Natalia Y. Kedishvili - Publications

Affiliations: 
Biochemistry and Molecular Genetics University of Alabama, Birmingham, Birmingham, AL, United States 
Area:
Cell Biology, Biochemistry

49 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2021 Belyaeva OV, Wirth SE, Boeglin WE, Karki S, Goggans KR, Wendell SG, Popov KM, Brash AR, Kedishvili NY. Dehydrogenase reductase 9 (SDR9C4) and related homologs recognize a broad spectrum of lipid mediator oxylipins as substrates. The Journal of Biological Chemistry. 298: 101527. PMID 34953854 DOI: 10.1016/j.jbc.2021.101527  0.343
2020 Ma Y, Brown PM, Lin DD, Ma J, Feng D, Belyaeva OV, Podszun MC, Roszik J, Allen J, Umarova R, Kleiner DE, Kedishvili NY, Gavrilova O, Gao B, Rotman Y. Hsd17b13 Deficiency Does not Protect Mice From Obesogenic Diet Injury. Hepatology (Baltimore, Md.). PMID 32779242 DOI: 10.1002/Hep.31517  0.309
2020 Adams MK, Belyaeva OV, Kedishvili NY. Generation and isolation of recombinant retinoid oxidoreductase complex. Methods in Enzymology. 637: 77-93. PMID 32359661 DOI: 10.1016/Bs.Mie.2020.02.005  0.404
2020 Klyuyeva AV, Goggans KR, Kedishvili NY, Belyaeva OV. Application of human organotypic skin raft cultures for analysis of retinoid metabolism, retinoic acid signaling, and screening of bioactive rexinoids. Methods in Enzymology. 637: 493-512. PMID 32359656 DOI: 10.1016/Bs.Mie.2020.02.013  0.511
2019 Belyaeva OV, Adams MK, Popov KM, Kedishvili NY. Generation of Retinaldehyde for Retinoic Acid Biosynthesis. Biomolecules. 10. PMID 31861321 DOI: 10.3390/biom10010005  0.301
2019 Wu L, Belyaeva OV, Adams MK, Klyuyeva A, Lee SA, Goggans KR, Kesterson RA, Popov KM, Kedishvili NY. Mice lacking the epidermal retinol dehydrogenases SDR16C5 and SDR16C6 display accelerated hair growth and enlarged meibomian glands. The Journal of Biological Chemistry. PMID 31562240 DOI: 10.1074/Jbc.Ra119.010835  0.602
2019 Wu L, Kedishvili NY, Belyaeva OV. Retinyl esters are elevated in progeny of retinol dehydrogenase 11 deficient dams. Chemico-Biological Interactions. PMID 30731079 DOI: 10.1016/J.Cbi.2019.01.041  0.393
2018 Klyuyeva A, Tuganova A, Kedishvili N, Popov KM. Tissue-specific kinase expression and activity regulate flux through the pyruvate dehydrogenase complex. The Journal of Biological Chemistry. 294: 838-851. PMID 30482839 DOI: 10.1074/Jbc.Ra118.006433  0.34
2018 Ma Y, Belyaeva OV, Brown PM, Fujita K, Valles K, Karki S, de Boer YS, Koh C, Chen Y, Du X, Handelman SK, Chen V, Speliotes EK, Nestlerode C, Thomas E, ... ... Kedishvili NY, et al. HSD17B13 is a Hepatic Retinol Dehydrogenase Associated with Histological Features of Non-Alcoholic Fatty Liver Disease. Hepatology (Baltimore, Md.). PMID 30415504 DOI: 10.1002/Hep.30350  0.345
2018 Belyaeva OV, Wu L, Shmarakov I, Nelson PS, Kedishvili NY. Retinol dehydrogenase 11 is essential for the maintenance of retinol homeostasis in liver and testis in mice. The Journal of Biological Chemistry. PMID 29567832 DOI: 10.1074/Jbc.Ra117.001646  0.356
2017 Belyaeva OV, Adams MK, Wu L, Kedishvili NY. The Antagonistically Bifunctional Retinoid Oxidoreductase Complex Is Required for Maintenance of All-trans-retinoic Acid Homeostasis. The Journal of Biological Chemistry. PMID 28232491 DOI: 10.1074/Jbc.M117.776914  0.379
2016 Kedishvili NY. Retinoic Acid Synthesis and Degradation. Sub-Cellular Biochemistry. 81: 127-161. PMID 27830503 DOI: 10.1007/978-94-024-0945-1_5  0.39
