Zobrazeno 1 - 10
of 69
pro vyhledávání: '"Yury S. Polikanov"'
Autor:
Chih-Wei Chen, Nadja Leimer, Egor A. Syroegin, Clémence Dunand, Zackery P. Bulman, Kim Lewis, Yury S. Polikanov, Maxim S. Svetlov
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-13 (2023)
Abstract The ever-growing rise of antibiotic resistance among bacterial pathogens is one of the top healthcare threats today. Although combination antibiotic therapies represent a potential approach to more efficiently combat infections caused by sus
Externí odkaz:
https://doaj.org/article/246bbb654cbb41e497335ae0c30d2797
Autor:
Anne Lanois-Nouri, Lucile Pantel, Jun Fu, Jessica Houard, Jean-Claude Ogier, Yury S. Polikanov, Emilie Racine, Hailong Wang, Sophie Gaudriault, Alain Givaudan, Maxime Gualtieri
Publikováno v:
mBio, Vol 13, Iss 1 (2022)
ABSTRACT Antibiotic resistance is an increasing threat to human health. A direct link has been established between antimicrobial self-resistance determinants of antibiotic producers, environmental bacteria, and clinical pathogens. Natural odilorhabdi
Externí odkaz:
https://doaj.org/article/fe7f244c90da4804ab9a2d51282d8ee5
Autor:
Dmitrii Y. Travin, Zoe L. Watson, Mikhail Metelev, Fred R. Ward, Ilya A. Osterman, Irina M. Khven, Nelli F. Khabibullina, Marina Serebryakova, Peter Mergaert, Yury S. Polikanov, Jamie H. D. Cate, Konstantin Severinov
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-11 (2019)
The authors report the identification of phazolicin (PHZ) - a prokaryotic translation inhibitory peptide - and its structure in complex with the E. coli ribosome, delineating PHZ’s mode of action and suggesting a basis for its bacterial species-spe
Externí odkaz:
https://doaj.org/article/259172219eaf426fbec6e6c02c364a14
Autor:
Chih-Wei Chen, Julia A. Pavlova, Dmitrii A. Lukianov, Andrey G. Tereshchenkov, Gennady I. Makarov, Zimfira Z. Khairullina, Vadim N. Tashlitsky, Alena Paleskava, Andrey L. Konevega, Alexey A. Bogdanov, Ilya A. Osterman, Natalia V. Sumbatyan, Yury S. Polikanov
Publikováno v:
Antibiotics, Vol 10, Iss 4, p 390 (2021)
Chloramphenicol (CHL) is a ribosome-targeting antibiotic that binds to the peptidyl transferase center (PTC) of the bacterial ribosome and inhibits peptide bond formation. As an approach for modifying and potentially improving the properties of this
Externí odkaz:
https://doaj.org/article/3bcc4395e05d4903a35a3ea5653542a7
Autor:
Dmitrii Y. Travin, Zoe Watson, Mikhail Metelev, Fred Ward, Ilya A. Osterman, Irina M. Khven, Marina Serebryakova, Yury S. Polikanov
Publikováno v:
International Journal of Biomedicine, Vol 9, Iss Suppl_1, Pp S25-S25 (2019)
Background: Ribosomally synthetized and posttranslationally modified peptides (RiPPs) form a rapidly expanding class of natural products and serve as a source of new compounds with various biological activities. Linear azole-containing peptides (LAPs
Externí odkaz:
https://doaj.org/article/bb16898bcf674795b7069ad7797b4778
Publikováno v:
Frontiers in Molecular Biosciences, Vol 5 (2018)
The ribosome is one of the major targets in the cell for clinically used antibiotics. However, the increase in multidrug resistant bacteria is rapidly reducing the effectiveness of our current arsenal of ribosome-targeting antibiotics, highlighting t
Externí odkaz:
https://doaj.org/article/2a97aa2934e94634a798f15dc96a52f2
Autor:
David Bulkley, Letizia Brandi, Yury S. Polikanov, Attilio Fabbretti, Michael O’Connor, Claudio O. Gualerzi, Thomas A. Steitz
Publikováno v:
Cell Reports, Vol 6, Iss 2, Pp 357-365 (2014)
The translocation of mRNA and tRNA through the ribosome is catalyzed by elongation factor G (EF-G), a universally conserved guanosine triphosphate hydrolase (GTPase). The mechanism by which the closely related decapeptide antibiotics dityromycin and
Externí odkaz:
https://doaj.org/article/0eef0a3e96dd4781ba82132d2fc7a839
Publikováno v:
Nat Chem
During protein synthesis, the growing polypeptide threads through the ribosomal exit tunnel and modulates ribosomal activity by itself or by sensing various small molecules, such as metabolites or antibiotics, appearing in the tunnel. While arrested
Autor:
Kyle Mangano, Dorota Klepacki, Irueosa Ohanmu, Chetana Baliga, Weiping Huang, Alexandra Brakel, Andor Krizsan, Yury S. Polikanov, Ralf Hoffmann, Nora Vázquez-Laslop, Alexander S. Mankin
Publikováno v:
Nature Chemical Biology.
Autor:
Madhura N Paranjpe, Valeria I Marina, Aleksandr A Grachev, Tinashe P Maviza, Olga A Tolicheva, Alena Paleskava, Ilya A Osterman, Petr V Sergiev, Andrey L Konevega, Yury S Polikanov, Matthieu G Gagnon
Publikováno v:
Nucleic acids research.
Thermorubin (THR) is an aromatic anthracenopyranone antibiotic active against both Gram-positive and Gram-negative bacteria. It is known to bind to the 70S ribosome at the intersubunit bridge B2a and was thought to inhibit factor-dependent initiation