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Xuemei Li

Researcher at Chinese Academy of Sciences

Publications -  100
Citations -  4499

Xuemei Li is an academic researcher from Chinese Academy of Sciences. The author has contributed to research in topics: Biology & Gene. The author has an hindex of 33, co-authored 85 publications receiving 3855 citations. Previous affiliations of Xuemei Li include Center for Excellence in Education & Tsinghua University.

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Crystal structure of an avian influenza polymerase PA N reveals an endonuclease active site

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.
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Structural Basis for the Recognition of Blood Group Trisaccharides by Norovirus

TL;DR: To determine the precise locations and receptor binding modes of HBGA carbohydrates on the viral capsids, a recombinant P protein of a GII-4 strain norovirus was cocrystallized with synthetic type A or B trisaccharides and demonstrated that the receptor binding site lies at the outermost end of the P domain and forms an extensive hydrogen-bonding network with the saccharide ligand.
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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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Crystal structure of the polymerase PA C –PB1 N complex from an avian influenza H5N1 virus

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.
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Hepatitis A virus and the origins of picornaviruses

TL;DR: High-resolution X-ray structures for the mature virus and the empty particle are reported, finding that HAV contains no pocket factor and can withstand remarkably high temperature and low pH, and empty particles are even more robust than full particles.