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The aldo-keto reductases (AKRs): Overview

Chemico-biological interactions, 2015-06, Vol.234, p.236-246

Penning, Trevor M.

2015

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The DHEA-sulfate depot following P450c17 inhibition supports the case for AKR1C3 inhibition in high risk localized and advanced castration resistant prostate cancer

Chemico-biological interactions, 2015-06, Vol.234, p.332-338

2015

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Aldo-keto reductase (AKR) superfamily website and database: An update

Chemico-biological interactions, 2024-08, Vol.398, p.111111, Article 111111

2024

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The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative

Chemico-biological interactions, 2009-03, Vol.178 (1), p.94-98

2009

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The rate-determining steps of aldo–keto reductases (AKRs), a study on human steroid 5β-reductase (AKR1D1)

Chemico-biological interactions, 2015-06, Vol.234, p.360-365

2015

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Human and murine steroid 5β-reductases (AKR1D1 and AKR1D4): insights into the role of the catalytic glutamic acid

Chemico-biological interactions, 2019-05, Vol.305, p.163-170

2019

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Type 5 17β-hydroxysteroid dehydrogenase/prostaglandin F synthase (AKR1C3): Role in breast cancer and inhibition by non-steroidal anti-inflammatory drug analogs

Chemico-biological interactions, 2009-03, Vol.178 (1), p.221-227

2009

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The aldo-keto reductase superfamily homepage

Chemico-biological interactions, 2003-02, Vol.143, p.621-631

2003

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Alternative splicing in the aldo–keto reductase superfamily: Implications for protein nomenclature

Chemico-biological interactions, 2013-02, Vol.202 (1-3), p.153-158

2013

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The aldo-keto reductase (AKR) superfamily: an update

Chemico-biological interactions, 2001-01, Vol.130 (1-3), p.499-525

2001

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The effect of disease associated point mutations on 5β-reductase (AKR1D1) enzyme function

Chemico-biological interactions, 2011-05, Vol.191 (1), p.250-254

2011

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Aldo-keto reductases in which the conserved catalytic histidine is substituted

Chemico-biological interactions, 2009-03, Vol.178 (1), p.127-133

2009

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Editorial

Chemico-biological interactions, 2015-06, Vol.234, p.1-3

Penning, Trevor M.

2015

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Role of human type 3 3α-hydroxysteroid dehydrogenase (AKR1C2) in androgen metabolism of prostate cancer cells

Chemico-biological interactions, 2003-02, Vol.143, p.401-409

2003

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Cytotoxicity and mutagenicity of polycyclic aromatic hydrocarbon o-quinones produced by dihydrodiol dehydrogenase

Chemico-biological interactions, 1996-01, Vol.99 (1), p.55-72

1996

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Editorial. 17th International Workshop on the Enzymology and Molecular Biology of Carbonyl Metabolism

Chemico-biological interactions, 2015-06, Vol.234, p.1-3

Penning, Trevor M

2015

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Metabolic activation of polycyclic aromatic hydrocarbon trans-dihydrodiols by ubiquitously expressed aldehyde reductase (AKR1A1)

Chemico-biological interactions, 2001-01, Vol.130 (1-3), p.815-824

2001

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Steroid-binding site residues dictate optimal substrate positioning in rat 3α-hydroxysteroid dehydrogenase (3α-HSD or AKR1C9)

Chemico-biological interactions, 2003-02, Vol.143, p.393-400

2003

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Engineering steroid hormone specificity into aldo-keto reductases

Chemico-biological interactions, 2001-01, Vol.130 (1-3), p.659-671

2001

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Type 5 17β-Hydroxysteroid Dehydrogenase/Prostaglandin F Synthase (AKR1C3): Role In Breast Cancer and Inhibition by Nonsteroidal Antiinflammatory Drug Analogs

Chemico-biological interactions, 2008-11, Vol.178 (1-3), p.221-227

2008

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Type 5 17beta-hydroxysteroid dehydrogenase/prostaglandin F synthase (AKR1C3): role in breast cancer and inhibition by non-steroidal anti-inflammatory drug analogs

Chemico-biological interactions, 2009-03, Vol.178 (1-3), p.221

2009

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Dihydrodiol dehydrogenase and its role in polycyclic aromatic hydrocarbon metabolism

Chemico-Biological Interactions, 1993-10, Vol.89 (1), p.1-34

Penning, Trevor M.

