The prion protein: structural features and related toxic peptides (544 views)
Chem Biol Drug Des (ISSN: 1747-0277, 1747-0285), 2006 Sep; 68(3): 139-147.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 2.507, 5-year impact factor: 2.479
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-33750342656&partnerID=40&md5=4b55086de5dfe6d2b5d51a81145ca505
Keywords: Amyloid, Copper Binding Protein, N-Linked Glycoprotein, Prion Structure, Prion Toxicity, Transmissible Spongiform Encephalopathies, Prion Protein, Alpha Helix, Amino Terminal Sequence, Carboxy Terminal Sequence, Cell Function, Cell Loss, Human, Nonhuman, Prion Disease, Priority Journal, Protein Binding, Protein Conformation, Protein Expression, Protein Structure, Review, Animals, Cell Survival, Peptides, Secondary, Structure-Activity Relationship, Thermodynamics, Mammalia,
Affiliations:
*** IBB - CNR ***
Dipartimento Delle Scienze Biologiche, C.I.R.Pe.B., CNR, Via Mezzocannone 16, 80134 Napoli, Italy
Dipartimento di Biochimica e Biofisica, CRISCEB, Seconda Università di Napoli, Via Costantinopoli 16, 80138 Napoli, Italy
Dipartimento di Scienze e Tecnologie Biologiche Ed Ambientali, Università degli Studi di Lecce, 73100 Lecce, Italy
References:
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
Blake, C., Serpell, L., Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix (1996) Structure, 4, pp. 989-998
Thompson, A., White, A.R., McLean, C., Masters, C.L., Cappai, R., Barrow, C.J., Amyloidogenicity and neurotoxicity of peptides corresponding to the helical regions of PrPC (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., Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis (1997) Nature, 385, pp. 787-793
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Collee, J.G., A dreadful challenge (1996) Lancet, 347, pp. 917-918
Hosszu, L.L.P., Jackson, G.S., Trevitt, C.R., Jones, S., Batchelor, M., Bhelt, D., Prodromidou, K., Collinge, J., The residue 129 polymorphism in human prion protein does not confer susceptibility to Creutzfeldt-Jakob disease by altering the structure or global stability of PrPC (2004) J Biol Chem, 279, pp. 28515-28521
Zou, W.-Q., Capellari, S., Parchi, P., Sy, M.-S., Gambetti, P., Chen, S.G., Identification of novel proteinase K-resistant C-terminal fragments of PrP in Creutzfeldt-Jakob Disease (2003) J Biol Chem, 278, pp. 40429-40436
Chesebro, B., Trifilo, M., Race, R., Meade-White, K., Teng, C., LaCasse, R., Raymond, L., Oldstone, M., Anchorless prion protein results in infectious amyloid disease without clinical scrapie (2005) Science, 308, pp. 1435-1439
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Pan, K.-H., Baldwin, M., Nguyen, J., Gasset, M., Serban, A., Groth, D., Mehlhorn, I., Prusiner, S.B., Conversion of α-helices into β-sheets features in the formation of the scrapie prion proteins (1993) Proc Natl Acad Sci USA, 90, pp. 10962-10966
Huang, Z., Prusiner, S.B., Cohen, F.E., Scrapie prions: A three-dimensional model of an infectious fragment (1996) Fold des, 1, pp. 13-19
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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Chem Biol Drug Des (ISSN: 1747-0277, 1747-0285), 2006 Sep; 68(3): 139-147.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 2.507, 5-year impact factor: 2.479
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-33750342656&partnerID=40&md5=4b55086de5dfe6d2b5d51a81145ca505
Keywords: Amyloid, Copper Binding Protein, N-Linked Glycoprotein, Prion Structure, Prion Toxicity, Transmissible Spongiform Encephalopathies, Prion Protein, Alpha Helix, Amino Terminal Sequence, Carboxy Terminal Sequence, Cell Function, Cell Loss, Human, Nonhuman, Prion Disease, Priority Journal, Protein Binding, Protein Conformation, Protein Expression, Protein Structure, Review, Animals, Cell Survival, Peptides, Secondary, Structure-Activity Relationship, Thermodynamics, Mammalia,
Affiliations:
*** IBB - CNR ***
Dipartimento Delle Scienze Biologiche, C.I.R.Pe.B., CNR, Via Mezzocannone 16, 80134 Napoli, Italy
