K. Y. Rhee

This paper studies how rpoB mutations in Bacillus subtilis confer rifampicin resistance and affect β-lactam susceptibility through changes in peptidoglycan precursor levels.

This paper predicts chemical substrate structures for orphan enzymes using protein language models, achieving high accuracy for Mycobacterium tuberculosis SDRs and SAM-methyltransferases.

The paper uses co-essentiality analysis of TnSeq data to identify gene modules in Mtb, focusing on an itaconate defense enzyme cluster and proposing novel functional associations.

This study identifies GlmR as an accessory uridyltransferase essential for Listeria monocytogenes cytosolic survival and virulence by synthesizing UDP-GlcNAc.

This study identifies EtfDMtb as an essential dehydrogenase for fatty acid β-oxidation in Mtb, showing that disrupting it kills the bacterium in vitro and in mice.

This study maps chemical-genetic interactions in Mycobacterium tuberculosis to identify how carbon metabolism and cell wall structure affect drug efficacy, revealing environment-dependent and -independent interactions.

The paper builds MtbTnDB, a database of Mtb TnSeq screens, enabling comparison of genetic essentiality across conditions and analysis of gene function.

The paper identifies potent inhibitors of Mycobacterium tuberculosis CoaB by targeting a novel allosteric site, based on structural and biochemical analyses of CoaBC.