Therapeutically Targeted Destabilization of the Quaternary Structure of the Spike Protein in the Dominant G614 Strain of SARS-CoV-2
Author:
Affiliation:
1. Daruma Institute for AI in Pharmaceutical Research, AF Innovation Pharma Consultancy, 4000 Pemberton Court, Winston-Salem, North Carolina 27106, United States
Publisher
American Chemical Society (ACS)
Subject
Pharmacology (medical),Pharmacology
Link
https://pubs.acs.org/doi/pdf/10.1021/acsptsci.0c00114
Reference12 articles.
1. Tracking Changes in SARS-CoV-2 Spike: Evidence that D614G Increases Infectivity of the COVID-19 Virus
2. Hu, J., He, C.L., Gao, Q.Z., Zhang, G.J., Cao, X.X., Long, Q.X., Deng, H.J., Huang, L.Y., Chen, J., and Wang, K., The D614G mutation of SARS-CoV-2 spike protein enhances viral infectivity and decreases neutralization sensitivity to individual convalescent sera. bioRxiv (Microbiology), June 20, 2020. https://doi.org/10.1101/2020.06.20.161323.
3. Ozono, S., Zhang, Y., Ode, H., Seng, T. T., Imai, K., Miyoshi, K., Kishigami, S., Ueno, T., Iwatani, Y., Suzuki, T., and Tokunaga, K. Naturally mutated spike proteins of SARS-CoV-2 variants show differential levels of cell entry. bioRxiv (Microbiology), June 15, 2020, https://doi.org/10.1101/2020.06.15.151779.
4. Structural Impact of Mutation D614G in SARS-CoV-2 Spike Protein: Enhanced Infectivity and Therapeutic Opportunity
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