Phosphopeptide interactions with BRCA1 BRCT domains: More than just a motif - Wikidata - thesis-toulmin - TriplyDB

Phosphopeptide interactions with BRCA1 BRCT domains: More than just a motif

Phosphopeptide interactions with BRCA1 BRCT domains: More than just a motif

http://www.wikidata.org/entity/Q26999072

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Dynamic structures in DNA damage responses & cancer.Identification of recurrent BRCA1 mutation and its clinical relevance in Chinese Triple-negative breast cancer cohort.Structure of BRCA1-BRCT/Abraxas Complex Reveals Phosphorylation-Dependent BRCT Dimerization at DNA Damage Sites.Gene-Specific Genetic Complementation between Brca1 and Cobra1 During Mouse Mammary Gland Development.ATM loss leads to synthetic lethality in BRCA1 BRCT mutant mice associated with exacerbated defects in homology-directed repair.A new bioinformatics tool to help assess the significance of BRCA1 variants.Homology-Directed Repair and the Role of BRCA1, BRCA2, and Related Proteins in Genome Integrity and Cancer

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Phosphopeptide interactions with BRCA1 BRCT domains: More than just a motif

http://www.wikidata.org/entity/Q26999072

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2015 nî lūn-bûn

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2015 թուականի Մարտին հրատարակուած գիտական յօդուած

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2015 թվականի մարտին հրատարակված գիտական հոդված

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2015年の論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年论文

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name

Phosphopeptide interactions with BRCA1 BRCT domains: More than just a motif

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Phosphopeptide interactions with BRCA1 BRCT domains: More than just a motif

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Phosphopeptide interactions with BRCA1 BRCT domains: More than just a motif

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type

label

Phosphopeptide interactions with BRCA1 BRCT domains: More than just a motif

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Phosphopeptide interactions with BRCA1 BRCT domains: More than just a motif

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Phosphopeptide interactions with BRCA1 BRCT domains: More than just a motif

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prefLabel

Phosphopeptide interactions with BRCA1 BRCT domains: More than just a motif

@ast

Phosphopeptide interactions with BRCA1 BRCT domains: More than just a motif

@en

Phosphopeptide interactions with BRCA1 BRCT domains: More than just a motif

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J.PBIOMOLBIO.2015.02.003

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Progress in Biophysics and Molecular Biology

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Phosphopeptide interactions with BRCA1 BRCT domains: More than just a motif

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Creative Commons Attribution 4.0 International

P2860

BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function

The BRCT domain is a phospho-protein binding domain

ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage

Abraxas and RAP80 form a BRCA1 protein complex required for the DNA damage response

CCDC98 targets BRCA1 to DNA damage sites

Structure of an XRCC1 BRCT domain: a new protein-protein interaction module

BRCT domains: easy as one, two, three

Structural evidence for direct interactions between the BRCT domains of human BRCA1 and a phospho-peptide from human ACC1

Crystal structure of the BRCT repeat region from the breast cancer-associated protein BRCA1

Structural consequences of a cancer-causing BRCA1-BRCT missense mutation

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10.1016/J.PBIOMOLBIO.2015.02.003

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nuclear protein

transcription factor

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Fanconi anemia complementation group proteins

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