2016 Adams MK, Lee SA, Belyaeva OV, Wu L, Kedishvili NY. Characterization of human short chain dehydrogenase/reductase SDR16C family members related to retinol dehydrogenase 10. Chemico-Biological Interactions. PMID 27793605 DOI: 10.1016/J.Cbi.2016.10.019  0.577
2016 Martí-Solans J, Belyaeva OV, Torres-Aguila NP, Kedishvili NY, Albalat R, Cañestro C. Co-elimination and survival in gene network evolution: dismantling the RA-signaling in a chordate. Molecular Biology and Evolution. PMID 27406791 DOI: 10.1093/Molbev/Msw118  0.317
2016 Wu L, Chaudhary SC, Atigadda VR, Belyaeva OV, Harville SR, Elmets CA, Muccio DD, Athar M, Kedishvili NY. Retinoid X Receptor Agonists Upregulate Genes Responsible for the Biosynthesis of All-Trans-Retinoic Acid in Human Epidermis. Plos One. 11: e0153556. PMID 27078158 DOI: 10.1371/Journal.Pone.0153556  0.351
2015 Belyaeva OV, Chang C, Berlett MC, Kedishvili NY. Evolutionary origins of retinoid active short-chain dehydrogenases/reductases of SDR16C family. Chemico-Biological Interactions. 234: 135-43. PMID 25451586 DOI: 10.1016/J.Cbi.2014.10.026  0.468
2014 Adams MK, Belyaeva OV, Wu L, Kedishvili NY. The retinaldehyde reductase activity of DHRS3 is reciprocally activated by retinol dehydrogenase 10 to control retinoid homeostasis. The Journal of Biological Chemistry. 289: 14868-80. PMID 24733397 DOI: 10.1074/Jbc.M114.552257  0.494
2013 Kedishvili NY. Enzymology of retinoic acid biosynthesis and degradation. Journal of Lipid Research. 54: 1744-60. PMID 23630397 DOI: 10.1194/Jlr.R037028  0.489
2012 Belyaeva OV, Lee SA, Adams MK, Chang C, Kedishvili NY. Short chain dehydrogenase/reductase rdhe2 is a novel retinol dehydrogenase essential for frog embryonic development. The Journal of Biological Chemistry. 287: 9061-71. PMID 22291023 DOI: 10.1074/Jbc.M111.336727  0.608
2011 Lee SA, Belyaeva OV, Wu L, Kedishvili NY. Retinol dehydrogenase 10 but not retinol/sterol dehydrogenase(s) regulates the expression of retinoic acid-responsive genes in human transgenic skin raft culture. The Journal of Biological Chemistry. 286: 13550-60. PMID 21345790 DOI: 10.1074/Jbc.M110.181065  0.591
2011 Lee SA, Belyaeva OV, Kedishvili NY. Evidence that proteosome inhibitors and chemical chaperones can rescue the activity of retinol dehydrogenase 12 mutant T49M. Chemico-Biological Interactions. 191: 55-9. PMID 21232531 DOI: 10.1016/J.Cbi.2011.01.001  0.567
2010 Lee SA, Belyaeva OV, Kedishvili NY. Disease-associated variants of microsomal retinol dehydrogenase 12 (RDH12) are degraded at mutant-specific rates. Febs Letters. 584: 507-10. PMID 20006610 DOI: 10.1016/J.Febslet.2009.12.009  0.528
2009 Belyaeva OV, Lee SA, Kolupaev OV, Kedishvili NY. Identification and characterization of retinoid-active short-chain dehydrogenases/reductases in Drosophila melanogaster. Biochimica Et Biophysica Acta. 1790: 1266-73. PMID 19520149 DOI: 10.1016/J.Bbagen.2009.06.002  0.531
2009 Persson B, Kallberg Y, Bray JE, Bruford E, Dellaporta SL, Favia AD, Duarte RG, Jörnvall H, Kavanagh KL, Kedishvili N, Kisiela M, Maser E, Mindnich R, Orchard S, Penning TM, et al. The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative. Chemico-Biological Interactions. 178: 94-8. PMID 19027726 DOI: 10.1016/J.Cbi.2008.10.040  0.429
