Conformational diseases and structure-toxicity relationships: Lessons from prion-derived peptides (253 visite)
Curr Protein Pept Sci (ISSN: 1389-2037), 2007 Feb; 8(1): 83-90.
Tipo di articolo: Journal Article,
Impact factor: 3.259, Impact factor a 5 anni: 3.641
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-33847296574&partnerID=40&md5=7b79d68467c13d854285e64f32260cbc
Parole chiave: Amyloid, Copper Binding Protein, N-Linked Glycoprotein, Prion Structure, Prion Toxicity, Transmissible Spongiform Encephalopathies, Amyloid Protein, Antibiotic Agent, Metal Ion, Polyamine Derivative, Polyanion, Polyene Antibiotic Agent, Polypeptide, Prion Protein, Proteinase, Tetracycline, Tetrapyrrole Derivative, Alpha Helix, Amino Terminal Sequence, Beta Sheet, Carboxy Terminal Sequence, Cell Function, Central Nervous System Disease, Conformational Transition, Copper Metabolism, Drug Protein Binding, Enzyme Inhibition, Human, Mammal Cell, Metal Binding, Neuropathology, Nonhuman, Oxidative Stress, Prion Disease, Protein Domain, Protein Expression, Protein Secondary Structure, Review, Scrapie, Species Conservation, Structure Activity Relation, Amino Acid Sequence, Animals, Models, Molecular, Molecular Sequence Data, Nerve Degeneration, Protein Conformation, Protein Structure, Tertiary, Thermodynamics,
Affiliazioni:
*** IBB - CNR ***
Dipartimento delle Scienze Biologiche, Università Federico II di Napoli, Istituto di Biostrutture e Bioimmagini, Via Mezzocannone 16, 80134 Napoli, Italy
Dipartimento di Biochimica e Biofisica, CRISCEB, Seconda Università di Napoli, Via Costantinopoli 16, 80138 Napoli, Italy
Istituto di Scienze dell'Alimentazione, CNR, 83100 Avellino, Italy
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Tan, S.Y., Pepys, M.B., (1994) Histopathology, 25, pp. 403-414
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Bosques, C.J., Imperiali, B., (2003) Proc. Natl. Acad. Sci. USA, 100, pp. 7593-7598
Zahn, R., Liu, A., Lührs, T., Riek, R., von Schroetter, C., Garcia, F.L., Billeter, M., Wüthrich, K., (2000) Proc. Natl. Acad. Sci. USA, 97, pp. 145-150
Garcia, F.L., Zahn, R., Riek, R., Wüthrich, K., (2000) Proc. Natl. Acad. Sci. USA, 97, pp. 8334-8339
Perez, D.R., Wüthrich, K., (2005) J. Biomol. NMR, 31, pp. 259-260
Calzolai, L., Lysek, D.A., Perez, D.R., Güntert, P., Wüthrich, K., (2005) Proc. Natl. Acad. Sci. USA, 102, pp. 651-655
Lysek, D.A., Schorn, C., Nivon, L.G., Esteve-Moya, V., Christen, B., Calzolai, L., von Schroetter, C., Wüthrich, K., (2005) Proc. Natl. Acad. Sci. USA, 102, pp. 640-645
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Hornemann, S., Glockshuber, R., (1998) Proc. Natl. Acad. Sci. USA, 95, pp. 6010-6014
Swietnicki, W., Morillas, M., Chen, S.G., Gambetti, P., Surewicz, W.K., (2000) Biochemistry, 39, pp. 424-431
Zou, W.-Q., Cashman, N.R., (2002) J. Biol. Chem., 277, pp. 43942-43947
Langella, E., Improta, R., Barone, V., (2004) Biophys. J., 87, pp. 3623-3632
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Liu, A., Riek, R., Zahn, R., Hornemann, S., Glockshuber, R., Wutrich, K., (1999) Biopolymers, 51, pp. 145-152
Ziegler, J., Sticht, H., Marx, U.C., Muller, W., Rosch, P., Schwarzinger, S., (2003) J. Biol. Chem., 278, pp. 50175-50181
Gallo, M., Paludi, D., Cicero, D.O., Chiovitti, K., Millo, E., Salis, A., Damonte, G., Aceto, A., (2005) Int. J. Immunopathol. Pharmacol., 18, pp. 95-112
Winklhofer, K.F., Heske, J., Heller, U., Reintjes, A., Muranyi, I.M., Tatzelt, J., (2003) J. Biol. Chem., 278, pp. 14961-14970
Hirschberger, T., Stork, M., Schropp, B., Winklhofer, K.F., Tatzelt, J., Tavan, P., (2006) Biophys. J., 90, pp. 3908-3918
Brown, D.R., Guantieri, V., Grasso, G., Impellizzeri, G., Pappalardo, G., Rizzarelli, E., (2004) J. Inorg. Biochem., 98, pp. 133-143
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Curr Protein Pept Sci (ISSN: 1389-2037), 2007 Feb; 8(1): 83-90.
