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Year | Number of Results |
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Human 3alpha-hydroxysteroid dehydrogenase isoforms (AKR1C1-AKR1C4) of the aldo-keto reductase superfamily: functional plasticity and tissue distribution reveals roles in the inactivation and formation of male and female sex hormones.
Biochem J. 2000 Oct 1;351(Pt 1):67-77. doi: 10.1042/0264-6021:3510067.
Biochem J. 2000.
PMID: 10998348
Free PMC article.
Role of human 3α-hydroxysteroid dehydrogenase isoforms (AKR1C1-AKR1C3) in the extrahepatic metabolism of the steroidal aromatase inactivator Formestane.
Wan R, Kong X, Yang Y, Tao S, Chen Y, Teichmann AT, Wieland FH.
Wan R, et al.
J Steroid Biochem Mol Biol. 2020 Apr;198:105527. doi: 10.1016/j.jsbmb.2019.105527. Epub 2019 Nov 13.
J Steroid Biochem Mol Biol. 2020.
PMID: 31733346
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Substrate specificity, gene structure, and tissue-specific distribution of multiple human 3 alpha-hydroxysteroid dehydrogenases.
Khanna M, Qin KN, Wang RW, Cheng KC.
Khanna M, et al.
J Biol Chem. 1995 Aug 25;270(34):20162-8. doi: 10.1074/jbc.270.34.20162.
J Biol Chem. 1995.
PMID: 7650035
Free article.
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Molecular cloning of two human liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase isoenzymes that are identical with chlordecone reductase and bile-acid binder.
Deyashiki Y, Ogasawara A, Nakayama T, Nakanishi M, Miyabe Y, Sato K, Hara A.
Deyashiki Y, et al.
Biochem J. 1994 Apr 15;299 ( Pt 2)(Pt 2):545-52. doi: 10.1042/bj2990545.
Biochem J. 1994.
PMID: 8172617
Free PMC article.
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