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Proline dehydrogenase 2 (PRODH2) is a hydroxyproline dehydrogenase (HYPDH) and molecular target for treating primary hyperoxaluria

Biochemical journal, 2015-03, Vol.466 (2), p.273-281

2015

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Crystal structure of the thioesterase domain of human fatty acid synthase inhibited by Orlistat

Nature structural & molecular biology, 2007-08, Vol.14 (8), p.704-709

2007

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Free methionine-(R)-sulfoxide reductase from Escherichia coli reveals a new GAF domain function

Proceedings of the National Academy of Sciences - PNAS, 2007-06, Vol.104 (23), p.9597-9602

2007

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Structure of the sulphiredoxin-peroxiredoxin complex reveals an essential repair embrace

Nature, 2008-01, Vol.451 (7174), p.98-101

2008

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Structural and biochemical studies of human 4-hydroxy-2-oxoglutarate aldolase: implications for hydroxyproline metabolism in primary hyperoxaluria

PloS one, 2011-10, Vol.6 (10), p.e26021-e26021

2011

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Reduction of Cysteine Sulfinic Acid in Peroxiredoxin by Sulfiredoxin Proceeds Directly through a Sulfinic Phosphoryl Ester Intermediate

The Journal of biological chemistry, 2008-08, Vol.283 (35), p.23846-23851

2008

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Specificity of Human Sulfiredoxin for Reductant and Peroxiredoxin Oligomeric State

Antioxidants, 2021-06, Vol.10 (6), p.946

2021

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Metabolism of [13C5]hydroxyproline in vitro and in vivo: implications for primary hyperoxaluria

American journal of physiology: Gastrointestinal and liver physiology, 2012-03, Vol.302 (6), p.G637-G643

2012

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The Thioredoxin Domain of Neisseria gonorrhoeae PilB Can Use Electrons from DsbD to Reduce Downstream Methionine Sulfoxide Reductases

The Journal of biological chemistry, 2006-10, Vol.281 (43), p.32668-32675

2006

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Use of Dimedone-Based Chemical Probes for Sulfenic Acid Detection: Evaluation of Conditions Affecting Probe Incorporation into Redox-Sensitive Proteins

Methods in enzymology, 2010, Vol.473, p.77-94

2010

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Crystal Structure and Substrate Specificity of Human Thioesterase 2: INSIGHTS INTO THE MOLECULAR BASIS FOR THE MODULATION OF FATTY ACID SYNTHASE

The Journal of biological chemistry, 2016-02, Vol.291 (7), p.3520-3530

2016

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Protein Engineering of the Quaternary Sulfiredoxin·Peroxiredoxin Enzyme·Substrate Complex Reveals the Molecular Basis for Cysteine Sulfinic Acid Phosphorylation

The Journal of biological chemistry, 2009-11, Vol.284 (48), p.33305-33310

2009

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Structural Basis for the Retroreduction of Inactivated Peroxiredoxins by Human Sulfiredoxin

Biochemistry (Easton), 2005-06, Vol.44 (24), p.8634-8642

2005

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Crystal Structure and Substrate Specificity of Human Thioesterase 2

The Journal of biological chemistry, 2016-02, Vol.291 (7), p.3520-3530

2016

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Metabolism of [13C5]hydroxyproline in vitro and in vivo: implications for primary hyperoxaluria

American journal of physiology: Gastrointestinal and liver physiology, 2012, Vol.65 (3)

2012

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Abstract 2675: Characterization of human thioesterase 2 and its potential for breast cancer drug discovery

Cancer research (Chicago, Ill.), 2010-04, Vol.70 (8_Supplement), p.2675-2675

2010

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Protein Engineering of the Quaternary SulfiredoxinÂ·Peroxiredoxin EnzymeÂ·Substrate Complex Reveals the Molecular Basis for Cysteine Sulfinic Acid Phosphorylation

The Journal of biological chemistry, 2009-11, Vol.284 (48), p.33305

2009

Volltextzugriff (PDF)

Reduction of Cysteine Sulfinic Acid in Peroxiredoxin by Sulfiredoxin Proceeds Directly through a Sulfinic Phosphoryl Ester IntermediateS

The Journal of biological chemistry, 2008-08, Vol.283 (35), p.23846-23851

2008

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Human fatty acid synthase complexed with the anti‐tumor compound Orlistat: mechanism of inhibition and chain‐length selectivity

