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3-hydroxysteroid dihydrodiol dehydrogenase
Known as:
3alpha-HSD DD enzyme
, AKR1C9
National Institutes of Health
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Related topics
Related topics
1 relation
Broader (1)
Hydroxysteroid Dehydrogenases
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
2008
2008
Tissue Distribution of Human AKR1C3 and Rat Homolog in the Adult Genitourinary System
J. Azzarello
,
K. Fung
,
Hsueh-Kung Lin
Journal of Histochemistry and Cytochemistry
2008
Corpus ID: 32425703
Human aldo-keto reductase (AKR) 1C3 (type 2 3α-hydroxysteroid dehydrogenase/type 5 17β-hydroxysteroid dehydrogenase) catalyzes…
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2008
2008
Fjord-region benzo[g]chrysene-11,12-dihydrodiol and benzo[c]phenanthrene-3,4-dihydrodiol as substrates for rat liver dihydrodiol dehydrogenase (AKR1C9): structural basis for stereochemical preference…
Carol A Shultz
,
N. Palackal
,
Dipti Mangal
,
R. Harvey
,
I. Blair
,
T. Penning
Chemical Research in Toxicology
2008
Corpus ID: 5177918
This study demonstrates that benzo[g]chrysene-11,12-dihydrodiol (B[g]C-11,12-dihydrodiol) derived from the fjord-region parent…
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Review
2007
Review
2007
Cofactors, redox state, and directional preferences of hydroxysteroid dehydrogenases
Daniel P. Sherbet
,
M. Papari-Zareei
,
+7 authors
R. Auchus
Molecular and Cellular Endocrinology
2007
Corpus ID: 22777337
2007
2007
3-Ketosteroid Reductase Activity and Expression by Fetal Rat Osteoblasts*
T. McCarthy
,
R. Hochberg
,
D. Labaree
,
M. Centrella
Journal of Biological Chemistry
2007
Corpus ID: 29874078
In addition to reproductive tissue, sex hormones induce transcriptional events in many connective tissue cells, including…
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2004
2004
Estren (4-estren-3alpha,17beta-diol) is a prohormone that regulates both androgenic and estrogenic transcriptional effects through the androgen receptor.
M. Centrella
,
T. McCarthy
,
Wei-zhong Chang
,
D. Labaree
,
R. Hochberg
Molecular Endocrinology
2004
Corpus ID: 24777846
Alternative mechanisms of steroid action, through both traditional nuclear receptors and indirect pathways of gene activation…
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2003
2003
Examination of the differences in structure-function of human and rat 3alpha-hydroxysteroid dehydrogenase.
Yi Jin
,
W. Cooper
,
T. Penning
Chemico-Biological Interactions
2003
Corpus ID: 25362156
2003
2003
Steroid-binding site residues dictate optimal substrate positioning in rat 3alpha-hydroxysteroid dehydrogenase (3alpha-HSD or AKR1C9).
Vladi V. Heredia
,
R. Kruger
,
T. Penning
Chemico-Biological Interactions
2003
Corpus ID: 22215747
Rat liver 3alpha-hydroxysteroid dehydrogenase (3alpha-HSD or AKR1C9), a member of the aldo-keto reductase (AKR) superfamily…
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2000
2000
Identification of the oxidative 3alpha-hydroxysteroid dehydrogenase activity of rat Leydig cells as type II retinol dehydrogenase.
D. Hardy
,
R. Ge
,
J. F. Catterall
,
Y. T. Hou
,
T. Penning
,
M. Hardy
Endocrinology
2000
Corpus ID: 9421334
Dihydrotestosterone (DHT) is the most potent naturally occurring androgen, and its production in the testis may have important…
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1999
1999
Genomic structure of rat 3alpha-hydroxysteroid/dihydrodiol dehydrogenase (3alpha-HSD/DD, AKR1C9).
H. K. Lin
,
C. Hung
,
M. Moore
,
T. Penning
Journal of Steroid Biochemistry and Molecular…
1999
Corpus ID: 10676464
Rat liver 3alpha-hydroxysteroid/dihydrodiol dehydrogenase (3alpha-HSD/DD) is a member of the aldo-keto reductase (AKR…
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Review
1999
Review
1999
Penning Dehydrogenase of PAH Activation Catalyzed by Human Dihydrodiol and Oxidative Stress : Implications for the Alternative Pathway by Polycyclic Aromatic Hydrocarbons ( PAHs ) , Electrophiles…
M. Burczynski
,
Hseuh-Kung Lin
,
M. Trevor
1999
Corpus ID: 15081414
Human dihydrodiol dehydrogenase (DD) isoforms are aldo-keto reductases (AKRs) that activate polycyclic aromatic hydrocarbons…
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