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Sergey Krupenko - Publications

Affiliations: 
Medical University of South Carolina, Charleston, SC, United States 
Area:
Biochemistry, Nutrition, Molecular Biology
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33 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
2022 Rushing BR, Fogle HM, Sharma J, You M, McCormac JP, Molina S, Sumner S, Krupenko NI, Krupenko SA. Exploratory Metabolomics Underscores the Folate Enzyme ALDH1L1 as a Regulator of Glycine and Methylation Reactions. Molecules (Basel, Switzerland). 27. PMID 36500483 DOI: 10.3390/molecules27238394  0.397
2021 Krupenko NI, Sharma J, Fogle HM, Pediaditakis P, Strickland KC, Du X, Helke KL, Sumner S, Krupenko SA. Knockout of Putative Tumor Suppressor Aldh1l1 in Mice Reprograms Metabolism to Accelerate Growth of Tumors in a Diethylnitrosamine (DEN) Model of Liver Carcinogenesis. Cancers. 13. PMID 34203215 DOI: 10.3390/cancers13133219  0.558
2020 Krupenko NI, Sharma J, Pediaditakis P, Helke KL, Hall MS, Du X, Sumner S, Krupenko SA. Aldh1l2 knockout mouse metabolomics links the loss of the mitochondrial folate enzyme to deregulation of a lipid metabolism observed in rare human disorder. Human Genomics. 14: 41. PMID 33168096 DOI: 10.1186/s40246-020-00291-3  0.354
2019 Krupenko NI, Sharma J, Pediaditakis P, Fekry B, Helke KL, Du X, Sumner S, Krupenko SA. Cytosolic 10-formyltetrahydrofolate dehydrogenase regulates glycine metabolism in mouse liver. Scientific Reports. 9: 14937. PMID 31624291 DOI: 10.1038/S41598-019-51397-1  0.339
2019 Sarret C, Ashkavand Z, Paules E, Dorboz I, Pediaditakis P, Sumner S, Eymard-Pierre E, Francannet C, Krupenko NI, Boespflug-Tanguy O, Krupenko SA. Deleterious mutations in suggest a novel cause for neuro-ichthyotic syndrome. Npj Genomic Medicine. 4: 17. PMID 31341639 DOI: 10.1038/s41525-019-0092-9  0.325
2019 Krupenko SA, Krupenko NI. Loss of ALDH1L1 folate enzyme confers a selective metabolic advantage for tumor progression. Chemico-Biological Interactions. 302: 149-155. PMID 30794800 DOI: 10.1016/j.cbi.2019.02.013  0.325
2018 Krupenko SA, Krupenko NI. ALDH1L1 and ALDH1L2 Folate Regulatory Enzymes in Cancer. Advances in Experimental Medicine and Biology. 1032: 127-143. PMID 30362096 DOI: 10.1007/978-3-319-98788-0_10  0.337
2018 Khan QA, Pediaditakis P, Malakhau Y, Esmaeilniakooshkghazi A, Ashkavand Z, Sereda V, Krupenko NI, Krupenko SA. CHIP E3 ligase mediates proteasomal degradation of the proliferation regulatory protein ALDH1L1 during the transition of NIH3T3 fibroblasts from G0/G1 to S-phase. Plos One. 13: e0199699. PMID 29979702 DOI: 10.1371/journal.pone.0199699  0.321
2017 Horita DA, Krupenko SA. Modeling of interactions between functional domains of ALDH1L1. Chemico-Biological Interactions. PMID 28414156 DOI: 10.1016/J.Cbi.2017.04.011  0.304
2016 Fekry B, Esmaeilniakooshkghazi A, Krupenko SA, Krupenko NI. Ceramide Synthase 6 Is a Novel Target of Methotrexate Mediating Its Antiproliferative Effect in a p53-Dependent Manner. Plos One. 11: e0146618. PMID 26783755 DOI: 10.1371/journal.pone.0146618  0.326
2015 Krupenko NI, Holmes RS, Tsybovsky Y, Krupenko SA. Aldehyde dehydrogenase homologous folate enzymes: Evolutionary switch between cytoplasmic and mitochondrial localization. Chemico-Biological Interactions. 234: 12-7. PMID 25549576 DOI: 10.1016/j.cbi.2014.12.022  0.355
2013 DebRoy S, Kramarenko II, Ghose S, Oleinik NV, Krupenko SA, Krupenko NI. A novel tumor suppressor function of glycine N-methyltransferase is independent of its catalytic activity but requires nuclear localization. Plos One. 8: e70062. PMID 23936142 DOI: 10.1371/journal.pone.0070062  0.36
2013 Hoeferlin LA, Fekry B, Ogretmen B, Krupenko SA, Krupenko NI. Folate stress induces apoptosis via p53-dependent de novo ceramide synthesis and up-regulation of ceramide synthase 6. The Journal of Biological Chemistry. 288: 12880-90. PMID 23519469 DOI: 10.1074/Jbc.M113.461798  0.674
2013 Tsybovsky Y, Malakhau Y, Strickland KC, Krupenko SA. The mechanism of discrimination between oxidized and reduced coenzyme in the aldehyde dehydrogenase domain of Aldh1l1. Chemico-Biological Interactions. 202: 62-9. PMID 23295222 DOI: 10.1016/J.Cbi.2012.12.015  0.609
2013 Strickland KC, Krupenko NI, Krupenko SA. Molecular mechanisms underlying the potentially adverse effects of folate. Clinical Chemistry and Laboratory Medicine. 51: 607-16. PMID 23241610 DOI: 10.1515/Cclm-2012-0561  0.564
2012 Krupenko N, Kramarenko I, DebRoy S, Krupenko S. A novel function for an old folate enzyme F1000research. 3. DOI: 10.7490/F1000Research.1089995.1  0.41
