Sarah E. Newkirk

This study investigates the structure-activity relationship of griselimycin, identifying key amino acids and modifications that enhance its antitubercular activity.

This paper evaluates peptidomimetic modifications of MHC-I epitopes to improve antigen design, finding position-dependent tolerance and non-additive effects on immunogenicity and pharmacokinetics.

The paper shows that chemical modifications of MHC-I epitopes affect T cell recognition, demonstrating that antigenic identity depends on both sequence and chemical history.

This paper introduces D-CLAP, a split-luciferin assay to measure real-time cytosolic accumulation of compounds in live mycobacteria, showing that modifying carboxylates increases accumulation and antimycobacterial activity.

The paper identifies Hsp90 inhibitors as MHC-I inducers and develops novel compounds using click chemistry to enhance T cell activation and reduce toxicity.