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Human aldo–keto reductases: Function, gene regulation, and single nucleotide polymorphisms

Archives of biochemistry and biophysics, 2007-08, Vol.464 (2), p.241-250

2007

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Lentiviral Vector Production from a Stable Packaging Cell Line Using a Packed Bed Bioreactor

Molecular therapy. Methods & clinical development, 2020-12, Vol.19, p.1-13

2020

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Distribution of AAV8 particles in cell lysates and culture media changes with time and is dependent on the recombinant vector

Molecular therapy. Methods & clinical development, 2016-01, Vol.3 (C), p.16015-16015, Article 16015

2016

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Substrate specificity and inhibitor analyses of human steroid 5β-reductase (AKR1D1)

Steroids, 2011-04, Vol.76 (5), p.484-490

2011

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Molecular Basis of 1‑Deoxygalactonojirimycin Arylthiourea Binding to Human α‑Galactosidase A: Pharmacological Chaperoning Efficacy on Fabry Disease Mutants

ACS chemical biology, 2014-07, Vol.9 (7), p.1460-1469

2014

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Conversion of human steroid 5β-reductase (AKR1D1) into 3β-hydroxysteroid dehydrogenase by single point mutation E120H: example of perfect enzyme engineering

The Journal of biological chemistry, 2012-05, Vol.287 (20), p.16609-16622

2012

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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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Catalytic Properties of Intramembrane Aspartyl Protease Substrate Hydrolysis Evaluated Using a FRET Peptide Cleavage Assay

ACS chemical biology, 2015-09, Vol.10 (9), p.2166-2174

2015

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Structure and catalytic mechanism of human steroid 5β-reductase (AKR1D1)

Molecular and cellular endocrinology, 2009-03, Vol.301 (1), p.191-198

2009

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Permeation and Activation of the M2 Ion Channel of Influenza A Virus

The Journal of biological chemistry, 2000-10, Vol.275 (40), p.31038-31050

2000

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Conversion of scFv peptide-binding specificity for crystal chaperone development

Protein engineering, design and selection, 2011-05, Vol.24 (5), p.419-428

2011

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Crystal Structure of Human Liver Δ4-3-Ketosteroid 5β-Reductase (AKR1D1) and Implications for Substrate Binding and Catalysis

The Journal of biological chemistry, 2008-06, Vol.283 (24), p.16830-16839

2008

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Characterization of Disease-related 5β-Reductase (AKR1D1) Mutations Reveals Their Potential to Cause Bile Acid Deficiency

The Journal of biological chemistry, 2010-08, Vol.285 (32), p.24529-24537

2010

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Inhibition of Human Steroid 5β-Reductase (AKR1D1) by Finasteride and Structure of the Enzyme-Inhibitor Complex

The Journal of biological chemistry, 2009-07, Vol.284 (30), p.19786-19790

2009

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Crystal Structure of Human Liver delta {4}-3-Ketosteroid 5 beta-Reductase (AKR1D1) and Implications for Substrate Binding and Catalysis

The Journal of biological chemistry, 2008-06, Vol.283 (24)

2008

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Conversion of Human Steroid 5[beta]-Reductase (AKR1D1) into 3[beta]-Hydroxysteroid Dehydrogenase by Single Point Mutation E120H: Example of Perfect Enzyme Engineering

The Journal of biological chemistry, 2012-10, Vol.287 ((20) ; 05, 2012)

2012

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Characterization of Disease-related 5b-Reductase (AKR1D1) Mutations Reveals Their Potential to Cause Bile Acid Deficiency

The Journal of biological chemistry, 2010-08, Vol.285 (32), p.24529-24537

2010

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Conversion of Human Steroid 5β-Reductase (AKR1D1) into 3β-Hydroxysteroid Dehydrogenase by Single Point Mutation E120H

The Journal of biological chemistry, 2012-05, Vol.287 (20), p.16609-16622

2012

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Molecular Basis of 1-Deoxygalactonojirimycin Arylthiourea Binding to Human [alpha]-Galactosidase A: Pharmacological Chaperoning Efficacy on Fabry Disease Mutants

ACS chemical biology, 2016-05, Vol.9 ((7) ; 07, 2014)

2016

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Inhibition of Human Steroid 5Î²-Reductase (AKR1D1) by Finasteride and Structure of the Enzyme-Inhibitor Complex

The Journal of biological chemistry, 2009-07, Vol.284 (30), p.19786

2009

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Inhibition of human steroid 5beta-reductase (AKR1D1) by finasteride and structure of the enzyme-inhibitor complex

