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

BRCT Domain Interactions in the Heterodimeric DNA Repair Protein XRCC1−DNA Ligase III

28 Apr 2001

Abstract excerpt

Proteins involved in DNA repair, or its coordination with DNA replication and mitosis through cell cycle checkpoints, are vital in the concerted cellular response to DNA damage that maintains the integrity of the genome. The "BRCT" domain (BRCA1 carboxy terminal) was noted as a putative protein-protein interaction motif in the breast cancer suppressor gene, BRCA1, and subsequently identified in over 50 proteins...

Read the complete abstract on PubMed

Topics

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

Share to Genetic Neurodegenerative Diseases
Share to DNA Repair Mechanisms
Share to PARP inhibition in cancer therapy

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 11352725
DOI: 10.1021/bi002701e

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

BRCT Domain Interactions in the Heterodimeric DNA Repair Protein XRCC1−DNA Ligase IIIPMID 11352725Read ↗

Structure of an XRCC1 BRCT domain: a new protein-protein interaction module.Semantic proximity Read ↗

Crystal structure of the BRCT repeat region from the breast cancer-associated protein BRCA1.Semantic proximity Read ↗

The structural basis for partitioning of the XRCC1/DNA ligase III-α BRCT-mediated dimer complexes.Semantic proximity Read ↗

A superfamily of conserved domains in DNA damage‐ responsive cell cycle checkpoint proteinsSemantic proximity Read ↗

An atypical BRCT-BRCT interaction with the XRCC1 scaffold protein compacts human DNA Ligase IIIα within a flexible DNA repair complex.Semantic proximity Read ↗

RAD51 Paralogs and RAD51 Paralog Complexes BCDX2 and CX3 Interact with BRCA2Semantic proximity Read ↗

BRCT domains: phosphopeptide binding and signaling modules.Semantic proximity Read ↗

Structural and Functional Interaction between the Human DNA Repair Proteins DNA Ligase IV and XRCC4Semantic proximity Read ↗

[Mapping of BRCT1 domain of BRCA1 with chromatin unfolding activity].Semantic proximity Read ↗

Distinct binding of BRCA2 BRC repeats to RAD51 generates differential DNA damage sensitivitySemantic proximity Read ↗

The BRCT domain is a phospho-protein binding domain.Semantic proximity Read ↗

A variant of the breast cancer type 2 susceptibility protein (BRC) repeat is essential for the RECQL5 helicase to interact with RAD51 recombinase for genome stabilization.Semantic proximity Read ↗

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