: a comprehensive Python-based system for macromolecular structure solution, Acta Crystallographica Section D Biological Crystallography, vol.64, issue.2, pp.213-221, 2010. ,
DOI : 10.1107/S0907444909052925
Typical 2-Cys peroxiredoxins - modulation by covalent transformations and noncovalent interactions, FEBS Journal, vol.275, issue.9, pp.2478-2493, 2009. ,
DOI : 10.1111/j.1742-4658.2009.06984.x
The oligomeric conformation of peroxiredoxins links redox state to function, FEBS Letters, vol.104, issue.12, pp.1809-1816, 2009. ,
DOI : 10.1016/j.febslet.2009.05.029
Proteomic analysis of Schistosoma mansoni egg secretions, Molecular and Biochemical Parasitology, vol.155, issue.2, pp.84-93, 2007. ,
DOI : 10.1016/j.molbiopara.2007.06.002
Unfolding of Metastable Linker Region Is at the Core of Hsp33 Activation as a Redox-regulated Chaperone, Journal of Biological Chemistry, vol.285, issue.15, pp.11243-11251, 2010. ,
DOI : 10.1074/jbc.M109.084350
URL : https://hal.archives-ouvertes.fr/hal-00677454
MOLPROBITY: structure validation and all-atom contact analysis for nucleic acids and their complexes, Nucleic Acids Research, vol.32, issue.Web Server, pp.615-619, 2004. ,
DOI : 10.1093/nar/gkh398
On the evolutionary origin of the chaperonins, Proteins: Structure, Function, and Bioinformatics, vol.17, issue.4, pp.1172-1192, 2011. ,
DOI : 10.1002/prot.22952
Features and development of Coot, Acta Crystallogr D Biol Crystallogr, vol.66, pp.2126-2132, 2010. ,
An introduction to data reduction: space-group determination, scaling and intensity statistics, Acta Crystallographica Section D Biological Crystallography, vol.64, issue.4, pp.282-292, 2011. ,
DOI : 10.1107/S090744491003982X
Peroxiredoxins in antioxidant defense and redox regulation, BioFactors, vol.268, issue.1, pp.3-10, 2003. ,
DOI : 10.1002/biof.5520190102
Structure-Function Analysis of Recombinant Substrate Protein 22 kDa (SP-22): A MITOCHONDRIAL 2-CYS PEROXIREDOXIN ORGANIZED AS A DECAMERIC TOROID, Journal of Biological Chemistry, vol.278, issue.35, pp.32631-32637, 2003. ,
DOI : 10.1074/jbc.M303862200
Modulation of Schistosoma mansoni egg-induced granuloma formation: I-J restriction of T cell-mediated suppression in a chronic parasitic infection., Proceedings of the National Academy of Sciences, vol.78, issue.2, pp.1152-1156, 1981. ,
DOI : 10.1073/pnas.78.2.1152
Typical 2-Cys peroxiredoxins - structures, mechanisms and functions, FEBS Journal, vol.283, issue.9, pp.2469-2477, 2009. ,
DOI : 10.1111/j.1742-4658.2009.06985.x
URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2747500
Comparison of the decameric structure of peroxiredoxin-II by transmission electron microscopy and X-ray crystallography, Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, vol.1547, issue.2, pp.221-255, 2001. ,
DOI : 10.1016/S0167-4838(01)00184-4
Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23 kDa/proliferation-associated gene product, Proceedings of the National Academy of Sciences, vol.96, issue.22, pp.12333-12338, 1999. ,
DOI : 10.1073/pnas.96.22.12333
Two Enzymes in One, Cell, vol.117, issue.5, pp.625-635, 2004. ,
DOI : 10.1016/j.cell.2004.05.002
Structure of the sulphiredoxin???peroxiredoxin complex reveals an essential repair embrace, Nature, vol.50, issue.7174, pp.98-101, 2008. ,
DOI : 10.1038/nature06415
Protein Engineering of the Quaternary Sulfiredoxin{middle dot}Peroxiredoxin Enzyme{middle dot}Substrate Complex Reveals the Molecular Basis for Cysteine Sulfinic Acid Phosphorylation, Journal of Biological Chemistry, vol.284, issue.48, pp.33305-33310, 2009. ,
DOI : 10.1074/jbc.M109.036400
Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features, Biopolymers, vol.33, issue.12, pp.2577-2637, 1983. ,
DOI : 10.1002/bip.360221211
Redox-Regulated Chaperones, Biochemistry, vol.48, issue.22, pp.4666-4676, 2009. ,
DOI : 10.1021/bi9003556
URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2848813
