Conformational diseases and structure-toxicity relationships: Lessons from prion-derived peptides (527 views visite)
Curr Protein Pept Sci (ISSN: 1389-2037), 2007 Feb; 8(1): 83-90.
Export to Esporta in BibTeX Export to Esporta in EndNote
Paper type Tipo di articolo: Journal Article,
Impact factor: 3.259, 5-year impact factor Impact factor a 5 anni: 3.641
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-33847296574&partnerID=40&md5=7b79d68467c13d854285e64f32260cbc
Keywords 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,
Affiliations 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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Curr Protein Pept Sci (ISSN: 1389-2037), 2007 Feb; 8(1): 83-90.
Export to Esporta in BibTeX Export to Esporta in EndNote
Paper type Tipo di articolo: Journal Article,
Impact factor: 3.259, 5-year impact factor Impact factor a 5 anni: 3.641
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-33847296574&partnerID=40&md5=7b79d68467c13d854285e64f32260cbc
Keywords 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,
Affiliations 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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Ronga, L., Langella, E., Palladino, P., Marasco, D., Tizzano, B., Saviano, M., Pedone, C., Ruvo, M., (2006) Proteins, , in press
Conformational diseases and structure-toxicity relationships: Lessons from prion-derived peptides
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.
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.
Conformational diseases and structure-toxicity relationships: Lessons from prion-derived peptides
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Conformational diseases and structure-toxicity relationships: Lessons from prion-derived peptides
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 (535 visite)
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 (523 visite)
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 (373 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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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 (267 visite)
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 (375 visite)
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 (387 visite)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2008; 14(10): 1096-1102.
Impact Factor: 1.654
Dettagli Esporta in BibTeX Esporta in 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 (414 visite)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2006 Dec; 12(12): 790-795.
Impact Factor: 1.801
Dettagli Esporta in BibTeX Esporta in EndNote
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 (440 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
Dettagli Esporta in BibTeX Esporta in EndNote
8 Records (8 escludendo Abstract e Conferenze).
Impact factor totale: 22.8 (22.8 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 21.597 (21.597 escludendo Abstract e Conferenze).
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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 (535 visite)
Journal Of Biomolecular Structure & Dynamics, 2013 May 1; 31(5): 441-452.
Impact Factor: 2.983
Dettagli Esporta in BibTeX Esporta in 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 (523 visite)
Cell Mol Life Sci (ISSN: 1420-9071electronic, 1420-682xlinking), 2010 Jun; 67(11): 1943-1955.
Impact Factor: 7.047
Dettagli Esporta in BibTeX Esporta in EndNote
Palladino P, Ronga L, Benedetti E, Rossi F, Ragone R
* Peptide Fragment Approach to Prion Misfolding: The Alpha-2 Domain (373 visite)
Int J Pept Res Ther (ISSN: 1573-3149, 0929-5666), 2009 Sep; 15(3): 165-176.
Impact Factor: 0.869
Dettagli Esporta in BibTeX Esporta in 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 (267 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 (375 visite)
Current Alzheimer Research (ISSN: 1567-2050), 2008 Dec; 5(6): 579-590.
Impact Factor: 4.132
Dettagli Esporta in BibTeX Esporta in 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 (387 visite)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2008; 14(10): 1096-1102.
Impact Factor: 1.654
Dettagli Esporta in BibTeX Esporta in 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 (414 visite)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2006 Dec; 12(12): 790-795.
Impact Factor: 1.801
Dettagli Esporta in BibTeX Esporta in EndNote
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 (440 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
Dettagli Esporta in BibTeX Esporta in EndNote
8 Records (8 escludendo Abstract e Conferenze).
Impact factor totale: 22.8 (22.8 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 21.597 (21.597 escludendo Abstract e Conferenze).
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