Výsledky vyhledávání - "E V, Petushkova"

Akademický článek

Endodontic retreatment in the appealability structure of the compulsory medical insurance on the example of the state dental practice

Autor: E. V. Ivanova, E. G. Sabantseva, E. V. Petushkova

Publikováno v: Эндодонтия Today, Vol 19, Iss 3, Pp 148-152 (2021)

Aim. To assess the need for repeated endodontic treatment and to determine the possible reasons for the repeated revision of the root canals according to the archival material of the state polyclinic in the period 2015-2020.Materials and methods. Arc

Externí odkaz: https://doaj.org/article/de1cf8fbaa514f4381c97b6b33c2b289

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ZMET-Analysis of Communication Codes of Visual Nature

Autor: A V Fedorova, V A Terentyev, E V Petushkova, S A Afonsky

Publikováno v: Proceedings of the International Scientific Conference "Far East Con" (ISCFEC 2020).

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::42041eb590bbfe1863b5473dcae19f1d
https://doi.org/10.2991/aebmr.k.200312.067

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[Characteristics of affinity modification of myosin ATPase under the action of monoaldehyde derivatives of ADP]

Autor: G M, Pronko, E V, Petushkova

Publikováno v: Biokhimiia (Moscow, Russia). 56(3)

It was shown that the highly purified monoaldehyde derivative of ADP obtained by partial reduction of the dialdehyde derivative of ADP causes strong irreversible inhibition of the Ca-ATPase activity of myosin subfragment I, the inhibiting effect bein

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::2962ad76b3ec43ad2d3062725e704854
https://pubmed.ncbi.nlm.nih.gov/1832050

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[pH-dependence characteristics of Ca-ATPase activity of heavy meromyosin with modified SH-groups]

Autor: T K, Semina, E V, Petushkova

Publikováno v: Biokhimiia (Moscow, Russia). 42(5)

Study of pH-dependence of Ca-ATPase activity of heavy meromyosin (HMM) at low and high ionic strength showed essential differences in the modifying effect of two sulfhydryl reagents, p-CMB and silver. Silver ions in conditions studied independently o

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e64cacc12d96e7d6fda6e292ffc84bf4
https://pubmed.ncbi.nlm.nih.gov/19101

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[Kinetic analysis of hydrolysis of free ATP and MgATP by natural actomyosin]

Autor: E V, Petushkova

Publikováno v: Biokhimiia (Moscow, Russia). 41(12)

Computer analysis of experimental data published in 1-3 allowed to establish the presence of two non-interacting inequivalent hydrolytic sites in actomyosin molecule, one of them being specific for binding and hydrolysis of free ATP, the other--for M

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d3a127718e1067cb2d9e240c288abb42
https://pubmed.ncbi.nlm.nih.gov/139171

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[Early differential diagnosis of gallbladder diseases]

Autor: A I, Purtokas, M F, Smolik, E V, Petushkova

Publikováno v: Sovetskaia meditsina. (3)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::19303340bb2a7ce4c9829880a2f52b6e
https://pubmed.ncbi.nlm.nih.gov/3413560

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[Several peculiarities of the purine-base fixation of the substrate in the active sites of myosin Ca2+-ATPase]

Autor: M N, Grishin, L A, Baranova, N N, Guliaev, E V, Petushkova

Publikováno v: Biokhimiia (Moscow, Russia). 49(11)

A comparative study of kinetic parameters (Km and V) of hydrolysis by heavy meromyosin of several synthetic ATP analogs with substituents at positions N(1) and N(C6) of the purine ring was carried out. Analysis of changes in the Km values suggests th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::2eff2a7c9bc45db3255eb4093a7b11a9
https://pubmed.ncbi.nlm.nih.gov/6240992

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[Kinetics of the interaction of a phosphorylating substrate analog with the Ca-ATPase of myosin and heavy meromyosin]

Autor: V M, Kodentsova, E V, Petushkova

Publikováno v: Nauchnye doklady vysshei shkoly. Biologicheskie nauki. (1)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::c47cd407789e3c396f12ca0daab6297c
https://pubmed.ncbi.nlm.nih.gov/6460531

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[Alkaline activation of myosin ATPase: some thermodynamic characteristics]

Autor: T I, Vlasova, E V, Petushkova

Publikováno v: Biokhimiia (Moscow, Russia). 41(4)

The increase in temperature leads to a decrease in pKa of the group responsible for the activation of CaATP2- hydrolysis by myosin in the alkaline zone of pH. At 20-25 degrees the pKa value is about 9. The value of ionization heat (deltaHi) calculate

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::291925ddbc6e2d194d0c22d268e0f865
https://pubmed.ncbi.nlm.nih.gov/14735

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[Dialdehyde derivatives of purine mononucleotides: substrate properties and affinity modification of myosin ATPase]

Autor: M N, Grishin, V M, Kodentsova, U A, Abdraimova, O P, Nikolaeva, E V, Petushkova

Publikováno v: Biokhimiia (Moscow, Russia). 50(9)

It was demonstrated that the dialdehyde derivative of ATP is a good substrate for Ca-ATPase of heavy meromyosin (Km = (1.2-1.4) X 10(-4) M; V = VATP). At the same time, this compound can induce irreversible inhibition of the enzyme. Since oxo-ATP is

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::3d0e5e4971d45829cda0e9cf0566c16b
https://pubmed.ncbi.nlm.nih.gov/2932167

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