Switching between the alternative structures and functions of a 2-Cys peroxiredoxin, by site-directed mutagenesis.

[1]  A. Giordano,et al.  Neuroprotective effects of PrxI over‐expression in an in vitro human Alzheimer's disease model , 2013, Journal of cellular biochemistry.

[2]  P. Karplus,et al.  Peroxiredoxins in parasites. , 2012, Antioxidants & redox signaling.

[3]  P. Andrew Karplus,et al.  Linking Crystallographic Model and Data Quality , 2012, Science.

[4]  A. Miele,et al.  Moonlighting by different stressors: crystal structure of the chaperone species of a 2-Cys peroxiredoxin. , 2012, Structure.

[5]  A. Miele,et al.  On the mechanism and rate of gold incorporation into thiol-dependent flavoreductases. , 2012, Journal of inorganic biochemistry.

[6]  A. Miele,et al.  Macromolecular bases of antischistosomal therapy. , 2011, Current topics in medicinal chemistry.

[7]  A. Miele,et al.  Structural and functional characterization of Schistosoma mansoni Thioredoxin , 2011, Protein science : a publication of the Protein Society.

[8]  G. Piszczek,et al.  Glutathionylation of peroxiredoxin I induces decamer to dimers dissociation with concomitant loss of chaperone activity. , 2011, Biochemistry.

[9]  W. Taylor,et al.  On the evolutionary origin of the chaperonins , 2011, Proteins.

[10]  Jacquelyn S. Fetrow,et al.  PREX: PeroxiRedoxin classification indEX, a database of subfamily assignments across the diverse peroxiredoxin family , 2010, Nucleic Acids Res..

[11]  A. Miele,et al.  Mapping the Catalytic Cycle of Schistosoma mansoni Thioredoxin Glutathione Reductase by X-ray Crystallography* , 2010, The Journal of Biological Chemistry.

[12]  Daphne H. E. W. Huberts,et al.  Moonlighting proteins: an intriguing mode of multitasking. , 2010, Biochimica et biophysica acta.

[13]  P. Emsley,et al.  Features and development of Coot , 2010, Acta crystallographica. Section D, Biological crystallography.

[14]  A. Miele,et al.  Inhibition of Schistosoma mansoni Thioredoxin-glutathione Reductase by Auranofin , 2009, The Journal of Biological Chemistry.

[15]  A. Miele,et al.  Combining crystallography and molecular dynamics: The case of Schistosoma mansoni phospholipid glutathione peroxidase , 2009, Proteins.

[16]  P. Karplus,et al.  Typical 2‐Cys peroxiredoxins – structures, mechanisms and functions , 2009, The FEBS journal.

[17]  B. Golinelli‐Pimpaneau,et al.  Pseudo-merohedral twinning in monoclinic crystals of wild-type human brain neuroglobin. , 2009, Acta crystallographica. Section D, Biological crystallography.

[18]  J. Dalton,et al.  Helminth 2‐Cys peroxiredoxin drives Th2 responses through a mechanism involving alternatively activated macrophages , 2008, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[19]  C. Winterbourn,et al.  Thiol chemistry and specificity in redox signaling. , 2008, Free radical biology & medicine.

[20]  A. Miele,et al.  Will new antischistosomal drugs finally emerge? , 2008, Trends in parasitology.

[21]  J. Yates,et al.  Proteomic analysis of Schistosoma mansoni egg secretions. , 2007, Molecular and biochemical parasitology.

[22]  D. Bhella,et al.  Reconstitution of the mitochondrial PrxIII antioxidant defence pathway: general properties and factors affecting PrxIII activity and oligomeric state. , 2007, Journal of molecular biology.

[23]  E. Davioud‐Charvet,et al.  Thioredoxin Glutathione Reductase from Schistosoma mansoni: An Essential Parasite Enzyme and a Key Drug Target , 2007, PLoS medicine.

