Effect of salts on the structural behavior of hPrP α2-helix-derived analogues: The counterion perspective (325 visite)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2006 Dec; 12(12): 790-795.
Tipo di articolo: Journal Article,
Impact factor: 1.801, Impact factor a 5 anni: 1.715
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-33845662273&partnerID=40&md5=c91b9da830e9a36bb0f540ad5eb00a1a
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
Riferimenti:
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
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
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2006 Dec; 12(12): 790-795.
Tipo di articolo: Journal Article,
Impact factor: 1.801, Impact factor a 5 anni: 1.715
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-33845662273&partnerID=40&md5=c91b9da830e9a36bb0f540ad5eb00a1a
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
Riferimenti:
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
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
Both theoretical studies and direct experimental evidence have emphasized the importance of electrostatic interactions in the general phenomenon of spontaneous amyloid fibril formation. A number of observations have recently spurred interest in the contribution of these interactions to the conformational behavior of the prion protein. In this paper, we show how salt addition and pH change can modify the conformation of two peptide analogues derived from the human prion protein helix 2 according to a Hofmeister-series-type dependence. Employment of various sodium salts allowed us to highlight the fact that chaotropic anions favor unstructured conformation, whereas kosmotropic anions promote the formation of compact structures like α-helix and β-sheet, which may ultimately facilitate fibril formation. This finding should warn people engaged in ion-based research on prion and derived peptides about cation-bound effects, which have been almost exclusively investigated to date, being easily confounded with modifications that are actually caused by anion activity, thus leading researchers into misunderstand ion-specific effects. To avoid the common complication of ion confounding, it is highly desirable that experiments be designed so that the species causing the modification can be unequivocally perceived. Copyright © 2006 European Peptide Society and John Wiley & Sons, Ltd.
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Vagliasindi LI, Arena G, Bonomo RP, Pappalardo G, Tabbì G
* Copper complex species within a fragment of the N-terminal repeat region in opossum PrP protein (238 visite)
Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2011 Mar 21; 40(11): 2441-2450.
Impact Factor: 3.838
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Di Natale G, Pappalardo G, Milardi D, Sciacca MF, Attanasio F, La Mendola D, Rizzarelli E
* Membrane interactions and conformational preferences of human and avian prion N-terminal tandem repeats: The role of copper(II) ions, pH, and membrane mimicking environments (367 visite)
J Phys Chem B (ISSN: 1520-6106, 1520-5207, 1520-5207electronic), 2010 Nov 4; 114(43): 13830-13838.
Impact Factor: 3.603
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Turi I, Kállay C, Szikszai D, Pappalardo G, Di Natale G, De Bona P, Rizzarelli E, Sóvágó I
* Nickel(II) complexes of the multihistidine peptide fragments of human prion protein (324 visite)
J Chem Res (ISSN: 1873-3344, 0162-0134, 0162-0134print), 2010 Sep; 104(8): 885-891.
Impact Factor: 3.317
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Benetti F, Pastorino L, Attanasio F, Rizzarelli E, Legname G
* Insights into Prion Protein Stability (161 visite)
Prion (ISSN: 1933-6896), 2010 Jul; 4(3): N/D-N/D.
Impact Factor: 2.468
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La Mendola D, Magrì A, Campagna T, Campitiello MA, Raiola L, Isernia C, Hansson O, Bonomo RP, Rizzarelli E
* A doppel alpha-helix peptide fragment mimics the copper(II) interactions with the whole protein (667 visite)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2010 Jun 1; 16(21): 6212-6223.
Impact Factor: 5.476
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Di Natale G, Pappalardo G, Milardi D, Sciacca MFM, Attanasio F, La Mendola D, Rizzarelli E
* Different Interactions Of Human And Avian Prion Proteins N-Terminal Tandem Repeat Peptides And Their Copper (ii) Complexes With Model Membranes (297 visite)
Journal Of Chemical Physics, 2010; 114: 13830-13838.
