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Sergey Korolev, Ph.D.
Associate Professor

Structure-functional studies of DNA recombination, replication and repair proteins.

Office: DRC 513
Voice: (314) 977-9261

Research Interests

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.

Recent Publications

Advances in structural studies of recombination mediator proteins

Erratum to: The loop-less ™Cdc34 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 and Skowyra D

A MUB E2 structure reveals E1 selectivity between cognate ubiquitin E2s in eukaryotes
Lu X, Malley KR, Brenner CC, Koroleva O, Korolev S and Downes BP

Rous sarcoma virus synaptic complex capable of concerted integration is kinetically trapped by human immunodeficiency virus integrase strand transfer inhibitors
Pandey KK, Bera S, Korolev S, Campbell M, Yin Z, Aihara H and Grandgenett DP

High resolution crystal structure of human β-glucuronidase reveals structural basis of lysosome targeting
Hassan MI, Waheed A, Grubb JH, Klei HE, Korolev S and Sly WS

Department of Biochemistry and Molecular Biology
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