| Literature DB >> 26457839 |
Tianlu Wang, Tingting Hong, Yue Huang1, Haomiao Su, Fan Wu, Yi Chen, Lai Wei, Wei Huang, Xiaoluan Hua, Yu Xia, Jinglei Xu, Jianhua Gan2, Bifeng Yuan, Yuqi Feng, Xiaolian Zhang, Cai-Guang Yang1, Xiang Zhou.
Abstract
The FTO protein is unequivocally reported to play a critical role in human obesity and in the regulation of cellular levels of m(6)A modification, which makes FTO a significant and worthy subject of study. Here, we identified that fluorescein derivatives can selectively inhibit FTO demethylation, and the mechanisms behind these activities were elucidated after we determined the X-ray crystal structures of FTO/fluorescein and FTO/5-aminofluorescein. Furthermore, these inhibitors can also be applied to the direct labeling and enrichment of FTO protein combined with photoaffinity labeling assay.Entities:
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Year: 2015 PMID： 26457839 DOI： 10.1021/jacs.5b06690
Source DB: PubMed Journal: J Am Chem Soc ISSN： 0002-7863 Impact factor: 15.419