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Proceedings of the National Academy of Sciences of the United States of America

Volumn 104, Issue 1, 2007, Pages 60-65

N-formylation of lysine in histone proteins as a secondary modification arising from oxidative DNA damage

(5) Jiang, Tao a,b Zhou, Xinfeng a,c Taghizadeh, Koli a Dong, Min a,d Dedon, Peter C a

a Massachusetts Institute of Technology Cambridge (United States)

b TUFTS UNIVERSITY SCHOOL OF MEDICINE (United States)

c Federal Service for Surveillance on Consumer Rights Protection and Human Well Being (United States)

d NOVARTIS PHARMA AG (Switzerland)

Author keywords

Enediyne; Histone acetylation; Oxidative stress

Indexed keywords

DEOXYRIBOSE; DNA; HISTONE; HISTONE H1; LYSINE; NUCLEAR PROTEIN; ZINOSTATIN;

ACETYLATION; ARTICLE; CHROMATIN; DNA DAMAGE; EPIGENETICS; GENE EXPRESSION; HUMAN; HUMAN CELL; ISOTOPE LABELING; LIQUID CHROMATOGRAPHY; MAMMAL CELL; METHYLATION; NITROSATIVE STRESS; OXIDATION; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN MODIFICATION; PROTEIN PROCESSING; SIGNAL TRANSDUCTION; TANDEM MASS SPECTROMETRY;

ACETYLATION; CELLS, CULTURED; CHROMATOGRAPHY, LIQUID; DEOXYRIBOSE; DNA DAMAGE; HISTONES; HUMANS; LYSINE; OXIDATION-REDUCTION; TANDEM MASS SPECTROMETRY;

MAMMALIA;

EID: 33846113751 PISSN: 00278424 EISSN: None Source Type: Journal
DOI: 10.1073/pnas.0606775103 Document Type: Article

Times cited : (166)

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