Extraordinary µs-ms backbone dynamics in Arabidopsis thaliana peroxiredoxin Q, Biochim. Biophys. Acta BBA -Proteins Proteomics, vol.1814, pp.1880-1890, 2011. ,
A Model of Redox Kinetics Implicates the Thiol Proteome in Cellular Hydrogen Peroxide Responses, Antioxid. Redox Signal, vol.13, pp.731-743, 2010. ,
Chemical proteomics reveals new targets of cysteine sulfinic acid reductase, Nat. Chem. Biol, vol.14, pp.995-1004, 2018. ,
Transit of H2O2 across the endoplasmic reticulum membrane is not sluggish. Free Radic, Biol. Med, vol.94, pp.157-160, 2016. ,
URL : https://hal.archives-ouvertes.fr/hal-02393406
Inhibition of cation efflux by antioxidants during oscillatory ion transport in mitochondria, FEBS Lett, vol.107, pp.151-154, 1979. ,
Kinetics and Mechanism of Peroxymonocarbonate Formation, Inorg. Chem, vol.49, pp.11287-11296, 2010. ,
Use of Viscogens, dNTP?S, and Rhodium(III) as Probes in Stopped-Flow Experiments To Obtain New Evidence for the Mechanism of Catalysis by DNA Polymerase ? ?, ? . Biochemistry, vol.44, pp.5177-5187, 2005. ,
Apparent Hydroxyl Radical Production by Peroxinitrite: Implications for Endothelial Injury from Nitric Oxide and Superoxide, Med. Sci, vol.5, 1990. ,
Protein Oxidation in Aging, Disease, and Oxidative Stress, J. Biol. Chem, vol.272, pp.20313-20316, 1997. ,
A scaffold protein that chaperones a cysteine-sulfenic acid in H2O2 signaling, Nat. Chem. Biol, vol.13, pp.909-915, 2017. ,
URL : https://hal.archives-ouvertes.fr/hal-01652643
Aquaporin-facilitated transmembrane diffusion of hydrogen peroxide, Biochim. Biophys. Acta BBA -Gen. Subj, vol.1840, pp.1596-1604, 2014. ,
ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin, Nature, vol.425, pp.980-984, 2003. ,
Novel hyperoxidation resistance motifs in 2-Cys peroxiredoxins, J. Biol. Chem, vol.293, pp.11901-11912, 2018. ,
Novel hyperoxidation resistance motifs in 2-Cys peroxiredoxins, J. Biol. Chem, vol.293, pp.11901-11912, 2018. ,
Evidence That Glutathione and the Glutathione System Efficiently Recycle 1-Cys Sulfiredoxin In Vivo, Antioxid. Redox Signal, vol.22, pp.731-743, 2015. ,
URL : https://hal.archives-ouvertes.fr/hal-01451669
Hyperoxidation of mitochondrial peroxiredoxin limits H 2 O 2 -induced cell death in yeast, EMBO J, vol.38, 2019. ,
, , 2013.
