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V I Tishkov

Showing results (51-60 of 61) with videos related to

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Biochimie|December 24, 2016
Structure-activity relationship for branched oxyquinoline HIF activators: Effect of modifications to phenylacetamide "tail"A A Poloznikov, A A Zakhariants, S V Nikulin, et al.
Prikladnaia Biokhimiia I Mikrobiologiia|August 2, 2006
[A comparative study of the thermal stability of formate dehydrogenases from microorganisms and plants]E G Sadykhov, A E Serov, N S Voĭnova, et al.
Biochemistry. Biokhimiia|June 27, 2020
Highly-Active Recombinant Formate Dehydrogenase from Pathogenic Bacterium Staphylococcus aureus: Preparation and CrystallizationA A Pometun, K M Boyko, T S Yurchenko, et al.
Journal of Chromatography. A|November 25, 2025
Development of hydrophilic interaction liquid chromatography method for determining enzymatic activity of cysteine synthase AA V Chernobrovkina, A V Gorbovskaia, N Yu Chikurova, et al.
FEBS Letters|July 15, 1996
Site-directed mutagenesis of the formate dehydrogenase active centre: role of the His332-Gln313 pair in enzyme catalysisV I Tishkov, A D Matorin, A M Rojkova, et al.
Antibiotiki I Khimioterapiia = Antibiotics and Chemoterapy [Sic]|November 29, 2005
[Etiology of severe hospital infections in intensive care units and antibiotic resistance of pathogens]S V Sidorenko, S P Rezvan, L V Eremina, et al.
Acta Naturae|April 20, 2022
Effect of Additional Amino Acid Replacements on the Properties of Multi-point Mutant Bacterial Formate Dehyderogenase PseFDH SM4SA A Pometun, P D Parshin, N P Galanicheva, et al.
Biochemistry. Biokhimiia|October 18, 2017
Enzyme-Substrate Reporters for Evaluation of Substrate Specificity of HIF Prolyl Hydroxylase IsoformsA I Osipyants, N A Smirnova, A Yu Khristichenko, et al.
Acta Naturae|January 25, 2023
Bioinformatics-Structural Approach to the Search for New D-Amino Acid OxidasesD L Atroshenko, D I Golovina, E P Sergeev, et al.
Biochemical and Biophysical Research Communications|June 6, 2022
The role of Tyr102 residue in the functioning of bacterial NAD<sup>+</sup>-dependent formate dehydrogenase of Pseudomonas sp. 101А V Popinako, А А Pometun, D K Nilov, et al.
Pageof 7

Showing results (51-60 of 61) with videos related to

Sort By:
Pageof 7
Biochimie|December 24, 2016
Structure-activity relationship for branched oxyquinoline HIF activators: Effect of modifications to phenylacetamide "tail"A A Poloznikov, A A Zakhariants, S V Nikulin, et al.
Prikladnaia Biokhimiia I Mikrobiologiia|August 2, 2006
[A comparative study of the thermal stability of formate dehydrogenases from microorganisms and plants]E G Sadykhov, A E Serov, N S Voĭnova, et al.
Biochemistry. Biokhimiia|June 27, 2020
Highly-Active Recombinant Formate Dehydrogenase from Pathogenic Bacterium Staphylococcus aureus: Preparation and CrystallizationA A Pometun, K M Boyko, T S Yurchenko, et al.
Journal of Chromatography. A|November 25, 2025
Development of hydrophilic interaction liquid chromatography method for determining enzymatic activity of cysteine synthase AA V Chernobrovkina, A V Gorbovskaia, N Yu Chikurova, et al.
FEBS Letters|July 15, 1996
Site-directed mutagenesis of the formate dehydrogenase active centre: role of the His332-Gln313 pair in enzyme catalysisV I Tishkov, A D Matorin, A M Rojkova, et al.
Antibiotiki I Khimioterapiia = Antibiotics and Chemoterapy [Sic]|November 29, 2005
[Etiology of severe hospital infections in intensive care units and antibiotic resistance of pathogens]S V Sidorenko, S P Rezvan, L V Eremina, et al.
Acta Naturae|April 20, 2022
Effect of Additional Amino Acid Replacements on the Properties of Multi-point Mutant Bacterial Formate Dehyderogenase PseFDH SM4SA A Pometun, P D Parshin, N P Galanicheva, et al.
Biochemistry. Biokhimiia|October 18, 2017
Enzyme-Substrate Reporters for Evaluation of Substrate Specificity of HIF Prolyl Hydroxylase IsoformsA I Osipyants, N A Smirnova, A Yu Khristichenko, et al.
Acta Naturae|January 25, 2023
Bioinformatics-Structural Approach to the Search for New D-Amino Acid OxidasesD L Atroshenko, D I Golovina, E P Sergeev, et al.
Biochemical and Biophysical Research Communications|June 6, 2022
The role of Tyr102 residue in the functioning of bacterial NAD<sup>+</sup>-dependent formate dehydrogenase of Pseudomonas sp. 101А V Popinako, А А Pometun, D K Nilov, et al.
Pageof 7