Tipo di articolo: Journal Article,
Impact factor: 3.259, Impact factor a 5 anni: 3.641
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-33847296574&partnerID=40&md5=7b79d68467c13d854285e64f32260cbc
Parole chiave: Amyloid, Copper Binding Protein, N-Linked Glycoprotein, Prion Structure, Prion Toxicity, Transmissible Spongiform Encephalopathies, Amyloid Protein, Antibiotic Agent, Metal Ion, Polyamine Derivative, Polyanion, Polyene Antibiotic Agent, Polypeptide, Prion Protein, Proteinase, Tetracycline, Tetrapyrrole Derivative, Alpha Helix, Amino Terminal Sequence, Beta Sheet, Carboxy Terminal Sequence, Cell Function, Central Nervous System Disease, Conformational Transition, Copper Metabolism, Drug Protein Binding, Enzyme Inhibition, Human, Mammal Cell, Metal Binding, Neuropathology, Nonhuman, Oxidative Stress, Prion Disease, Protein Domain, Protein Expression, Protein Secondary Structure, Review, Scrapie, Species Conservation, Structure Activity Relation, Amino Acid Sequence, Animals, Models, Molecular, Molecular Sequence Data, Nerve Degeneration, Protein Conformation, Protein Structure, Tertiary, Thermodynamics,
Affiliazioni:
*** IBB - CNR ***
Dipartimento delle Scienze Biologiche, Università Federico II di Napoli, Istituto di Biostrutture e Bioimmagini, Via Mezzocannone 16, 80134 Napoli, Italy
Dipartimento di Biochimica e Biofisica, CRISCEB, Seconda Università di Napoli, Via Costantinopoli 16, 80138 Napoli, Italy
Istituto di Scienze dell'Alimentazione, CNR, 83100 Avellino, Italy
Riferimenti:
Carrel, R.W., Lomas, D.A., (1997) Lancet, 350, pp. 134-13
Temussi, P.A., Masino, L., Pastore, A., (2003) EMBO J., 22, pp. 355-361
Blake, C., Serpell, L., (1996) Structure, 4, pp. 989-998
Thompson, A., White, A.R., McLean, C., Masters, C.L., Cappai, R., Barrow, C.J., (2000) J. Neurosci. Res., 62, pp. 293-301
Booth, D.R., Sunde, M., Bellotti, V., Robinson, C.V., Hutchinson, W.L., Fraser, P.E., Hawkins, P.N., Pepys, M.B., (1997) Nature, 385, pp. 787-793
Tan, S.Y., Pepys, M.B., (1994) Histopathology, 25, pp. 403-414
Sunde, M., Serpell, L.C., Bartlam, M., Fraser, P.E., Pepys, M.B., Blake, C.C., (1997) J. Mol. Biol., 273, pp. 729-739
Prusiner, S.B., (1998) Proc. Natl. Acad. Sci. USA, 95, pp. 13363-13383
Collinge, J., Rossor, M., (1996) Lancet, 347, pp. 916-917
Collee, J.G., (1996) Lancet, 347, pp. 917-918
Stahl, N., Borchelt, D.R., Hsiao, K., Prusiner, S.B., (1987) Cell, 51, pp. 229-240
Chesebro, B., Trifilo, M., Race, R., Meade-White, K., Teng, C., LaCasse, R., Raymond, L., Oldstone, M., (2005) Science, 308, pp. 1435-1439
Bosques, C.J., Imperiali, B., (2003) Proc. Natl. Acad. Sci. USA, 100, pp. 7593-7598
Zahn, R., Liu, A., Lührs, T., Riek, R., von Schroetter, C., Garcia, F.L., Billeter, M., Wüthrich, K., (2000) Proc. Natl. Acad. Sci. USA, 97, pp. 145-150
Garcia, F.L., Zahn, R., Riek, R., Wüthrich, K., (2000) Proc. Natl. Acad. Sci. USA, 97, pp. 8334-8339
Perez, D.R., Wüthrich, K., (2005) J. Biomol. NMR, 31, pp. 259-260
Calzolai, L., Lysek, D.A., Perez, D.R., Güntert, P., Wüthrich, K., (2005) Proc. Natl. Acad. Sci. USA, 102, pp. 651-655
