Structural impact on SARS-CoV-2 spike protein by D614G substitution

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Tracking Changes in SARS-CoV-2 Spike: Evidence that D614G Increases Infectivity of the COVID-19 Virus

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Spike mutation D614G alters SARS-CoV-2 fitness

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The Architecture of Inactivated SARS-CoV-2 with Postfusion Spikes Revealed by Cryo-EM and Cryo-ET

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Evolutionary and structural analyses of SARS-CoV-2 D614G spike protein mutation now documented worldwide

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D614G Spike Mutation Increases SARS CoV-2 Susceptibility to Neutralization

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Cryo-EM Structures of SARS-CoV-2 Spike without and with ACE2 Reveal a pH-Dependent Switch to Mediate Endosomal Positioning of Receptor-Binding Domains

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SARS-CoV-2 spike-protein D614G mutation increases virion spike density and infectivity

(2020) Lizhou Zhang et al.   Nature Communications

D614G Mutation Alters SARS-CoV-2 Spike Conformation and Enhances Protease Cleavage at the S1/S2 Junction

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