, Dissection of a Redox Relay: H2O2-Dependent Activation of the Transcription Factor Pap1 through the Peroxidatic Tpx1-Thioredoxin Cycle, Cell Rep, vol.5, pp.1413-1424
The Peroxiredoxin Family: An Unfolding Story, Macromolecular Protein Complexes, pp.127-147, 2017. ,
Lack of an Efficient Endoplasmic Reticulumlocalized Recycling System Protects Peroxiredoxin IV from Hyperoxidation, J. Biol. Chem, vol.289, pp.5490-5498, 2014. ,
In Vivo Characterization of I91T Sod2 Polymorphism of Saccharomyces cerevisiae, J. Cell. Biochem, vol.118, pp.1078-1086, 2017. ,
Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes, Proc. Natl. Acad. Sci, vol.91, pp.7017-7021, 1994. ,
Divergence of Function in the Thioredoxin Fold Suprafamily: Evidence for Evolution of Peroxiredoxins from a Thioredoxin-like Ancestor ?, Biochemistry, vol.43, pp.13981-13995, 2004. ,
The thioredoxin reductase inhibitor auranofin triggers apoptosis through a Bax/Bak-dependent process that involves peroxiredoxin 3 oxidation, Biochem. Pharmacol, vol.76, pp.1097-1109, 2008. ,
Protein Quality Control under Oxidative Stress Conditions, J. Mol. Biol, vol.427, pp.1549-1563, 2015. ,
Differential parameters between cytosolic 2-Cys peroxiredoxins, PRDX1 and PRDX2: PRDX1, PRDX2 differential parameters, Protein Sci, 2018. ,
Differential parameters between cytosolic 2-Cys peroxiredoxins, PRDX1 and PRDX2: PRDX1, PRDX2 differential parameters, Protein Sci, vol.28, pp.191-201, 2019. ,
Insights into the catalytic mechanism of the Bcp family: Functional and structural analysis of Bcp1 from Sulfolobus solfataricus, Proteins Struct. Funct. Bioinforma, vol.76, pp.995-1006, 2009. ,
Inhibition of copper-mediated low density lipoprotein peroxidation by quinoline and indolinone nitroxide radicals, Biochem. Pharmacol, vol.48, pp.1155-1161, 1994. ,
Inactivation of a Peroxiredoxin by Hydrogen Peroxide Is Critical for Thioredoxin-Mediated Repair of Oxidized Proteins and Cell Survival, Mol. Cell, vol.45, pp.398-408, 2012. ,
A thiol peroxidase is an H2O2 receptor and redox-transducer in gene activation, Cell, vol.111, pp.471-481, 2002. ,
URL : https://hal.archives-ouvertes.fr/hal-01637040
A Thiol Peroxidase Is an H2O2 Receptor and Redox-Transducer in Gene Activation, Cell, vol.111, pp.471-481, 2002. ,
URL : https://hal.archives-ouvertes.fr/hal-01637040
Diffusion of peroxynitrite across erythrocyte membranes, Proc. Natl. Acad. Sci, vol.95, pp.3566-3571, 1998. ,
Using in vivo oxidation status of oneand two-component redox relays to determine H2O2 levels linked to signaling and toxicity, BMC Biol, vol.16, p.61, 2018. ,
Roles for the Two Cysteine Residues of AhpC in Catalysis of Peroxide Reduction by Alkyl Hydroperoxide Reductase from Salmonella typhimurium ?, Biochemistry, vol.36, pp.13349-13356, 1997. ,
A methionine sulfoxide reductase in Escherichia coli that reduces the R enantiomer of methionine sulfoxide, Biochem. Biophys. Res. Commun, vol.300, pp.378-382, 2003. ,
Factors Affecting Protein Thiol Reactivity and Specificity in Peroxide Reduction, Chem. Res. Toxicol, vol.24, pp.434-450, 2011. ,
URL : https://hal.archives-ouvertes.fr/pasteur-00685049
Kinetics and Mechanisms of Hypochlorous Acid Reactions, Arch. Biochem. Biophys, vol.323, pp.120-126, 1995. ,
Superoxide dismutase: A comparison of rate constants, Arch. Biochem. Biophys, vol.158, pp.396-400, 1973. ,