2009 Parés X, Farrés J, Kedishvili N, Duester G. Medium- and short-chain dehydrogenase/reductase gene and protein families : Medium-chain and short-chain dehydrogenases/reductases in retinoid metabolism. Cellular and Molecular Life Sciences : Cmls. 65: 3936-49. PMID 19011747 DOI: 10.1007/S00018-008-8591-3  0.509
2009 Lee SA, Belyaeva OV, Kedishvili NY. Biochemical characterization of human epidermal retinol dehydrogenase 2. Chemico-Biological Interactions. 178: 182-7. PMID 18926804 DOI: 10.1016/J.Cbi.2008.09.019  0.579
2009 Audet M, Methot M, Beliaeva O, Kedishvili N, Breton R, Salesse C. Activity And Membrane Binding Of Retinol Dehydrogenase-11 And Its Deletants Biophysical Journal. 96: 613a-614a. DOI: 10.1016/J.Bpj.2008.12.3244  0.324
2008 Belyaeva OV, Johnson MP, Kedishvili NY. Kinetic analysis of human enzyme RDH10 defines the characteristics of a physiologically relevant retinol dehydrogenase. The Journal of Biological Chemistry. 283: 20299-308. PMID 18502750 DOI: 10.1074/Jbc.M800019200  0.487
2008 Lee SA, Belyaeva OV, Kedishvili NY. Effect of lipid peroxidation products on the activity of human retinol dehydrogenase 12 (RDH12) and retinoid metabolism. Biochimica Et Biophysica Acta. 1782: 421-5. PMID 18396173 DOI: 10.1016/J.Bbadis.2008.03.004  0.613
2008 Belyaeva OV, Korkina OV, Stetsenko AV, Kedishvili NY. Human retinol dehydrogenase 13 (RDH13) is a mitochondrial short-chain dehydrogenase/reductase with a retinaldehyde reductase activity. The Febs Journal. 275: 138-47. PMID 18039331 DOI: 10.1111/J.1742-4658.2007.06184.X  0.408
2007 Lee SA, Belyaeva OV, Popov IK, Kedishvili NY. Overproduction of bioactive retinoic acid in cells expressing disease-associated mutants of retinol dehydrogenase 12. The Journal of Biological Chemistry. 282: 35621-8. PMID 17925390 DOI: 10.1074/Jbc.M706372200  0.579
2007 Belyaeva OV, Chetyrkin SV, Clark AL, Kostereva NV, SantaCruz KS, Chronwall BM, Kedishvili NY. Role of microsomal retinol/sterol dehydrogenase-like short-chain dehydrogenases/reductases in the oxidation and epimerization of 3alpha-hydroxysteroids in human tissues. Endocrinology. 148: 2148-56. PMID 17289849 DOI: 10.1210/En.2006-1491  0.385
2007 Kedishvili NY, Belyaeva OV, Chetyrkin SV, Kostereva NV, Chronwall BM. Microsomal Short‐Chain Dehydrogenases/Reductases (SDRs) in the Oxidation and Epimerization of 3α‐Hydroxysteroids. The Faseb Journal. 21. DOI: 10.1096/Fasebj.21.5.A663-A  0.315
2006 Belyaeva OV, Kedishvili NY. Comparative genomic and phylogenetic analysis of short-chain dehydrogenases/reductases with dual retinol/sterol substrate specificity. Genomics. 88: 820-30. PMID 16860536 DOI: 10.1016/J.Ygeno.2006.06.004  0.412
2006 Gallego O, Belyaeva OV, Porté S, Ruiz FX, Stetsenko AV, Shabrova EV, Kostereva NV, Farrés J, Parés X, Kedishvili NY. Comparative functional analysis of human medium-chain dehydrogenases, short-chain dehydrogenases/reductases and aldo-keto reductases with retinoids. The Biochemical Journal. 399: 101-9. PMID 16787387 DOI: 10.1042/Bj20051988  0.511
2005 Belyaeva OV, Korkina OV, Stetsenko AV, Kim T, Nelson PS, Kedishvili NY. 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. Biochemistry. 44: 7035-47. PMID 15865448 DOI: 10.1021/Bi050226K  0.409
2005 Kim TS, Maeda A, Maeda T, Heinlein C, Kedishvili N, Palczewski K, Nelson PS. Delayed dark adaptation in 11-cis-retinol dehydrogenase-deficient mice: a role of RDH11 in visual processes in vivo. The Journal of Biological Chemistry. 280: 8694-704. PMID 15634683 DOI: 10.1074/Jbc.M413172200  0.339
