F
Fei Sun
Researcher at Chinese Academy of Sciences
Publications - 196
Citations - 7298
Fei Sun is an academic researcher from Chinese Academy of Sciences. The author has contributed to research in topics: Protein structure & Chemistry. The author has an hindex of 35, co-authored 173 publications receiving 5827 citations. Previous affiliations of Fei Sun include Protein Sciences & Center for Excellence in Education.
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Journal ArticleDOI
Secreted Monocytic miR-150 Enhances Targeted Endothelial Cell Migration
Yujing Zhang,Dan-Qing Liu,Xi Chen,Jing Li,Limin Li,Zhen Bian,Fei Sun,Jiuwei Lu,Yuan Yin,Xing Cai,Qi Sun,Kehui Wang,Yi Ba,Qiang Wang,Dongjin Wang,Junwei Yang,Pingsheng Liu,Tao Xu,Qiao Yan,Junfeng Zhang,Ke Zen,Chen-Yu Zhang +21 more
TL;DR: It is reported that secreted miRNAs can serve as signaling molecules mediating intercellular communication and demonstrate that cells can secrete miRNA and deliver them into recipient cells where the exogenous mi RNAs can regulate target gene expression and recipient cell function.
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Inhibition of SARS-CoV-2 (previously 2019-nCoV) infection by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion.
Shuai Xia,Meiqin Liu,Chao Wang,Wei Xu,Qiaoshuai Lan,Siliang Feng,Feifei Qi,Linlin Bao,Lanying Du,Shuwen Liu,Chuan Qin,Fei Sun,Zhengli Shi,Yun Zhu,Shibo Jiang,Shibo Jiang,Lu Lu +16 more
TL;DR: EK1C4 was the most potent fusion inhibitor against SARS-CoV-2 S protein-mediated membrane fusion and pseudovirus infection with IC50s of 1.3 and 15.8 nM, about 241- and 149-fold more potent than the original EK1 peptide, respectively.
Journal ArticleDOI
Crystal Structure of Mitochondrial Respiratory Membrane Protein Complex II
Fei Sun,Xia Huo,Yujia Zhai,Aojin Wang,Jianxing Xu,Dan Su,Mark Bartlam,Mark Bartlam,Zihe Rao,Zihe Rao +9 more
TL;DR: The structure correlates the protein environments around prosthetic groups with their unique midpoint redox potentials and provides a bona fide model for study of the mitochondrial respiratory system and human mitochondrial diseases related to mutations in this complex.
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Insights into SARS-CoV transcription and replication from the structure of the nsp7–nsp8 hexadecamer
TL;DR: The crystal structure of the hexadecameric nsp7–nsp8 supercomplex from the severe acute respiratory syndrome coronavirus is reported at 2.4-Å resolution and has a novel 'golf-club' fold with two conformations, implying that its role is to confer processivity on RNA-dependent RNA polymerase.
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The intra-S phase checkpoint targets Dna2 to prevent stalled replication forks from reversing.
Jiazhi Hu,Lei Sun,Fenfen Shen,Yufei Chen,Yu Hua,Yang Liu,Mian Zhang,Yiren Hu,Qingsong Wang,Wei Xu,Fei Sun,Jianguo Ji,Johanne M. Murray,Antony M. Carr,Daochun Kong +14 more
TL;DR: It is proposed that Dna2 cleavage of regressed nascent strands prevents fork reversal and thus stabilizes stalled forks to maintain genome stability during replication stress.