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Yingfang Liu
Researcher at Sun Yat-sen University
Publications - 56
Citations - 2907
Yingfang Liu is an academic researcher from Sun Yat-sen University. The author has contributed to research in topics: Protein structure & Polymerase. The author has an hindex of 22, co-authored 49 publications receiving 2569 citations. Previous affiliations of Yingfang Liu include University of Colorado Hospital & Chinese Academy of Sciences.
Papers
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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
Rational design of true monomeric and bright photoactivatable fluorescent proteins
Mingshu Zhang,Hao Chang,Hao Chang,Yongdeng Zhang,Yongdeng Zhang,Junwei Yu,Junwei Yu,Lijie Wu,Wei Ji,Juanjuan Chen,Bei Liu,Bei Liu,Jingze Lu,Yingfang Liu,Jun-Long Zhang,Pingyong Xu,Tao Xu,Tao Xu +17 more
TL;DR: It is shown that mEos2 forms oligomers at high concentrations and forms aggregates when labeling membrane proteins, limiting its application as a fusion partner.
Journal ArticleDOI
Crystal structure of the polymerase PA C –PB1 N complex from an avian influenza H5N1 virus
Xiaojing He,Jie Zhou,Mark Bartlam,Rongguang Zhang,Jianyuan Ma,Zhiyong Lou,Xuemei Li,Xuemei Li,Jingjing Li,Andrzej Joachimiak,Zonghao Zeng,Ruowen Ge,Zihe Rao,Zihe Rao,Zihe Rao,Yingfang Liu +15 more
TL;DR: The structure provides details for the binding of PB1N to PAC at the atomic level, demonstrating a potential target for novel anti-influenza therapeutics and proposing a model for the influenza RdRp heterotrimer.
Journal ArticleDOI
Crystal structure of sTALL-1 reveals a virus-like assembly of tnf family ligands
TL;DR: The mutant sTALL-1 still bound its receptor but could not activate NF-kappaB and did not stimulate B lymphocyte proliferation, and it is proposed that this virus-like assembly of sTall-1 is the functional unit for TALL- 1 in vivo.
Journal ArticleDOI
Ligand-receptor binding revealed by the TNF family member TALL-1.
Yingfang Liu,Xia Hong,John W. Kappler,John W. Kappler,Ling Jiang,Rongguang Zhang,Liang-Guo Xu,Cheol-Ho Pan,Wesley E. Martin,Robert C. Murphy,Hong-Bing Shu,Shaodong Dai,Gongyi Zhang,Gongyi Zhang +13 more
TL;DR: In this paper, the crystal structures of sTALL-1 complexed with the extracellular domains of BCMA and BAFF-R were determined at 2.6 and 2.5 A, respectively.