Effect of salts on the structural behavior of hPrP α2-helix-derived analogues: The counterion perspective(173 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
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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
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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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