Irreversible Oxidation of the Active-site Cysteine of Peroxiredoxin to Cysteine Sulfonic Acid for Enhanced Molecular Chaperone Activity, Journal of Biological Chemistry, vol.283, issue.43, pp.28873-80, 2008. ,
DOI : 10.1074/jbc.M804087200
Reduction of Cysteine Sulfinic Acid in Eukaryotic, Typical 2-Cys Peroxiredoxins by Sulfiredoxin, Antioxidants & Redox Signaling, vol.15, issue.1, pp.99-109, 2011. ,
DOI : 10.1089/ars.2010.3564
Oxidative Stress-dependent Structural and Functional Switching of a Human 2-Cys Peroxiredoxin Isotype II That Enhances HeLa Cell Resistance to H2O2-induced Cell Death, Journal of Biological Chemistry, vol.280, issue.31, pp.28775-28784, 2005. ,
DOI : 10.1074/jbc.M505362200
5 for the refinement of macromolecular crystal structures, Acta Crystallographica Section D Biological Crystallography, vol.57, issue.4, pp.355-367, 2011. ,
DOI : 10.1107/S0907444911001314
Analysis of the peroxiredoxin family: Using active-site structure and sequence information for global classification and residue analysis, Proteins: Structure, Function, and Bioinformatics, vol.45, issue.Suppl, pp.947-964, 2011. ,
DOI : 10.1002/prot.22936
Peroxiredoxin 1 and its role in cell signaling, Cell Cycle, vol.8, issue.24, pp.4072-4078, 2009. ,
DOI : 10.4161/cc.8.24.10242
[20] Processing of X-ray diffraction data collected in oscillation mode, Methods Enzymol, vol.276, pp.307-326, 1997. ,
DOI : 10.1016/S0076-6879(97)76066-X
Oxidation state governs structural transitions in peroxiredoxin II that correlate with cell cycle arrest and recovery, The Journal of Cell Biology, vol.114, issue.5, pp.779-789, 2006. ,
DOI : 10.1158/0008-5472.CAN-04-0946
Mildly Acidic pH Activates the Extracellular Molecular Chaperone Clusterin, Journal of Biological Chemistry, vol.277, issue.42, pp.39532-39540, 2002. ,
DOI : 10.1074/jbc.M204855200
4 molecular-graphics project, Acta Crystallographica Section D Biological Crystallography, vol.60, issue.12, pp.2288-2294, 2004. ,
DOI : 10.1107/S0907444904023716
Stabilization of protein structure by interaction of alpha-helix dipole with a charged side chain, Nature, vol.335, pp.740-743, 1988. ,
Biochemical Characterization of 2-Cys Peroxiredoxins from Schistosoma mansoni, Journal of Biological Chemistry, vol.279, issue.25, pp.26159-66, 2004. ,
DOI : 10.1074/jbc.M401748200
Redox Balance Mechanisms in Schistosoma mansoni Rely on Peroxiredoxins and Albumin and Implicate Peroxiredoxins as Novel Drug Targets, Journal of Biological Chemistry, vol.281, issue.25, pp.17001-17010, 2006. ,
DOI : 10.1074/jbc.M512601200
PREX: PeroxiRedoxin classification indEX, a database of subfamily assignments across the diverse peroxiredoxin family, Nucleic Acids Research, vol.39, issue.Database, pp.332-337, 2011. ,
DOI : 10.1093/nar/gkq1060
The role of T-cell anergy in the immunomodulation of schistosomiasis, Parasitology Today, vol.8, issue.6, pp.199-204, 1992. ,
DOI : 10.1016/0169-4758(92)90264-3
Schistosome infection stimulates host CD4(+) T helper cell and B-cell responses against a novel egg antigen, thioredoxin peroxidase, Infect Immun, vol.69, pp.1134-1175, 2001. ,
4 suite and current developments, Acta Crystallographica Section D Biological Crystallography, vol.65, issue.4, pp.235-242, 2011. ,
DOI : 10.1107/S0907444910045749
Severe Oxidative Stress Causes Inactivation of DnaK and Activation of the Redox-Regulated Chaperone Hsp33, Molecular Cell, vol.17, issue.3, pp.381-392, 2005. ,
DOI : 10.1016/j.molcel.2004.12.027
Thiol chemistry and specificity in redox signaling, Free Radical Biology and Medicine, vol.45, issue.5, pp.549-561, 2008. ,
DOI : 10.1016/j.freeradbiomed.2008.05.004
Structure, mechanism and regulation of peroxiredoxins, Trends in Biochemical Sciences, vol.28, issue.1, pp.32-40, 2003. ,
DOI : 10.1016/S0968-0004(02)00003-8
[22] Detecting and overcoming crystal twinning, Methods Enzymol, vol.276, pp.344-358, 1997. ,
DOI : 10.1016/S0076-6879(97)76068-3