Spectroscopic and Theoretical Study of CuI Binding to His111 in the Human Prion Protein Fragment 106–115
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K. Hodgson | Lina Rivillas-Acevedo | B. Hedman | E. Solomon | A. Vela | C. Fernández | L. Quintanar | Trinidad Arcos-López | Munzarin F. Qayyum | M. C. Miotto | R. Grande-Aztatzi | Alberto Vela | Edward I Solomon | Lina Rivillas-Acevedo | Claudio O. Fernández
[1] H. Kozłowski,et al. Specific binding modes of Cu(I) and Ag(I) with neurotoxic domain of the human prion protein. , 2016, Journal of inorganic biochemistry.
[2] Lina Rivillas-Acevedo,et al. Structural models for Cu(II) bound to the fragment 92-96 of the human prion protein. , 2013, The journal of physical chemistry. B.
[3] Lina Rivillas-Acevedo,et al. Copper coordination to the prion protein: Insights from theoretical studies , 2013 .
[4] G. Millhauser,et al. The Rich Electrochemistry and Redox Reactions of the Copper Sites in the Cellular Prion Protein. , 2012, Coordination chemistry reviews.
[5] J. H. Viles,et al. Methionine Oxidation Perturbs the Structural Core of the Prion Protein and Suggests a Generic Misfolding Pathway* , 2012, The Journal of Biological Chemistry.
[6] R. Linden,et al. Allosteric function and dysfunction of the prion protein , 2012, Cellular and Molecular Life Sciences.
[7] G. Bitan,et al. Induction of Methionine-sulfoxide Reductases Protects Neurons from Amyloid Β-protein Insults in Vitro and in Vivo Nih Public Access , 2022 .
[8] G. Millhauser,et al. Copper redox cycling in the prion protein depends critically on binding mode. , 2011, Journal of the American Chemical Society.
[9] Kathryn L Haas,et al. Model peptides provide new insights into the role of histidine residues as potential ligands in human cellular copper acquisition via Ctr1. , 2011, Journal of the American Chemical Society.
[10] Lina Rivillas-Acevedo,et al. Spectroscopic and electronic structure studies of copper(II) binding to His111 in the human prion protein fragment 106-115: evaluating the role of protons and methionine residues. , 2011, Inorganic chemistry.
[11] Christopher E. Jones,et al. The amyloidogenic region of the human prion protein contains a high affinity (Met)(2)(His)(2) Cu(I) binding site. , 2009, Journal of inorganic biochemistry.
[12] Florian Janetzko,et al. A MinMax self-consistent-field approach for auxiliary density functional theory. , 2009, The Journal of chemical physics.
[13] J. Shearer,et al. Both Met(109) and Met(112) are utilized for Cu(II) coordination by the amyloidogenic fragment of the human prion protein at physiological pH. , 2008, Journal of inorganic biochemistry.
[14] T. Mattioli,et al. Folding of the prion peptide GGGTHSQW around the copper(II) ion: identifying the oxygen donor ligand at neutral pH and probing the proximity of the tryptophan residue to the copper ion , 2008, JBIC Journal of Biological Inorganic Chemistry.
[15] I. Izquierdo,et al. Physiology of the prion protein. , 2008, Physiological reviews.
[16] K. Page,et al. Fast conventional Fmoc solid‐phase peptide synthesis with HCTU , 2008, Journal of peptide science : an official publication of the European Peptide Society.
[17] T. Kohzuma,et al. Protonation of a histidine copper ligand in fern plastocyanin. , 2007, Journal of the American Chemical Society.
[18] Keith O. Hodgson,et al. PySpline: A Modern, Cross‐Platform Program for the Processing of Raw Averaged XAS Edge and EXAFS Data , 2007 .
[19] Yi Lu,et al. Reorganization energy of the CuA center in purple azurin: impact of the mixed valence-to-trapped valence state transition. , 2007, The journal of physical chemistry. B.
[20] P. Calaminici,et al. Density functional theory optimized basis sets for gradient corrected functionals: 3d transition metal systems. , 2007, The Journal of chemical physics.
[21] J. Shearer,et al. The copper(II) adduct of the unstructured region of the amyloidogenic fragment derived from the human prion protein is redox-active at physiological pH. , 2007, Inorganic chemistry.
[22] T. Kawano. Prion-derived copper-binding peptide fragments catalyze the generation of superoxide anion in the presence of aromatic monoamines , 2006, International journal of biological sciences.
[23] Frank Neese,et al. Calculation of solvent shifts on electronic g-tensors with the conductor-like screening model (COSMO) and its self-consistent generalization to real solvents (direct COSMO-RS). , 2006, The journal of physical chemistry. A.
[24] K. Franz,et al. A Mets motif peptide found in copper transport proteins selectively binds Cu(I) with methionine-only coordination. , 2005, Inorganic chemistry.
