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Irina A. Sevostyanova
Researcher at Moscow State University
Publications - 20
Citations - 173
Irina A. Sevostyanova is an academic researcher from Moscow State University. The author has contributed to research in topics: Transketolase & Substrate (chemistry). The author has an hindex of 8, co-authored 19 publications receiving 137 citations.
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Binding of the coenzyme and formation of the transketolase active center.
TL;DR: This review summarizes the results of studies on the kinetics of the interaction of ThDP with TK from Saccharomyces cerevisae as well as the generation of the catalytically active form of the coenzyme within the holoenzyme and formation of the enzyme's active center.
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A hitherto unknown transketolase-catalyzed reaction.
TL;DR: Yeast transketolase, in addition to catalyzing the transferase reaction through utilization of two substrates--the donor substrate (ketose) and the acceptor substrate (aldose)--is also able to catalyze a one-substrate reaction with only aldose (glycolaldehyde) as substrate.
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Natural and Synthetic Derivatives of Hydroxycinnamic Acid Modulating the Pathological Transformation of Amyloidogenic Proteins.
Vladimir I. Muronetz,K.V. Barinova,S. S. Kudryavtseva,Maria Medvedeva,Aleksandra K. Melnikova,Irina A. Sevostyanova,Pavel I. Semenyuk,Yulia Yu. Stroylova,Yulia Yu. Stroylova,Matej Sova +9 more
TL;DR: The ability of HCA derivatives to preventAmyloid transformation of some amyloidogenic proteins, and their presence not only in food products but also as natural metabolites in human blood and tissues, makes them promising for the prevention and treatment of neurodegenerative diseases of amyloids nature.
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Sperm-specific glyceraldehyde-3-phosphate dehydrogenase is expressed in melanoma cells
Irina A. Sevostyanova,Kseniya V. Kulikova,M.L. Kuravsky,Elena V. Schmalhausen,Vladimir I. Muronetz +4 more
TL;DR: The results suggest that GAPDS is expressed in melanoma cells without N-terminal domain, and indicates that melanoma Cells express both isoenzymes, which results in the formation of heterotetrameric complexes.
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Effect of bivalent cations on the interaction of transketolase with its donor substrate.
Irina A. Sevostyanova,Vladimir A. Yurshev,Olga N. Solovjeva,Svetlana V. Zabrodskaya,German A. Kochetov +4 more
TL;DR: In the presence of magnesium, the active centers of the enzyme were functionally equivalent with respect to xylulose 5‐phosphate binding and exhibited identical affinities for the donor substrate, but substitution of Ca2+ for Mg2+ results in the loss of the equivalence.