The Dual Functions of Thiol-Based Peroxidases in H 2 O 2 Scavenging and Signaling, Antioxid. Redox Signal, vol.10, pp.1565-1576, 2008. ,
Lipid peroxidation in cell death, Biochem. Biophys. Res. Commun, vol.482, pp.419-425, 2017. ,
Hydrogen peroxide: a metabolic by-product or a common mediator of ageing signals? 7, 2007. ,
Structural diversity in the recognition between reduced thioredoxin and its oxidized enzyme partners, Biomol. Concepts, vol.3, 2012. ,
Structural and Biochemical Characterization of Free Methionine-R -sulfoxide Reductase from Neisseria meningitidis, J. Biol. Chem, vol.285, pp.25033-25043, 2010. ,
URL : https://hal.archives-ouvertes.fr/hal-01690430
Typical 2-Cys peroxiredoxins--structures, mechanisms and functions, Febs J, vol.276, pp.2469-2477, 2009. ,
Structural Evidence that Peroxiredoxin Catalytic Power Is Based on Transition-State Stabilization, J. Mol. Biol, vol.402, pp.194-209, 2010. ,
Structure-based insights into the catalytic power and conformational dexterity of peroxiredoxins, Antioxid. Redox Signal, vol.15, pp.795-815, 2011. ,
Lifespan Control by Redox-Dependent Recruitment of Chaperones to Misfolded Proteins, Cell, vol.166, pp.140-151, 2016. ,
Molecular Basis for the Resistance of Human Mitochondrial 2-Cys Peroxiredoxin 3 to Hyperoxidation, J. Biol. Chem, vol.288, pp.29714-29723, 2013. ,
Molecular basis for the resistance of human mitochondrial 2-Cys peroxiredoxin 3 to hyperoxidation, J. Biol. Chem, vol.288, pp.29714-29723, 2013. ,
Cell signalling by reactive lipid species: new concepts and molecular mechanisms, Biochem. J, vol.442, pp.453-464, 2012. ,
Quantifying intracellular hydrogen peroxide perturbations in terms of concentration, Redox Biol, vol.2, pp.955-962, 2014. ,
Selenium and iron, two elemental rivals in the ferroptotic death process, Oncotarget, vol.9, 2018. ,
Genetic Analysis of Glutathione Peroxidase in Oxidative Stress Response of Saccharomyces cerevisiae, J. Biol. Chem, vol.274, pp.27002-27009, 1999. ,
Oxidative stress responses of the yeast Saccharomyces cerevisiae, vol.17, 1998. ,
Two enzymes in one; two yeast peroxiredoxins display oxidative stressdependent switching from a peroxidase to a molecular chaperone function, Cell, vol.117, pp.625-635, 2004. ,
Peroxiredoxin 1 functions as a signal peroxidase to receive, transduce, and transmit peroxide signals in mammalian cells. Free Radic, Biol. Med, vol.53, pp.1522-1530, 2012. ,
High-resolution solution structures of oxidized and reduced Escherichia coli thioredoxin, Structure, vol.2, pp.853-868, 1994. ,
Reduction of cysteine sulfinic acid in peroxiredoxin by sulfiredoxin proceeds directly through a sulfinic phosphoryl ester intermediate, J Biol Chem, vol.283, pp.23846-23851, 2008. ,
Structure of the sulphiredoxin-peroxiredoxin complex reveals an essential repair embrace, Nature, vol.451, pp.98-101, 2008. ,
Protein engineering of the quaternary sulfiredoxin.peroxiredoxin enzyme.substrate complex reveals the molecular basis for cysteine sulfinic acid phosphorylation, J Biol Chem, vol.284, pp.33305-33310, 2009. ,
A primer on peroxiredoxin biochemistry. Free Radic, Biol. Med, vol.80, pp.183-190, 2015. ,
The Formation of Lipid Hydroperoxide-Derived Amide-Type Lysine Adducts on Proteins: A Review of Current Knowledge, Lipid Hydroperoxide-Derived Modification of Biomolecules, pp.21-39, 2014. ,
