Effect of salts on the structural behavior of hPrP α2-helix-derived analogues: The counterion perspective(130 visite) Ronga L, Palladino P, Tizzano B, Marasco D, Benedetti E, Ragone R, Rossi F
Parole chiave: Amyloid, Anions, Cations, Counterions, Hofmeister Series, Prion Helix 2 Derived Peptides, Prion Structure, Transmissible Spongiform Encephalopathies, Prion Protein, Prion Protein Helix 2 Derivative, Sodium Chloride, Alpha Helix, Article, Beta Sheet, Human, Ionic Strength, Peptide Synthesis, Priority Journal, Protein Binding, Protein Conformation, Protein Folding, Protein Function, Protein Modification, Amino Acid Sequence, Circular Dichroism, Electrostatics, Hydrogen-Ion Concentration, Models, Molecular, Molecular Sequence Data, Protein Structure, Secondary, Salts, Sulfates,
Affiliazioni:
*** IBB - CNR *** Dipartimento delle Scienze Biologiche, C.I.R.Pe.B, Università Federico II di Napoli, Via Mezzocannone 16, 80134 Napoli, Italy Dipartimento di Biochimica e Biofisica, CRISCEB, Seconda Università di Napoli, Via Costantinopoli 16, 80138 Napoli, Italy
Temussi, P.A., Masino, L., Pastore, A., From Alzheimer to Huntington: Why is a structural understanding so difficult? (2003) EMBO J., 22, pp. 355-361
Swietnicki, W., Petersen, R.B., Gambetti, P., Surewicz, W.K., pH-Dependent stability and conformation of the recombinant human prion protein PrP(90-231) (1997) J. Biol. Chem., 272, pp. 27517-27520
Swietnicki, W., Morillas, M., Chen, S.G., Gambetti, P., Surewicz, W.K., Aggregation and fibrillization of the recombinant human prion protein huPrP90-231 (2000) Biochemistry, 39, pp. 424-431
Liemann, S., Glockshuber, R., Influence of amino acid substitutions related to inherited human prion diseases on the thermodynamic stability of the cellular prion protein (1999) Biochemistry, 38, pp. 3258-3267
Hornemann, S., Glockshuber, R., A scrapie-like unfolding intermediate of the prion protein domain PrP(121-231) induced by acidic pH (1998) Proc. Natl. Acad. Sci. U.S.A., 95, pp. 6010-6014
Wildegger, G., Liemann, S., Glockshuber, R., Extremely rapid folding of the C-terminal domain of the prion protein without kinetic intermediates (1999) Nat. Struct. Biol., 6, pp. 550-553
Rezaei, H., Marc, D., Choiset, Y., Takahashi, M., Hoa, G.H.B., Haertle, T., Grosclaude, J., Debey, P., High yield purification and physicochemical properties of full-length recombinant allelic variants of sheep prion protein linked to scrapie susceptibility (2000) Eur. J. Biochem., 267, pp. 2833-2839
Zanusso, G., Farinazzo, A., Fiorini, M., Gelati, M., Castagna, A., Righetti, P.G., Rizzuto, N., Monaco, S., pH-Dependent prion protein conformation in classical Creutzfeldt-Jakob disease (2001) J. Biol. Chem., 276, pp. 40377-40380
Baskakov, I.V., Legname, G., Prusiner, S.B., Cohen, F.E., Folding of prion protein to its native α-helical conformation is under kinetic control (2001) J. Biol. Chem., 276, pp. 19687-19690
Morrissey, M.P., Shakhnovich, E.I., Evidence for the role of PrPc helix 1 in the hydrophilic seeding of prion aggregates (1999) Proc. Natl. Acad. Sci. U.S.A., 96, pp. 11293-11298
Apetri, A.C., Surewicz, W.K., Atypical effect of salts on the thermodynamic stability of human prion protein (2003) J. Biol. Chem., 278, pp. 22187-22192
Morillas, M., Vanik, D.L., Surewicz, W.K., On the mechanism of alpha-helix to beta-sheet transition in the recombinant prion protein (2001) Biochemistry, 40, pp. 6982-6987