[25] N. Makarava,et al. Methionine oxidation interferes with conversion of the prion protein into the fibrillar proteinase K-resistant conformation. , 2005, Biochemistry.
[26] D. La Mendola,et al. Copper(II) interaction with unstructured prion domain outside the octarepeat region: speciation, stability, and binding details of copper(II) complexes with PrP106-126 peptides. , 2005, Inorganic chemistry.
[27] E. Walter,et al. The octarepeat domain of the prion protein binds Cu(II) with three distinct coordination modes at pH 7.4. , 2005, Journal of the American Chemical Society.
[28] H. Kozłowski,et al. Copper-ion interaction with the 106-113 domain of the prion protein: a solution-equilibria study on model peptides. , 2005, Dalton transactions.
[29] M. Maher,et al. CopC protein from Pseudomonas syringae: intermolecular transfer of copper from both the copper(I) and copper(II) sites. , 2005, Inorganic chemistry.
[30] M. McEvoy,et al. A novel copper-binding fold for the periplasmic copper resistance protein CusF. , 2005, Biochemistry.
[31] C. Weissmann,et al. The role of PrP in health and disease. , 2004, Current molecular medicine.
[32] G. Millhauser. Copper binding in the prion protein. , 2004, Accounts of chemical research.
[33] X. Roucou,et al. Neuroprotective functions of prion protein , 2004, Journal of neuroscience research.
[34] H. Haraguchi,et al. Metallomics: An integrated biometal science , 2009 .
[35] D. Harris,et al. Copper and zinc cause delivery of the prion protein from the plasma membrane to a subset of early endosomes and the Golgi , 2003, Journal of neurochemistry.
[36] R. Niessner,et al. Methods for studying synaptosomal copper release , 2003, Journal of Neuroscience Methods.
[37] N. Vassallo,et al. Cellular prion protein function in copper homeostasis and redox signalling at the synapse , 2003, Journal of neurochemistry.
[38] David R. Brown,et al. Generation of hydrogen peroxide from mutant forms of the prion protein fragment PrP121-231. , 2003, Biochemistry.
[39] S. Prusiner,et al. Copper coordination in the full-length, recombinant prion protein. , 2003, Biochemistry.
[40] T. Kohzuma,et al. Introduction of a pi-pi interaction at the active site of a cupredoxin: characterization of the Met16Phe Pseudoazurin mutant. , 2003, Biochemistry.
[41] L. Guarente,et al. Nicotinamide adenine dinucleotide, a metabolic regulator of transcription, longevity and disease. , 2003, Current opinion in cell biology.
[42] I. Bertini,et al. A redox switch in CopC: An intriguing copper trafficking protein that binds copper(I) and copper(II) at different sites , 2003, Proceedings of the National Academy of Sciences of the United States of America.
[43] David R. Brown,et al. Copper-dependent generation of hydrogen peroxide from the toxic prion protein fragment PrP106–126 , 2003, Neuroscience Letters.
[44] D. Huffman,et al. The PcoC copper resistance protein coordinates Cu(I) via novel S-methionine interactions. , 2003, Journal of the American Chemical Society.
[45] A. Mangé,et al. PrP‐dependent cell adhesion in N2a neuroblastoma cells , 2002, FEBS letters.
[46] M. Nishikimi,et al. Carbonyl formation on a copper‐bound prion protein fragment, PrP23–98, associated with its dopamine oxidase activity , 2002, FEBS letters.
[47] A. LeBlanc,et al. Prion Protein Protects Human Neurons against Bax-mediated Apoptosis* , 2001, The Journal of Biological Chemistry.
[48] U. Ryde,et al. Geometry, reduction potential, and reorganization energy of the binuclear Cu(A) site, studied by density functional theory. , 2001, Journal of the American Chemical Society.
[49] S. Prusiner,et al. Copper-catalyzed oxidation of the recombinant SHa(29–231) prion protein , 2001, Proceedings of the National Academy of Sciences of the United States of America.
[50] I. Izquierdo,et al. Imbalance of antioxidant defense in mice lacking cellular prion protein. , 2001, Free radical biology & medicine.
[51] N. Hooper,et al. Ablation of the metal ion-induced endocytosis of the prion protein by disease-associated mutation of the octarepeat region , 2001, Current Biology.
[52] N. Handy,et al. Left-right correlation energy , 2001 .
[53] F. Cohen,et al. Identification of the Cu2+ binding sites in the N-terminal domain of the prion protein by EPR and CD spectroscopy. , 2000, Biochemistry.
[54] B. Matthews,et al. Structure and mechanism of peptide methionine sulfoxide reductase, an "anti-oxidation" enzyme. , 2000, Biochemistry.
[55] J. Laplanche,et al. Signal transduction through prion protein. , 2000, Science.