Dipartimento di Biochimica e Biofisica, CRISCEB, Seconda Università di Napoli, Via Costantinopoli 16, 80138 Napoli, Italy
Dipartimento di Scienze e Tecnologie Biologiche Ed Ambientali, Università degli Studi di Lecce, 73100 Lecce, Italy
References:
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
Blake, C., Serpell, L., Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix (1996) Structure, 4, pp. 989-998
Thompson, A., White, A.R., McLean, C., Masters, C.L., Cappai, R., Barrow, C.J., Amyloidogenicity and neurotoxicity of peptides corresponding to the helical regions of PrPC (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., Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis (1997) Nature, 385, pp. 787-793
Tan, S.Y., Pepys, M.B., Amyloidosis (1994) Histopathology, 25, pp. 403-414
Sunde, M., Serpell, L.C., Bartlam, M., Fraser, P.E., Pepys, M.B., Blake, C.F., Common core structure of amyloid fibrils by synchrotron x-ray diffraction (1997) J Mol Biol, 273, pp. 729-739
Prusiner, S.B., Prions (1998) Proc Natl Acad Sci USA, 95, pp. 13363-13383
Collinge, J., Rossor, M., A new variant of prion disease (1996) Lancet, 347, pp. 916-917
Collee, J.G., A dreadful challenge (1996) Lancet, 347, pp. 917-918
Hosszu, L.L.P., Jackson, G.S., Trevitt, C.R., Jones, S., Batchelor, M., Bhelt, D., Prodromidou, K., Collinge, J., The residue 129 polymorphism in human prion protein does not confer susceptibility to Creutzfeldt-Jakob disease by altering the structure or global stability of PrPC (2004) J Biol Chem, 279, pp. 28515-28521
Zou, W.-Q., Capellari, S., Parchi, P., Sy, M.-S., Gambetti, P., Chen, S.G., Identification of novel proteinase K-resistant C-terminal fragments of PrP in Creutzfeldt-Jakob Disease (2003) J Biol Chem, 278, pp. 40429-40436
Chesebro, B., Trifilo, M., Race, R., Meade-White, K., Teng, C., LaCasse, R., Raymond, L., Oldstone, M., Anchorless prion protein results in infectious amyloid disease without clinical scrapie (2005) Science, 308, pp. 1435-1439
Bosques, C.J., Imperiali, B., The interplay of glycosylation and disulfide formation influences fibrillization in a prion protein fragment (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., NMR solution structure of the human prion protein (2000) Proc Natl Acad Sci USA, 97, pp. 145-150
Garcia, F.L., Zahn, R., Riek, R., Wüthrich, K., NMR structure of the bovine prion protein (2000) Proc Natl Acad Sci USA, 97, pp. 8334-8339
Perez, D.R., Wüthrich, K., 1H, 13C, and15N resonance assignments of SAP18 (2005) J Biomol NMR, 31, pp. 259-260
Calzolai, L., Lysek, D.A., Perez, D.R., Güntert, P., Wüthrich, K., Prion protein NMR structures of chickens, turtles, and frogs (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., Prion protein NMR structures of cats, dogs, pigs, and sheep (2005) Proc Natl Acad Sci USA, 102, pp. 640-645
Gossert, A.D., Bonjour, S., Lysek, D.A., Fiorito, F., Wüthrich, K., Prion protein NMR structures of elk and of mouse/elk hybrids (2005) Proc Natl Acad Sci USA, 102, pp. 646-650
Riek, R., Hornemann, S., Wider, G., Billeter, M., Glockshuber, R., Wüthrich, K., NMR structure of the mouse prion protein domain PrP(121-231) (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., Reversible conversion of monomeric human prion protein between native and fibrilogenic conformations (1999) Science, 283, pp. 1935-1937
Shaked, G.M., Shaked, Y., Kariv-Inbal, Z., Halimi, M., Avraham, I., Gabizon, R., A protease-resistant prion protein isoform is present in urine of animals and humans affected with prion diseases (2001) J Biol Chem, 276, pp. 31479-31482
Georgieva, D., Rypniewski, W., Echner, H., Perbandt, M., Koker, M., Clos, J., Redecke, L., Betzel, C., Synthetic human prion protein octapeptide repeat binds to the proteinase K active site (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., Conversion of α-helices into β-sheets features in the formation of the scrapie prion proteins (1993) Proc Natl Acad Sci USA, 90, pp. 10962-10966
