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Analysis of the organic hydroperoxide response of Chromobacterium violaceum reveals that OhrR is a cys-based redox sensor regulated by thioredoxin

PloS one, 2012-10, Vol.7 (10), p.e47090

2012

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Global analysis of erythroid cells redox status reveals the involvement of Prdx1 and Prdx2 in the severity of beta thalassemia

PloS one, 2018-12, Vol.13 (12), p.e0208316-e0208316

2018

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Structural insights on the efficient catalysis of hydroperoxide reduction by Ohr: Crystallographic and molecular dynamics approaches

PloS one, 2018-05, Vol.13 (5), p.e0196918

2018

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Reduction of 1-Cys peroxiredoxins by ascorbate changes the thiol-specific antioxidant paradigm, revealing another function of vitamin C

Proceedings of the National Academy of Sciences - PNAS, 2007-03, Vol.104 (12), p.4886-4891

2007

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Monitoring H2O2 inside Aspergillus fumigatus with an Integrated Microelectrode: The Role of Peroxiredoxin Protein Prx1

Analytical chemistry (Washington), 2018-02, Vol.90 (4), p.2587-2593

2018

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Analyses of the three 1-Cys Peroxiredoxins from Aspergillus fumigatus reveal that cytosolic Prx1 is central to H2O2 metabolism and virulence

Scientific reports, 2018-08, Vol.8 (1), p.1-18, Article 12314

2018

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Thiol and Sulfenic Acid Oxidation of AhpE, the One-Cysteine Peroxiredoxin from Mycobacterium tuberculosis: Kinetics, Acidity Constants, and Conformational Dynamics

Biochemistry (Easton), 2009-10, Vol.48 (40), p.9416-9426

2009

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The Roles of Peroxiredoxin and Thioredoxin in Hydrogen Peroxide Sensing and in Signal Transduction

Molecules and Cells, 2016, 39(1), , pp.65-71

2016

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Disulfide Biochemistry in 2-Cys Peroxiredoxin: Requirement of Glu50 and Arg146 for the Reduction of Yeast Tsa1 by Thioredoxin

Journal of molecular biology, 2012-11, Vol.424 (1-2), p.28-41

2012

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Insights into the Specificity of Thioredoxin Reductase−Thioredoxin Interactions. A Structural and Functional Investigation of the Yeast Thioredoxin System

Biochemistry (Easton), 2010-04, Vol.49 (15), p.3317-3326

2010

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Ohr (Organic Hydroperoxide Resistance Protein) Possesses a Previously Undescribed Activity, Lipoyl-dependent Peroxidase

The Journal of biological chemistry, 2010-07, Vol.285 (29), p.21943-21950

2010

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The Peroxidatic Thiol of Peroxiredoxin 1 is Nitrosated by Nitrosoglutathione but Coordinates to the Dinitrosyl Iron Complex of Glutathione

Antioxidants, 2020-03, Vol.9 (4), p.276

2020

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The essential gene YMR134W from Saccharomyces cerevisiae is important for appropriate mitochondrial iron utilization and the ergosterol biosynthetic pathway

FEBS letters, 2013-09, Vol.587 (18), p.3008-3013

2013

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20S proteasome activity is modified via S-glutathionylation based on intracellular redox status of the yeast Saccharomyces cerevisiae: Implications for the degradation of oxidized proteins

Archives of biochemistry and biophysics, 2014-09, Vol.557, p.65-71

2014

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The bicarbonate/carbon dioxide pair increases hydrogen peroxide-mediated hyperoxidation of human peroxiredoxin 1

The Journal of biological chemistry, 2019-09, Vol.294 (38), p.14055-14067

2019

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Rapid peroxynitrite reduction by human peroxiredoxin 3: Implications for the fate of oxidants in mitochondria

Free radical biology & medicine, 2019-01, Vol.130, p.369-378

2019

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The promoter of filamentation (POF1) protein from Saccharomyces cerevisiae is an ATPase involved in the protein quality control process

BMC microbiology, 2011-12, Vol.11 (1), p.268-268, Article 268

2011

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Absence of Gem1 (mammalian Miro/Rhot) mitigates alpha-synuclein toxicity in a yeast model of Parkinson's disease

Molecular and cellular neuroscience, 2022-09, Vol.122, p.103757-103757, Article 103757

2022

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Role of glutaredoxin 2 and cytosolic thioredoxins in cysteinyl-based redox modification of the 20S proteasome

The FEBS journal, 2008-06, Vol.275 (11), p.2942-2955

2008

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Oxidative Modification of Proteins: From Damage to Catalysis, Signaling, and Beyond

