DNA Converts Cellular Prion Protein into the β-Sheet Conformation and Inhibits Prion Peptide Aggregation*
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Y. Cordeiro | Filipe A. Machado | L. Juliano | M. Juliano | R. Brentani | D. Foguel | Jerson L. Silva
[1] TIKVAH ALPER,et al. Does the Agent of Scrapie Replicate without Nucleic Acid ? , 1967, Nature.
[2] J. R. Bray. Volcanism and glaciation during the past 40 millennia , 1974, Nature.
[3] Á. Villanueva,et al. A study of interaction of thioflavine T with DNA: evidence for intercalation. , 1987, Cellular and molecular biology.
[4] C. Weissmann,et al. A 'unified theory' of prion propagation , 1991, Nature.
[5] R. Sauer,et al. Transcription factors: structural families and principles of DNA recognition. , 1992, Annual review of biochemistry.
[6] Conformation of concanavalin A and its fragments in aqueous solution and organic solvent-water mixtures , 1992, Journal of protein chemistry.
[7] S. Prusiner,et al. Further analysis of nucleic acids in purified scrapie prion preparations by improved return refocusing gel electrophoresis. , 1992, The Journal of general virology.
[8] S. Prusiner,et al. Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein , 1992, Nature.
[9] G. Forloni,et al. Neurotoxicity of a prion protein fragment , 1993, Nature.
[10] 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.
[11] P E Fraser,et al. A kinetic model for amyloid formation in the prion diseases: importance of seeding. , 1993, Proceedings of the National Academy of Sciences of the United States of America.
[12] P. Lansbury,et al. Seeding “one-dimensional crystallization” of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie? , 1993, Cell.
[13] G. J. Raymond,et al. Binding of the protease-sensitive form of PrP (prion protein) to sulfated glycosaminoglycan and congo red [corrected] , 1994, Journal of virology.
[14] Venyaminov SYu,et al. Determination of protein tertiary structure class from circular dichroism spectra. , 1994, Analytical biochemistry.
[15] D. Foguel,et al. Cold denaturation of a repressor-operator complex: the role of entropy in protein-DNA recognition. , 1994, Proceedings of the National Academy of Sciences of the United States of America.
[16] Robert T. Sauer,et al. DNA recognition by β-sheets in the Arc represser–operator crystal structure , 1994, Nature.
[17] S. Phillips. The beta-ribbon DNA recognition motif. , 1994, Annual review of biophysics and biomolecular structure.
[18] F. Cohen,et al. Scrapie prions: a three-dimensional model of an infectious fragment. , 1995, Folding & design.
[19] Fred E. Cohen,et al. Conformational Transformations in Peptides Containing Two Putative α-Helices of the Prion Protein , 1995 .
[20] F. Cohen,et al. Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein , 1995, Cell.
[21] A. Hofman,et al. A new variant of Creutzfeldt-Jakob disease in the UK , 1996, The Lancet.
[22] R. Riek,et al. NMR structure of the mouse prion protein domain PrP(121–231) , 1996, Nature.
[23] S. Venyaminov,et al. Determination of Protein Secondary Structure , 1996 .
[24] S. Burley. The TATA box binding protein. , 1996, Current opinion in structural biology.
[25] S. Lindquist,et al. Mad Cows Meet Psi-chotic Yeast: The Expansion of the Prion Hypothesis , 1997, Cell.
[26] K Wüthrich,et al. Human prion proteins expressed in Escherichia coli and purified by high‐affinity column refolding , 1997, FEBS letters.
[27] P. Nandi. Interaction of prion peptide HuPrP106–126 with nucleic acid , 1997, Archives of Virology.
[28] P. Lansbury,et al. Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. , 1997, Annual review of biochemistry.
[29] P S Kim,et al. Influenza hemagglutinin is spring-loaded by a metastable native conformation. , 1997, Proceedings of the National Academy of Sciences of the United States of America.
[30] 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.
[31] F E Cohen,et al. Pathologic conformations of prion proteins. , 1998, Annual review of biochemistry.
[32] S. Prusiner,et al. A transmembrane form of the prion protein in neurodegenerative disease. , 1998, Science.
