Zobrazeno 1 - 10
of 28
pro vyhledávání: '"Zhongyu Zou"'
Publikováno v:
Fundamental Research, Vol 3, Iss 5, Pp 760-762 (2023)
Genetic information flows from DNA to protein through RNA in the central dogma. Different RNA species are known to accomplish essential tasks of protein encoding (mRNAs), amino acid loading (tRNAs), and translation machinery assembly (rRNAs). However
Externí odkaz:
https://doaj.org/article/37adfe9801ea437eb56510be15b4aa92
Publikováno v:
Genome Biology, Vol 24, Iss 1, Pp 1-13 (2023)
Abstract The YTH N 6 -methyladenosine RNA binding proteins (YTHDFs) mediate the functional effects of N 6 -methyladenosine (m6A) on RNA. Recently, a report proposed that all YTHDFs work redundantly to facilitate RNA decay, raising questions about the
Externí odkaz:
https://doaj.org/article/490fa0bda2f6410d87d99b5a1f72bc47
Autor:
Runping Fang, Xin Chen, Sicong Zhang, Hui Shi, Youqiong Ye, Hailing Shi, Zhongyu Zou, Peng Li, Qing Guo, Li Ma, Chuan He, Suyun Huang
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-17 (2021)
EGFR is frequently constitutively active in glioblastoma (GBM). Here, the authors show that EGFR induces YTHDF2 protein stabilization, which reduces cholesterol homeostasis through an RNA m6A methylation dependent molecular mechanism to promote GBM t
Externí odkaz:
https://doaj.org/article/dbb72d0750a2491f8e7c06b1a87b4c5f
Publikováno v:
PLoS Biology, Vol 18, Iss 4, p e3000664 (2020)
The N6-methyladenosine (m6A) modification regulates mRNA stability and translation. Here, we show that transcriptomic m6A modification can be dynamic and the m6A reader protein YTH N6-methyladenosine RNA binding protein 2 (YTHDF2) promotes mRNA decay
Externí odkaz:
https://doaj.org/article/82ccdd9581b547038ec0d6319bdc2eb1
Autor:
P. Cody He, Jiangbo Wei, Xiaoyang Dou, Bryan T. Harada, Zijie Zhang, Ruiqi Ge, Chang Liu, Li-Sheng Zhang, Xianbin Yu, Shuai Wang, Ruitu Lyu, Zhongyu Zou, Mengjie Chen, Chuan He
Publikováno v:
Science. 379:677-682
N 6 -methyladenosine (m 6 A) is the most abundant messenger RNA (mRNA) modification and plays crucial roles in diverse physiological processes. Using a massively parallel assay for m 6 A (MPm 6 A), we discover that m 6 A specificity is globally regul
Autor:
Yuexiu, Zhang, Li-Sheng, Zhang, Qing, Dai, Phylip, Chen, Mijia, Lu, Elizabeth L, Kairis, Valarmathy, Murugaiah, Jiayu, Xu, Rajni Kant, Shukla, Xueya, Liang, Zhongyu, Zou, Estelle, Cormet-Boyaka, Jianming, Qiu, Mark E, Peeples, Amit, Sharma, Chuan, He, Jianrong, Li
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 119(42)
5-methylcytosine (m
Autor:
Jiangbo Wei, Xianbin Yu, Lei Yang, Xuelian Liu, Boyang Gao, Boxian Huang, Xiaoyang Dou, Jun Liu, Zhongyu Zou, Xiao-Long Cui, Li-Sheng Zhang, Xingsen Zhao, Qinzhe Liu, P. Cody He, Caraline Sepich-Poore, Nicole Zhong, Wenqiang Liu, Yanhe Li, Xiaochen Kou, Yanhong Zhao, You Wu, Xuejun Cheng, Chuan Chen, Yiming An, Xueyang Dong, Huanyu Wang, Qiang Shu, Ziyang Hao, Tao Duan, Yu-Ying He, Xuekun Li, Shaorong Gao, Yawei Gao, Chuan He
Publikováno v:
Science
N 6 -methyladenosine (m 6 A) is the most abundant internal modification on mammalian messenger RNA. It is installed by a writer complex and can be reversed by erasers such as the fat mass and obesity-associated protein FTO. Despite extensive research
Publikováno v:
Fundamental Research.
Autor:
Zhongyu Zou, Chuan He
Publikováno v:
Molecular Cell. 83:1022-1023
Autor:
Zhongyu Zou, Jiangbo Wei, Yantao Chen, Yunhee Kang, Hailing Shi, Fan Yang, Shijie Chen, Ying Zhou, Caraline Sepich-Poore, Xiaoxi Zhuang, Xiaoming Zhou, Hualiang Jiang, Zhexing Wen, Peng Jin, Cheng Luo, Chuan He
Translation activation of local synaptic mRNAs is critical to learning and memory1-3. Despite extensive studies on how phosphorylation of ribosomal proteins and translation factors enables timely response to exogenous stimuli4,our knowledge on molecu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dab506fa34c76d28887a325a6b9255e8
https://doi.org/10.1101/2022.11.29.518448
https://doi.org/10.1101/2022.11.29.518448