Daniel N. A. Bolon

The paper identifies mutations that affect HIV-1 protease self-cleavage but not viral fitness, and uses simulations to model its dynamic mechanism.

This study investigates how the two active sites of SARS-CoV-2 Mpro communicate and cooperate in catalysis using enzymatic assays, crystal structures, and engineered mutations.

This study investigates drug resistance mechanisms in SARS-CoV-2 Mpro caused by E166 mutations and their compensation by L50F, revealing structural and functional impacts on inhibitor binding and catalytic efficiency.

The paper identifies resistance mutations in SARS-CoV-2 main protease against nirmatrelvir and ensitrelvir using yeast screens, finding cross-resistant mutations and reduced enzyme function.

The paper performs a comprehensive mutational scan of SARS-CoV-2 Mpro to identify resistance mechanisms and guide inhibitor design.

The paper uses overexpression-based mutational scanning to reveal previously hidden deleterious effects of ubiquitin alleles when co-expressed with wild type, showing broader distribution of growth effects compared to single allele scans.

The paper uses deep mutational scanning to explore how chemical perturbations affect ubiquitin's mutational tolerance, revealing sensitization of most positions except two.

The paper introduces a synthetic biology approach to study nucleosome symmetry by creating asymmetric H3 heterodimers and demonstrates their utility in analyzing histone modification crosstalk.