Author

S. Bukhdruker

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 5

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Organism:human· 3 Assay:proteomics· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Research Focus:drug response / drug discovery· 1 Research Focus:host-pathogen & immune response· 1 Organism:mouse· 1

Frequent Co-Authors

V. Borshchevskiy· 5 shared A. Gilep· 4 shared A. Kavaleuski· 4 shared E. Marin· 4 shared I. Grabovec· 4 shared N. Strushkevich· 4 shared A. Mishin· 3 shared T. Varaksa· 3 shared

Activity by Year

2020-2022 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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5 shared papersBiochemistry

V. Borshchevskiy

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5 papers

Recent·Most cited

Structural insights into 3Fe-4S ferredoxins diversity in M.tuberculosis highlighted by a first redox complex with P450.

A. Gilep, T. Varaksa, S. Bukhdruker, A. Kavaleuski, Y. Ryzhykau, S. Smolskaya, T. Sushko, K. Tsumoto, I. Grabovec, I. Kapranov, I. Okhrimenko, E. Marin, M. Shevtsov, A. Mishin, K. Kovalev, , N. Strushkevich

The paper solves the structures of 3Fe-4S ferredoxins from M. tuberculosis and their complex with CYP143, revealing structural and functional insights into redox interactions.

bioRxiv · Nov 2, 2022 · PreprintBiochemistry

NanoFAST: Structure-based design of a small fluorogen-activating protein with only 98 amino acids

K. S. Mineev, S. A. Goncharuk, M. V. Goncharuk, N. V. Povarova, N. S. Baleeva, A. Y. Smirnov, I. N. Myasnyanko, D. A. Ruchkin, S. Bukhdruker, A. Remeeva, A. Mishin, V. Borshchevskiy, V. Gordeliy, A. S. Arseniev, D. A. Gorbachev, , M. S. Baranov

The paper designs a small fluorogen-activating protein (nanoFAST) by truncating FAST based on structural analysis, resulting in the shortest known genetically encoded tag with 98 amino acids.

bioRxiv · Dec 29, 2020Biochemistry

A new twist of rubredoxin function in M. tuberculosis

T. Sushko, A. Kavaleuski, I. Grabovec, A. Kavaleuskaya, D. Vakhrameev, S. Bukhdruker, E. Marin, A. Kuzikov, R. Masamrekh, V. Shumyantseva, K. Tsumoto, V. Borshchevskiy, A. Gilep, N. Strushkevich

This study identifies RubB as a cofactor for mycobacterial cytochrome P450s in M. tuberculosis, showing its role in bacterial survival and potential biotech applications.

bioRxiv · Oct 27, 2020Biochemistry

Hydroxylation of antitubercular drug candidate, SQ109, by mycobacterial cytochrome P450

S. Bukhdruker, T. Varaksa, I. Grabovec, E. Marin, P. Shabunya, M. Kadukova, S. Grudinin, A. Kavaleuski, A. Gusach, A. Gilep, V. Borshchevskiy, N. Strushkevich

The paper shows that Mycobacterium tuberculosis CYP124 hydroxylates SQ109, a drug candidate, and potentially affects its interaction with MmpL3.

bioRxiv · Aug 27, 2020Biochemistry

Metabolic fate of human immunoactive sterols in Mycobacterium tuberculosis

T. Varaksa, S. Bukhdruker, I. Grabovec, E. Marin, A. Kavaleuski, A. Gusach, K. Kovalev, I. Maslov, A. Luginina, D. Zabelskiy, R. Astashkin, M. Shevtsov, S. Smolskaya, A. Kavaleuskaya, P. Shabunya, , N. Strushkevich

The paper identifies Mtb enzymes that metabolize human immune oxysterols and vitamin D3 derivatives, revealing a potential drug target for tuberculosis treatment.

bioRxiv · Jul 7, 2020Biochemistry