RNF168 ubiquitylates 53BP1 and controls its response to DNA double-strand breaks.
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Writers, Readers, and Erasers of Histone Ubiquitylation in DNA Double-Strand Break RepairDiagnostics of primary immunodeficiency diseases: a sequencing capture approachRegulation of 53BP1 protein stability by RNF8 and RNF168 is important for efficient DNA double-strand break repairModulation of LSD1 phosphorylation by CK2/WIP1 regulates RNF168-dependent 53BP1 recruitment in response to DNA damageRNF17 blocks promiscuous activity of PIWI proteins in mouse testesINT6/EIF3E Controls the RNF8-Dependent Ubiquitylation Pathway and Facilitates DNA Double-Strand Break Repair in Human Cells.USP7 deubiquitinase promotes ubiquitin-dependent DNA damage signaling by stabilizing RNF168.Independent mechanisms recruit the cohesin loader protein NIPBL to sites of DNA damage.A Damage-Independent Role for 53BP1 that Impacts Break Order and Igh Architecture during Class Switch RecombinationRNF168 cooperates with RNF8 to mediate FOXM1 ubiquitination and degradation in breast cancer epirubicin treatmentChronic oxidative stress promotes H2AX protein degradation and enhances chemosensitivity in breast cancer patients.H2B ubiquitination regulates meiotic recombination by promoting chromatin relaxationThe de-ubiquitylating enzymes USP26 and USP37 regulate homologous recombination by counteracting RAP80.Recent advances in the study of immunodeficiency and DNA damage response.RNF168 and USP10 regulate topoisomerase IIα function via opposing effects on its ubiquitylationTRIP12 as a mediator of human papillomavirus/p16-related radiation enhancement effects.C9orf72 expansion disrupts ATM-mediated chromosomal break repair.Clinical and Biological Manifestation of RNF168 Deficiency in Two Polish Siblings.Acetylation of 53BP1 dictates the DNA double strand break repair pathway.An E2-guided E3 Screen Identifies the RNF17-UBE2U Pair as Regulator of the Radiosensitivity, Immunodeficiency, Dysmorphic Features, and Learning Difficulties (RIDDLE) Syndrome Protein RNF168.Reading chromatin signatures after DNA double-strand breaks.53BP1 loss induces chemoresistance of colorectal cancer cells to 5-fluorouracil by inhibiting the ATM-CHK2-P53 pathway.Trip12 is an E3 ubiquitin ligase for USP7/HAUSP involved in the DNA damage response.Recruitment of lysine demethylase 2A to DNA double strand breaks and its interaction with 53BP1 ensures genome stability.Shepherding DNA ends: Rif1 protects telomeres and chromosome breaks.Ubiquitin ligase RNF8 suppresses Notch signaling to regulate mammary development and tumorigenesis
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RNF168 ubiquitylates 53BP1 and controls its response to DNA double-strand breaks.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 09 December 2013
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
RNF168 ubiquitylates 53BP1 and controls its response to DNA double-strand breaks.
@en
RNF168 ubiquitylates 53BP1 and controls its response to DNA double-strand breaks.
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RNF168 ubiquitylates 53BP1 and controls its response to DNA double-strand breaks.
@en
RNF168 ubiquitylates 53BP1 and controls its response to DNA double-strand breaks.
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prefLabel
RNF168 ubiquitylates 53BP1 and controls its response to DNA double-strand breaks.
@en
RNF168 ubiquitylates 53BP1 and controls its response to DNA double-strand breaks.
@nl
P2093
P2860
P356
P1476
RNF168 ubiquitylates 53BP1 and controls its response to DNA double-strand breaks.
@en
P2093
Anne Hakem
Brian Raught
Georges Maire
Miyuki Bohgaki
Razqallah Hakem
Samah El Ghamrasni
Stephanie Panier
Tharan Srikumar
Toshiyuki Bohgaki
P2860
P304
20982-20987
P356
10.1073/PNAS.1320302111
P407
P577
2013-12-09T00:00:00Z