Feedback Control of Adrenal Steroidogenesis via H2O2-Dependent, Reversible Inactivation of Peroxiredoxin III in Mitochondria, Mol. Cell, vol.46, pp.584-594, 2012. ,
The Isolation and Purification of a Specific "Protector"Protein Which Inhibits Enzyme Inactivation by a Thiol/Fe(III)/02Mixed-function Oxidation System, vol.8, 1988. ,
Crystal structures of human peroxiredoxin 6 in different oxidation states, Biochem. Biophys. Res. Commun, vol.477, pp.717-722, 2016. ,
Comparative genomics and experimental evolution of, Escherichia coli, vol.21, p.3, 2015. ,
NOX enzymes and the biology of reactive oxygen, Nat. Rev. Immunol, vol.4, pp.181-189, 2004. ,
A New Antioxidant with Alkyl Hydroperoxide Defense Properties in Yeast, J. Biol. Chem, vol.274, pp.4537-4544, 1999. ,
Crystal Structure of AhpE from Mycobacterium tuberculosis, a 1-Cys Peroxiredoxin, J. Mol. Biol, vol.346, pp.1035-1046, 2005. ,
The rise of oxygen in Earth's early ocean and atmosphere, Nature, vol.506, pp.307-315, 2014. ,
Peroxynitrite rapidly permeates phospholipid membranes, Proc. Natl. Acad. Sci, vol.94, pp.14243-14248, 1997. ,
Thioredoxin -a fold for all reasons, Structure, vol.3, pp.245-250, 1995. ,
Peroxymonocarbonate and Carbonate Radical Displace the Hydroxyl-like Oxidant in the Sod1 Peroxidase Activity under Physiological Conditions, Chem. Res. Toxicol, vol.22, pp.639-648, 2009. ,
NADPH Oxidases: A Perspective on Reactive Oxygen Species Production in Tumor Biology, Antioxid. Redox Signal, vol.20, pp.2873-2889, 2014. ,
Cellular Timekeeping: It's Redox o'Clock, Cold Spring Harb. Perspect. Biol, vol.10, 2018. ,
Over-production of Proteins inEscherichia coli: Mutant Hosts that Allow Synthesis of some Membrane Proteins and Globular Proteins at High Levels, J. Mol. Biol, vol.260, pp.289-298, 1996. ,
Model for the Exceptional Reactivity of Peroxiredoxins 2 and 3 with Hydrogen Peroxide: A KINETIC AND COMPUTATIONAL STUDY, J. Biol. Chem, vol.286, pp.18048-18055, 2011. ,
, Evidence for a New Sub-class of, 2004.
URL : https://hal.archives-ouvertes.fr/hal-01636385
, Methionine Sulfoxide Reductases B with an Alternative Thioredoxin Recognition Signature, J. Biol. Chem, vol.279, pp.42462-42468
Analysis of the peroxiredoxin family: Using active-site structure and sequence information for global classification and residue analysis, Proteins Struct. Funct. Bioinforma, vol.79, pp.947-964, 2011. ,
Evaluating peroxiredoxin sensitivity towards inactivation by peroxide substrates, Methods Enzymol, vol.527, 2013. ,
Structure of TSA2 reveals novel features of the active-site loop of peroxiredoxins, Acta Crystallogr. Sect. Struct. Biol, vol.72, pp.158-167, 2016. ,
Reactions of yeast thioredoxin peroxidases I and II with hydrogen peroxide and peroxynitrite: Rate constants by competitive kinetics. Free Radic, Biol. Med, vol.42, pp.326-334, 2007. ,
A Robust Model for Circadian Redox Oscillations, Int. J. Mol. Sci, vol.20, p.2368, 2019. ,
Characterization of the methionine sulfoxide reductase activities of PILB, a probable virulence factor from Neisseria meningitidis, J Biol Chem, vol.277, pp.12016-12022, 2002. ,
URL : https://hal.archives-ouvertes.fr/hal-01690847
Circadian clocks in human red blood cells, Nature, vol.469, pp.498-503, 2011. ,
Circadian rhythms persist without transcription in a eukaryote, Nature, vol.469, pp.554-558 ,
