Histone acetylation by Trrap-Tip60 modulates loading of repair proteins and repair of DNA double-strand breaks

Nature Cell Biology

Volumn 8, Issue 1, 2006, Pages 91-99

  Murr, Rabih ^a   Loizou, Joanna I ^a   Yang, Yun Gui ^a   Cuenin, Cyrille ^a   Li, Hai ^a   Wang, Zhao Qi ^a   Herceg, Zdenko ^a  

^a INTERNATIONAL AGENCY FOR RESEARCH ON CANCER   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ATM PROTEIN; CELL PROTEIN; DOUBLE STRANDED DNA; HISTONE; HISTONE ACETYLTRANSFERASE; HISTONE ACETYLTRANSFERASE TIP60; HISTONE H4; PROTEIN TRRAP; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

ACETYLATION; ANIMAL CELL; ARTICLE; CHROMATIN; CONTROLLED STUDY; DNA DAMAGE; DNA PROTEIN COMPLEX; DNA REPAIR; DNA STRAND BREAKAGE; DNA TEMPLATE; EMBRYO; HOMOLOGOUS RECOMBINATION; HUMAN; HUMAN CELL; MOUSE; NONHUMAN; PRIORITY JOURNAL;

ACETYLATION; ADAPTOR PROTEINS, SIGNAL TRANSDUCING; ANIMALS; CELLS, CULTURED; CHROMATIN; CHROMATIN ASSEMBLY AND DISASSEMBLY; DEOXYRIBONUCLEASES, TYPE II SITE-SPECIFIC; DNA DAMAGE; DNA REPAIR; ELECTROPORATION; HELA CELLS; HISTONE ACETYLTRANSFERASES; HISTONES; HUMANS; MALE; MICE; MICE, TRANSGENIC; NUCLEAR PROTEINS; RECOMBINATION, GENETIC; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; RNA, SMALL INTERFERING; TRANSFECTION;

ANIMALIA;

EID: 30344444484     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/ncb1343     Document Type: Article

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