L. Yurkovetskiy

This study shows that S:D614G and S:H655Y mutations enhance SARS-CoV-2 infectivity by stabilizing the Spike protein in an open RBD conformation, acting epistatically with the polybasic S1/S2 cleavage site.

This study investigates how ACE2 and antibodies affect the conformational dynamics of the SARS-CoV-2 spike protein using smFRET and FCS, revealing that D614G modulates RBD energetics similar to ACE2 binding.

This study shows the D614G SARS-CoV-2 spike protein variant is more infectious but has reduced ACE2 affinity and altered trimer conformation, affecting viral entry and antibody neutralization.

This study shows that Cyclophilin A protects HIV-1 from restriction by human TRIM5α by shielding the viral capsid from early inhibition during infection.