Peroxynitrite Formed by Simultaneous Nitric Oxide and Superoxide Generation Causes Cyclosporin-A-Sensitive Mitochondrial Calcium Efflux and Depolarisation, Eur. J. Biochem, vol.234, pp.231-239, 1995. ,
A universal entropy-driven mechanism for thioredoxin-target recognition, Proc. Natl. Acad. Sci, vol.112, pp.7960-7965, 2015. ,
Distinct Physiological Functions of Thiol Peroxidase Isoenzymes in Saccharomyces cerevisiae, J. Biol. Chem, vol.275, pp.5723-5732, 2000. ,
Dissecting Peroxiredoxin Catalysis: Separating Binding, Peroxidation, and Resolution for a Bacterial AhpC, Biochemistry, vol.54, pp.1567-1575, 2015. ,
Orchestrating Redox Signaling Networks through Regulatory Cysteine Switches, ACS Chem. Biol, vol.5, pp.47-62, 2010. ,
Mapping the Active Site Helix-to-Strand Conversion of CxxxxC Peroxiredoxin Q Enzymes, Biochemistry, vol.51, pp.7638-7650, 2012. ,
The Sensitive Balance between the Fully Folded and Locally Unfolded Conformations of a Model Peroxiredoxin, Biochemistry, vol.52, pp.8708-8721, 2013. ,
Peroxiredoxins: guardians against oxidative stress and modulators of peroxide signaling, Trends Biochem. Sci, vol.40, pp.435-445, 2015. ,
, Peroxiredoxin Catalysis at Atomic Resolution. Structure, vol.24, pp.1668-1678, 2016.
, , 2007.
, The High Reactivity of Peroxiredoxin 2 with H 2 O 2 Is Not Reflected in Its Reaction with Other Oxidants and Thiol Reagents, J. Biol. Chem, vol.282, pp.11885-11892
Hyperoxidation of Peroxiredoxins 2 and 3: RATE CONSTANTS FOR THE REACTIONS OF THE SULFENIC ACID OF THE PEROXIDATIC CYSTEINE, J. Biol. Chem, vol.288, pp.14170-14177, 2013. ,
Enzymes or redox couples? The kinetics of thioredoxin and glutaredoxin reactions in a systems biology context, Biochem. J, vol.417, pp.269-277, 2009. ,
Differential Kinetics of Two-Cysteine Peroxiredoxin Disulfide Formation Reveal a Novel Model for Peroxide Sensing, Biochemistry, vol.57, pp.3416-3424, 2018. ,
Peroxynitrite, a potent macrophage-derived oxidizing cytotoxin to combat invading pathogens: Peroxynitrite in Pathogen Invasion, BioFactors, vol.40, pp.215-225, 2014. ,
Proteomics Analysis of Cellular Response to Oxidative Stress: EVIDENCE FOR IN VIVO OVEROXIDATION OF PEROXIREDOXINS AT THEIR ACTIVE SITE, J. Biol, 2002. ,
, Chem, vol.277, pp.19396-19401
Enzyme Active Site Loop Revealed as a Gatekeeper for Cofactor Flip by Targeted Molecular Dynamics Simulations and FRET-Based Kinetics, ACS Catal, vol.9, pp.1337-1346, 2019. ,
URL : https://hal.archives-ouvertes.fr/hal-02022828
Unraveling the effects of peroxiredoxin 2 nitration; role of C-terminal tyrosine 193. Free Radic, Biol. Med, vol.141, pp.492-501, 2019. ,
Expanding the functional diversity of proteins through cysteine oxidation, Curr. Opin. Chem. Biol, vol.12, pp.746-754, 2008. ,
Oxidizing substrate specificity of Mycobacterium tuberculosis alkyl hydroperoxide reductase E: kinetics and mechanisms of oxidation and overoxidation. Free Radic, Biol. Med, vol.51, pp.464-473, 2011. ,
Intracellular messenger function of hydrogen peroxide and its regulation by peroxiredoxins, Curr Opin Cell Biol, vol.17, pp.183-189, 2005. ,
Active site mutagenesis and phospholipid hydroperoxide reductase activity of poplar type II peroxiredoxin, Physiol. Plant, vol.120, pp.57-62, 2004. ,
URL : https://hal.archives-ouvertes.fr/hal-02672433
Evidence for the Formation of a Covalent Thiosulfinate Intermediate with Peroxiredoxin in the Catalytic Mechanism of Sulfiredoxin, J. Biol. Chem, vol.283, pp.22371-22382, 2008. ,
