Author

N. Zelinskaya

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

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Assay:structural biology· 3 Organism:bacteria (other)· 2 Research Focus:protein folding & dynamics· 2 Organism:E. coli· 1 Research Focus:protein structure prediction· 1

Frequent Co-Authors

C. M. Dunham· 3 shared D. Dey· 3 shared G. L. Conn· 3 shared L. R. Comstock· 2 shared M. Nosrati· 2 shared P. Srinivas· 2 shared A. Mehrani· 1 shared E. D. Hoffer· 1 shared

Activity by Year

2019-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 35 mutual co-author links

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3 shared papersBiochemistry

C. M. Dunham

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3 papers

Recent·Most cited

30S subunit recognition and G1405 modification by the aminoglycoside-resistance 16S ribosomal RNA methyltransferase RmtC

P. Srinivas, M. Nosrati, N. Zelinskaya, D. Dey, L. R. Comstock, C. M. Dunham, G. L. Conn

This paper determines the structure of RmtC bound to the 30S ribosomal subunit and identifies key residues involved in G1405 modification, providing insights for inhibitor development.

Proceedings of the National Academy of Sciences · Jun 12, 2023Peer-reviewedBiochemistry

50S subunit recognition and modification by the Mycobacterium tuberculosis ribosomal RNA methyltransferase TlyA

Z. T. Laughlin, S. Nandi, D. Dey, N. Zelinskaya, M. A. Witek, P. Srinivas, H. A. Nguyen, E. G. Kuiper, L. R. Comstock, C. M. Dunham, G. L. Conn

This paper reports the structure of the Mycobacterium tuberculosis TlyA enzyme bound to the 50S ribosomal subunit, revealing mechanisms of rRNA substrate recognition and modification that contribute to antibiotic resistance.

bioRxiv · Nov 11, 2021Biochemistry

Functionally critical residues in the aminoglycoside resistance-associated methyltransferase RmtC play distinct roles in 30S substrate recognition

M. Nosrati, D. Dey, A. Mehrani, S. E. Strassler, N. Zelinskaya, E. D. Hoffer, S. M. Stagg, C. M. Dunham, G. L. Conn

This study identifies functionally critical residues in RmtC that distinguish between 30S-binding affinity and 16S rRNA modification through structural and biochemical analysis.

bioRxiv · Oct 3, 2019Biochemistry