The target of the NSD family of histone lysine methyltransferases depends on the nature of the substrate

Journal of Biological Chemistry

Volumn 284, Issue 49, 2009, Pages 34283-34295

  Li, Yan ^a   Trojer, Patrick ^a,d   Xu, Chong Feng ^a   Cheung, Peggie ^b   Kuo, Alex ^b   Drury III, William J ^a   Qiao, Qi ^c   Neubert, Thomas A ^a   Xu, Rui Ming ^a,c   Gozani, Or ^b   Reinberg, Danny ^a,e  

^a NEW YORK UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b STANFORD UNIVERSITY   (United States)

^c INSTITUTE OF BIOPHYSICS   (China)

^d Department of Structural Biology   (United States)

^e NONE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALLOSTERIC EFFECTORS; DOUBLE STRANDED DNA; HISTONE H3; HISTONE H4; HUMAN CELLS; HUMAN DISEASE; METHYLTRANSFERASES; NUCLEAR RECEPTORS; NUCLEOSOMES; OCTAMERS;

AMINO ACIDS; DNA; ENZYMES; GENES; NUCLEIC ACIDS; PROTEINS; TARGETS;

SUBSTRATES;

CELL NUCLEUS RECEPTOR; DOUBLE STRANDED DNA; HISTONE LYSINE METHYLTRANSFERASE; SINGLE STRANDED DNA;

ARTICLE; ENZYME SPECIFICITY; METHYLATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN TARGETING;

ANIMALS; CELL LINE, TUMOR; CHROMATIN; DNA; GENETIC VECTORS; HISTONE-LYSINE N-METHYLTRANSFERASE; HISTONES; HUMANS; LYSINE; MASS SPECTROMETRY; NUCLEOSOMES; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; XENOPUS LAEVIS;

EID: 71749121455     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.034462     Document Type: Article

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