URL : https://hal.archives-ouvertes.fr/hal-01652689
Catalytic Mechanism of Sulfiredoxin from Saccharomyces cerevisiae Passes through an Oxidized Disulfide Sulfiredoxin Intermediate That Is Reduced by Thioredoxin, J. Biol. Chem, vol.284, pp.33048-33055, 2009. ,
URL : https://hal.archives-ouvertes.fr/hal-01682337
Moonlighting by Different Stressors: Crystal Structure of the Chaperone Species of a 2-Cys Peroxiredoxin, Structure, vol.20, pp.429-439, 2012. ,
URL : https://hal.archives-ouvertes.fr/pasteur-00952065
Deletion of the four phospholipid hydroperoxide glutathione peroxidase genes accelerates aging in Caenorhabditis elegans, Genes Cells, vol.19, pp.778-792, 2014. ,
The crystal structures of oxidized forms of human peroxiredoxin 5 with an intramolecular disulfide bond confirm the proposed enzymatic mechanism for atypical 2-Cys peroxiredoxins, Arch. Biochem. Biophys, vol.477, pp.98-104, 2008. ,
Peroxiredoxin-2 and STAT3 form a redox relay for H2O2 signaling, Nat. Chem. Biol, vol.11, pp.64-70, 2015. ,
PREX: PeroxiRedoxin classification indEX, a database of subfamily assignments across the diverse peroxiredoxin family, Nucleic Acids Res, vol.39, pp.332-337, 2011. ,
The Conundrum of Hydrogen Peroxide Signaling and the Emerging Role of Peroxiredoxins as Redox Relay Hubs, Antioxid. Redox Signal, vol.28, pp.558-573, 2018. ,
Protein production by auto-induction in high-density shaking cultures, Protein Expr. Purif, vol.41, pp.207-234, 2005. ,
Disulfide Biochemistry in 2-Cys Peroxiredoxin: Requirement of Glu50 and Arg146 for the Reduction of Yeast Tsa1 by Thioredoxin, J. Mol. Biol, vol.424, pp.28-41, 2012. ,
A Comparative Study on the Hydroperoxide and Thiol Specificity of the Glutathione Peroxidase Family and Selenoprotein P, J. Biol. Chem, vol.277, pp.41254-41258, 2002. ,
GPX2 , Encoding a Phospholipid Hydroperoxide Glutathione Peroxidase Homologue, Codes for an Atypical 2-Cys Peroxiredoxin in Saccharomyces cerevisiae, J. Biol. Chem, vol.280, pp.42078-42087, 2005. ,
Redox Regulation of Protein Tyrosine Phosphatases: Structural and Chemical Aspects, Antioxid. Redox Signal, vol.15, pp.77-97, 2011. ,
Regeneration Mechanisms of Arabidopsis thaliana Methionine Sulfoxide Reductases B by Glutaredoxins and Thioredoxins, J. Biol. Chem, vol.284, pp.18963-18971, 2009. ,
URL : https://hal.archives-ouvertes.fr/hal-02665795
Chaperone activation and client binding of a 2-cysteine peroxiredoxin, Nat. Commun, vol.10, 2019. ,
TB: the Yin and Yang of lipid mediators, Curr. Opin. Pharmacol, vol.13, pp.641-645, 2013. ,
Microbial H2O2 sensors as archetypical redox signaling modules, Trends Biochem Sci, vol.29, pp.351-357, 2004. ,
A Role for Peroxymonocarbonate in the Stimulation of Biothiol Peroxidation by the Bicarbonate/Carbon Dioxide Pair, Chem. Res. Toxicol, vol.19, pp.1475-1482, 2006. ,
The bicarbonate/carbon dioxide pair increases hydrogen peroxide-mediated hyperoxidation of human peroxiredoxin 1, J. Biol. Chem. jbc, 2019. ,
Role for Prdx1 as a specific sensor in redox-regulated senescence in breast cancer, Oncogene, vol.32, pp.5302-5314, 2013. ,
Free radicals, metals and antioxidants in oxidative stress-induced cancer, Chem. Biol. Interact, vol.160, pp.1-40, 2006. ,
Superoxide dismutase is dispensable for normal animal lifespan, Proc. Natl. Acad. Sci, vol.109, pp.5785-5790, 2012. ,
, , 2020.
