Author

S. Dubiley

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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Microbiology· 3 Biochemistry· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:host-pathogen & immune response· 3 Organism:bacteria (other)· 2 Research Focus:cell type annotation· 2 Approach:deep learning· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:clustering· 1 Research Focus:development & morphogenesis· 1

Frequent Co-Authors

E. Yagmurov· 2 shared K. V. Severinov· 2 shared M. Serebryakova· 2 shared Y. I. Wolf· 2 shared A. Alfi· 1 shared A. Kumar· 1 shared A. Livenskyi· 1 shared A. Popov· 1 shared

Activity by Year

2020-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 13 mutual co-author links

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2 shared papersMicrobiology

E. Yagmurov

Mutual co-authors in cluster

Author profile →

5 papers

Recent·Most cited

A widespread family of ribosomal peptide metallophores involved in bacterial adaptation to copper stress

L. Leprevost, S. Junger, G. Lippens, C. Guillaume, G. Sicoli, L. Oliveira Correia, A. Rivera-Millot, G. Billon, C. Henry, R. Antoine, S. Zirah, S. Dubiley, Y. Li, F. Jacob-Dubuisson

This paper identifies bufferins, a widespread family of ribosomal peptide metallophores that help bacteria adapt to copper stress by sequestering excess copper ions.

bioRxiv · Mar 18, 2024Microbiology

Cell-free mutant analysis combined with structure prediction of a lasso peptide biosynthetic protein B2

A. Alfi, A. Popov, A. Kumar, K. Y. J. Zhang, S. Dubiley, K. Severinov, S. Tagami

The paper combines cell-free mutagenesis with AlphaFold2 structure prediction to validate the function of TfuB2, revealing a hydrophobic binding site for TfuB1.

bioRxiv · Apr 6, 2022Biochemistry

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

An interplay between viruses and bacteria associated with marine sponges from the White Sea revealed by metagenomics

A. Rusanova, V. Fedorchuk, S. Toshchakov, S. Dubiley, D. Sutormin

The paper uses metagenomics to study virus-bacteria interactions in marine sponges from the White Sea, revealing species-specific communities and viral exchange mechanisms.

bioRxiv · Nov 12, 2021 · PreprintMicrobiology

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