期刊
NUCLEIC ACIDS RESEARCH
卷 34, 期 9, 页码 2653-2662出版社
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkl338
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资金
- NIGMS NIH HHS [R01 GM62970, R01 GM062970] Funding Source: Medline
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM062970] Funding Source: NIH RePORTER
Histone post-translational modifications occur, not only in the N-terminal tail domains, but also in the core domains. While modifications in the N-terminal tail function largely through the regulation of the binding of non-histone proteins to chromatin, based on their location in the nucleosome, core domain modifications may also function through distinct mechanisms involving structural alterations to the nucleosome. This article reviews the recent developments in regards to these novel histone modifications and discusses their important role in the regulation of chromatin structure.
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