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Structural and Functional Biology of Aldo-Keto Reductase Steroid-Transforming Enzymes

Endocrine reviews, 2019-04, Vol.40 (2), p.447-475

2019

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Conversion of Classical and 11-Oxygenated Androgens by Insulin-Induced AKR1C3 in a Model of Human PCOS Adipocytes

Endocrinology (Philadelphia), 2022-07, Vol.163 (7), p.1

2022

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Germline Mutations in Steroid Metabolizing Enzymes: A Focus on Steroid Transforming Aldo-Keto Reductases

International journal of molecular sciences, 2023-01, Vol.24 (3), p.1873

2023

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Steroid Hormone Transforming Aldo-Keto Reductases and Cancer

Annals of the New York Academy of Sciences, 2009-02, Vol.1155 (1), p.33-42

2009

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Mechanisms of activation of the transcription factor Nrf2 by redox stressors, nutrient cues, and energy status and the pathways through which it attenuates degenerative disease

Free radical biology & medicine, 2015-11, Vol.88 (Pt B), p.108-146

2015

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AKR1C1 and AKR1C3 may determine progesterone and estrogen ratios in endometrial cancer

Molecular and cellular endocrinology, 2006-03, Vol.248 (1), p.126-135

2006

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Insulin-Induced AKR1C3 Induces Fatty Acid Synthase in a Model of Human PCOS Adipocytes

Endocrinology (Philadelphia), 2023-03, Vol.164 (5)

2023

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Letter to the Editor From Penning and Detlefsen “Hydroxyeicosatetraenoic Acid Controls Androgen Reduction in Diverse Types of Human Epithelial Cells”

Endocrinology (Philadelphia), 2023-05, Vol.164 (5), p.1

2023

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Intracrinology-revisited and prostate cancer

The Journal of steroid biochemistry and molecular biology, 2020-02, Vol.196, p.105499-105499, Article 105499

2020

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Single-molecule enzymology of steroid transforming enzymes: Transient kinetic studies and what they tell us

The Journal of steroid biochemistry and molecular biology, 2016-07, Vol.161, p.5-12

Penning, Trevor M.

2016

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Inhibitors of type 5 17β-hydroxysteroid dehydrogenase (AKR1C3): Overview and structural insights

The Journal of steroid biochemistry and molecular biology, 2011-05, Vol.125 (1), p.95-104

2011

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A new nomenclature for the aldo-keto reductase superfamily

Biochemical pharmacology, 1997-09, Vol.54 (6), p.639-647

1997

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Characterization of a monoclonal antibody for human aldo-keto reductase AKR1C3 (type 2 3α-hydroxysteroid dehydrogenase/type 5 17β-hydroxysteroid dehydrogenase); immunohistochemical detection in breast and prostate

Steroids, 2004-12, Vol.69 (13), p.795-801

2004

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Using biochemistry and biophysics to extinguish androgen receptor signaling in prostate cancer

The Journal of biological chemistry, 2021-01, Vol.296, p.100240-100240, Article 100240

2021

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The androgen receptor

Vitamins and hormones, 2023, Vol.123, p.439-481

2023

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Detoxication of Benzo[a]pyrene-7,8-dione by Sulfotransferases (SULTs) in Human Lung Cells

The Journal of biological chemistry, 2012-08, Vol.287 (35), p.29909-29920

2012

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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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A 3-(4-nitronaphthen-1-yl) amino-benzoate analog as a bifunctional AKR1C3 inhibitor and AR antagonist: Head to head comparison with other advanced AKR1C3 targeted therapeutics

The Journal of steroid biochemistry and molecular biology, 2019-09, Vol.192, p.105283, Article 105283

2019

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Non-stereo-selective cytosolic human brain tissue 3-ketosteroid reductase is refractory to inhibition by AKR1C inhibitors

Biochimica et biophysica acta, 2010-11, Vol.1801 (11), p.1221-1231

2010

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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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Hydroxysteroid dehydrogenases and pre‐receptor regulation of steroid hormone action

Human reproduction update, 2003-05, Vol.9 (3), p.193-205

Penning, Trevor M

2003

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Aryl Hydrocarbon Receptor Facilitates DNA Strand Breaks and 8-Oxo-2′-deoxyguanosine Formation by the Aldo-Keto Reductase Product Benzo[a]pyrene-7,8-dione

The Journal of biological chemistry, 2009-10, Vol.284 (43), p.29725-29734

2009

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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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Crystal Structure of Perakine Reductase, Founding Member of a Novel Aldo-Keto Reductase (AKR) Subfamily That Undergoes Unique Conformational Changes during NADPH Binding

The Journal of biological chemistry, 2012-03, Vol.287 (14), p.11213-11221

2012

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Pre-receptor regulation of the androgen receptor

Molecular and cellular endocrinology, 2008-01, Vol.281 (1), p.1-8

2008

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Structural and Functional Biology of Aldo-Keto Reductase Steroid-Transforming Enzymes

Conversion of Classical and 11-Oxygenated Androgens by Insulin-Induced AKR1C3 in a Model of Human PCOS Adipocytes

Germline Mutations in Steroid Metabolizing Enzymes: A Focus on Steroid Transforming Aldo-Keto Reductases

Steroid Hormone Transforming Aldo-Keto Reductases and Cancer

Mechanisms of activation of the transcription factor Nrf2 by redox stressors, nutrient cues, and energy status and the pathways through which it attenuates degenerative disease

AKR1C1 and AKR1C3 may determine progesterone and estrogen ratios in endometrial cancer

Insulin-Induced AKR1C3 Induces Fatty Acid Synthase in a Model of Human PCOS Adipocytes

Letter to the Editor From Penning and Detlefsen “Hydroxyeicosatetraenoic Acid Controls Androgen Reduction in Diverse Types of Human Epithelial Cells”

Intracrinology-revisited and prostate cancer

Single-molecule enzymology of steroid transforming enzymes: Transient kinetic studies and what they tell us

Inhibitors of type 5 17β-hydroxysteroid dehydrogenase (AKR1C3): Overview and structural insights

A new nomenclature for the aldo-keto reductase superfamily

Characterization of a monoclonal antibody for human aldo-keto reductase AKR1C3 (type 2 3α-hydroxysteroid dehydrogenase/type 5 17β-hydroxysteroid dehydrogenase); immunohistochemical detection in breast and prostate

Using biochemistry and biophysics to extinguish androgen receptor signaling in prostate cancer

The androgen receptor

Detoxication of Benzo[a]pyrene-7,8-dione by Sulfotransferases (SULTs) in Human Lung Cells

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

A 3-(4-nitronaphthen-1-yl) amino-benzoate analog as a bifunctional AKR1C3 inhibitor and AR antagonist: Head to head comparison with other advanced AKR1C3 targeted therapeutics

Non-stereo-selective cytosolic human brain tissue 3-ketosteroid reductase is refractory to inhibition by AKR1C inhibitors

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

Hydroxysteroid dehydrogenases and pre‐receptor regulation of steroid hormone action

Aryl Hydrocarbon Receptor Facilitates DNA Strand Breaks and 8-Oxo-2′-deoxyguanosine Formation by the Aldo-Keto Reductase Product Benzo[a]pyrene-7,8-dione

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

Crystal Structure of Perakine Reductase, Founding Member of a Novel Aldo-Keto Reductase (AKR) Subfamily That Undergoes Unique Conformational Changes during NADPH Binding

Pre-receptor regulation of the androgen receptor

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