Hormone-dependent, CARM1-directed, arginine-specific methylation of histone H3 on a steroid-regulated promoter

Current Biology

Volumn 11, Issue 24, 2001, Pages 1981-1985

  Ma, Han ^a   Baumann, Christopher T ^b   Li, Hongwei ^a   Strahl, Brian D ^c   Rice, Rene ^e   Jelinek, Mary Anne ^e   Aswad, Dana W ^d   Allis, C David ^c   Hager, Gordon L ^b   Stallcup, Michael R ^a  

^a UNIVERSITY OF SOUTHERN CALIFORNIA   (United States)

^b NATIONAL CANCER INSTITUTE   (United States)

^c UNIVERSITY OF VIRGINIA HEALTH SYSTEM   (United States)

^d UNIVERSITY OF CALIFORNIA   (United States)

^e Upstate Biotechnology   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0035846640     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(01)00600-5     Document Type: Article

References (17)

1. The coregulator exchange in transcriptional functions of nuclear receptors
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3. The language of covalent histone modifications
4. Role of protein methylation in chromatin remodeling and transcriptional regulation
5. Re-SET-ting heterochromatin by histone methyltransferases
6. RNA and protein interactions modulated by protein arginine methylation
7. Methylation of histone H3 by aoactivator-associated arginine methyltransferase 1
8. Methylation of histone H4 at arginine 3 occurs in vivo and is mediated by the nuclear receptor coactivator PRMT1
9. Methylation of histone H4 at arginine 3 facilitates transcriptional activation by nuclear hormone receptor
10. Regulation of transcription by a protein methyltransferase
11. Synergistic, p160 coactivator-dependent enhancement of estrogen receptor function by CARM1 and p300
12. Steroid hormone receptors: Many actors in search of a plot
13. The RXR heterodimers and orphan receptors
14. Transcriptional regulation of mammalian genes in vivo. A tale of two templates
15. The glucocorticoid receptor: Rapid exchange with regulatory sites in living cells
16. Transcriptional state of the mouse mammary tumor virus promoter can affect topological domain size in vivo
17. The glucocorticoid receptor interacting protein 1 (GRIP1) localizes in discrete nuclear foci that associate with ND10 bodies and are enriched in components of the 26S proteasome