Search Results - "Karlinsky, David M." :: K.UTB vyhledávací portál

Crystal Structure of Inhibitor-Bound Bacterial Oligopeptidase B in the Closed State: Similarity and Difference between Protozoan and Bacterial Enzymes

by Petrenko, Dmitry E, Karlinsky, David M, Gordeeva, Veronika D, Arapidi, Georgij P, Britikova, Elena V, Britikov, Vladimir V, Nikolaeva, Alena Y, Boyko, Konstantin M, Timofeev, Vladimir I, Kuranova, Inna P, Mikhailova, Anna G, Bocharov, Eduard V, Rakitina, Tatiana V
Published in International journal of molecular sciences (24.01.2023)

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The Crystal Structure of Nα-p-tosyl-lysyl Chloromethylketone-Bound Oligopeptidase B from Serratia Proteamaculans Revealed a New Type of Inhibitor Binding

by Timofeev, Vladimir, Petrenko, Dmitry, Agapova, Yulia, Vlaskina, Anna, Karlinsky, David, Mikhailova, Anna, Kuranova, Inna, Rakitina, Tatiana
Published in Crystals (Basel) (01.11.2021)

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Activity modulation of the oligopeptidase B from Serratia proteamaculans by site-directed mutagenesis of amino acid residues surrounding catalytic triad histidine

by Mikhailova, Anna G., Rakitina, Tatiana V., Timofeev, Vladimir I., Karlinsky, David M., Korzhenevskiy, Dmitry A., Agapova, Yulia К., Vlaskina, Anna V., Ovchinnikova, Marina V., Gorlenko, Valentina A., Rumsh, Lev D.
Published in Biochimie (01.08.2017)

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Molecular dynamics complemented by site-directed mutagenesis reveals significant difference between the interdomain salt bridge networks stabilizing oligopeptidases B from bacteria and protozoa in their active conformations

by Petrenko, Dmitry E., Mikhailova, Anna G., Timofeev, Vladimir I., Agapova, Yulia К., Karlinsky, David M., Komolov, Aleksandr S., Korzhenevskiy, Dmitry A., Vlaskina, Anna V., Rumsh, Lev D., Rakitina, Tatiana V.
Published in Journal of biomolecular structure & dynamics (01.11.2020)

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Crystal Structure of Inhibitor-Bound Bacterial Oligopeptidase B in the Closed State: Similarity and Difference between Protozoan and Bacterial Enzymes

The Crystal Structure of Nα-p-tosyl-lysyl Chloromethylketone-Bound Oligopeptidase B from Serratia Proteamaculans Revealed a New Type of Inhibitor Binding

Activity modulation of the oligopeptidase B from Serratia proteamaculans by site-directed mutagenesis of amino acid residues surrounding catalytic triad histidine

Molecular dynamics complemented by site-directed mutagenesis reveals significant difference between the interdomain salt bridge networks stabilizing oligopeptidases B from bacteria and protozoa in their active conformations

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