2011 Hoeferlin LA, Oleinik NV, Krupenko NI, Krupenko SA. Activation of p21-Dependent G1/G2 Arrest in the Absence of DNA Damage as an Antiapoptotic Response to Metabolic Stress. Genes & Cancer. 2: 889-99. PMID 22593801 DOI: 10.1177/1947601911432495  0.679
2011 Strickland KC, Krupenko NI, Dubard ME, Hu CJ, Tsybovsky Y, Krupenko SA. Enzymatic properties of ALDH1L2, a mitochondrial 10-formyltetrahydrofolate dehydrogenase. Chemico-Biological Interactions. 191: 129-36. PMID 21238436 DOI: 10.1016/J.Cbi.2011.01.008  0.684
2011 Strickland KC, Holmes RS, Oleinik NV, Krupenko NI, Krupenko SA. Phylogeny and evolution of aldehyde dehydrogenase-homologous folate enzymes. Chemico-Biological Interactions. 191: 122-8. PMID 21215736 DOI: 10.1016/J.Cbi.2010.12.025  0.686
2010 Krupenko NI, Dubard ME, Strickland KC, Moxley KM, Oleinik NV, Krupenko SA. ALDH1L2 is the mitochondrial homolog of 10-formyltetrahydrofolate dehydrogenase. The Journal of Biological Chemistry. 285: 23056-63. PMID 20498374 DOI: 10.1074/Jbc.M110.128843  0.656
2010 Strickland KC, Hoeferlin LA, Oleinik NV, Krupenko NI, Krupenko SA. Acyl carrier protein-specific 4'-phosphopantetheinyl transferase activates 10-formyltetrahydrofolate dehydrogenase. The Journal of Biological Chemistry. 285: 1627-33. PMID 19933275 DOI: 10.1074/Jbc.M109.080556  0.662
2009 Krupenko SA. FDH: an aldehyde dehydrogenase fusion enzyme in folate metabolism. Chemico-Biological Interactions. 178: 84-93. PMID 18848533 DOI: 10.1016/j.cbi.2008.09.007  0.357
2007 Tsybovsky Y, Donato H, Krupenko NI, Davies C, Krupenko SA. Crystal structures of the carboxyl terminal domain of rat 10-formyltetrahydrofolate dehydrogenase: implications for the catalytic mechanism of aldehyde dehydrogenases. Biochemistry. 46: 2917-29. PMID 17302434 DOI: 10.1021/bi0619573  0.307
2006 Reuland SN, Vlasov AP, Krupenko SA. Modular organization of FDH: Exploring the basis of hydrolase catalysis. Protein Science : a Publication of the Protein Society. 15: 1076-84. PMID 16597835 DOI: 10.1110/ps.052062806  0.375
2005 Oleinik NV, Krupenko NI, Priest DG, Krupenko SA. Cancer cells activate p53 in response to 10-formyltetrahydrofolate dehydrogenase expression. The Biochemical Journal. 391: 503-11. PMID 16014005 DOI: 10.1042/BJ20050533  0.348
2002 Krupenko SA, Oleinik NV. 10-formyltetrahydrofolate dehydrogenase, one of the major folate enzymes, is down-regulated in tumor tissues and possesses suppressor effects on cancer cells. Cell Growth & Differentiation : the Molecular Biology Journal of the American Association For Cancer Research. 13: 227-36. PMID 12065246  0.347
2001 Krupenko SA, Vlasov AP, Wagner C. On the role of conserved histidine 106 in 10-formyltetrahydrofolate dehydrogenase catalysis: connection between hydrolase and dehydrogenase mechanisms. The Journal of Biological Chemistry. 276: 24030-7. PMID 11320079 DOI: 10.1074/JBC.M009257200  0.384
2000 Krupenko SA, Wagner C. Aspartate 142 is involved in both hydrolase and dehydrogenase catalytic centers of 10-formyltetrahydrofolate dehydrogenase. The Journal of Biological Chemistry. 274: 35777-84. PMID 10585460 DOI: 10.1074/JBC.274.50.35777  0.355
1998 Krupenko SA, Wagner C. Overexpression of functional hydrolase domain of rat liver 10-formyltetrahydrofolate dehydrogenase in Escherichia coli. Protein Expression and Purification. 14: 146-52. PMID 9758763 DOI: 10.1006/prep.1998.0937  0.331
1997 Krupenko SA, Wagner C, Cook RJ. Expression, purification, and properties of the aldehyde dehydrogenase homologous carboxyl-terminal domain of rat 10-formyltetrahydrofolate dehydrogenase. The Journal of Biological Chemistry. 272: 10266-72. PMID 9092577 DOI: 10.1074/jbc.272.15.10266  0.347
1996 Krupenko SA, Horstman DA, Wagner C, Cook RJ. Baculovirus expression and purification of rat 10-formyltetrahydrofolate dehydrogenase. Protein Expression and Purification. 6: 457-64. PMID 8527931 DOI: 10.1006/prep.1995.1061  0.352
1995 Krupenko SA, Wagner C, Cook RJ. Cysteine 707 is involved in the dehydrogenase activity site of rat 10-formyltetrahydrofolate dehydrogenase. The Journal of Biological Chemistry. 270: 519-22. PMID 7822273 DOI: 10.1074/jbc.270.2.519  0.321
1995 Krupenko SA, Wagner C, Cook RJ. Recombinant 10-formyltetrahydrofolate dehydrogenase catalyses both dehydrogenase and hydrolase reactions utilizing the synthetic substrate 10-formyl-5,8-dideazafolate. The Biochemical Journal. 651-5. PMID 7702556 DOI: 10.1042/bj3060651  0.403
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