identifiers

PMID: 24815189
DOI: 10.1016/j.cellsig.2014.05.004

Genes

CHEK2

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural basis of Rad53 kinase activation by dimerization and activation segment exchange.PMID 24815189Read ↗

Characterization of the activation domain of the Rad53 checkpoint kinase.Semantic proximity Read ↗

Structure and activation mechanism of the CHK2 DNA damage checkpoint kinase.Semantic proximity Read ↗

BRCA2 C-terminal clamp restructures RAD51 dimers to bind B-DNA for replication fork stability.Semantic proximity Read ↗

Phosphorylation-Dependent Activation of the XRCC1 Intrinsically Disordered Region: A Computational Structural AnalysisSemantic proximity Read ↗

Checking in on Cds1 (Chk2): A checkpoint kinase and tumor suppressorSemantic proximity Read ↗

Phosphorylation-regulated transitions in an oligomeric state control the activity of the Sae2 DNA repair enzyme.Semantic proximity Read ↗

The translocation activity of Rad54 reduces crossover outcomes during homologous recombination.Semantic proximity Read ↗

The translocation activity of Rad54 reduces crossover outcomes during homologous recombinationSemantic proximity Read ↗

The Saccharomyces cerevisiae 14-3-3 proteins Bmh1 and Bmh2 directly influence the DNA damage-dependent functions of Rad53.Semantic proximity Read ↗

Mislocalization of BRCA1-complex due to ABRAXAS Arg361Gln mutation.Semantic proximity Read ↗

Surprising complexity of the Asf1 histone chaperone-Rad53 kinase interaction.Semantic proximity Read ↗

A domain of Rad9 specifically required for activation of Chk1 in budding yeast.Semantic proximity Read ↗

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