Lysek, D.A., Schorn, C., Nivon, L.G., Esteve-Moya, V., Christen, B., Calzolai, L., von Schroetter, C., Wüthrich, K., (2005) Proc. Natl. Acad. Sci. USA, 102, pp. 640-645
Gossert, A.D., Bonjour, S., Lysek, D.A., Fiorito, F., Wüthrich, K., (2005) Proc. Natl. Acad. Sci. USA, 102, pp. 646-650
Riek, R., Hornemann, S., Wider, G., Billeter, M., Glockshuber, R., Wüthrich, K., (1996) Nature, 382, pp. 180-182
Jackson, G.S., Hosszu, L.L.P., Power, A., Hill, A.F., Kenney, J., Saibil, H., Craven, C.J., Collinge, J., (1999) Science, 283, pp. 1935-1937
Shaked, G.M., Shaked, Y., Kariv-Inbal, Z., Halimi, M., Avraham, I., Gabizon, R., (2001) J. Biol. Chem., 276, pp. 31479-31482
Georgieva, D., Rypniewski, W., Echner, H., Perbandt, M., Koker, M., Clos, J., Redecke, L., Betzel, C., (2004) Biochem. Biophys. Res. Commun., 325, pp. 1406-1411
Pan, K.-H., Baldwin, M., Nguyen, J., Gasset, M., Serban, A., Groth, D., Mehlhorn, I., Prusiner, S.B., (1993) Proc. Natl. Acad. Sci. USA, 90, pp. 10962-10966
Huang, Z., Prusiner, S.B., Cohen, F.E., (1996) Fold. Des., 1, pp. 13-19
Forloni, G., Angeretti, N., Chiesa, R., Monzani, E., Salmona, M., Bugiani, O., Tagliavini, F., (1993) Nature, 362, pp. 543-546
Fioriti, L., Quaglio, E., Massignan, T., Colombo, L., Stewart, R.S., Salmona, M., Harris, D.A., Chiesa, R., (2005) Mol. Cell. Neurosci., 28, pp. 165-176
De Gioia, L., Selvaggini, C., Ghibaudi, E., Diomede, L., Bugiani, O., Forloni, G., Tagliavini, F., Salmona, M., (1994) J. Biol. Chem., 269, pp. 7859-7862
Dupiereux, I., Zorzi, W., Lins, L., Brasseur, R., Colson, P., Heinen, E., Elmoualij, B., (2005) Biochem. Biophys. Res. Comm., 331, pp. 894-901
Jobling, M.F., Stewart, L.R., White, A.R., McLean, C., Friedhuber, A., Maher, F., Beyreuther, K., Cappai, R., (1999) J. Neurochem., 73, pp. 1557-1565
Selvaggini, C., De Gioia, L., Cantu, L., Ghibaudi, E., Diomede, L., Passerini, F., Forloni, G., Salmona, M., (1993) Biochem. Biophys. Res. Commun., 194, pp. 1380-1386
Haire, L.F., Whyte, S.M., Vasisht, N., Gill, A.C., Verma, C., Dodson, E.J., Dodson, G.G., Bayley, P.M., (2004) J. Mol. Biol., 336, pp. 1175-1183
Swietnicki, W., Petersen, R., Gambetti, P., Surewicz, W.K., (1997) J. Biol. Chem., 272, pp. 27517-27520
Hornemann, S., Glockshuber, R., (1998) Proc. Natl. Acad. Sci. USA, 95, pp. 6010-6014
Swietnicki, W., Morillas, M., Chen, S.G., Gambetti, P., Surewicz, W.K., (2000) Biochemistry, 39, pp. 424-431
Zou, W.-Q., Cashman, N.R., (2002) J. Biol. Chem., 277, pp. 43942-43947
Langella, E., Improta, R., Barone, V., (2004) Biophys. J., 87, pp. 3623-3632
Borchelt, D.R., Taraboulos, A., Prusiner, S.B., (1992) J. Biol. Chem., 267, pp. 16188-16199
Knaus, K.J., Morillas, M., Swietnicki, W., Malone, M., Surewicz, W., Yee, V.C., (2001) Nat. Struct. Biol., 8, pp. 770-774
Wopfner, F., Weidenhöfer, G., Schneider, R., von Brunn, A., Gilch, S., Schwarz, T.F., Werner, T., Schätz, H.M., (1999) J. Mol. Biol., 289, pp. 1163-1178
Minor Jr., D.L., Kim, P.S., (1994) Nature, 367, pp. 660-663
Welker, E., Raymond, L.D., Scheraga, H.A., Caughey, B., (2002) J. Biol. Chem., 277, pp. 33477-33481
