Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Natalia, Zelinskaya"'
Autor:
Pooja Srinivas, Meisam Nosrati, Natalia Zelinskaya, Debayan Dey, Lindsay R. Comstock, Christine M. Dunham, Graeme L. Conn
Publikováno v:
bioRxiv
Acquired ribosomal RNA (rRNA) methylation has emerged as a significant mechanism of aminoglycoside resistance in pathogenic bacterial infections. Modification of a single nucleotide in the ribosome decoding center by the aminoglycoside-resistance 16S
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f36a7687d6663ee93546431136a6f16f
https://europepmc.org/articles/PMC10054953/
https://europepmc.org/articles/PMC10054953/
Publikováno v:
Balneo Research Journal, Vol 11, Iss 2, Pp 125-132 (2020)
Introduction. Diseases of parodontal tissues occupy a leading place in the structure of dental diseases. Early diagnosis of the initial degree of generalized parodontitis (GP) is an effective way of secondary prevention. This is due to the complexity
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::770c103f5348bb3f118c4262a9cb3767
https://doi.org/10.12680/balneo.2020.327
https://doi.org/10.12680/balneo.2020.327
Autor:
Zane T, Laughlin, Suparno, Nandi, Debayan, Dey, Natalia, Zelinskaya, Marta A, Witek, Pooja, Srinivas, Ha An, Nguyen, Emily G, Kuiper, Lindsay R, Comstock, Christine M, Dunham, Graeme L, Conn
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 119(14)
Changes in bacterial ribosomal RNA (rRNA) methylation status can alter the activity of diverse groups of ribosome-targeting antibiotics. These modifications are typically incorporated by a single methyltransferase that acts on one nucleotide target a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::08fd42be2df7e73cd6d00fa51f067dd0
https://pubmed.ncbi.nlm.nih.gov/35357969
https://pubmed.ncbi.nlm.nih.gov/35357969
Autor:
Zane T. Laughlin, Suparno Nandi, Debayan Dey, Natalia Zelinskaya, Marta A. Witek, Pooja Srinivas, Ha An Nguyen, Emily G. Kuiper, Lindsay R. Comstock, Christine M. Dunham, Graeme L. Conn
Publikováno v:
Proceedings of the National Academy of Sciences. 119
Changes in bacterial ribosomal RNA methylation status can alter the activity of diverse groups of ribosome-targeting antibiotics. These modifications are typically incorporated by a single methyltransferase that acts on one nucleotide target and rRNA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de19c1be54a879fcbdcd449537763fa6
https://doi.org/10.1073/pnas.2120352119
https://doi.org/10.1073/pnas.2120352119
Autor:
Atousa Mehrani, Sarah E. Strassler, Debayan Dey, Scott M. Stagg, Natalia Zelinskaya, Christine M. Dunham, Eric D. Hoffer, Graeme L. Conn, Meisam Nosrati
Publikováno v:
J Biol Chem
Methylation of the small ribosome subunit rRNA in the ribosomal decoding center results in exceptionally high-level aminoglycoside resistance in bacteria. Enzymes that methylate 16S rRNA on N7 of nucleotide G1405 (m7G1405) have been identified in bot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f800a1408054ade5a8f12cebccc936a
Autor:
Natalia Zelinskaya, Renata Cristina Picão, Marta A. Witek, Graeme L. Conn, Laís Lisboa Corrêa
Publikováno v:
Antimicrobial Agents and Chemotherapy. 60:699-702
The exogenously acquired 16S rRNA methyltransferases RmtD, RmtD2, and RmtG were cloned and heterologously expressed in Escherichia coli , and the recombinant proteins were purified to near homogeneity. Each methyltransferase conferred an aminoglycosi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::60adb9430cb32564ece545817fdfac59
https://doi.org/10.1128/aac.02482-15
https://doi.org/10.1128/aac.02482-15
Autor:
Kellie Vinal, Miloje Savic, Rachel Macmaster, Natalia Zelinskaya, S. Sunita, Graeme L. Conn, Pooja M. Desai
Publikováno v:
Antimicrobial Agents and Chemotherapy. 59:2807-2816
Methylation of bacterial 16S rRNA within the ribosomal decoding center confers exceptionally high resistance to aminoglycoside antibiotics. This resistance mechanism is exploited by aminoglycoside producers for self-protection while functionally equi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::466d2030ab619b29a81cff97ab62727b
https://doi.org/10.1128/aac.00056-15
https://doi.org/10.1128/aac.00056-15
Autor:
Graeme L. Conn, Dayne M. West, Pooja M. Desai, Jack A. Dunkle, Kellie Vinal, Natalia Zelinskaya, Miloje Savic, Christine M. Dunham
Publikováno v:
Proceedings of the National Academy of Sciences. 111:6275-6280
Aminoglycosides are potent, broad spectrum, ribosome-targeting antibacterials whose clinical efficacy is seriously threatened by multiple resistance mechanisms. Here, we report the structural basis for 30S recognition by the novel plasmid-mediated am
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5323ea9c4bbe81764ffa7b19576d81c3
https://doi.org/10.1073/pnas.1402789111
https://doi.org/10.1073/pnas.1402789111
Autor:
Eric B. Dammer, Samantha M. Prezioso, Joanna B. Goldberg, Jeffrey Meisner, Nicholas T. Seyfried, Natalia Zelinskaya, Duc M. Duong, Sebastián Albertí, John J. Varga, Graeme L. Conn, Emily G. Kuiper, Joshua P. Owings
Pseudomonas aeruginosa is a Gram-negative opportunistic pathogen that trimethylates elongation factor-thermo-unstable (EF-Tu) on lysine 5. Lysine 5 methylation occurs in a temperature-dependent manner and is generally only seen when P. aeruginosa is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2543c3405684255baa3f4e494d6f4269
https://doi.org/10.1074/jbc.m115.706853
https://doi.org/10.1074/jbc.m115.706853
Publikováno v:
Nucleic Acids Research
X-ray crystal structures were determined of the broad-spectrum aminoglycoside-resistance A1408 16S rRNA methyltransferases KamB and NpmA, from the aminoglycoside-producer Streptoalloteichus tenebrarius and human pathogenic Escherichia coli, respectiv
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::291b58fa3a749376a3f2c485c88e7923
http://europepmc.org/articles/PMC2995053
http://europepmc.org/articles/PMC2995053