The Journal of biological chemistry, 2009-07, Vol.284 (30), p.19786

2009

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Crystal Structure of Human Liver [delta][superscript 4]-3-Ketosteroid 5[beta]-Reductase (AKR1D1) and Implications for Substrate Binding and Catalysis

The Journal of biological chemistry, 2008-07, Vol.283 ((24) ; 06, 2008)

2008

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Crystal Structure of Human Liver Î4-3-Ketosteroid 5Î²-Reductase (AKR1D1) and Implications for Substrate Binding and Catalysis

The Journal of biological chemistry, 2008-06, Vol.283 (24), p.16830

2008

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Crystal Structure of Human Liver Δ4-3-Ketosteroid 5β-Reductase (AKR1D1) and Implications for Substrate Binding and CatalysisS

The Journal of biological chemistry, 2008-06, Vol.283 (24), p.16830-16839

2008

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Crystal structure of human liver Delta4-3-ketosteroid 5beta-reductase (AKR1D1) and implications for substrate binding and catalysis

The Journal of biological chemistry, 2008-06, Vol.283 (24), p.16830-16839

2008

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Human aldo–keto reductases: Function, gene regulation, and single nucleotide polymorphisms

Lentiviral Vector Production from a Stable Packaging Cell Line Using a Packed Bed Bioreactor

Distribution of AAV8 particles in cell lysates and culture media changes with time and is dependent on the recombinant vector

Substrate specificity and inhibitor analyses of human steroid 5β-reductase (AKR1D1)

Molecular Basis of 1‑Deoxygalactonojirimycin Arylthiourea Binding to Human α‑Galactosidase A: Pharmacological Chaperoning Efficacy on Fabry Disease Mutants

Conversion of human steroid 5β-reductase (AKR1D1) into 3β-hydroxysteroid dehydrogenase by single point mutation E120H: example of perfect enzyme engineering

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

Catalytic Properties of Intramembrane Aspartyl Protease Substrate Hydrolysis Evaluated Using a FRET Peptide Cleavage Assay

Structure and catalytic mechanism of human steroid 5β-reductase (AKR1D1)

Permeation and Activation of the M2 Ion Channel of Influenza A Virus

Conversion of scFv peptide-binding specificity for crystal chaperone development

Crystal Structure of Human Liver Δ4-3-Ketosteroid 5β-Reductase (AKR1D1) and Implications for Substrate Binding and Catalysis

Characterization of Disease-related 5β-Reductase (AKR1D1) Mutations Reveals Their Potential to Cause Bile Acid Deficiency

Inhibition of Human Steroid 5β-Reductase (AKR1D1) by Finasteride and Structure of the Enzyme-Inhibitor Complex

Crystal Structure of Human Liver delta {4}-3-Ketosteroid 5 beta-Reductase (AKR1D1) and Implications for Substrate Binding and Catalysis

Conversion of Human Steroid 5[beta]-Reductase (AKR1D1) into 3[beta]-Hydroxysteroid Dehydrogenase by Single Point Mutation E120H: Example of Perfect Enzyme Engineering

Characterization of Disease-related 5b-Reductase (AKR1D1) Mutations Reveals Their Potential to Cause Bile Acid Deficiency

Conversion of Human Steroid 5β-Reductase (AKR1D1) into 3β-Hydroxysteroid Dehydrogenase by Single Point Mutation E120H

Molecular Basis of 1-Deoxygalactonojirimycin Arylthiourea Binding to Human [alpha]-Galactosidase A: Pharmacological Chaperoning Efficacy on Fabry Disease Mutants

Inhibition of Human Steroid 5Î²-Reductase (AKR1D1) by Finasteride and Structure of the Enzyme-Inhibitor Complex

Inhibition of human steroid 5beta-reductase (AKR1D1) by finasteride and structure of the enzyme-inhibitor complex

Crystal Structure of Human Liver [delta][superscript 4]-3-Ketosteroid 5[beta]-Reductase (AKR1D1) and Implications for Substrate Binding and Catalysis

Crystal Structure of Human Liver Î4-3-Ketosteroid 5Î²-Reductase (AKR1D1) and Implications for Substrate Binding and Catalysis

Crystal Structure of Human Liver Δ4-3-Ketosteroid 5β-Reductase (AKR1D1) and Implications for Substrate Binding and CatalysisS

Crystal structure of human liver Delta4-3-ketosteroid 5beta-reductase (AKR1D1) and implications for substrate binding and catalysis

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