Impact Factor: 2.028
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Palladino P, Ronga L, Benedetti E, Rossi F, Ragone R
* Peptide Fragment Approach to Prion Misfolding: The Alpha-2 Domain (269 visite)
Int J Pept Res Ther (ISSN: 1573-3149, 0929-5666), 2009 Sep; 15(3): 165-176.
Impact Factor: 0.869
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Pietropaolo A, Muccioli L, Zannoni C, Rizzarelli E
* Conformational preferences of the full chicken prion protein in solution and its differences with respect to mammals (236 visite)
Chemphyschem (ISSN: 1439-7641, 1439-4235, 1439-7641electronic), 2009 Jul 13; 10(9-10): 1500-1510.
Impact Factor: 3.453
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La Mendola D, Pietropaolo A, Pappalardo G, Zannoni C, Rizzarelli E
* Prion Proteins Leading to Neurodegeneration (vol 5, pg 579, 2008) (159 visite)
Current Alzheimer Research (ISSN: 1567-2050), 2009 Jun; 6(3): N/D-N/D.
Impact Factor: 4.971
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Di Natale G, Osz K, Nagy Z, Sanna D, Micera G, Pappalardo G, Sovago I, Rizzarelli E
* The Interaction Of Copper (ii) With The Prion Peptide Fragment Huprp (76-114) Encompassing Four Histidyl Residues Within And Outside The Octarepeat Domain (211 visite)
Inorg Chem (ISSN: 0020-1669, 1520-510x, 1520-510xelectronic), 2009 May 4; 48(9): 4239-4250.
Impact Factor: 4.657
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La Mendola D, Magrì A, Hansson O, Bonomo RP, Rizzarelli E
* Copper(II) complexes with peptide fragments encompassing the sequence 122-130 of human doppel protein (242 visite)
Journal Of Inorganic Biochemistry, 2009 May; 103(5): 758-765.
Impact Factor: 3.444
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Bonomo RP, Di Natale G, Rizzarelli E, Tabbì G, Vagliasindi LI
* Copper(II) complexes of prion protein PEG11-tetraoctarepeat fragment: spectroscopic and voltammetric studies (279 visite)
Dalton T (ISSN: 1477-9226, 1477-7922, 1477-9234), 2009 Apr 14; (14): 2637-2646.
Impact Factor: 2.908
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Ronga L, Palladino P, Ragone R, Benedetti E, Rossi F
* A thermodynamic approach to the conformational preferences of the 180-195 segment derived from the human prion protein α2-helix (192 visite)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2009; 15(1): 30-35.
Impact Factor: 1.807
Dettagli Esporta in BibTeX Esporta in EndNote
La Mendola D, Pietropaolo A, Pappalardo G, Zannoni C, Rizzarelli E
* Prion proteins leading to neurodegeneration (251 visite)
Current Alzheimer Research (ISSN: 1567-2050), 2008 Dec; 5(6): 579-590.
Impact Factor: 4.132
Dettagli Esporta in BibTeX Esporta in EndNote
Bonomo RP, Pappalardo G, Rizzarelli E, Tabbì G, Vagliasindi LI
* Studies of nitric oxide interaction with mono- and dinuclear copper(II) complexes of prion protein bis-octarepeat fragments (225 visite)
Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2008 Sep 7; (29): 3805-3816.
Impact Factor: 3.58
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Pietropaolo A, Muccioli L, Zannoni C, La Mendola D, Maccarrone G, Pappalardo G, Rizzarelli E
* Unveiling the role of histidine and tyrosine residues on the conformation of the avian prion hexarepeat domain (240 visite)
J Phys Chem B (ISSN: 1520-6106, 1520-5207, 1520-5207electronic), 2008 Apr 24; 112(16): 5182-5188.