Nandi, P.K., Leclerc, E., Marc, D., Unusual property of prion protein unfolding in neutral salt solution (2002) Biochemistry, 41, pp. 11017-11024
Ziegler, J., Sticht, H., Marx, U.C., Müller, W., Rösch, P., Schwarzinger, S., CD and NMR studies of prion protein (PrP) helix 1: Novel implications for its role in the PrPc to PrPSc conversion process (2003) J. Biol. Chem., 278, pp. 50175-50181
Tizzano, B., Palladino, P., De Capua, A., Marasco, D., Rossi, F., Benedetti, E., Pedone, C., Ruvo, M., The human prion protein alpha2 helix: A thermodynamic study of its conformational preferences (2005) Proteins, 59, pp. 72-79
Haire, L.F., Whyte, S.M., Vasisht, N., Gill, A.C., Verma, C., Dodson, E.J., Dodson, G.G., Bayley, P.M., The crystal structure of the globular domain of sheep prion protein (2004) J. Mol. Biol., 336, pp. 1175-1183
Brown, D.R., Guantieri, V., Grasso, G., Impellizzeri, G., Pappalardo, G., Rizzarelli, E., Copper(II) complexes of peptide fragments of the prion protein. Conformation changes induced by copper(II) and the binding motif in C-terminal protein region (2004) J. Inorg. Biochem., 98, pp. 133-143
Brown, D.R., Qin, K., Herms, J.W., Madlung, A., Manson, J., Strome, R., Fraser, P.E., Kretzschmar, H., The cellular prion protein binds copper in vivo (1997) Nature, 390, pp. 684-687
Millhauser, G.L., Copper binding in the prion protein (2004) Acc. Chem. Res., 37, pp. 79-85
Cereghetti, G.M., Schweiger, A., Glockshuber, R., van Doorslaer, S., Stability and Cu(II) binding of prion protein variants related to inherited human prion diseases (2003) Biophys. J., 84, pp. 1985-1997
Zuegg, J., Gready, J.E., Molecular dynamics simulations of human prion protein: Importance of correct treatment of electrostatic interactions (1999) Biochemistry, 38, pp. 13862-13876
Wong, C., Xiong, L.-W., Horiuchi, M., Raymond, L., Wehrly, K., Chesebro, B., Caughey, B., Sulfated glycans and elevated temperature stimulate PrPSc-dependent cell-free formation of protease-resistant prion protein (2001) EMBO J., 20, pp. 377-386
Cordeiro, Y., Machado, F., Juliano Neto, L., Juliano, M.A., Brentani, R.R., Foguel, D., Silva, J.L., DNA converts cellular prion protein into the beta-sheet conformation and inhibits prion peptide aggregation (2001) J. Biol. Chem., 276, pp. 49400-49409
Calzolai, L., Zahn, R., Influence of pH on NMR structure and stability of the human prion protein globular domain (2003) J. Biol. Chem., 278, pp. 35592-35596
De Simone, A., Dodson, G.G., Verma, C.S., Zagari, A., Fraternali, F., Prion and water: Tight and dynamical hydration sites have a key role in structural stability (2005) Proc. Natl. Acad. Sci. U.S.A., 102, pp. 7535-7540
Kawatake, S., Nishimura, Y., Sakaguchi, S., Iwaki, T., Doh-ura, K., Surface plasmon resonance analysis for the screening of anti-prion compounds (2006) Biol. Pharm. Bull., 29, pp. 927-932
Collins, K.D., Charge density-dependent strength of hydration and biological structure (1997) Biophys. J., 72, pp. 65-76
Collins, K.D., Ions from the hofmeister series and osmolytes: Effects on proteins in solution and in the crystallization process (2004) Methods, 34, pp. 300-311
Niedz, R.P., Evens, T.J., A solution to the problem of ion confounding in experimental biology (2006) Nat. Methods, 3, p. 417
Chen, Y.R., Huang, H.B., Chyan, C.L., Shiao, M.S., Lin, T.H., Chen, Y.C., The effect of Aβ conformation on the metal affinity and aggregation mechanism studied by circular dichroism spectroscopy (2006) J. Biochem. (Tokyo), 139, pp. 733-740
