Methylation of histone H4 at arginine 3 facilitating transcriptional activation by nuclear hormone receptor.

Wang, H; Huang, Z Q; Xia, L; Feng, Q; Erdjument-Bromage, H; Strahl, B D; Briggs, S D; Allis, C D; Wong, J; Tempst, P; Zhang, Y

Wang, H; Huang, Z Q; Xia, L; Feng, Q; Erdjument-Bromage, H; Strahl, B D; Briggs, S D; Allis, C D; Wong, J; Tempst, P; Zhang, Y.

Affiliation

Wang H; Department of Biochemistry and Biophysics, Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-7295, USA.

Science ; 293(5531): 853-7, 2001 Aug 03.

Article in En | MEDLINE | ID: mdl-11387442

Subject(s)

Arginine/metabolism; Histones/metabolism; Methyltransferases/metabolism; Receptors, Androgen/metabolism; Transcriptional Activation; Acetylation; Amino Acid Sequence; Animals; Binding Sites; Cell Nucleus/metabolism; HeLa Cells; Histones/chemistry; Humans; Hydroxamic Acids/pharmacology; Intracellular Signaling Peptides and Proteins; Lysine/metabolism; Methylation; Methyltransferases/chemistry; Methyltransferases/genetics; Methyltransferases/isolation & purification; Molecular Sequence Data; Mutation; Oocytes; Protein-Arginine N-Methyltransferases; Recombinant Proteins/metabolism; S-Adenosylmethionine/metabolism; Xenopus

Search on Google

XML

PubMed Links

Collection: 01-internacional Database: MEDLINE Main subject: Arginine / Histones / Receptors, Androgen / Transcriptional Activation / Methyltransferases Type of study: Prognostic_studies Limits: Animals / Humans Language: En Journal: Science Year: 2001 Type: Article Affiliation country: United States

Search on Google

XML

PubMed Links