H
Huimin Yan
Researcher at Wuhan University
Publications - 6
Citations - 361
Huimin Yan is an academic researcher from Wuhan University. The author has contributed to research in topics: Coronavirus & Virus. The author has an hindex of 6, co-authored 6 publications receiving 336 citations. Previous affiliations of Huimin Yan include Case Western Reserve University.
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Journal ArticleDOI
SARS coronavirus induces apoptosis in Vero E6 cells.
Huimin Yan,Gengfu Xiao,Jiamin Zhang,Yuanyang Hu,Fang Yuan,David K. Cole,Congyi Zheng,George F. Gao +7 more
TL;DR: Results do show that the CPE was induced by apoptosis rather than necrosis, shown by typical DNA fragmentation, through the existence of apoptotic bodies and swollen mitochondria, which has some implications for the SARS‐CoV pathogenicity.
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Following the rule: formation of the 6-helix bundle of the fusion core from severe acute respiratory syndrome coronavirus spike protein and identification of potent peptide inhibitors.
Jieqing Zhu,Gengfu Xiao,Yanhui Xu,Fang Yuan,Congyi Zheng,Yueyong Liu,Huimin Yan,David K. Cole,John I. Bell,Zihe Rao,Po Tien,Po Tien,George F. Gao,George F. Gao +13 more
TL;DR: It is reported that by using in vitro bio-engineering techniques, SARS-CoV HR1 and HR2 bind to each other and form a typical 6-helix bundle and lays the ground for identification of virus fusion/entry inhibitors for this devastating emerging virus.
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Test for Detection of Disease-Associated Prion Aggregate in the Blood of Infected but Asymptomatic Animals
Binggong Chang,Xin Cheng,Shaoman Yin,Tao Pan,Hongtao Zhang,Poki Wong,Shin Chung Kang,Fan Xiao,Huimin Yan,Huimin Yan,Chaoyang Li,Lisa L. Wolfe,Michael W. Miller,Thomas Wisniewski,Mark I. Greene,Man Sun Sy +15 more
TL;DR: The new assay, named aggregation-specific FACTT (AS-FACTT), is much more sensitive than AS-ELISA and could detect prion aggregates in the brain of mice as early as 7 days after an intraperitoneal inoculation of PrPSc, and also detects prions in blood of mule deer infected with the agent causing a naturally occurring prion disease, chronic wasting disease.
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Prion proteins with insertion mutations have altered N-terminal conformation and increased ligand binding activity and are more susceptible to oxidative attack.
Shaoman Yin,Shuiliang Yu,Chaoyang Li,Poki Wong,Binggong Chang,Fan Xiao,Shin Chung Kang,Huimin Yan,Huimin Yan,Gengfu Xiao,Jacques Grassi,Po Tien,Po Tien,Man Sun Sy +13 more
TL;DR: In insertion mutants appear to share common features, and the degree of abnormality is proportional to the number of insertions, which may contribute to the pathogenesis of inherited human prion disease.
Journal ArticleDOI
Isolation of virus from a SARS patient and genome-wide analysis of genetic mutations related to pathogenesis and epidemiology from 47 SARS-CoV isolates.
Ying Zhu,Mo Liu,Weiguang Zhao,Jianlin Zhang,Xue Zhang,Ke Wang,Chunfang Gu,Kailang Wu,Yan Li,Congyi Zheng,Gengfu Xiao,Huimin Yan,Jiamin Zhang,Deyin Guo,Po Tien,Jianguo Wu +15 more
TL;DR: A SARS-CoV in China is isolated and its genome sequences are analyzed with the aims to reveal the evolution trends of the virus and provide insights into understanding pathogenesis and SARS epidemic.