有哪些信誉好的足球投注网站crystal structure of tdrd3 and methyl-arginine binding characterization of tdrd3, smn and spf30晶体结构tdrd3 tdrd3和methyl-arginine绑定描述,smn spf30.pdfVIP
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crystal structure of tdrd3 and methyl-arginine binding characterization of tdrd3, smn and spf30晶体结构tdrd3 tdrd3和methyl-arginine绑定描述,smn spf30
Crystal Structure of TDRD3 and Methyl-Arginine Binding Characterization of TDRD3, SMN and SPF30 1,2. 2. 3. 2 2 2 Ke Liu , Yahong Guo , Haiping Liu , Chuanbing Bian , Robert Lam , Yongsong Liu , Farrell 2 4 4 5 3 1,2,6 Mackenzie , Luis Alejandro Rojas , Danny Reinberg , Mark T. Bedford , Rui-Ming Xu *, Jinrong Min * 1 Hubei Key Laboratory of Genetic Regulation and Integrative Biology, College of Life Science, Huazhong Normal University, Wuhan, People’s Republic of China, 2 Structural Genomics Consortium, University of Toronto, Toronto, Ontario, Canada, 3 National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, People’s Republic of China, 4 Howard Hughes Medical Institute, Department of Biochemistry, New York University School of Medicine, New York, New York, United States of America, 5 The University of Texas MD Anderson Cancer Center, Science Park-Research Division, Smithville, Texas, United States of America, 6 Department of Physiology, University of Toronto, Toronto, Ontario, Canada Abstract SMN (Survival motor neuron protein) was characterized as a dimethyl-arginine binding protein over ten years ago. TDRD3 (Tudor domain-containing protein 3) and SPF30 (Splicing factor 30 kDa) were found to bind to various methyl-arginine proteins including Sm proteins as well later on. Recently, TDRD3 was shown to be a transcriptional coactivator, and its transcriptional activity is dependent on its ability to bind arg
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