[24]  M. Brunori,et al.  The anti-schistosomal drug praziquantel is an adenosine antagonist , 2007, Parasitology.

[25]  S. Cook,et al.  Redox Balance Mechanisms in Schistosoma mansoni Rely on Peroxiredoxins and Albumin and Implicate Peroxiredoxins as Novel Drug Targets* , 2006, Journal of Biological Chemistry.

[26]  M. Cho,et al.  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* , 2005, Journal of Biological Chemistry.

[27]  Ahmed A. Sayed,et al.  Biochemical Characterization of 2-Cys Peroxiredoxins from Schistosoma mansoni* , 2004, Journal of Biological Chemistry.

[28]  Sang Yeol Lee,et al.  Two Enzymes in One Two Yeast Peroxiredoxins Display Oxidative Stress-Dependent Switching from a Peroxidase to a Molecular Chaperone Function , 2004, Cell.

[29]  M. Toledano,et al.  ATP-dependent reduction of cysteine–sulphinic acid by S. cerevisiae sulphiredoxin , 2003, Nature.

[30]  N. C. Price,et al.  Structure-Function Analysis of Recombinant Substrate Protein 22 kDa (SP-22) , 2003, Journal of Biological Chemistry.

[31]  J. Carver,et al.  Mildly Acidic pH Activates the Extracellular Molecular Chaperone Clusterin* , 2002, The Journal of Biological Chemistry.

[32]  Sue Goo Rhee,et al.  Inactivation of Human Peroxiredoxin I during Catalysis as the Result of the Oxidation of the Catalytic Site Cysteine to Cysteine-sulfinic Acid* , 2002, The Journal of Biological Chemistry.

[33]  G Jogl,et al.  COMO: a program for combined molecular replacement. , 2001, Acta crystallographica. Section D, Biological crystallography.

[34]  J. Harris,et al.  Comparison of the decameric structure of peroxiredoxin-II by transmission electron microscopy and X-ray crystallography. , 2001, Biochimica et biophysica acta.

[35]  A. Vagin,et al.  Crystal structure of decameric 2-Cys peroxiredoxin from human erythrocytes at 1.7 A resolution. , 2000, Structure.

[36]  K. Furtak,et al.  Multivalent Binding of Nonnative Substrate Proteins by the Chaperonin GroEL , 2000, Cell.

[37]  K. Acharya,et al.  Analysis and characterization of data from twinned crystals. , 1999, Acta crystallographica. Section D, Biological crystallography.

[38]  P. Steinert,et al.  Activation of active-site cysteine residues in the peroxiredoxin-type tryparedoxin peroxidase of Crithidia fasciculata. , 1999, European journal of biochemistry.

[39]  T. Yeates,et al.  Protein crystals and their evil twins. , 1999, Structure.

[40]  H. Edelsbrunner,et al.  Anatomy of protein pockets and cavities: Measurement of binding site geometry and implications for ligand design , 1998, Protein science : a publication of the Protein Society.

[41]  L. R. Manning,et al.  Subunit dissociations in natural and recombinant hemoglobins , 1996, Protein science : a publication of the Protein Society.

[42]  E. Stanley.  The identification of twins from intensity statistics , 1972 .

[43]  J. Harris.  Some negative contrast staining features of a protein from erythrocyte ghosts. , 1969, Journal of molecular biology.

[44]  J. Harris,et al.  Formation, TEM study and 3D reconstruction of the human erythrocyte peroxiredoxin-2 dodecahedral higher-order assembly. , 2007, Micron.

[45]  Ram Seshadri.  Crystal structures , 2004 .

[46]  P. Afonine,et al.  research papers Acta Crystallographica Section D Biological , 2003 .

[47]  J. Buchner,et al.  Analysis of chaperone function using citrate synthase as nonnative substrate protein. , 1998, Methods in enzymology.

[48]  P Andrew Karplus,et al.  Structure-based Insights into the Catalytic Power and Conformational Dexterity of Peroxiredoxins , 2022 .