Zobrazeno 1 - 10
of 39
pro vyhledávání: '"S. A. Kurilova"'
Autor:
S. N. Kurilova
Publikováno v:
Научный диалог, Vol 12, Iss 9, Pp 60-76 (2023)
The foreign language insertions in the language of the tundra Yukagirs-polyglots of the Lower Kolyma in Yakutia are considered for the first time. The relevance of the study is primarily dictated by the lack of research on contact phenomena in the Yu
Externí odkaz:
https://doaj.org/article/7851987ff6ac43ae9689d2fd6090eed3
Autor:
S. N. Kurilova
Publikováno v:
Научный диалог, Vol 12, Iss 5, Pp 72-92 (2023)
The linguistic repertoire of the tundra Yukaghir-Polylinguals in Lower Kolyma, Yakutia, with a population of approximately 400 and fewer than 50 speakers, is represented by the Yukaghir, Chukchi, Even, Yakut, and Russian languages. Their speech can b
Externí odkaz:
https://doaj.org/article/4f144a6dc3bf4fdfa81a7e35208d4416
Publikováno v:
Biochemistry (Moscow). 85:326-333
Hexameric inorganic pyrophosphatase from Mycobacterium tuberculosis (Mt-PPase) has a number of structural and functional features that distinguish it from homologous enzymes widely occurring in living organisms. In particular, it has unusual zones of
Autor:
Ekaterina A. Osipova, Viktor A. Anashkin, Anu Salminen, S. A. Kurilova, Ilia D Deltsov, Reijo Lahti, Alexander A. Baykov
Publikováno v:
ACS Omega, Vol 4, Iss 13, Pp 15549-15559 (2019)
ACS Omega
ACS Omega
Inorganic pyrophosphatase containing regulatory cystathionine β-synthase (CBS) domains (CBS-PPase) is inhibited by adenosine monophosphate (AMP) and adenosine diphosphate and activated by adenosine triphosphate (ATP) and diadenosine polyphosphates;
Autor:
Anna V. Vlasova, S. A. Kurilova, Natalia N. Vorobyeva, Alexander A. Baykov, E. V. Rodina, Tatiana I. Nazarova, Viktor A. Anashkin
Publikováno v:
Biochimica et Biophysica Acta (BBA) - General Subjects. 1865:129762
Background Previous studies have demonstrated the formation of stable complexes between inorganic pyrophosphatase (PPase) and three other Escherichia coli enzymes – cupin-type phosphoglucose isomerase (cPGI), class I fructose-1,6-bisphosphate aldol
Autor:
L. A. Dadinova, E. V. Rodina, N. N. Vorobyeva, S. A. Kurilova, T. I. Nazarova, E. V. Shtykova
Publikováno v:
Microsoft Academic Graph
Dihydrolipoamide dehydrogenase from Escherichia coli (LpD) is a bacterial enzyme that is involved in the central metabolism and shared in common between the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes. In the crystal structure,
Autor:
S. A. Kurilova, Galina Ya. Kolomijtseva, Natalia N. Vorobjeva, E. V. Rodina, Anastasia F. Petukhova, Alexander A. Baykov, Tatiana I. Nazarova
Publikováno v:
Biochimica et Biophysica Acta (BBA) - General Subjects. 1864:129601
Background Escherichia coli cells contain a homolog of presumed 5-keto-4-deoxyuronate isomerase (KduI) from pectin-degrading soil bacteria, but the catalytic activity of the E. coli protein (o-KduI) was never demonstrated. Methods The known three-dim
Publikováno v:
Biochemistry. Biokhimiia. 82(8)
Pyrophosphate regulates vital cellular reactions, and its level in E. coli cells is under the ultimate control of inorganic pyrophosphatase. The mechanisms involved in the regulation of pyrophosphatase activity still need to be elucidated. The presen
Autor:
L. A. Dadinova, Tatyana I. Nazarova, Natalia E. Snalina, Natalia N. Vorobyeva, S. A. Kurilova, Petr V. Konarev, E. V. Rodina, Eleonora V. Shtykova, Cy M. Jeffries, Dmitri I. Svergun
Publikováno v:
PLoS ONE
PLoS ONE, Vol 11, Iss 5, p e0156105 (2016)
PLoS one 11(5), e0156105-(2016). doi:10.1371/journal.pone.0156105
PLoS ONE, Vol 11, Iss 5, p e0156105 (2016)
PLoS one 11(5), e0156105-(2016). doi:10.1371/journal.pone.0156105
PLoS one 11(5), e0156105 -(2016). doi:10.1371/journal.pone.0156105
The structural analyses of four metabolic enzymes that maintain and regulate the stationary growth phase of Escherichia coli have been performed primarily drawing on the results
The structural analyses of four metabolic enzymes that maintain and regulate the stationary growth phase of Escherichia coli have been performed primarily drawing on the results
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f168a4d97f0efce3348888b7b38855dd
Publikováno v:
Biochemistry (Moscow). 74:734-742
In this paper, kinetic properties of a soluble inorganic pyrophosphatase of family I from Vibrio cholerae (V-PPase), intestinal pathogen and causative agent of human cholera, are characterized in detail, and the crystal structure of a metal-free enzy