J. A. Jaimes

The paper designs SARS-CoV-2 Spike proteins with novel mutations to evaluate vaccine effectiveness against future viral variants using a deep learning model.

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 assesses the furin cleavage site of the SARS-CoV-2 Omicron variant, finding increased intrinsic cleavability due to mutations N679K and P681H compared to ancestral and other variants.

This study identifies specific Ca2+ binding residue pairs in SARS-CoV-1 fusion peptide that promote or inhibit membrane insertion through molecular dynamics and biological assays.

This study tests L-type calcium channel blockers for inhibiting SARS-CoV-2 infection in cell culture, finding that felodipine and nifedipine limit virus entry and infection with minimal toxicity.

The paper analyzes the P681R mutation in the SARS-CoV-2 spike protein of variant A.23.1, showing increased furin cleavage and infectivity compared to earlier variants, but only when combined with other spike changes.

This study evaluates the impact of the P681H mutation in the SARS-CoV-2 B.1.1.7 spike on furin cleavage and viral entry, finding no significant effect on these processes.

This study shows coagulation factors like factor Xa and thrombin directly cleave SARS-CoV-2 spike, enhancing viral entry, and suggests anticoagulation could reduce infection.

This study investigates the role of S1/S2 cleavage in SARS-CoV-2 spike protein activation, showing its necessity for early pathway entry in Calu-3 cells and involvement of proteases beyond furin.

The paper models the structure of 2019-nCoV spike protein and identifies a proteolytically-sensitive loop that distinguishes it from SARS-CoV.