Impact Factor: 4.189
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De Simone A, Pedone C, Vitagliano L
* Structure, dynamics, and stability of assemblies of the human prion fragment SNQNNF (328 visite)
Biochem Biophys Res Commun (ISSN: 1090-2104, 0006-291x, 1090-2104electronic), 2008 Feb 15; 366(3): 800-806.
Impact Factor: 2.648
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Ronga L, Palladino P, Saviano G, Tancredi T, Benedetti E, Ragone R, Rossi F
* Structural characterization of a neurotoxic threonine-rich peptide corresponding to the human prion protein α2-helical 180-195 segment and comparison with full-length α2-helix-derived peptides (309 visite)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2008; 14(10): 1096-1102.
Impact Factor: 1.654
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Bonomo RP, Pappalardo G, Rizzarelli E, Santoro AM, Tabbì G, Vagliasindi LI
* Nitrogen oxide interaction with copper complexes formed by small peptides belonging to the prion protein octa-repeat region (337 visite)
Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2007 Apr 14; (14): 1400-1408.
Impact Factor: 3.212
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Ronga L, Langella E, Palladino P, Marasco D, Tizzano B, Saviano M, Pedone C, Improta R, Ruvo M
* Does Tetracycline Bind Helix 2 Of Prion? An Integrated Spectroscopical And Computational Study Of The Interaction Between The Antibiotic And Alpha Helix 2 Human Prion Protein Fragments (332 visite)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2007 Feb 15; 66(3): 707-715.
Impact Factor: 3.354
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Ronga L, Palladino P, Costantini S, Facchiano A, Ruvo M, Benedetti E, Ragone R, Rossi F
* Conformational diseases and structure-toxicity relationships: Lessons from prion-derived peptides (401 visite)
Curr Protein Pept Sci (ISSN: 1389-2037), 2007 Feb; 8(1): 83-90.
Impact Factor: 3.259
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Rao M, Russo F, Granata V, Berisio R, Zagari A, Gianfreda L
* Fate of prions in soil: Interaction of a recombinant ovine prion protein with synthetic humic-like mineral complexes (244 visite)
Soil Biol Biochem (ISSN: 0038-0717), 2007 Feb; 39(2): 493-504.
Impact Factor: 2.58
Dettagli Esporta in BibTeX Esporta in EndNote
Osz K, Nagy Z, Pappalardo G, Di Natale G, Sanna D, Micera G, Rizzarelli E, Sóvágó I
* Copper(II) interaction with prion peptide fragments encompassing histidine residues within and outside the octarepeat domain: speciation, stability constants and binding details (306 visite)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2007; 13(25): 7129-7143.
Impact Factor: 5.33
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Pappalardo M, Milardi D, Grasso D, La Rosa C
* Steered molecular dynamics studies reveal different unfolding pathways of prions from mammalian and non-mammalian species (216 visite)
New J Chem (ISSN: 1144-0546), 2007; 31(6): 901-905.
Impact Factor: 2.651
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Esposito L, Pedone C, Vitagliano L
* Molecular dynamics analyses of cross-beta-spine steric zipper models: beta-sheet twisting and aggregation (398 visite)
P Natl Acad Sci Usa (ISSN: 0027-8424, 1091-6490, 0027-8424print), 2006 Sep 1; 103(31): 11533-11538.
Impact Factor: 9.643
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Ronga L, Tizzano B, Palladino P, Ragone R, Urso E, Maffia M, Ruvo M, Benedetti E, Rossi F
* The prion protein: structural features and related toxic peptides (318 visite)
Chem Biol Drug Des Chemical Biology And Drug Design (ISSN: 1747-0277, 1747-0285), 2006 Sep; 68(3): 139-147.
Impact Factor: 2.507
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Joszal V, Nagy Z, Osz K, Sanna D, Di Natale G, La Mendola D, Pappalardo G, Rizzarelli E, Sovago I
* Transition metal complexes of terminally protected peptides containing histidyl residues (331 visite)
J Chem Res (ISSN: 0162-0134, 1873-3344, 0162-0134print), 2006 Sep; 100(8): 1399-1409.