Huang, Z., Prusiner, S.B., Cohen, F.E., Scrapie prions: A three-dimensional model of an infectious fragment (1996) Fold des, 1, pp. 13-19
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
Swietnicki, W., Petersen, R., 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
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 USA, 95, pp. 6010-6014
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
Zou, W.-Q., Cashman, N.R., Acidic pH and detergents enhance in vitro conversion of human brain PrPC to a PrPSc-like form (2002) J Biol Chem, 277, pp. 43942-43947
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The prion protein: structural features and related toxic peptides
Prion diseases are characterized by the conversion of the physiological cellular form of the prion protein (PrPC) into an insoluble, partially protease-resistant abnormal scrapie form (PrPSc). PrPC is normally expressed in mammalian cell and is highly conserved among species, although its role in cellular function remains elusive. The conversion of PrPC to PrPSc parallels a conformational change of the polypeptide from a predominantly alpha-helical to a highly beta-sheet secondary structure. The pathogenesis and molecular basis of the consequent nerve cell loss 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. This brief overview focuses on the large amount of structure-activity studies based on the prion fragment approach, hinging on peptides derived from the unstructured N-terminal and globular C-terminal domains. It is well documented that most of the fragments with regular secondary structure, with the exception of helices 1 and 3, possess a high beta-sheet propensity and tendency to form beta-sheet-like aggregates. In this context, helix 2 plays a crucial role because it is able to adopt both misfolded and partially helical conformation. However, only a few mutants are able to display its intrinsic neurotoxicity.
Prion diseases are characterized by the conversion of the physiological cellular form of the prion protein (PrPC) into an insoluble, partially protease-resistant abnormal scrapie form (PrPSc). PrPC is normally expressed in mammalian cell and is highly conserved among species, although its role in cellular function remains elusive. The conversion of PrPC to PrPSc parallels a conformational change of the polypeptide from a predominantly alpha-helical to a highly beta-sheet secondary structure. The pathogenesis and molecular basis of the consequent nerve cell loss 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. This brief overview focuses on the large amount of structure-activity studies based on the prion fragment approach, hinging on peptides derived from the unstructured N-terminal and globular C-terminal domains. It is well documented that most of the fragments with regular secondary structure, with the exception of helices 1 and 3, possess a high beta-sheet propensity and tendency to form beta-sheet-like aggregates. In this context, helix 2 plays a crucial role because it is able to adopt both misfolded and partially helical conformation. However, only a few mutants are able to display its intrinsic neurotoxicity.
The prion protein: structural features and related toxic peptides
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The prion protein: structural features and related toxic peptides
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De Simonea A, Stanzione F, Marasco D, Vitagliano L, Esposito L
* The Intrinsic Stability Of The Human Prion Beta-Sheet Region Investigated By Molecular Dynamics (700 views)
Journal Of Biomolecular Structure & Dynamics, 2013 May 1; 31(5): 441-452.
Impact Factor: 2.983
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Tosco A, Monti MC, Fontanella B, Montefusco S, D'Andrea LD, Ziaco B, Baldantoni D, Rio MC, Marzullo L
* Copper binds the carboxy-terminus of trefoil protein 1 (TFF1), favoring its homodimerization and motogenic activity (1286 views)
Cell Mol Life Sci (ISSN: 1420-9071electronic, 1420-682xlinking), 2010 Jun; 67(11): 1943-1955.
