The histone variant macroH2A1.1 is recruited to DSBs through a mechanism involving PARP1

FEBS Letters

Volumn 586, Issue 21, 2012, Pages 3920-3925

  Xu, Chang ^a,b   Xu, Ye ^b   Gursoy Yuzugullu, Ozge ^b   Price, Brendan D ^b  

^a INSTITUTE OF RADIATION MEDICINE   (China)

^b HARVARD MEDICAL SCHOOL   (United States)

Author keywords

53BP1; DNA repair; Ionizing radiation; MacroH2A1; Nucleosome

Indexed keywords

53BP1 PROTEIN; CHECKPOINT KINASE 2; HISTONE H2A; HISTONE H2A1.1; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 1; NUCLEIC ACID BINDING PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CHROMATIN STRUCTURE; CONTROLLED STUDY; DNA END JOINING REPAIR; DNA REPAIR; DOUBLE STRANDED DNA BREAK; ENZYME ACTIVITY; NUCLEOSOME; PRIORITY JOURNAL; RADIOSENSITIVITY;

CELL LINE, TUMOR; CHROMATIN; CHROMATIN ASSEMBLY AND DISASSEMBLY; DNA BREAKS, DOUBLE-STRANDED; DNA REPAIR; HISTONES; HUMANS; INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS; NUCLEOSOMES; PLASMIDS; POLY(ADP-RIBOSE) POLYMERASES; PROTEIN TRANSPORT; PROTEIN-SERINE-THREONINE KINASES; RADIATION TOLERANCE; RADIATION, IONIZING; SIGNAL TRANSDUCTION; TRANSFECTION;

EID: 84868093509     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2012.09.030     Document Type: Article

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