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

Serines 440 and 467 in the Werner syndrome protein are phosphorylated by DNA-PK and affects its dynamics in response to DNA double strand breaks.

Aging - 1 Jan 2014

Kusumoto-Matsuo Rika, Ghosh Deblina, Karmakar Parimal, May Alfred, Ramsden Dale, Bohr Vilhelm A

Abstract excerpt

WRN protein, defective in Werner syndrome (WS), a human segmental progeria, is a target of serine/threonine kinases involved in sensing DNA damage. DNA-PK phosphorylates WRN in response to DNA double strand breaks (DSBs). However, the main phosphorylation sites and functional importance of the phosphorylation of WRN has remained unclear. Here, we identify Ser-440 and -467 in WRN as major phosphorylation sites...

Read the complete abstract on PubMed

Topics

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

Share to Bleomycin
Share to Cell Nucleolus

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to DNA-Activated Protein Kinase

Share to DNA Breaks, Double-Stranded

Share to Etoposide

Share to Exodeoxyribonucleases

Share to RecQ Helicases

Share to Werner Syndrome Helicase

Source

Open in PubMed Open full text

Identifiers

PMID: 24429382
DOI: 10.18632/aging.100629
PMCID: PMC3927811

Genes

WRN

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Serines 440 and 467 in the Werner syndrome protein are phosphorylated by DNA-PK and affects its dynamics in response to DNA double strand breaks.PMID 24429382Read ↗

CDK2 phosphorylation of Werner protein (WRN) contributes to WRN’s DNA double‐strand break repair pathway choiceSemantic proximity Read ↗

Werner Protein Is a Target of DNA-dependent Protein Kinase in Vivo and in Vitro, and Its Catalytic Activities Are Regulated by PhosphorylationSemantic proximity Read ↗

Response to Replication Stress and Maintenance of Genome Stability by WRN, the Werner Syndrome ProteinSemantic proximity Read ↗

Cooperation of DNA-PKcs and WRN helicase in the maintenance of telomeric D-loopsSemantic proximity Read ↗

Werner syndrome: molecular insights into the relationships between defective DNA metabolism, genomic instability, cancer and aging.Semantic proximity Read ↗

ATM pathway activation limits R-loop-associated genomic instability in Werner syndrome cellsSemantic proximity Read ↗

Checkpoint-dependent and independent roles of the Werner syndrome protein in preserving genome integrity in response to mild replication stress.Semantic proximity Read ↗

Werner syndrome: Clinical features, pathogenesis and potential therapeutic interventions.Semantic proximity Read ↗

Werner Syndrome Protein Phosphorylation by Abl Tyrosine Kinase Regulates Its Activity and DistributionSemantic proximity Read ↗

Werner syndrome protein: functions in the response to DNA damage and replication stress in S-phase.Semantic proximity Read ↗

WRN mutations in Werner syndrome.Semantic proximity Read ↗

Physical and Functional Interaction between p53 and the Werner's Syndrome ProteinSemantic proximity Read ↗

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