2003 Belyaeva OV, Stetsenko AV, Nelson P, Kedishvili NY. Properties of short-chain dehydrogenase/reductase RalR1: characterization of purified enzyme, its orientation in the microsomal membrane, and distribution in human tissues and cell lines. Biochemistry. 42: 14838-45. PMID 14674758 DOI: 10.1021/Bi035288U  0.416
2003 Lapshina EA, Belyaeva OV, Chumakova OV, Kedishvili NY. Differential recognition of the free versus bound retinol by human microsomal retinol/sterol dehydrogenases: characterization of the holo-CRBP dehydrogenase activity of RoDH-4. Biochemistry. 42: 776-84. PMID 12534290 DOI: 10.1021/Bi026836R  0.458
2002 Belyaeva OV, Kedishvili NY. Human pancreas protein 2 (PAN2) has a retinal reductase activity and is ubiquitously expressed in human tissues. Febs Letters. 531: 489-93. PMID 12435598 DOI: 10.1016/S0014-5793(02)03588-3  0.313
2002 Kedishvili NY, Chumakova OV, Chetyrkin SV, Belyaeva OV, Lapshina EA, Lin DW, Matsumura M, Nelson PS. Evidence that the human gene for prostate short-chain dehydrogenase/reductase (PSDR1) encodes a novel retinal reductase (RalR1). The Journal of Biological Chemistry. 277: 28909-15. PMID 12036956 DOI: 10.1074/jbc.M202588200  0.335
2002 Kedishvili NY. Multifunctional nature of human retinol dehydrogenases Current Organic Chemistry. 6: 1247-1257. DOI: 10.2174/1385272023373400  0.412
2001 Chetyrkin SV, Hu J, Gough WH, Dumaual N, Kedishvili NY. Further characterization of human microsomal 3α-hydroxysteroid dehydrogenase Archives of Biochemistry and Biophysics. 386: 1-10. PMID 11360992 DOI: 10.1006/abbi.2000.2203  0.314
2000 Kedishvili NY, Goodwin GW, Popov KM, Harris RA. Mammalian methylmalonate-semialdehyde dehydrogenase Methods in Enzymology. 324: 207-218. PMID 10989432  0.331
1998 Kedishvili NY, Gough WH, Davis WI, Parsons S, Li TK, Bosron WF. Effect of cellular retinol-binding protein on retinol oxidation by human class IV retinol/alcohol dehydrogenase and inhibition by ethanol Biochemical and Biophysical Research Communications. 249: 191-196. PMID 9705855 DOI: 10.1006/Bbrc.1998.9105  0.332
1998 Gough WH, VanOoteghem S, Sint T, Kedishvili NY. cDNA cloning and characterization of a new human microsomal NAD+- dependent dehydrogenase that oxidizes all-trans-retinol and 3α- hydroxysteroids Journal of Biological Chemistry. 273: 19778-19785. PMID 9677409 DOI: 10.1074/jbc.273.31.19778  0.355
1997 Kedishvili NY, Gough WH, Chernoff EA, Hurley TD, Stone CL, Bowman KD, Popov KM, Bosron WF, Li TK. cDNA sequence and catalytic properties of a chick embryo alcohol dehydrogenase that oxidizes retinol and 3beta,5alpha-hydroxysteroids. The Journal of Biological Chemistry. 272: 7494-500. PMID 9054452 DOI: 10.1074/Jbc.272.11.7494  0.33
1995 Kedishvili NY, Bosron WF, Stone CL, Hurley TD, Peggs CF, Thomasson HR, Popov KM, Carr LG, Edenberg HJ, Li TK. Expression and kinetic characterization of recombinant human stomach alcohol dehydrogenase: Active-site amino acid sequence explains substrate specificity compared with liver isozymes Journal of Biological Chemistry. 270: 3625-3630. PMID 7876099 DOI: 10.1074/Jbc.270.8.3625  0.39
1994 Kedishvili NY, Popov KM, Jaskiewicz JA, Harris RA. Coordinated Expression of Valine Catabolic Enzymes During Adipogenesis: Analysis of Activity, mRNA, Protein Levels, and Metabolic Consequences Archives of Biochemistry and Biophysics. 315: 317-322. PMID 7527207 DOI: 10.1006/Abbi.1994.1506  0.334
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