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

Cancer-related mutations in BRCA1-BRCT cause long-range structural changes in protein-protein binding sites: a molecular dynamics study.

Proteins - 1 Jan 2007

Gough Craig A, Gojobori Takashi, Imanishi Tadashi

Abstract excerpt

Cancer-associated mutations in the BRCT domain of BRCA1 (BRCA1-BRCT) abolish its tumor suppressor function by disrupting interactions with other proteins such as BACH1. Many cancer-related mutations do not cause sufficient destabilization to lead to global unfolding under physiological conditions, and thus abrogation of function probably is due to localized structural changes. To explore the reasons for...

Read the complete abstract on PubMed

Topics

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

Share to Algorithms
Share to BRCA1 Protein
Share to Breast Neoplasms

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Computer Simulation

Share to Crystallography, X-Ray

Share to Databases, Protein

Share to Entropy

Share to Protein Conformation

Source

Identifiers

PMID: 17063491
DOI: 10.1002/prot.21188

Genes

BACH1
BRCA1

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

Cancer-related mutations in BRCA1-BRCT cause long-range structural changes in protein-protein binding sites: a molecular dynamics study.PMID 17063491Read ↗

Structure and mechanism of BRCA1 BRCT domain recognition of phosphorylated BACH1 with implications for cancer.Semantic proximity Read ↗

Thermal unfolding of human BRCA1 BRCT-domain variants.Semantic proximity Read ↗

Characterisation of the BRCT domains of the breast cancer susceptibility gene product BRCA1.Semantic proximity Read ↗

Mutations in the BRCT domain confer temperature sensitivity to BRCA1 in transcription activation.Semantic proximity Read ↗

Insights into the molecular basis of human hereditary breast cancer from studies of the BRCA1 BRCT domain.Semantic proximity Read ↗

Structural basis of BACH1 phosphopeptide recognition by BRCA1 tandem BRCT domains.Semantic proximity Read ↗

Unraveling the Allosteric Mechanism of Four Cancer-related Mutations in the Disruption of p53-DNA Interaction.Semantic proximity Read ↗

Classification of VUS and unclassified variants in BRCA1 BRCT repeats by molecular dynamics simulationSemantic proximity Read ↗

Inter-BRCT linker is probably the most intolerant region of the BRCA1 BRCT domain.Semantic proximity Read ↗

"Similarity trap" in protein-protein interactions could be carcinogenic: simulations of p53 core domain complexed with 53BP1 and BRCA1 BRCT domains.Semantic proximity Read ↗

Computational and experimental studies of the interaction between phospho-peptides and the C-terminal domain of BRCA1.Semantic proximity Read ↗

Structure-based assessment of missense mutations in human BRCA1: implications for breast and ovarian cancer predisposition.Semantic proximity Read ↗

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