Recombinant amyloidogenic domain of ApoA-I: analysis of its fibrillogenic potential (365 views)
Biochemical And Biophysical Research Communications (ISSN: 0006-291x, 0006-291xprint), 2006 Dec 8; 351(1): 223-228.
Export to BibTeX Export to EndNote
Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 2.855, 5-year impact factor: 2.474
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-33750411236&partnerID=40&md5=d32ac16b62e4da224f03d319a2119446
Keywords: Apoa-I Amyloidosis, Conformational Analysis, Fibrillogenesis, Recombinant Amyloidogenic Proteins, Apolipoprotein A1, Amino Terminal Sequence, Article, Carboxy Terminal Sequence, Gene Identification, Genetic Transfection, Human, Molecular Dynamics, Priority Journal, Protein Interaction, Thermodynamics, Binding Sites, Dimerization, Hydrogen-Ion Concentration, Multiprotein Complexes, Protein Binding, Chemistry, Ultrastructure,
Affiliations:
*** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini, CNR, Napoli, 80134, Italy
Dipartimento di Biologia Strutturale e Funzionale, Università di Napoli Federico II, via Cinthia 4, Napoli, 80126, Italy
CEINGE Biotecnologie Avanzate, Napoli, 80131, Italy
Dipartimento di Chimica Organica e Biochimica, Università di Napoli Federico II, Napoli, 80126, Italy
Laboratorio di Biotecnologie IRCCS, Pavia, 27100, Italy
Dipartimento di Fisica, Università di Genova, Genova, 16146, Italy
Department of Chemistry, University of Cambridge, Cambridge, CB2 IEW, United Kingdom
References:
Chiti, F., Dobson, C.M., Protein misfolding, functional amyloid, and human disease (2006) Annu. Rev. Biochem., 75, pp. 333-36
Obici, L., Franceschini, G., Calabresi, L., Giorgetti, S., Stoppini, M., Merlini, G., Bellotti, V., Structure, function and amyloidogenic propensity of apolipoprotein A-I (2006) Amyloid, 13, pp. 1-15
Andreola, A., Bellotti, V., Giorgetti, S., Mangione, P., Obici, L., Stoppini, M., Torres, J., Sunde, M., Conformational switching and fibrillogenesis in the amyloidogenic fragment of apolipoprotein A-I (2003) J. Biol. Chem., 278, pp. 2444-2451
Shevchenko, A., Keller, P., Scheiffele, P., Mann, M., Simons, K., Identification of components of trans-Golgi network-derived transport vesicles and detergent-insoluble complexes by nanoelectrospray tandem mass spectrometry (1997) Electrophoresis, 18, pp. 2591-2600
Scaloni, A., Miraglia, N., Orru, S., Amodeo, P., Motta, A., Marino, G., Pucci, P., Topology of the calmodulin-melittin complex (1998) J. Mol. Biol., 277, pp. 945-958
Rogers, D.P., Brouillette, C.G., Engler, J.A., Tendian, S.W., Roberts, L., Mishra, V.K., Anantharamaiah, G.M., Ray, M.J., Truncation of the amino terminus of human apolipoprotein A-I substantially alters only the lipid-free conformation (1997) Biochemistry, 36, pp. 288-300
Relini, A., Rolandi, R., Bolognesi, M., Gliozzi, A., Aboudan, M., Merlini, G., Bellotti, V., Ultrastructural organization of ex-vivo amyloid fibrils formed by the apolipoprotein A-I Leu174Ser variant: an atomic force microscopy study (2004) Biochim. Biophys. Acta, 1690, pp. 33-41
Obici, L., Bellotti, V., Mangione, P., Stoppini, M., Arbustini, E., Verga, R., Zorzoli, I., Merlini, G., The new apolipoprotein A-I variant Leu174 → Ser causes chardiac amyloidosis, and the fibrils are constituted by the 93-residue N-terminal polypeptide (1999) Am. J. Pathol., 155, pp. 695-702
Semisotnov, G.V., Rodinova, N.A., Razgulyaev, O.I., Uversky, V.N., Gripas, A.F., Gilmanshin, R.I., Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe (1991) Biopolymers, 31, pp. 119-128
