Independent and sequential recruitment of NHEJ and HR factors to DNA damage sites in mammalian cells. - Wikidata - awgldk - TriplyDB

Independent and sequential recruitment of NHEJ and HR factors to DNA damage sites in mammalian cells.

Independent and sequential recruitment of NHEJ and HR factors to DNA damage sites in mammalian cells.

http://www.wikidata.org/entity/Q33220843

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Altered hematopoiesis in mice lacking DNA polymerase mu is due to inefficient double-strand break repair Chk1 phosphorylation of Metnase enhances DNA repair but inhibits replication fork restart The E3 ligase RNF8 regulates KU80 removal and NHEJ repair The annealing helicase HARP is recruited to DNA repair sites via an interaction with RPA The dynamics of Ku70/80 and DNA-PKcs at DSBs induced by ionizing radiation is dependent on the complexity of damage Dynamics of DNA damage response proteins at DNA breaks: a focus on protein modifications A polycomb group protein, PHF1, is involved in the response to DNA double-strand breaks in human cell Dynamic assembly of end-joining complexes requires interaction between Ku70/80 and XRCC4 Lack of MSH2 involvement differentiates V(D)J recombination from other non-homologous end joining events Human Ku70/80 protein blocks exonuclease 1-mediated DNA resection in the presence of human Mre11 or Mre11/Rad50 protein complex.Spatial organization of the mammalian genome surveillance machinery in response to DNA strand breaks The efficiency of homologous recombination and non-homologous end joining systems in repairing double-strand breaks during cell cycle progression Expanded roles of the Fanconi anemia pathway in preserving genomic stability The yin-yang of DNA damage response: roles in tumorigenesis and cellular senescence.Comparative analysis of different laser systems to study cellular responses to DNA damage in mammalian cells The protein phosphatase 1 regulator PNUTS is a new component of the DNA damage response.Analysis of DNA double-strand break response and chromatin structure in mitosis using laser microirradiation.Autophosphorylation of DNA-PKCS regulates its dynamics at DNA double-strand breaks.Rapid recruitment of BRCA1 to DNA double-strand breaks is dependent on its association with Ku80 Radiation microbeams as spatial and temporal probes of subcellular and tissue response.Autophosphorylation at serine 1981 stabilizes ATM at DNA damage sites.Damage site chromatin: open or closed?Regulation of the DNA Damage Response to DSBs by Post-Translational Modifications.Condensin I recruitment to base damage-enriched DNA lesions is modulated by PARP1.DNA Ligase IV regulates XRCC4 nuclear localization.The MRN complex in double-strand break repair and telomere maintenance.Persistently bound Ku at DNA ends attenuates DNA end resection and homologous recombination Recruitment and retention dynamics of RECQL5 at DNA double strand break sites.Pathway choice in DNA double strand break repair: observations of a balancing act.Parp-1 protects homologous recombination from interference by Ku and Ligase IV in vertebrate cells.Repair of DNA strand breaks in a minichromosome in vivo: kinetics, modeling, and effects of inhibitors.Mouse DNA polymerase kappa has a functional role in the repair of DNA strand breaks The role of hnRPUL1 involved in DNA damage response is related to PARP1.Riccardin D Exerts Its Antitumor Activity by Inducing DNA Damage in PC-3 Prostate Cancer Cells In Vitro and In Vivo.Choosing the right path: does DNA-PK help make the decision?Homologous recombination conserves DNA sequence integrity throughout the cell cycle in embryonic stem cells Mechanisms of DNA damage response to targeted irradiation in organotypic 3D skin cultures.Interaction with OGG1 is required for efficient recruitment of XRCC1 to base excision repair and maintenance of genetic stability after exposure to oxidative stress Regulatory networks integrating cell cycle control with DNA damage checkpoints and double-strand break repair.Organization and dynamics of the nonhomologous end-joining machinery during DNA double-strand break repair

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P2860

Independent and sequential recruitment of NHEJ and HR factors to DNA damage sites in mammalian cells.

http://www.wikidata.org/entity/Q33220843

description

2005 nî lūn-bûn

@nan

2005 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2005 թվականի օգոստոսին հրատարակված գիտական հոդված

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年论文

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name

Independent and sequential rec ...... mage sites in mammalian cells.

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Independent and sequential rec ...... mage sites in mammalian cells.

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type

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Independent and sequential rec ...... mage sites in mammalian cells.

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Independent and sequential rec ...... mage sites in mammalian cells.

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Independent and sequential rec ...... mage sites in mammalian cells.

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Independent and sequential rec ...... mage sites in mammalian cells.

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Journal of Cell Biology

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Independent and sequential rec ...... mage sites in mammalian cells.

@en

P2093

A Malcolm R Taylor

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David J Chen

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Jong-Soo Kim

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Kyoko Yokomori

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Tatiana B Krasieva

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P2860

A potential role for human cohesin in mitotic spindle aster assembly

ATM activation by DNA double-strand breaks through the Mre11-Rad50-Nbs1 complex

The 3' to 5' exonuclease activity of Mre 11 facilitates repair of DNA double-strand breaks

The hMre11/hRad50 protein complex and Nijmegen breakage syndrome: linkage of double-strand break repair to the cellular DNA damage response

Human Rad51 protein promotes ATP-dependent homologous pairing and strand transfer reactions in vitro

hMre11 and hRad50 nuclear foci are induced during the normal cellular response to DNA double-strand breaks

Mre11 assembles linear DNA fragments into DNA damage signaling complexes

Postreplicative recruitment of cohesin to double-strand breaks is required for DNA repair.

Relocalization of telomeric Ku and SIR proteins in response to DNA strand breaks in yeast.

DNA damage response pathway uses histone modification to assemble a double-strand break-specific cohesin domain.

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341-347

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10.1083/JCB.200411083

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3

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170

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Hitoshi Kurumizaka

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2005-08-01T00:00:00Z

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7685594

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16061690

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2171485

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