Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Bing-lan Xie"'
Autor:
Wen-juan Li, Ying Huang, Yi-an Lin, Bao-ding Zhang, Mei-Yan Li, Yi-qin Zou, Guo-sheng Hu, Yao-hui He, Jing-jing Yang, Bing-lan Xie, Hai-hua Huang, Xianming Deng, Wen Liu
Publikováno v:
Cell Reports, Vol 42, Iss 11, Pp 113385- (2023)
Summary: PRMT1 plays a vital role in breast tumorigenesis; however, the underlying molecular mechanisms remain incompletely understood. Herein, we show that PRMT1 plays a critical role in RNA alternative splicing, with a preference for exon inclusion
Externí odkaz:
https://doaj.org/article/ade4efd1b9394bd298d24afc3ff21873
Autor:
Wen-juan Li, Yao-hui He, Jing-jing Yang, Guo-sheng Hu, Yi-an Lin, Ting Ran, Bing-ling Peng, Bing-lan Xie, Ming-feng Huang, Xiang Gao, Hai-hua Huang, Helen He Zhu, Feng Ye, Wen Liu
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-20 (2021)
Arginine methyltransferases (PRMTs) are involved in the regulation of various physiological and pathological conditions. Using proteomics, the authors here profile the methylation substrates of PRMTs 4, 5 and 7 and characterize the roles of these enz
Externí odkaz:
https://doaj.org/article/8e1165b1d3b04a91a453caaef784fec5
Autor:
Ting Ran, Rong-quan Xiao, Wen Liu, Wen-Juan Li, Hai-feng Shen, Xiang Gao, Zi-Rui Wang, Bing-Lan Xie, Jiancheng Ding, Tian-yi Ye, Yaohui He, Bing-ling Peng, Weiwei Gao
Publikováno v:
Theranostics
While protein arginine methyltransferases (PRMTs) and PRMT-catalyzed protein methylation have been well-known to be involved in a myriad of biological processes, their functions and the underlying molecular mechanisms in cancers, particularly in estr
Publikováno v:
Journal of Chemical Information and Modeling. 59:522-534
CARM1 (coactivator-associated arginine methyltransferase 1), also known as PRMT4 (protein arginine N-methyltransferase 4), belongs to the protein arginine methyltransferase (PRMT) family, which has emerged as a potential anticancer drug target. To di
Autor:
Helen He Zhu, Feng Ye, Ming-feng Huang, Yaohui He, Hai-hua Huang, Bing-Lan Xie, Jing-Jing Yang, Wen-Juan Li, Yi-An Lin, Bing-ling Peng, Ting Ran, Wen Liu, Guo-sheng Hu, Xiang Gao
Publikováno v:
Nature Communications
Nature Communications, Vol 12, Iss 1, Pp 1-20 (2021)
Nature Communications, Vol 12, Iss 1, Pp 1-20 (2021)
Numerous substrates have been identified for Type I and II arginine methyltransferases (PRMTs). However, the full substrate spectrum of the only type III PRMT, PRMT7, and its connection to type I and II PRMT substrates remains unknown. Here, we use m