Author

S. Borukhov

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· 1 Biophysics· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:host-pathogen & immune response· 3 Organism:bacteria (other)· 2 Research Focus:cell signaling & trafficking· 1 Assay:CRISPR screen· 1 Organism:E. coli· 1

Frequent Co-Authors

K. Severinov· 2 shared A. Arseniev· 1 shared A. Kirillov· 1 shared A. Livenskyi· 1 shared A. Potyseva· 1 shared A. Shiriaeva· 1 shared D. Tsibulskaya· 1 shared E. Semenova· 1 shared

Activity by Year

2020-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 16 mutual co-author links

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2 shared papersBiophysics

K. Severinov

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Single-molecule studies reveal the off-pathway elemental pause state as a target of streptolydigin inhibition of RNA polymerase and its dramatic enhancement by Gre factors

A. Arseniev, M. Panfilov, G. Pobegalov, A. Potyseva, P. Pavlinova, M. Yakunina, J. Lee, S. Borukhov, K. Severinov, M. Khodorkovskii

This study uses single-molecule techniques to show streptolydigin induces pauses in RNA polymerase, which are enhanced by Gre factors, revealing a new mechanism for antibiotic action.

bioRxiv · Jun 5, 2023 · PreprintBiophysics

tRNA anticodon cleavage by target-activated CRISPR-Cas13a effector

I. Jain, M. Kolesnik, L. Minakhin, N. Morozova, A. Shiriaeva, A. Kirillov, S. Medvedeva, K. Kuznedelov, S. Borukhov, K. S. Makarova, E. V. Koonin, K. Severinov, E. Semenova

The paper shows that Cas13a cleaves tRNA anticodons to induce bacterial dormancy and activates toxin-antitoxin modules for mRNA and rRNA cleavage.

bioRxiv · Nov 10, 2021Microbiology

Histidine-Triad Hydrolases Provide Resistance to Peptide-Nucleotide Antibiotics

E. Yagmurov, D. Tsibulskaya, A. Livenskyi, M. Serebryakova, Y. I. Wolf, S. Borukhov, K. V. Severinov, S. Dubiley

The paper identifies histidine triad hydrolases as enzymes conferring resistance to peptide-nucleotide antibiotics like microcin C by hydrolyzing their toxic phosphoramide bond.

bioRxiv · Mar 4, 2020Biochemistry