Impact Factor: 2.654
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Langella E, Improta R, Crescenzi O, Barone V
* Assessing the acid-base and conformational properties of histidine residues in human prion protein (125-228) by means of pKα calculations and molecular dynamics simulations (355 visite)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2006 Jul 1; 64(1): 167-177.
Impact Factor: 3.73
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Granata V, Palladino P, Tizzano B, Negro A, Berisio R, Zagari A
* The effect of the osmolyte trimethylamine N-oxide on the stability of the prion protein at low pH (260 visite)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2006 Jun 15; 82(3): 234-240.
Impact Factor: 2.48
Dettagli Esporta in BibTeX Esporta in EndNote
Palladino P, Ronga L, Tizzano B, Rossi F, Ragone R, Tancredi T, Saviano G, Facchiano A, Costantini S, Ruvo M, Benedetti E
* Prion protein misfolding: Conformational stability of the alpha 2-helix (199 visite)
Understanding Biology Using Peptides, 2006; N/D: N/D-N/D.
Impact Factor: 2.614
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Grasso D, Grasso G, Guantieri V, Impellizzeri G, La Rosa C, Milardi D, Micera G, Osz K, Pappalardo G, Rizzarelli E, Sanna D, Sovago I
* Environmental effects on a prion's helix II domain: copper(II) and membrane interactions with PrP180-193 and its analogues (297 visite)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2005 Dec 23; 12(2): 537-547.
Impact Factor: 4.907
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La Mendola D, Bonomo RP, Impellizzeri G, Maccarrone G, Pappalardo G, Pietropaolo A, Rizzarelli E, Zito V
* Copper(II) complexes with chicken prion repeats: Influence of proline and tyrosine residues on the coordination features (201 visite)
J Biol Inorg Chem (ISSN: 0949-8257, 1432-1327electronic, 0949-8257print), 2005 Sep; 10(5): 463-475.
Impact Factor: 3.224
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Tizzano B, Palladino P, De Capua A, Marasco D, Rossi F, Benedetti E, Pedone C, Ragone R, Ruvo M
* The Human Prion Protein Alpha2 Helix: A Thermodynamic Study Of Its Conformational Preferences (316 visite)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2005 Apr 1; 59(1): 72-79.
Impact Factor: 4.684
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Di Natale G, Impellizzeri G, Pappalardo G
* Conformational properties of peptide fragments homologous to the 106-114 and 106-126 residues of the human prion protein: a CD and NMR spectroscopic study (288 visite)
Org Biomol Chem (ISSN: 1477-0520, 1477-0539, 1477-0539electronic), 2005 Feb 7; 3(3): 490-497.
Impact Factor: 2.547
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Bonomo RP, Cucinotta V, Giuffrida A, Impellizzeri G, Magrì A, Pappalardo G, Rizzarelli E, Santoro AM, Tabbì G, Vagliasindi LI
* A re-investigation of copper coordination in the octa-repeats region of the prion protein (281 visite)
Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2005 Jan 7; (1): 150-158.
Impact Factor: 3.003
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Langella E, Improta R, Barone V
* Checking the pH-induced conformational transition of prion protein by molecular dynamics simulations: Effect of protonation of histidine residues (246 visite)
Biophysical Journal (ISSN: 0006-3495, 1542-0086), 2004 Dec; 87(6): 3623-3632.
Impact Factor: 4.585
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Pappalardo M, Milardi D, La Rosa C, Zannoni C, Rizzarelli E, Grasso D
* A molecular dynamics study on the conformational stability of PrP 180-193 helix II prion fragment (206 visite)
Chem Phys Lett (ISSN: 0009-2614), 2004 Jun 1; 390(4-6): 511-516.
