共查询到20条相似文献,搜索用时 15 毫秒
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Wei LN Hu X Chandra D Seto E Farooqui M 《The Journal of biological chemistry》2000,275(52):40782-40787
Receptor-interacting protein 140 (RIP140) encodes a histone deacetylase (HDAC) inhibitor-sensitive repressive activity. Direct interaction of RIP140 with HDAC1 and HDAC3 occurs in vitro and in vivo as demonstrated in co-immunoprecipitation and glutathione S-transferase pull-down experiments. The HDAC-interacting domain of RIP140 is mapped to its N-terminal domain, between amino acids 78 and 303 based upon glutathione S-transferase pull-down experiments. In chromatin immunoprecipitation assays, it is demonstrated that histone deacetylation occurs at the chromatin region of the Gal4 binding sites as a result of Gal4 DNA binding domain-tethered RIP expression. The immunocomplexes of RIP140 from cells transfected with RIP140 and HDAC are able to deacetylate histone proteins in vitro. This study presents the first evidence for RIP140 as a negative coregulator for nuclear receptor actions by directly recruiting histone deacetylases and categorizes RIP140 as a novel negative coregulator that is able to directly interact with HDACs. 相似文献
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Calderon MR Verway M An BS DiFeo A Bismar TA Ann DK Martignetti JA Shalom-Barak T White JH 《The Journal of biological chemistry》2012,287(12):8662-8674
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A dynamic role for HDAC7 in MEF2-mediated muscle differentiation 总被引:14,自引:0,他引:14
Dressel U Bailey PJ Wang SC Downes M Evans RM Muscat GE 《The Journal of biological chemistry》2001,276(20):17007-17013
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Functional domains of histone deacetylase-3. 总被引:9,自引:0,他引:9
Wen-Ming Yang Shih-Chang Tsai Yu-Der Wen Gyorgy Fejer Edward Seto 《The Journal of biological chemistry》2002,277(11):9447-9454
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