期刊文献+
共找到1篇文章
< 1 >
每页显示 20 50 100
The ubiquitin ligase E6AP facilitates HDAC6-mediated deacetylation and degradation of tumor suppressors 被引量:1
1
作者 Yanan Zhang Zhida Chen +7 位作者 Jing lin Jie Liu yahong lin Huayue Li Yongyi Xi Bo Wei Lihua Ding Qinong Ye 《Signal Transduction and Targeted Therapy》 SCIE CSCD 2020年第1期414-417,共4页
Dear Editor,Protein acetylation status can regulate protein stability via the ubiquitin-proteasome pathway,which plays a critical role in the regulation of various cellular functions and becomes a target for cancer th... Dear Editor,Protein acetylation status can regulate protein stability via the ubiquitin-proteasome pathway,which plays a critical role in the regulation of various cellular functions and becomes a target for cancer therapy.1,2 Histone deacetylase 6(HDAC6)belongs to the class II of the histone deacetylase/acuc/apha family and regulates cancer cell proliferation,invasion,and metastasis.3 Combination of HDAC6 inhibitors(HDAC6i)with proteasome inhibitors(PI)shows synergistic anticancer activity.4 Although many studies reveal how acetyltransferases/deacetylases regulate protein acetylation and subsequent protein ubiquitination and degradation,whether an E3 ubiquitin ligase regulates protein acetylation remains largely unknown.In addition,the mechanisms undelying synergistic anticancer activity of HDAC6i and PI remain poorly understood. 展开更多
关键词 HDAC6 UBIQUITIN INVASION
原文传递
上一页 1 下一页 到第
使用帮助 返回顶部