Gobeil, S. M.-C., Janowska, K., McDowell, S., Mansouri, K., Parks, R., Manne, K., Stalls, V., Kopp, M. F., Henderson, R., Edwards, R. J., Haynes, B. F., & Acharya, P. (2021). D614G Mutation Alters SARS-CoV-2 Spike Conformation and Enhances Protease Cleavage at the S1/S2 Junction. Cell Reports, 34, Article ID: 108630.
https://doi.org/10.1016/j.celrep.2020.108630

has been cited by the following article:

• TITLE: Use of the D614G Mutation of the SARS-CoV-2 Spike Protein as a Biophysical Model to Explain Coulomb’s Law Function

  AUTHORS: Michelle Fuentes-Acosta, Jorge Mulia-Rodríguez, Daniel Osorio-González

  KEYWORDS: Spike, Coulomb’s Law, Electrostatic Interactions

  JOURNAL NAME: Creative Education, Vol.14 No.1, January 20, 2023

  ABSTRACT: The scientific work of Charles-Augustin de Coulomb has transcended as a significant contribution to explain phenomena in nature and generate crucial technological development in recent daily activities. We used Coulomb’s law to calculate the changes generated in the electrostatic interactions of residue 614 of SARS-CoV-2 Spike protein when the D614G mutation occurs. We made a physical analysis of the transformation and the biological implications in the whole molecule’s structural stability, obtaining that a greater electronegativity of the mutation stage favors the open state of Spike, which is manifested as a greater efficiency to bind to the ACE2 human receptor.