期刊
ACS CHEMICAL BIOLOGY
卷 11, 期 3, 页码 632-642出版社
AMER CHEMICAL SOC
DOI: 10.1021/acschembio.5b00841
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资金
- NCI NIH HHS [P30 CA010815] Funding Source: Medline
- NIA NIH HHS [P01 AG031862] Funding Source: Medline
- NIGMS NIH HHS [T32 GM008275, R35 GM118090, R01 GM060293] Funding Source: Medline
Acetylation is a post-translational modification (PTM) that regulates chromatin dynamics and function. Dysregulation of acetylation or acetyltransferase activity has been correlated with several human diseases. Many, if not all, histone acetyltransferases (HATs) are regulated in part through tethered domains, association with binding partners, or post-translational modification, including predominantly acetylation. This review focuses on what is currently understood at the molecular level of HAT regulation as it occurs via binding partners, associated domains, and autoacetylation.
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