We study mechanisms required for the pathogenesis of infection and cancer and discover novel compounds to inhibit these mechanisms by using a combination of enzymology, structural biology and biophysical chemistry.
We have openings for graduate and undergraduate students. Graduate students should first apply to the Ph.D. Program in Pharmaceutical Sciences at the University of Kentucky.
- Congratulations to Caixia on her manuscript recently accepted to Acta Crystallographica D on a Zn+2 phasing method for determining nucleic acid crystal structures.
- We welcome Dr. Ankita Punetha, a new Postdoctoral Scholar, in our group.
- Congratulations to Caixia on her fantastic manuscript describing the first crystal structures of non-covalent complexes of bacterial primase DnaG with DNA that was published in Biochemistry.
- Congratulations to Allan, Shogo and Taylor on a Nature Chemical Biology manuscript on the structure and mechanism of an interrupted adenylation domain, solving a mystery of how non-ribosomal peptides are methylated in Nature.
- Congratulations to Max Qiu on winning the 2nd place in Chemistry at the Central Kentucky Regional Science and Engineering Fair.
- Congratulations to Keith and Allan on a Biochemistry manuscript on structure-function studies of acetylation and deacetylation of a Mycobacterium tuberculosis histone-like nucleoid protein HupB by Eis and a Sir2 homolog Rv1151c, respectively.
- Congratulations to Caixia, Atefeh, Keith, Huy and Selina on the acceptance of their manuscript on novel inhibitors of Mycobacterium tuberculosis Eis protein that abolish kanamycin resistance in this pathogen, to the ACS Infectious Diseases journal. This is another stepping stone in our efforts to combat and prevent the spread of multidrug-resistant TB!
- Congratulations to Allan! His fantastic methodology review of HTS assays used to discover DNA metabolism inhibitors for novel antibiotic development has been published in Methods in Molecular Biology (Springer).
- Congratulations to Caixia! She co-authored our recently published J. Med. Chem manuscript on discovery and validation of novel inhibitors of Mycobacterium tuberculosis Eis protein, a cause of drug resistance in tuberculosis.
- Congratulations to Allan and Atefeh (from the Garneau-Tsodikova group)! Their manuscript on species-specific allosteric inhibitors of inorganic pyrophosphatase from Mycobacterium tuberculosis was accepted for publication in ACS Chemical Biology.
- The SBGrid Consortium at Harvard University publishes an article on our group.
- Congratulations to Caixia! Her manuscript on structural studies of mithramycin-DNA complexes and mithramycin interactions with FLI1-DNA complexes, a collaboration with the Rohr and Ivanov laboratories, was accepted for publication in Nucleic Acids Research.
- Congratulations to Caixia and Keith! Their manuscript on the discovery of potent inhibitors of acetyltransferase Eis that overcome resistance to kanamycin in Mycobacterium tuberculosis was accepted for publication in the ACS Chemical Biology.
- Congratulations to Stevi and Caixia! Their manuscript on dimerization and DNA binding of mithramycins was accepted for publication in the Journal of Inorganic Biochemistry.
- Congratulations to Caixia on the acceptance of her manuscript on oncogenic transcription factor FLI1 for publication in Biochemistry.
- Congratulations to Allan! His manuscript on a crystal structure of PltA halogenase from the pyoluteorin pathway was accepted for publication in the Journal of Structural Biology.
- Congratulations to Allan on his authorship on a publication on the structure and mechanism of inorganic pyrophosphatase from Mycobacteirum tuberculosis in the Journal of Structural Biology.
- Congratulations to Caixia on her authorship on a publication on a crystal structure of methyltransferase CalO6 from the calicheamicin biosynthetic pathway in BMC Structural Biology.
- Dimitri Leggas wins a highly competitive 2015 Presidential Scholarship. Only ~140 graduating high-school seniors across the US receive this award. Congratulations, Dimitri!