Structure and mechanism of action of the histone acetyltransferase Gcn5 and similarity to other N-acetyltransferases.
Sternglanz
R
R
Department of Biochemistry and Cell Biology, State University of New York, Stony Brook, NY 11794, USA. rolf@life.bio.sunysb.edu
Schindelin
H
H
D000123:Acetyltransferases / Q000737:chemistry* / Q000378:metabolism; D000818:Animals; D017124:Conserved Sequence; D004268:DNA-Binding Proteins; D005656:Fungal Proteins / Q000737:chemistry* / Q000378:metabolism; D051548:Histone Acetyltransferases; D011487:Protein Conformation; D011494:Protein Kinases / Q000737:chemistry* / Q000378:metabolism; D017433:Protein Structure, Secondary; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins; D000099224:p300-CBP-Associated Factor
D000123:Acetyltransferases; D004268:DNA-Binding Proteins; D005656:Fungal Proteins; D051548:Histone Acetyltransferases; D011494:Protein Kinases; D029701:Saccharomyces cerevisiae Proteins; C501392:GCN5 protein, S cerevisiae; D000099224:p300-CBP-Associated Factor