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Shilong Fan

Researcher at Tsinghua University

Publications -  27
Citations -  6445

Shilong Fan is an academic researcher from Tsinghua University. The author has contributed to research in topics: Medicine & Biology. The author has an hindex of 13, co-authored 19 publications receiving 4128 citations.

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Journal ArticleDOI

Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor.

TL;DR: High-resolution crystal structures of the receptor-binding domain of the spike protein of SARS-CoV-2 and SARS -CoV in complex with ACE2 provide insights into the binding mode of these coronaviruses and highlight essential ACE2-interacting residues.
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DWARF14 is a non-canonical hormone receptor for strigolactone

TL;DR: The crystal structure of the strigolactone-induced AtD14–D3–ASK1 complex is reported, and it is revealed that Arabidopsis thaliana (At)D14 undergoes an open-to-closed state transition to trigger striglactone signalling, and that strigOLactone is hydrolysed into a covalently linked intermediate molecule (CLIM) to initiate a conformational change of AtD 14 to facilitate interaction with D
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Molecular basis of ligand recognition and transport by glucose transporters

TL;DR: Comparison of the outward-facing GLUT3 structures with the inward-open GLUT1 provides insights into the alternating access cycle for GLUTs, whereby the C-terminal domain provides the primary substrate-binding site and the amino-Terminal domain undergoes rigid-body rotation with respect to theC- terminal domain.
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The crystal structure of Cpf1 in complex with CRISPR RNA

TL;DR: The study reveals the crRNA recognition mechanism and provides insight into crRNA-guided substrate binding of LbCpf1, establishing a framework for engineering LbPf1 to improve its efficiency and specificity for genome editing.
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Structural and biochemical basis for induced self-propagation of NLRC4

TL;DR: The wheel-like structure of a PrgJ-NAIP2-NLRC4 complex determined by cryogenic electron microscopy reveals that NLRC4 activation involves substantial structural reorganization that creates one oligomerization surface (catalytic surface).