Impact Factor: 2.438
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Grasso D, Milardi D, La Rosa C, Rizzarelli E
* The different role of Cu++ and Zn++ ions in affecting the interaction of prion peptide PrP106-126 with model membranes (205 visite)
Chem Commun (ISSN: 1359-7345, 1364-548x, 1364-548xelectronic), 2004 Jan 21; 10(2): 246-247.
Impact Factor: 3.997
Dettagli Esporta in BibTeX Esporta in EndNote
Brown DR, 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 (374 visite)
J Chem Res (ISSN: 0162-0134, 1873-3344, 0162-0134print), 2004 Jan; 98(1): 133-143.
Impact Factor: 2.225
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Barone V, Improta R, Rega N
* Computation of protein pK's values by an integrated density functional theory/Polarizable Continuum Model approach (207 visite)
Theor Chem Acc (ISSN: 1432-881x), 2004; 111(2-6): 237-245.
Impact Factor: 2.209
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Tizzano B, Marasco D, Benedetti E, De Capua A, Palladino P, Pedone C, Perretta G, Rossi F, Ragone R, Ruvo M
* Conformational conversion of prion proteins: Role synthetic PRP 173-195 fibrillogenic peptide (246 visite)
Peptide Revolution, 2004; N/D: N/D-N/D.
Impact Factor: 4.659
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Pappalardo G, Impellizzeri G, Campagna T
* Copper(II) binding of prion protein's octarepeat model peptides (377 visite)
Inorg Chim Acta (ISSN: 0020-1693), 2004; 357(1): 185-194.
Impact Factor: 1.554
Dettagli Esporta in BibTeX Esporta in EndNote
La Mendola D, Bonomo R, Maccarrone G, Pappalardo G, Rizzarelli E
* A thermodynamic and spectroscopic study on the copper(II) complexes with hexarepeats fragments of the avian prion protein (246 visite)
J Chem Res (ISSN: 0162-0134, 1873-3344, 0162-0134print), 2003 Jul 15; 96(1): N/D-N/D.
Impact Factor: 2.343
Dettagli Esporta in BibTeX Esporta in EndNote
Bonomo RP, Grasso D, Grasso G, Guantieri V, Impellizzeri G, La Rosa C, Milardi D, Pappalardo G, Tabbì G, Rizzarelli E
* Metal binding to prion protein (205 visite)
Metal-Ligand Interactions - Molecular Nano- Micro- And Macro-Systems In Complex Environments, 2003 Jan 01; 116: 21-39.
Impact Factor: 5.664
Dettagli Esporta in BibTeX Esporta in EndNote
Grasso D, Milardi D, Guantieri V, La Rosa C, Rizzarelli E
* Interaction of prion peptide PrP 180-193 with DPPC model membranes: A thermodynamic study (284 visite)
New J Chem (ISSN: 1144-0546), 2003; 27(2): 359-364.
Impact Factor: 2.272
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Menziani MC, De Benedetti PG, Langella E, Barone V
* Seeking for binding determinants of the prion protein to human plasminogen (243 visite)
Mol Phys (ISSN: 0026-8976), 2003; 101(17): 2763-2773.
Impact Factor: 1.591
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Grasso D, Milardi D, La Rosa C, Rizzarelli E
* DSC study of the interaction of the prion peptide PrP106-126 with artificial membranes (259 visite)
New J Chem (ISSN: 1144-0546), 2001; 25(12): 1543-1548.
Impact Factor: 2.44
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Bonomo RP, Imperllizzeri G, Pappalardo G, Rizzarelli E, Tabbì G
Copper(II) binding modes in the prion octapeptide PHGGGWGQ: A spectroscopic and voltammetric study (370 visite)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2000 Nov 17; 6(22): 4195-4202.
Impact Factor: 4.698
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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).
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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Ultima modifica di Marco Comerci in data Sunday 12 July 2020, 13:15:06
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