Impact Factor: 7.047
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Palladino P, Ronga L, Benedetti E, Rossi F, Ragone R
* Peptide Fragment Approach to Prion Misfolding: The Alpha-2 Domain (402 views)
Int J Pept Res Ther (ISSN: 1573-3149, 0929-5666), 2009 Sep; 15(3): 165-176.
Impact Factor: 0.869
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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 (287 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2009; 15(1): 30-35.
Impact Factor: 1.807
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La Mendola D, Pietropaolo A, Pappalardo G, Zannoni C, Rizzarelli E
* Prion proteins leading to neurodegeneration (449 views)
Current Alzheimer Research (ISSN: 1567-2050), 2008 Dec; 5(6): 579-590.
Impact Factor: 4.132
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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 (413 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2008; 14(10): 1096-1102.
Impact Factor: 1.654
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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 (553 views)
Curr Protein Pept Sci (ISSN: 1389-2037, 1389-2037linking), 2007 Feb; 8(1): 83-90.
Impact Factor: 3.259
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Ronga L, Palladino P, Tizzano B, Marasco D, Benedetti E, Ragone R, Rossi F
* Effect of salts on the structural behavior of hPrP α2-helix-derived analogues: The counterion perspective (470 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2006 Dec; 12(12): 790-795.
Impact Factor: 1.801
View Export to BibTeX Export to EndNote
* The Intrinsic Stability Of The Human Prion Beta-Sheet Region Investigated By Molecular Dynamics (700 views)
Journal Of Biomolecular Structure & Dynamics, 2013 May 1; 31(5): 441-452.
Impact Factor: 2.983
View Export to BibTeX Export to EndNote
Tosco A, Monti MC, Fontanella B, Montefusco S, D'Andrea LD, Ziaco B, Baldantoni D, Rio MC, Marzullo L
* Copper binds the carboxy-terminus of trefoil protein 1 (TFF1), favoring its homodimerization and motogenic activity (1286 views)
Cell Mol Life Sci (ISSN: 1420-9071electronic, 1420-682xlinking), 2010 Jun; 67(11): 1943-1955.
Impact Factor: 7.047
View Export to BibTeX Export to EndNote
Palladino P, Ronga L, Benedetti E, Rossi F, Ragone R
* Peptide Fragment Approach to Prion Misfolding: The Alpha-2 Domain (402 views)
Int J Pept Res Ther (ISSN: 1573-3149, 0929-5666), 2009 Sep; 15(3): 165-176.
Impact Factor: 0.869
View Export to BibTeX Export to EndNote
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 (287 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2009; 15(1): 30-35.
Impact Factor: 1.807
View Export to BibTeX Export to EndNote
La Mendola D, Pietropaolo A, Pappalardo G, Zannoni C, Rizzarelli E
* Prion proteins leading to neurodegeneration (449 views)
Current Alzheimer Research (ISSN: 1567-2050), 2008 Dec; 5(6): 579-590.
Impact Factor: 4.132
View Export to BibTeX Export to EndNote
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 (413 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2008; 14(10): 1096-1102.
Impact Factor: 1.654
View Export to BibTeX Export to EndNote
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 (553 views)
Curr Protein Pept Sci (ISSN: 1389-2037, 1389-2037linking), 2007 Feb; 8(1): 83-90.
Impact Factor: 3.259
View Export to BibTeX Export to EndNote
Ronga L, Palladino P, Tizzano B, Marasco D, Benedetti E, Ragone R, Rossi F
* Effect of salts on the structural behavior of hPrP α2-helix-derived analogues: The counterion perspective (470 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2006 Dec; 12(12): 790-795.
Impact Factor: 1.801
View Export to BibTeX Export to EndNote
8 Records (8 excluding Abstracts).
Total impact factor: 23.552 (23.552 excluding Abstracts).
Total 5 year impact factor: 22.759 (22.759 excluding Abstracts).
Total impact factor: 23.552 (23.552 excluding Abstracts).
Total 5 year impact factor: 22.759 (22.759 excluding Abstracts).
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