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Publications by Christopher Horst Lillig

Both Thioredoxin 2 and Glutaredoxin 2 Contribute to the Reduction of the Mitochondrial 2-Cys Peroxiredoxin Prx3

Journal of Biological Chemistry

English

The Reducing Activity of Glutaredoxin 3 Toward Cytoplasmic Substrate Proteins Is Restricted by Methionine 43†

Biochemistry

2007

English

Related publications

Molecular Basis for the Resistance of Human Mitochondrial 2-Cys Peroxiredoxin 3 to Hyperoxidation

Journal of Biological Chemistry

English

Reaction Mechanism of Plant 2-Cys Peroxiredoxin

Journal of Biological Chemistry

English

Chloroplast NADPH-Dependent Thioredoxin Reductase From Chlorella Vulgaris Alleviates Environmental Stresses in Yeast Together With 2-Cys Peroxiredoxin

PLoS ONE

Multidisciplinary

2012

English

Catalytic THR or Ser Residue Modulates Structural Switches in 2-Cys Peroxiredoxin by Distinct Mechanisms

Scientific Reports

Multidisciplinary

2016

English

Oxidation of a Eukaryotic 2-Cys Peroxiredoxin Is a Molecular Switch Controlling the Transcriptional Response to Increasing Levels of Hydrogen Peroxide

Journal of Biological Chemistry

English

Calcium and Magnesium Ions Modulate the Oligomeric State and Function of Mitochondrial 2-Cys Peroxiredoxins in Leishmania Parasites

Journal of Biological Chemistry

English

Characterization ofEscherichia coliNull Mutants for Glutaredoxin 2

Journal of Biological Chemistry

English

The Plastidic 2-Cysteine Peroxiredoxin Is a Target for a Thioredoxin Involved in the Protection of the Photosynthetic Apparatus Against Oxidative Damage

English

Crystallization and Preliminary X-Ray Analysis of a Truncated Mutant of Yeast Nuclear Thiol Peroxidase, a Novel Atypical 2-Cys Peroxiredoxin

Acta Crystallographica Section F Structural Biology and Crystallization Communications

2005

English

Amanote Research

Discover open access scientific publications

Search, annotate, share and cite publications

Publications by Christopher Horst Lillig

Both Thioredoxin 2 and Glutaredoxin 2 Contribute to the Reduction of the Mitochondrial 2-Cys Peroxiredoxin Prx3

The Reducing Activity of Glutaredoxin 3 Toward Cytoplasmic Substrate Proteins Is Restricted by Methionine 43†

Related publications

Molecular Basis for the Resistance of Human Mitochondrial 2-Cys Peroxiredoxin 3 to Hyperoxidation

Reaction Mechanism of Plant 2-Cys Peroxiredoxin

Chloroplast NADPH-Dependent Thioredoxin Reductase From Chlorella Vulgaris Alleviates Environmental Stresses in Yeast Together With 2-Cys Peroxiredoxin

Catalytic THR or Ser Residue Modulates Structural Switches in 2-Cys Peroxiredoxin by Distinct Mechanisms

Oxidation of a Eukaryotic 2-Cys Peroxiredoxin Is a Molecular Switch Controlling the Transcriptional Response to Increasing Levels of Hydrogen Peroxide

Calcium and Magnesium Ions Modulate the Oligomeric State and Function of Mitochondrial 2-Cys Peroxiredoxins in Leishmania Parasites

Characterization ofEscherichia coliNull Mutants for Glutaredoxin 2

The Plastidic 2-Cysteine Peroxiredoxin Is a Target for a Thioredoxin Involved in the Protection of the Photosynthetic Apparatus Against Oxidative Damage

Crystallization and Preliminary X-Ray Analysis of a Truncated Mutant of Yeast Nuclear Thiol Peroxidase, a Novel Atypical 2-Cys Peroxiredoxin