共 99 条
Histone lysine methylation: a signature for chromatin function
被引:526
作者:

Sims, RJ
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机构: Univ Med & Dent New Jersey, Robert Wood Johnson Med Sch, Howard Hughes Med Inst, Div Nucle Acids Enzymol,Dept Biochem, Piscataway, NJ 08854 USA

Nishioka, K
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机构: Univ Med & Dent New Jersey, Robert Wood Johnson Med Sch, Howard Hughes Med Inst, Div Nucle Acids Enzymol,Dept Biochem, Piscataway, NJ 08854 USA

Reinberg, D
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机构:
Univ Med & Dent New Jersey, Robert Wood Johnson Med Sch, Howard Hughes Med Inst, Div Nucle Acids Enzymol,Dept Biochem, Piscataway, NJ 08854 USA Univ Med & Dent New Jersey, Robert Wood Johnson Med Sch, Howard Hughes Med Inst, Div Nucle Acids Enzymol,Dept Biochem, Piscataway, NJ 08854 USA
机构:
[1] Univ Med & Dent New Jersey, Robert Wood Johnson Med Sch, Howard Hughes Med Inst, Div Nucle Acids Enzymol,Dept Biochem, Piscataway, NJ 08854 USA
[2] Natl Inst Genet, Dept Dev Genet, Mishima, Shizuoka 4118540, Japan
关键词:
D O I:
10.1016/j.tig.2003.09.007
中图分类号:
Q3 [遗传学];
学科分类号:
071007 ;
090102 ;
摘要:
The rapid progress in deciphering the processes of covalent histone modifications has broadened our understanding of transcriptional regulation. Histone lysine methylation, along with DNA methylation, establishes the framework for long-term epigenetic maintenance. Recent studies of the mechanisms of specific histone lysine methylation have revealed a complex process that controls aspects of short- and long-term transcriptional regulation, in addition to the propagation of bulk chromosome structure and stability. In this article, we review the functional properties of histone lysine methylation and the enzymes that catalyze this covalent modification.
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页码:629 / 639
页数:11
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