O
Oleg V. Tsodikov
Researcher at University of Kentucky
Publications - 107
Citations - 3887
Oleg V. Tsodikov is an academic researcher from University of Kentucky. The author has contributed to research in topics: DNA & Binding site. The author has an hindex of 32, co-authored 97 publications receiving 3508 citations. Previous affiliations of Oleg V. Tsodikov include University of Michigan & University of Wisconsin-Madison.
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Novel computer program for fast exact calculation of accessible and molecular surface areas and average surface curvature.
TL;DR: Fast, memory‐efficient and robust execution make this software attractive for applications both in computationally expensive energy minimization algorithms, such as docking or molecular dynamics simulations, and in stand‐alone surface area and curvature calculations.
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Crystal structure and DNA binding functions of ERCC1, a subunit of the DNA structure-specific endonuclease XPF-ERCC1.
TL;DR: It is shown that a truncated form of XPF lacking the N-terminal helicase-like domain in complex with ERCC1 exhibits a structure-specific endonuclease activity with similar specificity to that of full-length XPF-ERCC1.
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A Flexible Interface between DNA Ligase and PCNA Supports Conformational Switching and Efficient Ligation of DNA.
John M. Pascal,Oleg V. Tsodikov,Greg L. Hura,Wei Song,Elizabeth A. Cotner,Elizabeth A. Cotner,Scott Classen,Alan E. Tomkinson,John A. Tainer,John A. Tainer,Tom Ellenberger,Tom Ellenberger +11 more
TL;DR: In this article, the Sulfolobus solfataricus DNA ligase and heterotrimeric PCNA were determined by X-ray diffraction and in complex by small-angle Xray scattering (SAXS).
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New Insights into Fluoroquinolone Resistance in Mycobacterium tuberculosis: Functional Genetic Analysis of gyrA and gyrB Mutations
TL;DR: It is indicated that certain mutations in gyrB confer fluoroquinolone resistance, but the level and pattern of resistance varies among the different mutations.
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Structural basis for the recruitment of ERCC1-XPF to nucleotide excision repair complexes by XPA
Oleg V. Tsodikov,Dmitri N. Ivanov,Barbara Orelli,Lidija Staresincic,Ilana Shoshani,Robert Oberman,Orlando D. Schärer,Gerhard Wagner,Tom Ellenberger +8 more
TL;DR: An essential protein–protein interaction of the NER pathway is investigated, the binding of the XPA protein to the ERCC1 subunit of the repair endonuclease ER CC1‐XPF, which reveals a binding interface that is amenable to the development of small molecule peptidomimetics that could be used to modulate NER repair activities in vivo.