Celia A. Schiffer

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 uses single-molecule imaging to show that maturation inhibitors alter Gag conformational dynamics and spatial heterogeneity in immature HIV-1 virions.

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 uses cryo-electron tomography to show that sialic acid binding causes influenza HA trimers to cluster and form triplets on virions.

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.

This study designs and tests optimized oligonucleotide inhibitors for APOBEC3 enzymes, showing improved potency and nuclease stability compared to previous inhibitors.

This study develops stabilized Cas-embedded base editors (sCE_CBEs) that enable efficient and accurate C-to-T editing with minimal off-target effects in hematopoietic stem and progenitor cells.

This study identifies mutations to improve prime editing efficiency in low-dNTP environments by enhancing MMLV-reverse transcriptase and reducing SAMHD1 activity.

This study identifies hyperactive mutations in SARS-CoV-2 Mpro that increase enzyme activity and contribute to drug resistance, finding them more prevalent than binding-reducing mutations.

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.

This study investigates how the distal mutation V36M confers drug resistance in HCV NS3/4A protease through allosteric modulation of the active site, in the context of R155K.

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.