Liming Yan

TL;DR: The structure of the COVID-19 virus polymerase essential for viral replication provides a basis for the design of new antiviral drugs that target viral RdRp, also named nsp12, and it appears to be a primary target for the antiviral drug remdesivir.

TL;DR: The molecular basis of SARS-CoV-2 RNA replication is examined by determining the cryo-EM structures of the stalled pre-/post- translocated polymerase complexes and the inhibition mechanisms of the triphosphate metabolite of remdesivir are investigated through structural and kinetic analyses.

TL;DR: These studies provide the first glimpses into the architecture of the nsp14–nsp10 complex involved in RNA viral proofreading, and show that a DEEDh (the five catalytic amino acids) motif drives nucleotide excision.

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

TL;DR: The structure of the full-length Nsp13 helicase of SARS-CoV (SARS-Nsp13) is presented and the structural coordination of its five domains is investigated, which provides new insights into the Replication and Transcription Complex (RTC) of CoVs.