, Exploring the conformational transition between the fully folded and locally unfolded substates of Escherichia coli thiol peroxidase, Phys. Chem. Chem. Phys
Role/s of 'Antioxidant' Enzymes in Ageing, Biochemistry and Cell Biology of Ageing: Part I Biomedical Science, pp.425-450, 2018. ,
Hyperoxidation of Peroxiredoxins: Gain or Loss of Function?, Antioxid. Redox Signal, 2017. ,
, , 2005.
, A cysteine-sulfinic acid in peroxiredoxin regulates H2O2-sensing by the antioxidant Pap1 pathway, Proc. Natl. Acad. Sci. U. S. A, vol.102, pp.8875-8880
Superoxide dismutases: Dual roles in controlling ROS damage and regulating ROS signaling, J. Cell Biol, vol.217, pp.1915-1928, 2018. ,
The Effects of Linoleate Hydroperoxide on Respiration and Oxidative Phosphorylation of Rat Liver Mitochondria, J. Biochem, vol.86, pp.1041-1047, 1979. ,
Piecing Together How Peroxiredoxins Maintain Genomic Stability, Antioxidants, vol.7, p.177, 2018. ,
Reconciling the chemistry and biology of reactive oxygen species, Nat. Chem. Biol, vol.4, pp.278-286, 2008. ,
The Biological Chemistry of Hydrogen Peroxide, In Methods in Enzymology, pp.3-25, 2013. ,
Thiol chemistry and specificity in redox signaling. Free Radic, Biol. Med, vol.45, pp.549-561, 2008. ,
Reactivity of biologically important thiol compounds with superoxide and hydrogen peroxide. Free Radic, Biol. Med, vol.27, pp.322-328, 1999. ,
Effect of Lipid Peroxidation on the Properties of Lipid Bilayers: A Molecular Dynamics Study, Biophys. J, 2017. ,
Reversible Oxidation of the Active Site Cysteine of Peroxiredoxins to Cysteine Sulfinic Acid: IMMUNOBLOT DETECTION WITH ANTIBODIES SPECIFIC FOR THE HYPEROXIDIZED CYSTEINE-CONTAINING SEQUENCE, J. Biol. Chem, vol.278, pp.47361-47364, 2003. ,
Structure, mechanism and regulation of peroxiredoxins, Trends Biochem. Sci, vol.28, pp.32-40, 2003. ,
Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling, Science, vol.300, pp.650-653, 2003. ,
Structures of Human Peroxiredoxin 3 Suggest Self-Chaperoning Assembly that Maintains Catalytic State, Structure, vol.24, pp.1120-1129, 2016. ,
Catalysis of Peroxide Reduction by Fast Reacting Protein Thiols: Focus Review, Chem. Rev. acs.chemrev.9b00371, 2019. ,
, Marouane Libiad 3 , Hélène Le Cordier 1 , Samia Boukhenouna 1 , Michel B Toledano 3 & Sophie Rahuel, Alexandre Kriznik, vol.1
Campus Biologie Santé, F-54000 Nancy, France 2 UMS2008 IBSLor, Biophysics and Structural Biology core facility, vol.2 ,
,