Roberts, M.F., Organic compatible solutes of halotolerant and halophilic microorganisms (2005) Saline Syst., 1, pp. 1-30
Arora, A., Ha, C., Park, C.B., Inhibition of insulin amyloid formation by small stress molecules (2004) FEBS Lett., 564, pp. 121-125
Carrel, R. W., Lomas, D. A., Conformational disease (1997) Lancet, 350, pp. 134-13
Temussi, P. A., Masino, L., Pastore, A., From Alzheimer to Huntington: Why is a structural understanding so difficult? (2003) EMBO J., 22, pp. 355-361
Baskakov, I. V., Legname, G., Prusiner, S. B., Cohen, F. E., Folding of prion protein to its native -helical conformation is under kinetic control (2001) J. Biol. Chem., 276, pp. 19687-19690
Morrissey, M. P., Shakhnovich, E. I., Evidence for the role of PrPc helix 1 in the hydrophilic seeding of prion aggregates (1999) Proc. Natl. Acad. Sci. U. S. A., 96, pp. 11293-11298
Apetri, A. C., Surewicz, W. K., Atypical effect of salts on the thermodynamic stability of human prion protein (2003) J. Biol. Chem., 278, pp. 22187-22192
Nandi, P. K., Leclerc, E., Marc, D., Unusual property of prion protein unfolding in neutral salt solution (2002) Biochemistry, 41, pp. 11017-11024
Haire, L. F., Whyte, S. M., Vasisht, N., Gill, A. C., Verma, C., Dodson, E. J., Dodson, G. G., Bayley, P. M., The crystal structure of the globular domain of sheep prion protein (2004) J. Mol. Biol., 336, pp. 1175-1183
Brown, D. R., Guantieri, V., Grasso, G., Impellizzeri, G., Pappalardo, G., Rizzarelli, E., Copper (II) complexes of peptide fragments of the prion protein. Conformation changes induced by copper (II) and the binding motif in C-terminal protein region (2004) J. Inorg. Biochem., 98, pp. 133-143
Brown, D. R., Qin, K., Herms, J. W., Madlung, A., Manson, J., Strome, R., Fraser, P. E., Kretzschmar, H., The cellular prion protein binds copper in vivo (1997) Nature, 390, pp. 684-687
Millhauser, G. L., Copper binding in the prion protein (2004) Acc. Chem. Res., 37, pp. 79-85
Cereghetti, G. M., Schweiger, A., Glockshuber, R., van Doorslaer, S., Stability and Cu (II) binding of prion protein variants related to inherited human prion diseases (2003) Biophys. J., 84, pp. 1985-1997
Wong, C., Xiong, L. -W., Horiuchi, M., Raymond, L., Wehrly, K., Chesebro, B., Caughey, B., Sulfated glycans and elevated temperature stimulate PrPSc-dependent cell-free formation of protease-resistant prion protein (2001) EMBO J., 20, pp. 377-386
Collins, K. D., Charge density-dependent strength of hydration and biological structure (1997) Biophys. J., 72, pp. 65-76
Collins, K. D., Ions from the hofmeister series and osmolytes: Effects on proteins in solution and in the crystallization process (2004) Methods, 34, pp. 300-311
Niedz, R. P., Evens, T. J., A solution to the problem of ion confounding in experimental biology (2006) Nat. Methods, 3, p. 417
Chen, Y. R., Huang, H. B., Chyan, C. L., Shiao, M. S., Lin, T. H., Chen, Y. C., The effect of A conformation on the metal affinity and aggregation mechanism studied by circular dichroism spectroscopy (2006) J. Biochem. (Tokyo), 139, pp. 733-740
Roberts, M. F., Organic compatible solutes of halotolerant and halophilic microorganisms (2005) Saline Syst., 1, pp. 1-30
56 Records (50 escludendo Abstract e Conferenze). Impact factor totale: 189.557 (169.652 escludendo Abstract e Conferenze). Impact factor a 5 anni totale: 201.659 (180.375 escludendo Abstract e Conferenze).
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