K. Kosovrasti

This paper introduces ROBUST, a machine learning framework that identifies energetic determinants of inhibitor potency against evolving targets, demonstrating its utility in predicting and optimizing inhibitors with improved resistance profiles.

This study identifies two independent resistance pathways to fifth-generation protease inhibitors in HIV-1 by analyzing mutations under high drug concentrations.

The paper investigates how fluorination of HCV protease inhibitors improves resistance to the D168A variant by enabling alternate binding conformations through co-crystal structure analysis.

This study determines the crystal structures of HCV NS3/4A protease from multiple genotypes bound to glecaprevir, revealing molecular mechanisms of pan-genotypic inhibition and resistance-associated substitutions.

The paper investigates how structural changes in HIV-1 protease affect the potency of Darunavir and its analogs against primary resistance mutations using crystal structures and vdW interaction analysis.