Sirt1 physically interacts with Tip60 and negatively regulates Tip60-mediated acetylation of H2AX

Biochemical and Biophysical Research Communications

Volumn 390, Issue 4, 2009, Pages 1355-1360

  Yamagata, Kazutsune ^a   Kitabayashi, Issay ^a  

^a NATIONAL CANCER CENTER RESEARCH INSTITUTE   (Japan)

Author keywords

H2AX; IR induced foci (IRIF); Sirt1; Tip60

Indexed keywords

BRCA1 PROTEIN; HISTONE ACETYLTRANSFERASE; HISTONE H2AX; RAD51 PROTEIN; SIRTUIN 1; TIP60; UNCLASSIFIED DRUG;

ACETYLATION; ARTICLE; DNA DAMAGE; GAMMA IRRADIATION; PRIORITY JOURNAL; PROTEIN DEPLETION; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN INTERACTION; REGULATORY MECHANISM; RNA INTERFERENCE;

ACETYLATION; CELL LINE; DNA DAMAGE; DNA REPAIR; GENE DELETION; HISTONE ACETYLTRANSFERASES; HISTONES; HUMANS; LYSINE; RAD51 RECOMBINASE; SIRTUIN 1;

MAMMALIA;

EID: 70450233493     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.10.156     Document Type: Article

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