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Pengqi Xu

Researcher at VU University Amsterdam

Publications -  27
Citations -  1794

Pengqi Xu is an academic researcher from VU University Amsterdam. The author has contributed to research in topics: Photosystem II & Quenching (fluorescence). The author has an hindex of 13, co-authored 24 publications receiving 1007 citations. Previous affiliations of Pengqi Xu include Sun Yat-sen University & Francis Crick Institute.

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Receptor binding and priming of the spike protein of SARS-CoV-2 for membrane fusion.

TL;DR: Cryo-electron microscopy structures of consecutive binding events of ACE2 in complex with the spikeprotein of SARS-CoV-2 reveal the mechanisms of receptor binding by the spike protein and activation for membrane fusion by the Spike protein of Sars-Co V-2.
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SARS-CoV-2 and bat RaTG13 spike glycoprotein structures inform on virus evolution and furin-cleavage effects.

TL;DR: Cryo-EM and functional analyses of furin-cleaved spike from SARS-CoV-2 and the closely related spike from bat virus RaTG13 reveal differences in protein stability and binding to human receptor ACE2.
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The effect of the D614G substitution on the structure of the spike glycoprotein of SARS-CoV-2.

TL;DR: In this paper, the authors used cryo-electron microscopy to compare G614 and D614 spikes and showed that the G614 mutant spike adopts a range of more open conformations that may facilitate binding to the SARS-CoV-2 receptor, ACE2, and subsequent structural rearrangements required for viral membrane fusion.
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Molecular insights into Zeaxanthin-dependent quenching in higher plants

TL;DR: Zeaxanthin is acting in between the complexes, helping to create/participating in a variety of quenching sites, which can explain why none of the antennas appears to be essential for NPQ and the multiple quench mechanisms that have been observed in plants.
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Single-Molecule Identification of Quenched and Unquenched States of LHCII.

TL;DR: The results suggest that there are at least two distinct quenching sites with different molecular compositions, meaning multiple dissipative pathways in LHCII, and one of the quenched conformations significantly increases in relative population under environmental conditions mimicking high light.