Mangione, P., Sunde, M., Giorgetti, S., Stoppini, M., Esposito, G., Gianelli, L., Obici, L., Bellotti, V., Amyloid fibrils derived from the apolipoprotein A-I Leu174Ser variant contain elements of ordered helical structure (2001) Protein Sci., 10, pp. 187-199
Buck, M., Trifluoroethanol and colleagues: cosolvents come of age. Recent studies with peptides and proteins (1998) Q. Rev. Biophys., 31, pp. 297-355
Rogers, D. P., Brouillette, C. G., Engler, J. A., Tendian, S. W., Roberts, L., Mishra, V. K., Anantharamaiah, G. M., Ray, M. J., Truncation of the amino terminus of human apolipoprotein A-I substantially alters only the lipid-free conformation (1997) Biochemistry, 36, pp. 288-300
Semisotnov, G. V., Rodinova, N. A., Razgulyaev, O. I., Uversky, V. N., Gripas, A. F., Gilmanshin, R. I., Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe (1991) Biopolymers, 31, pp. 119-128
Biochemical And Biophysical Research Communications (ISSN: 0006-291x, 0006-291xprint), 2006 Dec 8; 351(1): 223-228.
Export to BibTeX Export to EndNote
Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 2.855, 5-year impact factor: 2.474
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-33750411236&partnerID=40&md5=d32ac16b62e4da224f03d319a2119446
Keywords: Apoa-I Amyloidosis, Conformational Analysis, Fibrillogenesis, Recombinant Amyloidogenic Proteins, Apolipoprotein A1, Amino Terminal Sequence, Article, Carboxy Terminal Sequence, Gene Identification, Genetic Transfection, Human, Molecular Dynamics, Priority Journal, Protein Interaction, Thermodynamics, Binding Sites, Dimerization, Hydrogen-Ion Concentration, Multiprotein Complexes, Protein Binding, Chemistry, Ultrastructure,
Affiliations:
*** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini, CNR, Napoli, 80134, Italy
Dipartimento di Biologia Strutturale e Funzionale, Università di Napoli Federico II, via Cinthia 4, Napoli, 80126, Italy
CEINGE Biotecnologie Avanzate, Napoli, 80131, Italy
Dipartimento di Chimica Organica e Biochimica, Università di Napoli Federico II, Napoli, 80126, Italy
Laboratorio di Biotecnologie IRCCS, Pavia, 27100, Italy
Dipartimento di Fisica, Università di Genova, Genova, 16146, Italy
Department of Chemistry, University of Cambridge, Cambridge, CB2 IEW, United Kingdom
References:
Chiti, F., Dobson, C.M., Protein misfolding, functional amyloid, and human disease (2006) Annu. Rev. Biochem., 75, pp. 333-36
Obici, L., Franceschini, G., Calabresi, L., Giorgetti, S., Stoppini, M., Merlini, G., Bellotti, V., Structure, function and amyloidogenic propensity of apolipoprotein A-I (2006) Amyloid, 13, pp. 1-15
Andreola, A., Bellotti, V., Giorgetti, S., Mangione, P., Obici, L., Stoppini, M., Torres, J., Sunde, M., Conformational switching and fibrillogenesis in the amyloidogenic fragment of apolipoprotein A-I (2003) J. Biol. Chem., 278, pp. 2444-2451
Shevchenko, A., Keller, P., Scheiffele, P., Mann, M., Simons, K., Identification of components of trans-Golgi network-derived transport vesicles and detergent-insoluble complexes by nanoelectrospray tandem mass spectrometry (1997) Electrophoresis, 18, pp. 2591-2600
Scaloni, A., Miraglia, N., Orru, S., Amodeo, P., Motta, A., Marino, G., Pucci, P., Topology of the calmodulin-melittin complex (1998) J. Mol. Biol., 277, pp. 945-958
Rogers, D.P., Brouillette, C.G., Engler, J.A., Tendian, S.W., Roberts, L., Mishra, V.K., Anantharamaiah, G.M., Ray, M.J., Truncation of the amino terminus of human apolipoprotein A-I substantially alters only the lipid-free conformation (1997) Biochemistry, 36, pp. 288-300
Relini, A., Rolandi, R., Bolognesi, M., Gliozzi, A., Aboudan, M., Merlini, G., Bellotti, V., Ultrastructural organization of ex-vivo amyloid fibrils formed by the apolipoprotein A-I Leu174Ser variant: an atomic force microscopy study (2004) Biochim. Biophys. Acta, 1690, pp. 33-41
