P
Peilong Lu
Researcher at University of Washington
Publications - 23
Citations - 2185
Peilong Lu is an academic researcher from University of Washington. The author has contributed to research in topics: Transmembrane protein & Membrane protein. The author has an hindex of 14, co-authored 18 publications receiving 1741 citations. Previous affiliations of Peilong Lu include Protein Sciences & Tsinghua University.
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Journal ArticleDOI
An atomic structure of human γ-secretase
Xiao Chen Bai,Chuangye Yan,Guanghui Yang,Peilong Lu,Dan Ma,Linfeng Sun,Rui Zhou,Sjors H.W. Scheres,Yigong Shi +8 more
TL;DR: The atomic structure of human γ-secretase at 3.4 Å resolution is reported, determined by single-particle cryo-electron microscopy, serving as a molecular basis for mechanistic understanding ofγ- secretase function.
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Three-dimensional structure of human γ-secretase
Peilong Lu,Xiao Chen Bai,Dan Ma,Tian Xie,Chuangye Yan,Linfeng Sun,Guanghui Yang,Yanyu Zhao,Rui Zhou,Sjors H.W. Scheres,Yigong Shi +10 more
TL;DR: The three-dimensional structure of an intact human γ-secretase complex at 4.5 Å resolution is reported, determined by cryo-electron-microscopy single-particle analysis, and nicastrin ECD is structurally similar to a large family of peptidases exemplified by the glutamate carboxypeptidase PSMA.
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Structure and mechanism of a glutamate–GABA antiporter
TL;DR: Structural and biochemical analyses reveal the essential transport residues, identify the transport path and suggest a conserved transport mechanism involving the rigid-body rotation of a helical bundle for GadC and other amino acid antiporters.
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L-glutamine provides acid resistance for Escherichia coli through enzymatic release of ammonia
TL;DR: It is shown that YbaS and the amino acid antiporter GadC, which exchanges extracellular Gln with intracellular Glu, together constitute an acid resistance system that is sufficient for E. coli survival under extremely acidic environment.
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Crystal structure and biochemical analyses reveal Beclin 1 as a novel membrane binding protein
Weijiao Huang,Wooyoung Choi,Wanqiu Hu,Na Mi,Qiang Guo,Meisheng Ma,Mei Liu,Yuan Tian,Peilong Lu,Feng-Liang Wang,Haiteng Deng,Lei Liu,Ning Gao,Li Yu,Yigong Shi +14 more
TL;DR: The crystal structure of the evolutionarily conserved domain (ECD) of Beclin 1 at 1.6 Å resolution is reported, which exhibits a previously unreported fold and defines a novel class of membrane-binding domain, with a strong preference for lipid membrane enriched with cardiolipin.