Author

M. Serebryakova

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· 3 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:host-pathogen & immune response· 2 Organism:virus· 2 Organism:bacteria (other)· 1 Organism:E. coli· 1

Frequent Co-Authors

A. A. Baykov· 2 shared A. V. Bogachev· 2 shared E. Yagmurov· 2 shared K. V. Severinov· 2 shared S. Dubiley· 2 shared Y. I. Wolf· 2 shared Y. V. Bertsova· 2 shared A. Livenskyi· 1 shared

Activity by Year

2020-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 22 mutual co-author links

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2 shared papersBiochemistry

A. A. Baykov

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Author profile →

4 papers

Recent·Most cited

A redox-regulated, heterodimeric NADH:cinnamate reductase in Vibrio ruber

Y. V. Bertsova, M. Serebryakova, V. A. Anashkin, A. A. Baykov, A. V. Bogachev

The paper identifies a redox-regulated, heterodimeric NADH-dependent cinnamate reductase in Vibrio ruber that protects against cinnamate poisoning.

bioRxiv · Mar 4, 2023 · PreprintBiochemistry

S51 family peptidases provide resistance to peptidyl-nucleotide antibiotic McC

E. Yagmurov, K. Gilep, M. Serebryakova, Y. I. Wolf, S. Dubiley, K. V. Severinov

The paper identifies S51 family peptidases, named MccG, that cleave toxic isoaspartyl-nucleotides from peptide-nucleotide antibiotics, providing resistance in bacteria.

bioRxiv · Mar 27, 2022Microbiology

A novel, NADH-dependent acrylate reductase in Vibrio harveyi

Y. V. Bertsova, M. Serebryakova, A. A. Baykov, A. V. Bogachev

This paper identifies and characterizes a novel NADH-dependent acrylate reductase in Vibrio harveyi, showing its role in acrylate detoxification and potential use as a terminal electron acceptor.

bioRxiv · Jan 20, 2022Biochemistry

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