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Shoudeng Chen
Researcher at Sun Yat-sen University
Publications - 36
Citations - 5821
Shoudeng Chen is an academic researcher from Sun Yat-sen University. The author has contributed to research in topics: Coronavirus & Medicine. The author has an hindex of 15, co-authored 30 publications receiving 3906 citations. Previous affiliations of Shoudeng Chen include Chinese Academy of Sciences & Wuhan University.
Papers
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Journal ArticleDOI
The origin, transmission and clinical therapies on coronavirus disease 2019 (COVID-19) outbreak - an update on the status.
Yan Rong Guo,Qing Dong Cao,Zhong Si Hong,Yuan Yang Tan,Shoudeng Chen,Hong Jun Jin,Kai Sen Tan,De Yun Wang,Yan Yan +8 more
TL;DR: The latest research progress of the epidemiology, pathogenesis, and clinical characteristics of COVID-19 are summarized, and the current treatment and scientific advancements to combat the epidemic novel coronavirus are discussed.
Posted ContentDOI
Evidence for gastrointestinal infection of SARS-CoV-2
Fei Xiao,Meiwen Tang,Xiaobin Zheng,Chunna Li,Jianzhong He,Zhongsi Hong,Siwen Huang,Zhenyi Zhang,Xianqi Lin,Zhaoxiong Fang,Renxu Lai,Shoudeng Chen,Jing Liu,Jin Huang,Jinyu Xia,Zhonghe Li,Guanmin Jiang,Ye Liu,Xiaofeng Li,Hong Shan +19 more
TL;DR: Evidence is provided for gastrointestinal infection of SARS-CoV-2, highlighting its potential fecal-oral transmission route and positive immunofluorescent staining of viral host receptor ACE2 and viral nucleocapsid protein in a case of Sars-Co V-2 infection.
Journal ArticleDOI
Crystal structure of SARS-CoV-2 nucleocapsid protein RNA binding domain reveals potential unique drug targeting sites.
Sisi Kang,Mei Yang,Zhongsi Hong,Liping Zhang,Zhaoxia Huang,Xiaoxue Chen,Suhua He,Ziliang Zhou,Zhechong Zhou,Qiuyue Chen,Yan Yan,Changsheng Zhang,Hong Shan,Shoudeng Chen +13 more
TL;DR: The crystal structure of the N-terminal RNA binding domain of SARS-CoV-2 nucleocapsid protein is determined and several atomic resolution features are provided, guiding the design of novel antiviral agents specific targeting to Sars-Cov-2.
Journal ArticleDOI
Crystal structure of an avian influenza polymerase PA N reveals an endonuclease active site
Puwei Yuan,Mark Bartlam,Zhiyong Lou,Shoudeng Chen,Jie Zhou,Xiaojing He,Zongyang Lv,Ruowen Ge,Xuemei Li,Xuemei Li,Tao Deng,Tao Deng,Ervin Fodor,Zihe Rao,Zihe Rao,Zihe Rao,Yingfang Liu +16 more
TL;DR: Structural comparisons and mutagenesis analysis of the motif identified in PAN provide further evidence that PAN holds an endonuclease active site and has critical roles in end onuclease activity of the influenza virus polymerase, rather than PB1.
Journal ArticleDOI
A unique binding mode enables MCM2 to chaperone histones H3-H4 at replication forks
Hongda Huang,Caroline B Strømme,Giulia Saredi,Martina Hödl,Anne Strandsby,Cristina González-Aguilera,Shoudeng Chen,Anja Groth,Dinshaw J. Patel +8 more
TL;DR: The unique histone-binding mode of MCM2 endows the replicative helicase with ideal properties for recycling histones genome wide during DNA replication and is shown to chaperone both new and old canonical histones H3–H4.