Phosphopeptide binding specificities of BRCA1 COOH-terminal (BRCT) domains - Wikidata - wikimedia - TriplyDB

Phosphopeptide binding specificities of BRCA1 COOH-terminal (BRCT) domains

Phosphopeptide binding specificities of BRCA1 COOH-terminal (BRCT) domains

http://www.wikidata.org/entity/Q28212425

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Microcephalin Is a DNA Damage Response Protein Involved in Regulation of CHK1 and BRCA1 Function of BRCA1 in the DNA damage response is mediated by ADP-ribosylation Phosphorylation and regulation of DNA ligase IV stability by DNA-dependent protein kinase BARD1 induces apoptosis by catalysing phosphorylation of p53 by DNA-damage response kinase Growth factor pleiotropy is controlled by a receptor Tyr/Ser motif that acts as a binary switch Abraxas and RAP80 form a BRCA1 protein complex required for the DNA damage response DNA damage-induced cell cycle checkpoint control requires CtIP, a phosphorylation-dependent binding partner of BRCA1 C-terminal domains CCDC98 targets BRCA1 to DNA damage sites The human Rap1 protein complex and modulation of telomere length TopBP1 recruits Brg1/Brm to repress E2F1-induced apoptosis, a novel pRb-independent and E2F1-specific control for cell survival Structural basis of BACH1 phosphopeptide recognition by BRCA1 tandem BRCT domains Functional Evolution of BRCT Domains from Binding DNA to Protein BRCT domains: easy as one, two, three Structural and functional interaction between the human DNA repair proteins DNA ligase IV and XRCC4 Comparison of BRCT domains of BRCA1 and 53BP1: a biophysical analysis Structural evidence for direct interactions between the BRCT domains of human BRCA1 and a phospho-peptide from human ACC1 The ePHD protein SPBP interacts with TopBP1 and together they co-operate to stimulate Ets1-mediated transcription The BRCT domain of mammalian Rev1 is involved in regulating DNA translesion synthesis A guide for functional analysis of BRCA1 variants of uncertain significance Phosphopeptide interactions with BRCA1 BRCT domains: More than just a motif Acetylation of lysine 382 and phosphorylation of serine 392 in p53 modulate the interaction between p53 and MDC1 in vitro A microchip platform for structural oncology applications.Solution Structure of Polymerase μ's BRCT Domain Reveals an Element Essential for Its Role in Nonhomologous End Joining †Molecular basis of BACH1/FANCJ recognition by TopBP1 in DNA replication checkpoint control Impact of BRCA1 BRCT Domain Missense Substitutions on Phosphopeptide Recognition Molecular Basis for the Association of Microcephalin (MCPH1) Protein with the Cell Division Cycle Protein 27 (Cdc27) Subunit of the Anaphase-promoting Complex A CDK-catalysed regulatory phosphorylation for formation of the DNA replication complex Sld2-Dpb11 14-3-3 proteins--an update The DNA damage response mediator MDC1 directly interacts with the anaphase-promoting complex/cyclosome Peptide library approach to uncover phosphomimetic inhibitors of the BRCA1 C-terminal domain Structure and mechanism of BRCA1 BRCT domain recognition of phosphorylated BACH1 with implications for cancer Sibling rivalry: competition between Pol X family members in V(D)J recombination and general double strand break repair Phospho-Ser/Thr-binding domains: navigating the cell cycle and DNA damage response NFBD1/MDC1 associates with p53 and regulates its function at the crossroad between cell survival and death in response to DNA damage Topoisomerase IIalpha controls the decatenation checkpoint Histone ubiquitination associates with BRCA1-dependent DNA damage response BRCT domains: A little more than kin, and less than kind Viral transport of DNA damage that mimics a stalled replication fork.SIRT1 shows no substrate specificity in vitro.Rtt107/Esc4 binds silent chromatin and DNA repair proteins using different BRCT motifs.

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Phosphopeptide binding specificities of BRCA1 COOH-terminal (BRCT) domains

http://www.wikidata.org/entity/Q28212425

description

2003 nî lūn-bûn

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2003 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2003年の論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年论文

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name

Phosphopeptide binding specificities of BRCA1 COOH-terminal (BRCT) domains

@ast

Phosphopeptide binding specificities of BRCA1 COOH-terminal (BRCT) domains

@en

Phosphopeptide binding specificities of BRCA1 COOH-terminal (BRCT) domains

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type

label

Phosphopeptide binding specificities of BRCA1 COOH-terminal (BRCT) domains

@ast

Phosphopeptide binding specificities of BRCA1 COOH-terminal (BRCT) domains

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Phosphopeptide binding specificities of BRCA1 COOH-terminal (BRCT) domains

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prefLabel

Phosphopeptide binding specificities of BRCA1 COOH-terminal (BRCT) domains

@ast

Phosphopeptide binding specificities of BRCA1 COOH-terminal (BRCT) domains

@en

Phosphopeptide binding specificities of BRCA1 COOH-terminal (BRCT) domains

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P1433

Journal of Biological Chemistry

P1476

Phosphopeptide binding specificities of BRCA1 COOH-terminal (BRCT) domains

@en

P2093

Junjie Chen

http://www.w3.org/2001/XMLSchema#string

Maria Rodriguez

http://www.w3.org/2001/XMLSchema#string

Xiaochun Yu

http://www.w3.org/2001/XMLSchema#string

Zhou Songyang

http://www.w3.org/2001/XMLSchema#string

P2860

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

Structure of the 53BP1 BRCT region bound to p53 and its comparison to the Brca1 BRCT structure

MDC1 is a mediator of the mammalian DNA damage checkpoint

The BRCT domain is a phospho-protein binding domain

Identification of a RING protein that can interact in vivo with the BRCA1 gene product

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

Conserved domains in DNA repair proteins and evolution of repair systems

An interaction between the mammalian DNA repair protein XRCC1 and DNA ligase III

Regulation of E2F1 by BRCT domain-containing protein TopBP1

Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding

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scholarly article

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4771271

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10.1074/JBC.C300407200

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P433

52

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278

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2003-12-26T00:00:00Z

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14578343

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