The FASEB journal, 2007, Vol.21 (6), p.LB23-LB23

2007

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Protein engineering of the quaternary sulfiredoxin.peroxiredoxin enzyme.substrate complex reveals the molecular basis for cysteine sulfinic acid phosphorylation

The Journal of biological chemistry, 2009-11, Vol.284 (48), p.33305

2009

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Use of Dimedone-Based Chemical Probes for Sulfenic Acid Detection

Methods in Enzymology, 2010, Vol.473, p.77-94

2010

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Association of In Utero Exposures With Risk of Early Natural Menopause

American journal of epidemiology, 2022-03, Vol.191 (5), p.775-786

2022

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Association of oral contraceptives and tubal ligation with antimüllerian hormone

Menopause (New York, N.Y.), 2022-02, Vol.29 (2), p.225

2022

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Association of Parity and Breastfeeding With Risk of Early Natural Menopause

JAMA network open, 2020-01, Vol.3 (1), p.e1919615-e1919615

2020

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Association of Premenstrual Syndrome with Blood Pressure in Young Adult Women

Journal of women's health (Larchmont, N.Y. 2002), 2016-11, Vol.25 (11), p.1122

2016

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Proline dehydrogenase 2 (PRODH2) is a hydroxyproline dehydrogenase (HYPDH) and molecular target for treating primary hyperoxaluria

Crystal structure of the thioesterase domain of human fatty acid synthase inhibited by Orlistat

Free methionine-(R)-sulfoxide reductase from Escherichia coli reveals a new GAF domain function

Structure of the sulphiredoxin-peroxiredoxin complex reveals an essential repair embrace

Structural and biochemical studies of human 4-hydroxy-2-oxoglutarate aldolase: implications for hydroxyproline metabolism in primary hyperoxaluria

Reduction of Cysteine Sulfinic Acid in Peroxiredoxin by Sulfiredoxin Proceeds Directly through a Sulfinic Phosphoryl Ester Intermediate

Specificity of Human Sulfiredoxin for Reductant and Peroxiredoxin Oligomeric State

Metabolism of [13C5]hydroxyproline in vitro and in vivo: implications for primary hyperoxaluria

The Thioredoxin Domain of Neisseria gonorrhoeae PilB Can Use Electrons from DsbD to Reduce Downstream Methionine Sulfoxide Reductases

Use of Dimedone-Based Chemical Probes for Sulfenic Acid Detection: Evaluation of Conditions Affecting Probe Incorporation into Redox-Sensitive Proteins

Crystal Structure and Substrate Specificity of Human Thioesterase 2: INSIGHTS INTO THE MOLECULAR BASIS FOR THE MODULATION OF FATTY ACID SYNTHASE

Protein Engineering of the Quaternary Sulfiredoxin·Peroxiredoxin Enzyme·Substrate Complex Reveals the Molecular Basis for Cysteine Sulfinic Acid Phosphorylation

Structural Basis for the Retroreduction of Inactivated Peroxiredoxins by Human Sulfiredoxin

Crystal Structure and Substrate Specificity of Human Thioesterase 2

Metabolism of [13C5]hydroxyproline in vitro and in vivo: implications for primary hyperoxaluria

Abstract 2675: Characterization of human thioesterase 2 and its potential for breast cancer drug discovery

Protein Engineering of the Quaternary SulfiredoxinÂ·Peroxiredoxin EnzymeÂ·Substrate Complex Reveals the Molecular Basis for Cysteine Sulfinic Acid Phosphorylation

Reduction of Cysteine Sulfinic Acid in Peroxiredoxin by Sulfiredoxin Proceeds Directly through a Sulfinic Phosphoryl Ester IntermediateS

Human fatty acid synthase complexed with the anti‐tumor compound Orlistat: mechanism of inhibition and chain‐length selectivity

Protein engineering of the quaternary sulfiredoxin.peroxiredoxin enzyme.substrate complex reveals the molecular basis for cysteine sulfinic acid phosphorylation

Use of Dimedone-Based Chemical Probes for Sulfenic Acid Detection

Association of In Utero Exposures With Risk of Early Natural Menopause

Association of oral contraceptives and tubal ligation with antimüllerian hormone

Association of Parity and Breastfeeding With Risk of Early Natural Menopause

Association of Premenstrual Syndrome with Blood Pressure in Young Adult Women

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