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Olga V. Belyaeva
Researcher at University of Alabama at Birmingham
Publications - 51
Citations - 1557
Olga V. Belyaeva is an academic researcher from University of Alabama at Birmingham. The author has contributed to research in topics: Retinol dehydrogenase & Retinoic acid. The author has an hindex of 21, co-authored 46 publications receiving 1333 citations. Previous affiliations of Olga V. Belyaeva include Russian Academy of Sciences & University of Missouri–Kansas City.
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Journal ArticleDOI
17-Beta Hydroxysteroid Dehydrogenase 13 Is a Hepatic Retinol Dehydrogenase Associated With Histological Features of Nonalcoholic Fatty Liver Disease
Yanling Ma,Olga V. Belyaeva,Philip M. Brown,Koji Fujita,Katherine Valles,Suman Karki,Ynto S. de Boer,Christopher Koh,Yanhua Chen,Xiaomeng Du,Samuel K. Handelman,Vincent L. Chen,Elizabeth K. Speliotes,Cara Nestlerode,Emmanuel Thomas,David E. Kleiner,Joseph M. Zmuda,Arun J. Sanyal,Natalia Y. Kedishvili,T. Jake Liang,Yaron Rotman +20 more
TL;DR: The association of variants in HSD17B13 with specific features of NAFLD histology is demonstrated and the enzyme is identified as a lipid droplet–associated RDH; the data suggest that HSD 17B13 plays a role inNAFLD through its enzymatic activity.
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Comparative functional analysis of human medium-chain dehydrogenases, short-chain dehydrogenases/reductases and aldo-keto reductases with retinoids.
Oriol Gallego,Olga V. Belyaeva,Sergio Porté,F. Xavier Ruiz,Anton V. Stetsenko,Elena V. Shabrova,Natalia V. Kostereva,Jaume Farrés,Xavier Parés,Natalia Y. Kedishvili +9 more
TL;DR: It is demonstrated that none of the enzymes, including the SDR members, are active withCRBPI-bound retinoids, which questions the previously suggested role of CRBPI as a retinol supplier in the retinoic acid synthesis pathway.
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Biochemical properties of purified human retinol dehydrogenase 12 (RDH12) : Catalytic efficiency toward retinoids and C9 aldehydes and effects of cellular retinol-binding protein type I (CRBPI) and cellular retinaldehyde-binding protein (CRALBP) on the oxidation and reduction of retinoids
Olga V. Belyaeva,Olga V. Korkina,Anton V. Stetsenko,Tom S. Kim,Peter S. Nelson,Natalia Y. Kedishvili +5 more
TL;DR: Tissue distribution of RDH12 and its catalytic properties suggest that, in most tissues,RDH12 primarily contributes to the reduction of all-trans-retinaldehyde; however, at saturating concentrations of peroxidic aldehydes in the cells undergoing oxidative stress, for example, photoreceptors, RDH 12 might also play a role in detoxification of lipid peroxidation products.
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Lipoprotein particles of intraocular origin in human Bruch membrane: an unusual lipid profile.
L. Wang,Chuan-Ming Li,Martin Rudolf,Olga V. Belyaeva,Byung Hong Chung,Jeffrey D. Messinger,Natalia Y. Kedishvili,Christine A. Curcio +7 more
TL;DR: Analysis of BrM-LLP composition has revealed new aspects of retinal cholesterol and retinoid homeostasis, and an EC-rich core is possible for newly synthesized lipoproteins as well as those processed in plasma.
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The retinaldehyde reductase activity of DHRS3 is reciprocally activated by retinol dehydrogenase 10 to control retinoid homeostasis.
TL;DR: It is demonstrated that DHRS3 requires the presence of retinol dehydrogenase 10 (RDH10) to display its full catalytic activity and, in turn, activates RDH10, which acts as a robust high affinity all-trans-retinaldehyde-specific reductase that effectively converts retinal dehyde back to retinl, decreasing the rate of retinoic acid biosynthesis.