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

Fine-tuning of DNA damage-dependent ubiquitination by OTUB2 supports the DNA repair pathway choice.

Molecular cell - 20 Feb 2014

Kato Kiyoko, Nakajima Kazuhiro, Ui Ayako, Muto-Terao Yuri, Ogiwara Hideaki, Nakada Shinichiro

Abstract excerpt

DNA double-strand breaks (DSBs) are deleterious lesions that lead to genetic mutations and cell death. Protein ubiquitination mediated by the E3 ubiquitin ligase RNF8 within the regions surrounding DSBs recruits DNA DSB response (DDR) factors and induces chromatin remodeling, which supports cell survival after DNA damage. Nevertheless, the impact of RNF8-mediated ubiquitination on DNA repair remains to be...

Read the complete abstract on PubMed

Topics

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

Share to Cell Death
Share to DNA Breaks, Double-Stranded

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Histone Chaperones

Share to Homologous Recombination

Share to Lysine

Share to Thiolester Hydrolases

Share to Tumor Suppressor p53-Binding Protein 1

Share to Ubiquitin

Source

Identifiers

PMID: 24560272
DOI: 10.1016/j.molcel.2014.01.030

Genes

OTUB2
RNF8

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.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Fine-tuning of DNA damage-dependent ubiquitination by OTUB2 supports the DNA repair pathway choice.PMID 24560272Read ↗

The E3 ubiquitin ligase DTX3L and the deubiquitinase USP28 fine-tune DNA double strand repair through mutual regulation of their protein levelsSemantic proximity Read ↗

E3 ligases: a ubiquitous link between DNA repair, DNA replication and human diseaseSemantic proximity Read ↗

Role of deubiquitinating enzymes in DNA double-strand break repairSemantic proximity Read ↗

The E3 ubiquitin ligase DTX3L and the deubiquitinase USP28 fine-tune DNA repair through mutual regulation of their protein levelsSemantic proximity Read ↗

The emerging role of deubiquitinating enzymes in genomic integrity, diseases, and therapeuticsSemantic proximity Read ↗

A PALB2-interacting domain in RNF168 couples homologous recombination to DNA break-induced chromatin ubiquitylationSemantic proximity Read ↗

Degradation‐linked ubiquitin signal and proteasome are integral components of DNA double strand break repair: New perspectives for anti‐cancer therapySemantic proximity Read ↗

HERC2 coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes.Semantic proximity Read ↗

Interaction between RNF8 and DYRK2 is required for the recruitment of DNA repair molecules to DNA double-strand breaks.Semantic proximity Read ↗

Regulation of the DNA damage response by ubiquitin conjugationSemantic proximity Read ↗

A p53-dependent FBXO44-RAD18 axis limits mutagenesis by terminating translesion DNA synthesisSemantic proximity Read ↗

Spatiotemporal regulation of PCNA ubiquitination in damage tolerance pathwaysSemantic proximity Read ↗

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