Výsledky vyhledávání - "Yulia К. Agapova"

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

Autor: David M. Karlinsky, Vladimir I. Timofeev, Lev D. Rumsh, Yulia К. Agapova, A. G. Mikhailova, Aleksandr S. Komolov, Tatiana V. Rakitina, D.E. Petrenko, D.A. Korzhenevskiy, Anna V. Vlaskina

Oligopeptidases B (OpdBs) are trypsin-like peptidases from protozoa and bacteria that belong to the prolyl oligopeptidase (POP) family. All POPs consist of C-terminal catalytic domain and N-terminal β-propeller domain and exist in two major conforma

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5fc870a6792cdd4a741171e79995900c

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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

Autor: D.A. Korzhenevskiy, Valentina A. Gorlenko, Anna V. Vlaskina, Yulia К. Agapova, Marina V. Ovchinnikova, David M. Karlinsky, Tatiana V. Rakitina, Lev D. Rumsh, A. G. Mikhailova, Vladimir I. Timofeev

Publikováno v: Biochimie. 139

Oligopeptidase B (OpdB; EC 3.4.21.83) is a trypsin-like peptidase belonging to the family of serine prolyl oligopeptidases; two-domain structure of the enzyme includes C-terminal peptidase catalytic domain and N-terminal seven-bladed β-propeller dom

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2f20fbe398e8308797fd8241b7b29ab2
https://pubmed.ncbi.nlm.nih.gov/28554571

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Comparison of histone-like HU protein DNA-binding properties and HU/IHF protein sequence alignment

Autor: Konstantin M. Boyko, Sergey M. Rastorguev, A. A. Talyzina, Tatiana V. Rakitina, Dmitri E. Kamashev, Yulia К. Agapova, D.A. Korzhenevskiy, Anna V. Vlaskina, R. G. Vasilov, Vladimir I. Timofeev

Publikováno v: PLoS ONE
PLoS ONE, Vol 12, Iss 11, p e0188037 (2017)

Background The structure and function of bacterial nucleoid are controlled by histone-like proteins of HU/IHF family, omnipresent in bacteria and also founding archaea and some eukaryotes.HU protein binds dsDNA without sequence specificity and avidly

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3b818db1711222b3acb36872823c22b1
https://doi.org/10.1371/journal.pone.0188037

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