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V I Tishkov

Showing results (41-50 of 61) with videos related to

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Biochemistry. Biokhimiia|December 4, 2002
Effect of interactions between amino acid residues 43 and 61 on thermal stability of bacterial formate dehydrogenasesV V Fedorchuk, A G Galkin, I E Yasny, et al.
Acta Naturae|May 1, 2015
The role of ala198 in the stability and coenzyme specificity of bacterial formate dehydrogenasesA A Alekseeva, V V Fedorchuk, S A Zarubina, et al.
Acta Naturae|January 24, 2014
3D Structure Modeling of Alpha-Amino Acid Ester Hydrolase from Xanthomonas rubrilineansS A Zarubina, I V Uporov, E A Fedorchuk, et al.
Biochemical and Biophysical Research Communications|April 30, 1993
Catalytic properties and stability of a Pseudomonas sp.101 formate dehydrogenase mutants containing Cys-255-Ser and Cys-255-Met replacementsV I Tishkov, A G Galkin, G N Marchenko, et al.
Biochemistry. Biokhimiia|June 24, 2020
Effect of His<sub>6</sub>-tag Position on the Expression and Properties of Phenylacetone Monooxygenase from Thermobifida fuscaP D Parshin, A A Pometun, U A Martysuk, et al.
Biochemistry. Biokhimiia|June 13, 2000
Catalytic properties of tryptophanless recombinant horseradish peroxidaseO V Ignatenko, I G Gazaryan, E A Mareeva, et al.
Acta Crystallographica. Section D, Biological Crystallography|December 8, 2009
Structures of the apo and holo forms of formate dehydrogenase from the bacterium Moraxella sp. C-1: towards understanding the mechanism of the closure of the interdomain cleftI G Shabalin, E V Filippova, K M Polyakov, et al.
Biochemical and Biophysical Research Communications|August 17, 1999
Tryptophanless recombinant horseradish peroxidase: stability and catalytic propertiesI G Gazaryan, T A Chubar, O V Ignatenko, et al.
Biochemistry. Biokhimiia|December 4, 2003
Expression and refolding of tobacco anionic peroxidase from E. coli inclusion bodiesD M Hushpulian, P A Savitski, A M Rojkova, et al.
Acta Naturae|July 26, 2017
Bacteriolytic Activity Of Human Interleukin-2, Chicken Egg Lysozyme In The Presence Of Potential EffectorsP A Levashov, D A Matolygina, E D Ovchinnikova, et al.
Pageof 7

Showing results (41-50 of 61) with videos related to

Sort By:
Pageof 7
Biochemistry. Biokhimiia|December 4, 2002
Effect of interactions between amino acid residues 43 and 61 on thermal stability of bacterial formate dehydrogenasesV V Fedorchuk, A G Galkin, I E Yasny, et al.
Acta Naturae|May 1, 2015
The role of ala198 in the stability and coenzyme specificity of bacterial formate dehydrogenasesA A Alekseeva, V V Fedorchuk, S A Zarubina, et al.
Acta Naturae|January 24, 2014
3D Structure Modeling of Alpha-Amino Acid Ester Hydrolase from Xanthomonas rubrilineansS A Zarubina, I V Uporov, E A Fedorchuk, et al.
Biochemical and Biophysical Research Communications|April 30, 1993
Catalytic properties and stability of a Pseudomonas sp.101 formate dehydrogenase mutants containing Cys-255-Ser and Cys-255-Met replacementsV I Tishkov, A G Galkin, G N Marchenko, et al.
Biochemistry. Biokhimiia|June 24, 2020
Effect of His<sub>6</sub>-tag Position on the Expression and Properties of Phenylacetone Monooxygenase from Thermobifida fuscaP D Parshin, A A Pometun, U A Martysuk, et al.
Biochemistry. Biokhimiia|June 13, 2000
Catalytic properties of tryptophanless recombinant horseradish peroxidaseO V Ignatenko, I G Gazaryan, E A Mareeva, et al.
Acta Crystallographica. Section D, Biological Crystallography|December 8, 2009
Structures of the apo and holo forms of formate dehydrogenase from the bacterium Moraxella sp. C-1: towards understanding the mechanism of the closure of the interdomain cleftI G Shabalin, E V Filippova, K M Polyakov, et al.
Biochemical and Biophysical Research Communications|August 17, 1999
Tryptophanless recombinant horseradish peroxidase: stability and catalytic propertiesI G Gazaryan, T A Chubar, O V Ignatenko, et al.
Biochemistry. Biokhimiia|December 4, 2003
Expression and refolding of tobacco anionic peroxidase from E. coli inclusion bodiesD M Hushpulian, P A Savitski, A M Rojkova, et al.
Acta Naturae|July 26, 2017
Bacteriolytic Activity Of Human Interleukin-2, Chicken Egg Lysozyme In The Presence Of Potential EffectorsP A Levashov, D A Matolygina, E D Ovchinnikova, et al.
Pageof 7