Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Dmitry M. Baitin"'
Publikováno v:
Computational and Structural Biotechnology Journal, Vol 19, Iss, Pp 777-783 (2021)
Computational and Structural Biotechnology Journal
Computational and Structural Biotechnology Journal
Antibiotic resistance is acquired in response to antibiotic therapy by activating SOS-depended mutagenesis and horizontal gene transfer pathways. Compounds able to inhibit SOS response are extremely important to develop new combinatorial strategies a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cb39aa724e800477cf3d376c14c6c8f7
http://www.sciencedirect.com/science/article/pii/S2001037021000076
http://www.sciencedirect.com/science/article/pii/S2001037021000076
Autor:
Irina V Bakhlanova, Alexandra V Dudkina, Elizabeth A Wood, Vladislav A Lanzov, Michael M Cox, Dmitry M Baitin
Publikováno v:
PLoS ONE, Vol 11, Iss 4, p e0154137 (2016)
The RecA recombinase of Escherichia coli has not evolved to optimally promote DNA pairing and strand exchange, the key processes of recombinational DNA repair. Instead, the recombinase function of RecA protein represents an evolutionary compromise be
Externí odkaz:
https://doaj.org/article/7086179af1704635832daaad2efa9e8e
Autor:
Irina V. Bakhlanova, Mikhail Khodorkovskii, Maksim Serdakov, Aleksandr Alekseev, Georgii Pobegalov, Alexandr Yakimov, Dmitry M. Baitin
Publikováno v:
FEBS Letters. 594:3464-3476
The RecA protein plays a key role in bacterial homologous recombination (HR) and acts through assembly of long helical filaments around single-stranded DNA in the presence of ATP. Large-scale conformational changes induced by ATP hydrolysis result in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4ed29056f365b94cbdb01c7dd38e41b0
https://doi.org/10.1002/1873-3468.13922
https://doi.org/10.1002/1873-3468.13922
Autor:
Khavinson Vladimir Kh, Michael Petukhov, Nina Kolchina, Natalia Linkova, Alexander Yakimov, Arina Afanasyeva, Dmitry M. Baitin
Publikováno v:
Nucleic Acids Research
A large variety of short biologically active peptides possesses antioxidant, antibacterial, antitumour, anti-ageing and anti-inflammatory activity, involved in the regulation of neuro-immuno-endocrine system functions, cell apoptosis, proliferation a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2f3b07bec9e1220d53b3a22b2ed50d42
https://doi.org/10.1093/nar/gkz850
https://doi.org/10.1093/nar/gkz850
Autor:
Georgii Pobegalov, Alexander Yakimov, Dmitry M. Baitin, Irina V. Bakhlanova, Michael Petukhov, Mikhail Khodorkovskii
Publikováno v:
Nucleic Acids Research
The RecX protein, a very active natural RecA protein inhibitor, can completely disassemble RecA filaments at nanomolar concentrations that are two to three orders of magnitude lower than that of RecA protein. Based on the structure of RecX protein co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::94544ac86c15e8c08f8fd1ac1c2d7e92
https://doi.org/10.1093/nar/gkx687
https://doi.org/10.1093/nar/gkx687
Autor:
Maksim Serdakov, Aleksandr Alekseev, Galina Cherevatenko, Georgii Pobegalov, Irina V. Bakhlanova, Mikhail Khodorkovskii, Alexander Yakimov, Dmitry M. Baitin
Publikováno v:
International Journal of Molecular Sciences
Volume 21
Issue 19
International Journal of Molecular Sciences, Vol 21, Iss 7389, p 7389 (2020)
Volume 21
Issue 19
International Journal of Molecular Sciences, Vol 21, Iss 7389, p 7389 (2020)
Deinococcus radiodurans (Dr) has one of the most robust DNA repair systems, which is capable of withstanding extreme doses of ionizing radiation and other sources of DNA damage. DrRecA, a central enzyme of recombinational DNA repair, is essential for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c62eeef03c40c0ecb567ed8434ebb347
https://doi.org/10.3390/ijms21197389
https://doi.org/10.3390/ijms21197389
Publikováno v:
Molecular Biology. 47:181-191
The RecA protein is a central homologous recombination enzyme in the bacterial cell. Forming a right-handed filament on ssDNA, RecA provides for a homology search between two DNA molecules and homologous strand exchange. RecA protects the cell from i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6e006fdf42193be5db6dc03be8004cd5
https://doi.org/10.1134/s0026893313020039
https://doi.org/10.1134/s0026893313020039
Autor:
Elizabeth A. Wood, Vladislav A. Lanzov, Dmitry M. Baitin, Michael M. Cox, Irina V. Bakhlanova, Alexandra V. Dudkina
Publikováno v:
PLoS ONE, Vol 11, Iss 4, p e0154137 (2016)
PLoS ONE
PLoS ONE
The RecA recombinase of Escherichia coli has not evolved to optimally promote DNA pairing and strand exchange, the key processes of recombinational DNA repair. Instead, the recombinase function of RecA protein represents an evolutionary compromise be
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a40f855bf417988c5849c69a2873345c
http://europepmc.org/articles/PMC4849656?pdf=render
http://europepmc.org/articles/PMC4849656?pdf=render
Publikováno v:
Molecular Biology. 45:500-507
It was discovered that the mutant D112R RecA protein is more resistant to the action of its negative regulator, the RecX protein, than wild type protein both in vitro and in vivo. By means of molecular modeling methods, we showed that amino-acid resi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::14f41df956b9c0d81c02e41c14ab138b
https://doi.org/10.1134/s0026893311030046
https://doi.org/10.1134/s0026893311030046
Publikováno v:
Journal of Biological Chemistry. 283:14198-14204
The RecX protein of Escherichia coli inhibits the extension of RecA protein filaments on DNA, presumably by binding to and blocking the growing filament end. The direct binding of RecX protein to single-stranded DNA is weak, and previous reports sugg
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f7405821ae2aa7582ea530882c4c7ce1
https://doi.org/10.1074/jbc.m801511200
https://doi.org/10.1074/jbc.m801511200