El-Kabbani O - Search Results

1

Rabbit 3-hydroxyhexobarbital dehydrogenase is a NADPH-preferring reductase with broad substrate specificity for ketosteroids, prostaglandin D₂, and other endogenous and xenobiotic carbonyl compounds.

Endo S, Matsunaga T, Matsumoto A, Arai Y, Ohno S, El-Kabbani O, Tajima K, Bunai Y, Yamano S, Hara A, Kitade Y. Endo S, et al. Biochem Pharmacol. 2013 Nov 1;86(9):1366-75. doi: 10.1016/j.bcp.2013.08.024. Epub 2013 Aug 27. Biochem Pharmacol. 2013. PMID: 23994167

2

Human carbonyl reductase 4 is a mitochondrial NADPH-dependent quinone reductase.

Endo S, Matsunaga T, Kitade Y, Ohno S, Tajima K, El-Kabbani O, Hara A. Endo S, et al. Biochem Biophys Res Commun. 2008 Dec 26;377(4):1326-30. doi: 10.1016/j.bbrc.2008.11.003. Epub 2008 Nov 10. Biochem Biophys Res Commun. 2008. PMID: 19000905

3

Potent and selective inhibition of the tumor marker AKR1B10 by bisdemethoxycurcumin: probing the active site of the enzyme with molecular modeling and site-directed mutagenesis.

Matsunaga T, Endo S, Soda M, Zhao HT, El-Kabbani O, Tajima K, Hara A. Matsunaga T, et al. Biochem Biophys Res Commun. 2009 Nov 6;389(1):128-32. doi: 10.1016/j.bbrc.2009.08.107. Epub 2009 Aug 23. Biochem Biophys Res Commun. 2009. PMID: 19706287

4

Properties and tissue distribution of a novel aldo-keto reductase encoding in a rat gene (Akr1b10).

Endo S, Matsunaga T, Kuragano T, Ohno S, Kitade Y, Tajima K, El-Kabbani O, Hara A. Endo S, et al. Arch Biochem Biophys. 2010 Nov 15;503(2):230-7. doi: 10.1016/j.abb.2010.08.010. Epub 2010 Aug 13. Arch Biochem Biophys. 2010. PMID: 20709016

5

Rat aldose reductase-like protein (AKR1B14) efficiently reduces the lipid peroxidation product 4-oxo-2-nonenal.

Endo S, Matsunaga T, Fujita A, Tajima K, El-Kabbani O, Hara A. Endo S, et al. Biol Pharm Bull. 2010;33(11):1886-90. doi: 10.1248/bpb.33.1886. Biol Pharm Bull. 2010. PMID: 21048316 Free article.

6

Characterization of rabbit aldose reductase-like protein with 3β-hydroxysteroid dehydrogenase activity.

Endo S, Matsunaga T, Kumada S, Fujimoto A, Ohno S, El-Kabbani O, Hu D, Toyooka N, Mano J, Tajima K, Hara A. Endo S, et al. Arch Biochem Biophys. 2012 Nov 1;527(1):23-30. doi: 10.1016/j.abb.2012.07.012. Epub 2012 Aug 1. Arch Biochem Biophys. 2012. PMID: 22874434

7

Characterization of rabbit morphine 6-dehydrogenase and two NAD(+)-dependent 3α(17β)-hydroxysteroid dehydrogenases.

Endo S, Matsunaga T, Fujimoto A, Kumada S, Arai Y, Miura Y, Mikamo H, El-Kabbani O, Yamano S, Iinuma M, Hara A. Endo S, et al. Arch Biochem Biophys. 2013 Jan 15;529(2):131-9. doi: 10.1016/j.abb.2012.11.013. Epub 2012 Dec 7. Arch Biochem Biophys. 2013. PMID: 23228597

8

Modulation of activity and inhibitor sensitivity of rabbit aldose reductase-like protein (AKR1B19) by oxidized glutathione and SH-reagents.

Endo S, Fujimoto A, Kumada S, Matsunaga T, Ohno S, Mano J, Tajima K, El-Kabbani O, Hara A. Endo S, et al. Chem Biol Interact. 2013 Feb 25;202(1-3):146-52. doi: 10.1016/j.cbi.2012.11.026. Epub 2012 Dec 19. Chem Biol Interact. 2013. PMID: 23261715

9

Substrate specificity and inhibitor sensitivity of rabbit 20α-hydroxysteroid dehydrogenase.

Endo S, Arai Y, Hara A, Kitade Y, Bunai Y, El-Kabbani O, Matsunaga T. Endo S, et al. Biol Pharm Bull. 2013;36(9):1514-8. doi: 10.1248/bpb.b13-00342. Biol Pharm Bull. 2013. PMID: 23995665 Free article.

10

Cloning and characterization of four rabbit aldo-keto reductases featuring broad substrate specificity for xenobiotic and endogenous carbonyl compounds: relationship with multiple forms of drug ketone reductases.

Endo S, Matsunaga T, Arai Y, Ikari A, Tajima K, El-Kabbani O, Yamano S, Hara A, Kitade Y. Endo S, et al. Drug Metab Dispos. 2014 Apr;42(4):803-12. doi: 10.1124/dmd.113.056044. Epub 2014 Feb 7. Drug Metab Dispos. 2014. PMID: 24510382

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