Dean Cuebas
Missouri State University
20 Papers
527 Citations
Dean Cuebas is an academic researcher from Missouri State University. The author has contributed to research in topics: Peroxisome & Dehydrogenase. The author has an hindex of 17, co-authored 20 publications. Previous affiliations of Dean Cuebas include City University of New York.
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Papers
Peroxisomal d-hydroxyacyl-CoA dehydrogenase deficiency: Resolution of the enzyme defect and its molecular basis in bifunctional protein deficiency
E. G. van Grunsven,E. van Berkel,Lodewijk IJlst,Peter Vreken,J. B. C. De Klerk,Jerzy Adamski,Hugh Lemonde,Peter E. Clayton,Dean Cuebas,R. J. A. Wanders +9 more
TL;DR: In this article, a new peroxisomal β-oxidation enzyme called d-bifunctional protein with enoyl-CoA hydratase and 3-hydroxyacyl CoA dehydrogenase activity was described.
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Participation of two members of the very long-chain acyl-CoA synthetase family in bile acid synthesis and recycling.
Stephanie J. Mihalik,Steven J. Steinberg,Zhengtong Pei,Joseph Park,Do G. Kim,Ann K. Heinzer,Georges Dacremont,Ronald J.A. Wanders,Dean Cuebas,Kirby D. Smith,Paul A. Watkins +10 more
TL;DR: Results of in situ hybridization, topographic orientation, and inhibition studies are consistent with the proposed roles of these enzymes in bile acid metabolism.
121
NADPH-dependent beta-oxidation of unsaturated fatty acids with double bonds extending from odd-numbered carbon atoms
TL;DR: It is concluded that odd-numbered double bonds, like even-numbereddouble bonds, can be reductively removed during the beta-oxidation of polyunsaturated fatty acids.
98
The human liver-specific homolog of very long-chain acyl-CoA synthetase is cholate:CoA ligase.
TL;DR: Results are consistent with a role for hVLCS-H2 in the re-activation and re-conjugation of bile acids entering liver from the enterohepatic circulation rather than in de novo bile acid synthesis.
68
3-Mercaptopropionic acid, a potent inhibitor of fatty acid oxidation in rat heart mitochondria.
TL;DR: Observations together lead us to suggest that the inhibition of beta-oxidation by 3-mercaptopropionic acid in coupled rat heart mitochondria is most likely a consequence of the reversible inhibition of acyl-CoA dehydrogenase by long-chain S-acyl-3-mer Captopropionyl- CoA thioesters and possibly by3-Mercaptoacetic acid.
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