An oligomerized 53BP1 tudor domain suffices for recognition of DNA double-strand breaks. - Wikidata - awgldk - TriplyDB

An oligomerized 53BP1 tudor domain suffices for recognition of DNA double-strand breaks.

An oligomerized 53BP1 tudor domain suffices for recognition of DNA double-strand breaks.

http://www.wikidata.org/entity/Q37099895

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A-type lamins maintain the positional stability of DNA damage repair foci in mammalian nuclei 53BP1: pro choice in DNA repair Femtosecond near-infrared laser microirradiation reveals a crucial role for PARP signaling on factor assemblies at DNA damage sites.Impact of histone H4 lysine 20 methylation on 53BP1 responses to chromosomal double strand breaks Structural Insight into p53 Recognition by the 53BP1 Tandem Tudor Domain The molecular basis of ATM-dependent dimerization of the Mdc1 DNA damage checkpoint mediator Msl2 is a novel component of the vertebrate DNA damage response Double strand break repair functions of histone H2AX RIF1 is essential for 53BP1-dependent nonhomologous end joining and suppression of DNA double-strand break resection.53BP1 is a reader of the DNA-damage-induced H2A Lys 15 ubiquitin mark.Dephosphorylation enables the recruitment of 53BP1 to double-strand DNA breaks.Single cell resolution in vivo imaging of DNA damage following PARP inhibition USP28 is recruited to sites of DNA damage by the tandem BRCT domains of 53BP1 but plays a minor role in double-strand break metabolism.Dynamics of Rad9 chromatin binding and checkpoint function are mediated by its dimerization and are cell cycle-regulated by CDK1 activity Development and validation of 'AutoRIF': software for the automated analysis of radiation-induced foci.TopBP1 functions with 53BP1 in the G1 DNA damage checkpoint.The 53BP1 homolog in C. elegans influences DNA repair and promotes apoptosis in response to ionizing radiation Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1 Regulation of DNA end joining, resection, and immunoglobulin class switch recombination by 53BP1.KAP1 Deacetylation by SIRT1 Promotes Non-Homologous End-Joining Repair Dimerization Mediated by a Divergent Forkhead-associated Domain Is Essential for the DNA Damage and Spindle Functions of Fission Yeast Mdb1.CtIP protein dimerization is critical for its recruitment to chromosomal DNA double-stranded breaks.Ubiquitin-H2AX fusions render 53BP1 recruitment to DNA damage sites independent of RNF8 or RNF168 Proteomic analysis of murine Piwi proteins reveals a role for arginine methylation in specifying interaction with Tudor family members.A role for the p53 tumour suppressor in regulating the balance between homologous recombination and non-homologous end joining.Ser1778 of 53BP1 Plays a Role in DNA Double-strand Break Repairs.RNF168 ubiquitylates 53BP1 and controls its response to DNA double-strand breaks.53BP1, BRCA1, and the choice between recombination and end joining at DNA double-strand breaks.The cellular response to DNA damage: a focus on MDC1 and its interacting proteins.Role of 53BP1 in the regulation of DNA double-strand break repair pathway choice.Ultraviolet-B-mediated induction of protein-protein interactions in mammalian cells.53BP1 Integrates DNA Repair and p53-Dependent Cell Fate Decisions via Distinct Mechanisms.Dissection of Rad9 BRCT domain function in the mitotic checkpoint response to telomere uncapping.The function of classical and alternative non-homologous end-joining pathways in the fusion of dysfunctional telomeres.ASF1a Promotes Non-homologous End Joining Repair by Facilitating Phosphorylation of MDC1 by ATM at Double-Strand Breaks.FLUORO/NO: A Nitric Oxide Donor with a Fluorescence Reporter.53BP1 represses mitotic catastrophe in syncytia elicited by the HIV-1 envelope.A small molecule for theraNOstic targeting of cancer cells.Laser Microirradiation to Study In Vivo Cellular Responses to Simple and Complex DNA Damage.Reading chromatin signatures after DNA double-strand breaks.

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P2860

An oligomerized 53BP1 tudor domain suffices for recognition of DNA double-strand breaks.

http://www.wikidata.org/entity/Q37099895

description

article científic

@ca

article scientifique

@fr

articolo scientifico

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artigo científico

@pt

bilimsel makale

@tr

scientific article published on 08 December 2008

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

An oligomerized 53BP1 tudor domain suffices for recognition of DNA double-strand breaks.

@en

An oligomerized 53BP1 tudor domain suffices for recognition of DNA double-strand breaks.

@nl

type

label

An oligomerized 53BP1 tudor domain suffices for recognition of DNA double-strand breaks.

@en

An oligomerized 53BP1 tudor domain suffices for recognition of DNA double-strand breaks.

@nl

prefLabel

An oligomerized 53BP1 tudor domain suffices for recognition of DNA double-strand breaks.

@en

An oligomerized 53BP1 tudor domain suffices for recognition of DNA double-strand breaks.

@nl

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P1433

Molecular and Cellular Biology

P1476

An oligomerized 53BP1 tudor domain suffices for recognition of DNA double-strand breaks.

@en

P2093

Juergen Brugger

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

Kristopher Pataky

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

Omar Zgheib

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

Thanos D Halazonetis

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

P2860

MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks

RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins

RNF8 transduces the DNA-damage signal via histone ubiquitylation and checkpoint protein assembly

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

RAP80 targets BRCA1 to specific ubiquitin structures at DNA damage sites

Ubiquitin-binding protein RAP80 mediates BRCA1-dependent DNA damage response

The ubiquitin-interacting motif containing protein RAP80 interacts with BRCA1 and functions in DNA damage repair response

Orchestration of the DNA-damage response by the RNF8 ubiquitin ligase

Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair

Solution structure of Vps27 UIM-ubiquitin complex important for endosomal sorting and receptor downregulation

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1050-1058

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scholarly article

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10.1128/MCB.01011-08

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4

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29

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2008-12-08T00:00:00Z

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19064641

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2643802

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