Antioxidants & redox signaling, 2021-10, Vol.35 (12), p.1016-1080

2021

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Yeast oxidative stress response. Influences of cytosolic thioredoxin peroxidase I and of the mitochondrial functional state

The FEBS journal, 2006-02, Vol.273 (4), p.805-816

2006

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Urate hydroperoxide oxidizes human peroxiredoxin 1 and peroxiredoxin 2

The Journal of biological chemistry, 2017-05, Vol.292 (21), p.8705-8715

2017

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Assessment of Submitochondrial Protein Localization in Budding Yeast Saccharomyces cerevisiae

Journal of visualized experiments, 2021-07 (173)

2021

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Molecular Structure and Functional Analysis of Pyocin S8 from Pseudomonas aeruginosa Reveals the Essential Requirement of a Glutamate Residue in the H-N-H Motif for DNase Activity

Journal of bacteriology, 2020-10, Vol.202 (21)

2020

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Proteolytic cleavage by the inner membrane peptidase (IMP) complex or Oct1 peptidase controls the localization of the yeast peroxiredoxin Prx1 to distinct mitochondrial compartments

The Journal of biological chemistry, 2017-10, Vol.292 (41), p.17011-17024

2017

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Analysis of the organic hydroperoxide response of Chromobacterium violaceum reveals that OhrR is a cys-based redox sensor regulated by thioredoxin

Global analysis of erythroid cells redox status reveals the involvement of Prdx1 and Prdx2 in the severity of beta thalassemia

Structural insights on the efficient catalysis of hydroperoxide reduction by Ohr: Crystallographic and molecular dynamics approaches

Reduction of 1-Cys peroxiredoxins by ascorbate changes the thiol-specific antioxidant paradigm, revealing another function of vitamin C

Monitoring H2O2 inside Aspergillus fumigatus with an Integrated Microelectrode: The Role of Peroxiredoxin Protein Prx1

Analyses of the three 1-Cys Peroxiredoxins from Aspergillus fumigatus reveal that cytosolic Prx1 is central to H2O2 metabolism and virulence

Thiol and Sulfenic Acid Oxidation of AhpE, the One-Cysteine Peroxiredoxin from Mycobacterium tuberculosis: Kinetics, Acidity Constants, and Conformational Dynamics

The Roles of Peroxiredoxin and Thioredoxin in Hydrogen Peroxide Sensing and in Signal Transduction

Disulfide Biochemistry in 2-Cys Peroxiredoxin: Requirement of Glu50 and Arg146 for the Reduction of Yeast Tsa1 by Thioredoxin

Insights into the Specificity of Thioredoxin Reductase−Thioredoxin Interactions. A Structural and Functional Investigation of the Yeast Thioredoxin System

Ohr (Organic Hydroperoxide Resistance Protein) Possesses a Previously Undescribed Activity, Lipoyl-dependent Peroxidase

The Peroxidatic Thiol of Peroxiredoxin 1 is Nitrosated by Nitrosoglutathione but Coordinates to the Dinitrosyl Iron Complex of Glutathione

The essential gene YMR134W from Saccharomyces cerevisiae is important for appropriate mitochondrial iron utilization and the ergosterol biosynthetic pathway

20S proteasome activity is modified via S-glutathionylation based on intracellular redox status of the yeast Saccharomyces cerevisiae: Implications for the degradation of oxidized proteins

The bicarbonate/carbon dioxide pair increases hydrogen peroxide-mediated hyperoxidation of human peroxiredoxin 1

Rapid peroxynitrite reduction by human peroxiredoxin 3: Implications for the fate of oxidants in mitochondria

The promoter of filamentation (POF1) protein from Saccharomyces cerevisiae is an ATPase involved in the protein quality control process

Absence of Gem1 (mammalian Miro/Rhot) mitigates alpha-synuclein toxicity in a yeast model of Parkinson's disease

Role of glutaredoxin 2 and cytosolic thioredoxins in cysteinyl-based redox modification of the 20S proteasome

Oxidative Modification of Proteins: From Damage to Catalysis, Signaling, and Beyond

Yeast oxidative stress response. Influences of cytosolic thioredoxin peroxidase I and of the mitochondrial functional state

Urate hydroperoxide oxidizes human peroxiredoxin 1 and peroxiredoxin 2

Assessment of Submitochondrial Protein Localization in Budding Yeast Saccharomyces cerevisiae

Molecular Structure and Functional Analysis of Pyocin S8 from Pseudomonas aeruginosa Reveals the Essential Requirement of a Glutamate Residue in the H-N-H Motif for DNase Activity

Proteolytic cleavage by the inner membrane peptidase (IMP) complex or Oct1 peptidase controls the localization of the yeast peroxiredoxin Prx1 to distinct mitochondrial compartments

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