Structural basis of SARS-CoV-2 polymerase inhibition by Favipiravir
Qi Peng(Chinese Academy of Sciences), Yi Shi(Chinese Academy of Medical Sciences & Peking Union Medical College), Jianxun Qi(Chinese Academy of Sciences), Min Wang(Institute of Vertebrate Paleontology and Paleoanthropology), Jingru Zhao(Institute of Microbiology), Ruchao Peng(Institute of Microbiology), Bin Yuan(China Academy of Chinese Medical Sciences), Lifeng Fu(Chinese Academy of Sciences)
Cited by 50
Related Papers
Receptor binding and complex structures of human ACE2 to spike RBD from omicron and delta SARS-CoV-2
|Cell|2022|538
Enabling the 'host jump': structural determinants of receptor-binding specificity in influenza A viruses
|Nature Reviews Microbiology|2014|312
Structural and Biochemical Characterization of the nsp12-nsp7-nsp8 Core Polymerase Complex from SARS-CoV-2
|Cell Reports|2020|281
Omicron SARS-CoV-2 mutations stabilize spike up-RBD conformation and lead to a non-RBM-binding monoclonal antibody escape
|Nature Communications|2022|165
A novel strategy for forensic age prediction by DNA methylation and support vector regression model
|Scientific Reports|2015|162