Suivre
Dmitry Baitin
Dmitry Baitin
Autres nomsДМ Байтин
Peter the Great St.Petersburg Polytechnic University
Adresse e-mail validée de nanobio.spbstu.ru
Titre
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Année
A novel function of DNA polymerase ζ regulated by PCNA
MR Northam, P Garg, DM Baitin, PMJ Burgers, PV Shcherbakova
The EMBO journal 25 (18), 4316-4325, 2006
1162006
Systematic search for structural motifs of peptide binding to double-stranded DNA
N Kolchina, V Khavinson, N Linkova, A Yakimov, D Baitin, A Afanasyeva, ...
Nucleic Acids Research 47 (20), 10553-10563, 2019
542019
Blocking the RecA activity and SOS-response in bacteria with a short α-helical peptide
A Yakimov, G Pobegalov, I Bakhlanova, M Khodorkovskii, M Petukhov, ...
Nucleic acids research 45 (16), 9788-9796, 2017
402017
Biochemical basis of hyper‐recombinogenic activity of Pseudomonas aeruginosa RecA protein in Escherichia coli cells
EA Namsaraev, D Baitin, IV Bakhlanova, AA Alexseyev, H Ogawa, ...
Molecular microbiology 27 (4), 727-738, 1998
341998
Efficient Strand Transfer by the RadA Recombinase from the Hyperthermophilic Archaeon Desulfurococcus amylolyticus
YV Kil, DM Baitin, R Masui, EA Bonch-Osmolovskaya, S Kuramitsu, ...
Journal of Bacteriology 182 (1), 130-134, 2000
332000
Analytical model for determination of parameters of helical structures in solution by small angle scattering: comparison of RecA structures by SANS
DV Lebedev, DM Baitin, AK Islamov, AI Kuklin, VK Shalguev, VA Lanzov, ...
FEBS letters 537 (1-3), 182-186, 2003
282003
SSB antagonizes RecX-RecA interaction
DM Baitin, MC Gruenig, MM Cox
Journal of biological chemistry 283 (21), 14198-14204, 2008
242008
Targeting evolution of antibiotic resistance by SOS response inhibition
A Yakimov, I Bakhlanova, D Baitin
Computational and structural biotechnology journal 19, 777-783, 2021
202021
Structure of RecX protein complex with the presynaptic RecA filament: Molecular dynamics simulations and small angle neutron scattering
AV Shvetsov, DV Lebedev, DB Chervyakova, IV Bakhlanova, IA Yung, ...
FEBS letters 588 (6), 948-955, 2014
202014
Modulating cellular recombination potential through alterations in RecA structure and regulation
IV Bakhlanova, AV Dudkina, DM Baitin, KL Knight, MM Cox, VA Lanzov
Molecular microbiology 78 (6), 1523-1538, 2010
192010
Hyper-recombinogenic RecA protein from Pseudomonas aeruginosa with enhanced activity of its primary DNA binding site
DM Baitin, EN Zaitsev, VA Lanzov
Journal of molecular biology 328 (1), 1-7, 2003
192003
Deinococcus radiodurans RecA nucleoprotein filaments characterized at the single-molecule level with optical tweezers
G Pobegalov, G Cherevatenko, A Alekseev, A Sabantsev, O Kovaleva, ...
Biochemical and biophysical research communications 466 (3), 426-430, 2015
172015
Distinguishing Characteristics of Hyperrecombinogenic RecA Protein from Pseudomonas aeruginosa Acting in Escherichia coli
DM Baitin, IV Bakhlanova, YV Kil, MM Cox, VA Lanzov
Journal of bacteriology 188 (16), 5812-5820, 2006
172006
Fluorescence and excitation Escherichia coli RecA protein spectra analyzed separately for tyrosine and tryptophan residues
VV Isaev-Ivanov, MG Kozlov, DM Baitin, R Masui, S Kuramitsu, VA Lanzov
Archives of Biochemistry and Biophysics 376 (1), 124-140, 2000
162000
Two RecA protein types that mediate different modes of hyperrecombination
DM Baitin, IV Bakhlanova, DV Chervyakova, YV Kil, VA Lanzov, MM Cox
Journal of bacteriology 190 (8), 3036-3045, 2008
152008
A recombinational defect in the C‐terminal domain of Escherichia coli RecA2278‐5 protein is compensated by protein binding to ATP
AA Alexseyev, DM Baitin, S Kuramitsu, T Ogawa, H Ogawa, VA Lanzov
Molecular microbiology 23 (2), 255-265, 1997
121997
A new insight into RecA filament regulation by RecX from the analysis of conformation-specific interactions
A Alekseev, G Pobegalov, N Morozova, A Vedyaykin, G Cherevatenko, ...
Elife 11, e78409, 2022
72022
DNA metabolism in balance: Rapid loss of a RecA-based hyperrec phenotype
IV Bakhlanova, AV Dudkina, EA Wood, VA Lanzov, MM Cox, DM Baitin
Plos one 11 (4), e0154137, 2016
62016
Single‐molecule analysis reveals two distinct states of the compressed RecA filament on single‐stranded DNA
A Alekseev, M Serdakov, G Pobegalov, A Yakimov, I Bakhlanova, D Baitin, ...
FEBS letters 594 (21), 3464-3476, 2020
42020
Enzymatic control of homologous recombination in Escherichia coli cells and hyper-recombination
IV Bakhlanova, AV Dudkina, DM Baĭtin
Molekuliarnaia Biologiia 47 (2), 205-217, 2013
42013
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