Zobrazeno 1 - 10
of 12
pro vyhledávání: '"I. A. Kriklivyi"'
Autor:
Anastasia E. Priss, Mykola M. Ilchenko, Michael Tukalo, K. S. Boyarshin, Igor Dubey, Anna Yaremchuk, I. A. Kriklivyi, Alexsey V. Rayevskiy
Publikováno v:
Journal of Biomolecular Structure and Dynamics. 35:669-682
Aminoacyl tRNA synthetases are enzymes that specifically attach amino acids to cognate tRNAs for use in the ribosomal stage of translation. For many aminoacyl tRNA synthetases, the required level of amino acid specificity is achieved either by specif
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::baec690b13e1b230b93770853e04d061
https://doi.org/10.1080/07391102.2016.1155171
https://doi.org/10.1080/07391102.2016.1155171
Publikováno v:
Biopolymers and Cell, Vol 29, Iss 5, Pp 382-388 (2013)
Aim. To characterize the process of tRNA-dependent pretransfer edi- ting of alanine by prolyl-tRNA synthetase of bacteria Enterococcus faecalis (ProRSEf). Methods. Velocity of the editing processes in vitro was determined by ATP hydrolysis by ProRSEf
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7cd5560760cca7dbe53d15380eb25f12
http://www.biopolymers.org.ua/pdf/ru/29/5/382/
http://www.biopolymers.org.ua/pdf/ru/29/5/382/
Publikováno v:
Biopolymers and Cell, Vol 29, Iss 4, Pp 311-323 (2013)
In prokaryotic cells three tRNA species, tRNASer, tRNALeu and tRNATyr, possess a long variable arm of 11–20 nucleotides (type 2 tRNA) rather than usual 4 or 5 nucleotides (type 1 tRNA). In this review we have summarized the results of our research
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::22b12ce9564b9b41049dc84bba5b1e10
http://biopolymers.org.ua/pdf/en/29/4/311/
http://biopolymers.org.ua/pdf/en/29/4/311/
Publikováno v:
Biopolymers and Cell, Vol 25, Iss 6, Pp 445-450 (2009)
Aim. To elaborate the method of expression and purification of bacteria Enterococcus faecalis tRNAPro transcript. Methods. tRNA, co-expressed in vitro with cis-hydrolytical ribozyme, was purified by high performance liquid chromatography using anion-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::91b7f600157136e0e6c813138d76a080
http://www.biopolymers.org.ua/archive/2009/06/ru/Boyar.pdf
http://www.biopolymers.org.ua/archive/2009/06/ru/Boyar.pdf
Autor:
Alexey Rayevsky, I. A. Kriklivyi, Michael Tukalo, K. S. Boyarshin, A. A. Himin, A. D. Yaremchuk
Publikováno v:
Biopolymers and Cell, Vol 25, Iss 1, Pp 39-43 (2009)
The maintenance of amino acid specificity by aminoacyl-tRNA synthetases can require the hydrolysis of missynthesized products that is known as amino acid editing. Bacterial prolyl-tRNA synthetase includes a special editing domain, that deacylates ala
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f1892685bd2ae2a57601b8e39a6fb120
https://doi.org/10.7124/bc.0007c8
https://doi.org/10.7124/bc.0007c8
Autor:
S. S. Lukashov, Galyna P. Volynets, Andriy G. Golub, Sergiy A. Starosyla, Sergiy M. Yarmoluk, O. I. Gudzera, O. P. Kovalenko, Michail A. Tukalo, Anna Yaremchuk, I. A. Kriklivyi, Volodymyr G. Bdzhola
Publikováno v:
Bioorganicmedicinal chemistry. 24(5)
Tuberculosis is a serious infectious disease caused by human pathogen bacteria Mycobacterium tuberculosis. Bacterial drug resistance is a very significant medical problem nowadays and development of novel antibiotics with different mechanisms of acti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::69ea428cc8003d9e5f2e2fb42d54d859
https://pubmed.ncbi.nlm.nih.gov/26822568
https://pubmed.ncbi.nlm.nih.gov/26822568
Publikováno v:
Biopolymers and Cell. 19:151-156
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1a32c7b427d7b80fb6a5d229c871c566
https://doi.org/10.7124/bc.000647
https://doi.org/10.7124/bc.000647
Publikováno v:
The EMBO Journal. 21:3829-3840
Bacterial tyrosyl-tRNA synthetases (TyrRS) possess a flexibly linked C-terminal domain of approximately 80 residues, which has hitherto been disordered in crystal structures of the enzyme. We have determined the structure of Thermus thermophilus TyrR
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fbc2d70abd2cb922f13b209c1405efcd
https://doi.org/10.1093/emboj/cdf373
https://doi.org/10.1093/emboj/cdf373
Publikováno v:
Biopolymers and Cell. 16:115-123
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8c312735ba63c116f0f1bcfe92249131
https://doi.org/10.7124/bc.00055e
https://doi.org/10.7124/bc.00055e
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 56:197-199
The complex between Thermus thermophilus prolyl-tRNA synthetase (ProRSTT) and its cognate tRNA has been crystallized using two different isoacceptors of tRNA(Pro). Similar bipyramidal crystals of the complexes of ProRSTT with the two different tRNA(P
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67037e594d8bb67ef65619900266489c
https://doi.org/10.1107/s0907444999015504
https://doi.org/10.1107/s0907444999015504