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SARS-CoV-2 and bat RaTG13 spike glycoprotein structures inform on virus evolution and furin-cleavage effects

Nature Structural & Molecular Biology · 2020 · Vol. 27(8) · pp. 763–767
Antoni G. WrobelD.J. BentonPengqi XuChloë RoustanStephen R. MartinPeter B. RosenthalJ.J. SkehelS.J. Gamblin
SARS-CoV-2 and COVID-19 ResearchViral Infections and Outbreaks ResearchViral gastroenteritis research and epidemiologyFurinGlycoproteinCleavage (geology)VirusBiologyReceptorSevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2)VirologyCell biologyCoronavirus disease 2019 (COVID-19)

MeSH terms

Protein Conformation, alpha-HelicalProtein Conformation, beta-StrandBetacoronavirusAngiotensin-Converting Enzyme 2COVID-19SARS-CoV-2AnimalsBinding SitesChiropteraHumansPeptidyl-Dipeptidase AModels, MolecularPneumonia, ViralProtein BindingReceptors, Virus

Funding

  • Wellcome
  • Wellcome Trust
  • Francis Crick Institute
  • Cancer Research UK
  • Sun Yat-sen University
  • Medical Research Council
  • Sanming Project of Medicine in Shenzhen
Citations
619
FWCI
13.26
field-weighted impact
References
36
Percentile
99%
vs. same field & year
Citations per year
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