Obici, L., Bellotti, V., Mangione, P., Stoppini, M., Arbustini, E., Verga, R., Zorzoli, I., Merlini, G., The new apolipoprotein A-I variant Leu174 → Ser causes chardiac amyloidosis, and the fibrils are constituted by the 93-residue N-terminal polypeptide (1999) Am. J. Pathol., 155, pp. 695-702
Semisotnov, G.V., Rodinova, N.A., Razgulyaev, O.I., Uversky, V.N., Gripas, A.F., Gilmanshin, R.I., Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe (1991) Biopolymers, 31, pp. 119-128
Mangione, P., Sunde, M., Giorgetti, S., Stoppini, M., Esposito, G., Gianelli, L., Obici, L., Bellotti, V., Amyloid fibrils derived from the apolipoprotein A-I Leu174Ser variant contain elements of ordered helical structure (2001) Protein Sci., 10, pp. 187-199
Buck, M., Trifluoroethanol and colleagues: cosolvents come of age. Recent studies with peptides and proteins (1998) Q. Rev. Biophys., 31, pp. 297-355
Rogers, D. P., Brouillette, C. G., Engler, J. A., Tendian, S. W., Roberts, L., Mishra, V. K., Anantharamaiah, G. M., Ray, M. J., Truncation of the amino terminus of human apolipoprotein A-I substantially alters only the lipid-free conformation (1997) Biochemistry, 36, pp. 288-300
Semisotnov, G. V., Rodinova, N. A., Razgulyaev, O. I., Uversky, V. N., Gripas, A. F., Gilmanshin, R. I., Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe (1991) Biopolymers, 31, pp. 119-128
Recombinant amyloidogenic domain of ApoA-I: analysis of its fibrillogenic potential
A variety of amyloid diseases are associated with fibrillar aggregates from N-terminal fragments of ApoA-I generated through a largely unexplored multi-step process. The understanding of the molecular mechanism is impaired by the lack of suitable amounts of the fibrillogenic polypeptides that could not be produced by recombinant methods so far. We report the production and the conformational analysis of recombinant ApoA-I 1-93 fragment. Similarly to the polypeptide isolated ex vivo, a pH switch from 7 to 4 induces a fast and reversible conformational transition to a helical state and leads to the identification of a key intermediate in the fibrillogenesis process. Limited proteolysis experiments suggested that the C-terminal region is involved in helix formation. The recombinant polypeptide generates fibrils at pH 4 on a time scale comparable with that of the native fragment. These findings open the way to studies on structural, thermodynamic, and kinetic aspects of ApoA-I fibrillogenesis. (c) 2006 Elsevier Inc. All rights reserved.
A variety of amyloid diseases are associated with fibrillar aggregates from N-terminal fragments of ApoA-I generated through a largely unexplored multi-step process. The understanding of the molecular mechanism is impaired by the lack of suitable amounts of the fibrillogenic polypeptides that could not be produced by recombinant methods so far. We report the production and the conformational analysis of recombinant ApoA-I 1-93 fragment. Similarly to the polypeptide isolated ex vivo, a pH switch from 7 to 4 induces a fast and reversible conformational transition to a helical state and leads to the identification of a key intermediate in the fibrillogenesis process. Limited proteolysis experiments suggested that the C-terminal region is involved in helix formation. The recombinant polypeptide generates fibrils at pH 4 on a time scale comparable with that of the native fragment. These findings open the way to studies on structural, thermodynamic, and kinetic aspects of ApoA-I fibrillogenesis. (c) 2006 Elsevier Inc. All rights reserved.
