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

RETRACTED: Structural analysis of BRCA1 reveals modification hotspot.

Science advances - 1 Sept 2017

Liang Yanping, Dearnaley William J, Varano A Cameron, Winton Carly E, Gilmore Brian L, Alden Nick A, Sheng Zhi, Kelly Deborah F

Abstract excerpt

Cancer cells afflicted with mutations in the breast cancer susceptibility protein (BRCA1) often suffer from increased DNA damage and genomic instability. The precise manner in which physical changes to BRCA1 influence its role in DNA maintenance remains unclear. We used single-particle electron microscopy to study the three-dimensional properties of BRCA1 naturally produced in breast cancer cells. Structural...

Read the complete abstract on PubMed

Topics

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

Share to BRCA1 Protein
Share to Oxidation-Reduction

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Oxidative Stress

Share to Protein Interaction Domains and Motifs

Share to Protein Processing, Post-Translational

Share to Structure-Activity Relationship

Share to Tumor Suppressor Proteins

Share to Ubiquitin-Protein Ligases

Source

Open in PubMed Open full text

Identifiers

PMID: 28948225
DOI: 10.1126/sciadv.1701386
PMCID: PMC5606707

Genes

BRCA1
BARD1

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

RETRACTED: Structural analysis of BRCA1 reveals modification hotspot.PMID 28948225Read ↗

Molecular Analysis of BRCA1 in Human Breast Cancer Cells Under Oxidative Stress.Semantic proximity Read ↗

Mechanisms of BRCA1-BARD1 nucleosome recognition and ubiquitylation.Semantic proximity Read ↗

Research Progress of BAP1 in Structure, Function, and Cancer.Semantic proximity Read ↗

Structural insight into BRCA1-BARD1 complex recruitment to damaged chromatin.Semantic proximity Read ↗

Histone H3 Orchestrates the Ubiquitination of Nucleosomal H2A by BRCA1/BARD1-UbcH5c ComplexSemantic proximity Read ↗

DNA clamp function of the mono-ubiquitinated Fanconi Anemia FANCI-FANCD2 complexSemantic proximity Read ↗

Histone Tail Electrostatics Modulate E2-E3 Enzyme Dynamics: A Gateway to Regulate Ubiquitination MachinerySemantic proximity Read ↗

Functional analysis of BRCA1 RING domain variants: computationally derived structural data can improve upon experimental features for training predictive models.Semantic proximity Read ↗

Structure and function of the RAD51B–RAD51C–RAD51D–XRCC2 tumour suppressorSemantic proximity Read ↗

The BRCA1/BARD1 ubiquitin ligase and its substrates.Semantic proximity Read ↗

Structure of the human Bre1 complex bound to the nucleosomeSemantic proximity Read ↗

Structural basis for stabilisation of the RAD51 nucleoprotein filament by BRCA2Semantic proximity Read ↗

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