1993

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Steroid-binding site residues dictate optimal substrate positioning in rat 3alpha-hydroxysteroid dehydrogenase (3alpha-HSD or AKR1C9)

Chemico-biological interactions, 2003-02, Vol.143-144, p.393-400

2003

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Role of human type 3 3alpha-hydroxysteroid dehydrogenase (AKR1C2) in androgen metabolism of prostate cancer cells

Chemico-biological interactions, 2003-02, Vol.143-144, p.401-409

2003

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Examination of the differences in structure-function of human and rat 3alpha-hydroxysteroid dehydrogenase

Chemico-biological interactions, 2003-02, Vol.143-144, p.383-392

2003

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The aldo-keto reductases (AKRs): Overview

The DHEA-sulfate depot following P450c17 inhibition supports the case for AKR1C3 inhibition in high risk localized and advanced castration resistant prostate cancer

Aldo-keto reductase (AKR) superfamily website and database: An update

The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative

The rate-determining steps of aldo–keto reductases (AKRs), a study on human steroid 5β-reductase (AKR1D1)

Human and murine steroid 5β-reductases (AKR1D1 and AKR1D4): insights into the role of the catalytic glutamic acid

Type 5 17β-hydroxysteroid dehydrogenase/prostaglandin F synthase (AKR1C3): Role in breast cancer and inhibition by non-steroidal anti-inflammatory drug analogs

The aldo-keto reductase superfamily homepage

Alternative splicing in the aldo–keto reductase superfamily: Implications for protein nomenclature

The aldo-keto reductase (AKR) superfamily: an update

The effect of disease associated point mutations on 5β-reductase (AKR1D1) enzyme function

Aldo-keto reductases in which the conserved catalytic histidine is substituted

Editorial

Role of human type 3 3α-hydroxysteroid dehydrogenase (AKR1C2) in androgen metabolism of prostate cancer cells

Cytotoxicity and mutagenicity of polycyclic aromatic hydrocarbon o-quinones produced by dihydrodiol dehydrogenase

Editorial. 17th International Workshop on the Enzymology and Molecular Biology of Carbonyl Metabolism

Metabolic activation of polycyclic aromatic hydrocarbon trans-dihydrodiols by ubiquitously expressed aldehyde reductase (AKR1A1)

Steroid-binding site residues dictate optimal substrate positioning in rat 3α-hydroxysteroid dehydrogenase (3α-HSD or AKR1C9)

Engineering steroid hormone specificity into aldo-keto reductases

Type 5 17β-Hydroxysteroid Dehydrogenase/Prostaglandin F Synthase (AKR1C3): Role In Breast Cancer and Inhibition by Nonsteroidal Antiinflammatory Drug Analogs

Type 5 17beta-hydroxysteroid dehydrogenase/prostaglandin F synthase (AKR1C3): role in breast cancer and inhibition by non-steroidal anti-inflammatory drug analogs

Dihydrodiol dehydrogenase and its role in polycyclic aromatic hydrocarbon metabolism

Steroid-binding site residues dictate optimal substrate positioning in rat 3alpha-hydroxysteroid dehydrogenase (3alpha-HSD or AKR1C9)

Role of human type 3 3alpha-hydroxysteroid dehydrogenase (AKR1C2) in androgen metabolism of prostate cancer cells

Examination of the differences in structure-function of human and rat 3alpha-hydroxysteroid dehydrogenase

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