[56] J. Rehr,et al. Theoretical approaches to x-ray absorption fine structure , 2000 .
[57] K Wüthrich,et al. NMR solution structure of the human prion protein. , 2000, Proceedings of the National Academy of Sciences of the United States of America.
[58] S. Haswell,et al. Normal prion protein has an activity like that of superoxide dismutase. , 1999, The Biochemical journal.
[59] P. Schürmann,et al. Evidence of Presynaptic Location and Function of the Prion Protein , 1999, The Journal of Neuroscience.
[60] W. Markesbery,et al. Decrease in Peptide Methionine Sulfoxide Reductase in Alzheimer's Disease Brain , 1999, Journal of neurochemistry.
[61] J. Ironside,et al. Neuronal apoptosis in Creutzfeldt-Jakob disease. , 1999, Journal of neuropathology and experimental neurology.
[62] D. Harris,et al. Copper Stimulates Endocytosis of the Prion Protein* , 1998, The Journal of Biological Chemistry.
[63] Stanley B. Prusiner,et al. Nobel Lecture: Prions , 1998 .
[64] D. Westaway,et al. The cellular prion protein binds copper in vivo , 1997, Nature.
[65] P E Wright,et al. Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible. , 1997, Proceedings of the National Academy of Sciences of the United States of America.
[66] A. Winkler,et al. Reorganization Energy of Blue Copper: Effects of Temperature and Driving Force on the Rates of Electron Transfer in Ruthenium- and Osmium-Modified Azurins , 1997 .
[67] S. Prusiner,et al. Prion diseases and the BSE crisis. , 1997, Science.
[68] Burke,et al. Generalized Gradient Approximation Made Simple. , 1996, Physical review letters.
[69] F. Cohen,et al. Prion protein gene variation among primates. , 1995, Journal of molecular biology.
[70] S. Larsson,et al. Reorganization energies in benzene, naphthalene, and anthracene , 1994 .
[71] T. Kohzuma,et al. Reactivity of Pseudoazurin from Achromobacter cycloclastes with Inorganic Redox Partners and Related NMR and Electrochemical Studies , 1994 .
[72] R J Fletterick,et al. Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins. , 1993, Proceedings of the National Academy of Sciences of the United States of America.
[73] H. Thorp,et al. Bond valence sum analysis of metal-ligand bond lengths in metalloenzymes and model complexes. 2. Refined distances and other enzymes , 1993 .
[74] Rudolph A. Marcus,et al. Electron Transfer Reactions in Chemistry: Theory and Experiment (Nobel Lecture) , 1993 .
[75] H. Thorp. Bond valence sum analysis of metal-ligand bond lengths in metalloenzymes and model complexes , 1992 .
[76] Dennis R. Salahub,et al. Optimization of Gaussian-type basis sets for local spin density functional calculations. Part I. Boron through neon, optimization technique and validation , 1992 .
[77] F. Hajós,et al. Nerve endings from rat brain tissue release copper upon depolarization. A possible role in regulating neuronal excitability , 1989, Neuroscience Letters.
[78] P. Wood. The potential diagram for oxygen at pH 7. , 1988, The Biochemical journal.
[79] K. Hodgson,et al. X-ray absorption edge determination of the oxidation state and coordination number of copper: application to the type 3 site in Rhus vernicifera laccase and its reaction with oxygen , 1987 .
[80] C. Locht,et al. Molecular cloning and complete sequence of prion protein cDNA from mouse brain infected with the scrapie agent. , 1986, Proceedings of the National Academy of Sciences of the United States of America.
[81] S. Prusiner,et al. Separation and properties of cellular and scrapie prion proteins. , 1986, Proceedings of the National Academy of Sciences of the United States of America.
[82] I. D. Brown,et al. Bond‐valence parameters obtained from a systematic analysis of the Inorganic Crystal Structure Database , 1985 .
[83] J. Neff,et al. Comparison of methods for determination of ascorbic acid in animal tissues. , 1983, Analytical chemistry.
[84] S. Prusiner. Novel proteinaceous infectious particles cause scrapie. , 1982, Science.
[85] John R. Sabin,et al. On some approximations in applications of Xα theory , 1979 .
[86] Rudolph A. Marcus,et al. Chemical and Electrochemical Electron-Transfer Theory , 1964 .
[87] Jeffrey T. Rubino,et al. A comparison of methionine, histidine and cysteine in copper(I)-binding peptides reveals differences relevant to copper uptake by organisms in diverse environments. , 2011, Metallomics : integrated biometal science.
[88] J. H. Viles,et al. Prion protein does not redox-silence Cu2+, but is a sacrificial quencher of hydroxyl radicals. , 2007, Free radical biology & medicine.
[89] A. Klamt,et al. COSMO : a new approach to dielectric screening in solvents with explicit expressions for the screening energy and its gradient , 1993 .