Liu, A., Riek, R., Zahn, R., Hornemann, S., Glockshuber, R., Wutrich, K., (1999) Biopolymers, 51, pp. 145-152
Ziegler, J., Sticht, H., Marx, U.C., Muller, W., Rosch, P., Schwarzinger, S., (2003) J. Biol. Chem., 278, pp. 50175-50181
Gallo, M., Paludi, D., Cicero, D.O., Chiovitti, K., Millo, E., Salis, A., Damonte, G., Aceto, A., (2005) Int. J. Immunopathol. Pharmacol., 18, pp. 95-112
Winklhofer, K.F., Heske, J., Heller, U., Reintjes, A., Muranyi, I.M., Tatzelt, J., (2003) J. Biol. Chem., 278, pp. 14961-14970
Hirschberger, T., Stork, M., Schropp, B., Winklhofer, K.F., Tatzelt, J., Tavan, P., (2006) Biophys. J., 90, pp. 3908-3918
Brown, D.R., Guantieri, V., Grasso, G., Impellizzeri, G., Pappalardo, G., Rizzarelli, E., (2004) J. Inorg. Biochem., 98, pp. 133-143
Tizzano, B., Palladino, P., De Capua, A., Marasco, D., Rossi, F., Benedetti, E., Pedone, C., Ruvo, M., (2005) Proteins, 59, pp. 72-79
Ikeda, K., Higo, J., (2003) Protein Sci., 12, pp. 2542-2548
Ronga, L., Palladino, P., Tizzano, B., Marasco, D., Benedetti, E., Ragone, R., Rossi, F., (2006) J. Pept. Sci., , in press
Riek, R., Wider, G., Billeter, M., Hornemann, S., Glockshuber, R., Wütrich, K., (1998) Proc. Natl. Acad. Sci. USA, 95, pp. 11667-11672
Salmona, M., Morbin, M., Massignan, T., Colombo, L., Mazzoleni, G., Capobianco, R., Diomede, L., Tagliavini, F., (2003) J. Biol. Chem., 278, pp. 48146-48153
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The physiological form of the prion protein is normally expressed in mammalian cell and is highly conserved among species, although its role in cellular function remains elusive. Available evidence suggests that this protein is essential for neuronal integrity in the brain, possibly with a role in copper metabolism and cellular response to oxidative stress. In prion diseases, the benign cellular form of the protein is converted into an insoluble, protease-resistant abnormal scrapie form. This conversion parallels a conformational change of the polypeptide from a predominantly a-helical to a highly P-sheet secondary structure. The scrapie form accumulates in the central nervous system of affected individuals, and its protease-resistant core aggregates into amyloid Fibrils outside the cell. The pathogenesis and molecular basis of the nerve cell loss that accompanies this process are not understood. Limited structural information is available on aggregate formation by this protein as the possible cause of these diseases and on its toxicity. A large amount of structure-activity studies is based on the prion fragment approach, but the resulting information is often difficult to untangle. This overview focuses on the most relevant structural and functional aspects of the prion-induced conformational disease linked to peptides derived from the unstructured N-terminal and globular C-terminal domains.
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Impact factor a 5 anni totale: 127.338 (120.992 escludendo Abstract e Conferenze).
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