[33] J. W. Kelly. The environmental dependency of protein folding best explains prion and amyloid diseases. , 1998, Proceedings of the National Academy of Sciences of the United States of America.
[34] Stanley B. Prusiner,et al. Nobel Lecture: Prions , 1998 .
[35] P. Nandi. Polymerization of human prion peptide HuPrP 106–126 to amyloid in nucleic acid solution , 1998, Archives of Virology.
[36] P. Brown,et al. Natural and experimental oral infection of nonhuman primates by bovine spongiform encephalopathy agents. , 1999, Proceedings of the National Academy of Sciences of the United States of America.
[37] J Collinge,et al. Reversible conversion of monomeric human prion protein between native and fibrilogenic conformations. , 1999, Science.
[38] F E Cohen,et al. Protein misfolding and prion diseases. , 1999, Journal of molecular biology.
[39] M. Brown,et al. A proteolytic pathway that controls the cholesterol content of membranes, cells, and blood. , 1999, Proceedings of the National Academy of Sciences of the United States of America.
[40] Prions of Yeast and Fungi , 1999, The Journal of Biological Chemistry.
[41] F. Cohen,et al. Prion Protein of 106 Residues Creates an Artificial Transmission Barrier for Prion Replication in Transgenic Mice , 1999, Cell.
[42] F. Cohen,et al. Elimination of prions by branched polyamines and implications for therapeutics. , 1999, Proceedings of the National Academy of Sciences of the United States of America.
[43] C. Weissmann,et al. Molecular Genetics of Transmissible Spongiform Encephalopathies* , 1999, The Journal of Biological Chemistry.
[44] B. Caughey. Transmissible spongiform encephalopathies, amyloidoses and yeast prions: Common threads? , 2000, Nature Medicine.
[45] A A Antson,et al. Single-stranded-RNA binding proteins. , 2000, Current opinion in structural biology.
[46] D. Foguel,et al. The preaggregated state of an amyloidogenic protein: hydrostatic pressure converts native transthyretin into the amyloidogenic state. , 2000, Proceedings of the National Academy of Sciences of the United States of America.
[47] D. Foguel,et al. DNA tightens the dimeric DNA-binding domain of human papillomavirus E2 protein without changes in volume. , 2000, Proceedings of the National Academy of Sciences of the United States of America.
[48] F E Cohen,et al. A synthetic peptide initiates Gerstmann-Sträussler-Scheinker (GSS) disease in transgenic mice. , 2000, Journal of molecular biology.
[49] S. Lindquist,et al. Nucleated conformational conversion and the replication of conformational information by a prion determinant. , 2000, Science.
[50] D. Foguel,et al. LexA Repressor Forms Stable Dimers in Solution , 2000, The Journal of Biological Chemistry.
[51] 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.
[52] M. Y. Lee,et al. Regulation of protein function by native metastability. , 2000, Proceedings of the National Academy of Sciences of the United States of America.
[53] Fred E. Cohen,et al. Folding of Prion Protein to Its Native α-Helical Conformation Is under Kinetic Control* , 2001, The Journal of Biological Chemistry.
[54] F. Cohen,et al. Local structural plasticity of the prion protein. Analysis of NMR relaxation dynamics. , 2001, Biochemistry.
[55] J. Weissman,et al. Conformational diversity in a yeast prion dictates its seeding specificity , 2001, Nature.
[56] B. Caughey,et al. Reversibility of Scrapie-associated Prion Protein Aggregation* , 2001, The Journal of Biological Chemistry.
[57] C. Péchoux,et al. The prion protein has DNA strand transfer properties similar to retroviral nucleocapsid protein. , 2001, Journal of molecular biology.
[58] C. Gabus,et al. The Prion Protein Has RNA Binding and Chaperoning Properties Characteristic of Nucleocapsid Protein NCp7 of HIV-1* , 2001, The Journal of Biological Chemistry.
[59] D. Foguel,et al. The Metastable State of Nucleocapsids of Enveloped Viruses as Probed by High Hydrostatic Pressure* , 2001, The Journal of Biological Chemistry.