Sergey Korolev, Ph.D.
Structure-functional studies of DNA recombination, replication and repair proteins.
Office: DRC, Room 513
Phone: (314) 977-9261
Ph.D., 1993 Engelhardt Institute of Biochemistry and Molecular Biology, Moscow, Russian Academy of Sciences
Our lab studies the mechanism of protein function at the atomic resolution level utilizing X-ray crystallography and biochemical approaches. The main focus is recombination mediator proteins (RMPs), which are essential for genome stability and DNA repair in all organisms.
- Erratum to: The loop-less tmCdc34 E2 mutant defective polyubiquitination in vitro and in vivo supports yeast growth in a manner dependent on Ubp14 and Cka2.
Lass A, Cocklin R, Scaglione KM, Skowyra M, Korolev S, Goebl M, Skowyra D. Cell Div. (2016) 11:13.
- A MUB E2 structure reveals E1 selectivity between cognate ubiquitin E2s in eukaryotes.
Lu X, Malley KR, et al. Nat Commun. (2016) Aug 23 [Epub ahead of print].
- Correction: High resolution crystal structure of human beta-glucuronidase reveals structural basis of lysosome targeting.
Hassan MI, Waheed A, et al. PLoS One. (2015) 10(9):e0138401.
- RecO protein initiates DNA recombination and strand annealing through two alternative DNA binding mechanisms.
Ryzhikov M, Gupta R, et al. J Biol Chem. (2014) 289(42):28846-28855.
- Rous sarcoma virus synaptic complex capable of concerted integration is kinetically trapped by human immunodeficiency virus integrase strand transfer inhibitors.
Pandey KK, Bera S, et al. J Biol Chem. (2014) 289(28):19648-58.