Recombinant amyloidogenic domain of ApoA-I: analysis of its fibrillogenic potential
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Recombinant amyloidogenic domain of ApoA-I: analysis of its fibrillogenic potential
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* Impact of a Single Point Mutation on the Antimicrobial and Fibrillogenic Properties of Cryptides from Human Apolipoprotein (14 views)
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View Export to BibTeX Export to EndNote
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* NMR spectroscopy in the conformational analysis of peptides: an overview (91 views)
Curr Med Chem (ISSN: 0929-8673linking, 1875-533xelectronic), 2021; 28(14): 2729-2782.
Impact Factor: 4.184
View Export to BibTeX Export to EndNote
Gaglione R, Smaldone G, Di Girolamo R, Piccoli R, Pedone E, Arciello A
* Cell milieu significantly affects the fate of AApoAI amyloidogenic variants: predestination or serendipity? (403 views)
Bba-Gen Subjects (ISSN: 0005-2728, 0006-3002print, 1570-9639print), 2017 Nov 23; 1862(3): 377-384.
Impact Factor: 4.28
View Export to BibTeX Export to EndNote
Mercurio FA, Marasco D, Di Natale C, Pirone L, Costantini S, Pedone EM, Leone M
* Targeting EphA2-Sam and Its Interactome: Design and Evaluation of Helical Peptides Enriched in Charged Residues (416 views)
Chembiochem (ISSN: 1439-4227, 1439-7633, 1439-4227linking), 2016 Nov 17; 17(22): 2179-2188.
Impact Factor: 2.847
View Export to BibTeX Export to EndNote
Mercurio FA, Di Natale C, Pirone L, Scognamiglio PL, Marasco D, Pedone EM, Saviano M, Leone M
* Peptide Fragments of Odin-Sam1: Conformational Analysis and Interaction Studies with EphA2-Sam (464 views)
Chembiochem (ISSN: 1439-4227, 1439-7633, 1439-4227linking), 2015; 16(11): 1629-1636.
Impact Factor: 2.85
View Export to BibTeX Export to EndNote
Carotenuto A, Cipolletta E, Gomez-Monterrey I, Sala M, Vernieri E, Limatola A, Bertamino A, Musella S, Sorriento D, Grieco P, Trimarco B, Novellino E, Iaccarino G, Campiglia P
* Design, synthesis and efficacy of novel G protein-coupled receptor kinase 2 inhibitors (526 views)
Eur J Med Chem (ISSN: 0223-5234, 1768-3254, 1768-3254electronic), 2013; 69: 384-392.
Impact Factor: 3.432
View Export to BibTeX Export to EndNote
Ziaco B, Diana D, Capasso D, Palumbo R, Celentano V, Di Stasi R, Fattorusso R, D'Andrea LD
* C-terminal truncation of Vascular Endothelial Growth Factor mimetic helical peptide preserves structural and receptor binding properties (367 views)
Biochem Biophys Res Commun (ISSN: 0006-291x), 2012 Jul 27; 424(2): 290-294.
Impact Factor: 2.406
View Export to BibTeX Export to EndNote
Bucci M, Cigliano L, Vellecco V, D'Andrea LD, Ziaco B, Rossi A, Sautebin L, Carlucci A, Abrescia P, Pedone C, Ianaro A, Cirino G
* Apolipoprotein A-I (ApoA-I) mimetic peptide P2a by restoring cholesterol esterification unmasks ApoA-I anti-inflammatory endogenous activity in vivo (386 views)
J Pharmacol Exp Ther (ISSN: 1521-0103, 0022-3565), 2012 Mar; 340(3): 716-722.
Impact Factor: 3.891
View Export to BibTeX Export to EndNote
Diana D, Basile A, De Rosa L, Di Stasi R, Auriemma S, Arra C, Pedone C, Turco MC, Fattorusso R, D'Andrea LD
* Beta-Hairpin Peptide That Targets Vascular Endothelial Growth Factor (vegf) Receptors: Design, Nmr Characterization, And Biological Activity (620 views)
Jbc Papers (ISSN: 1083-351x, 0021-9258, 0021-9258linking), 2011 Dec 2; 286(48): 41680-41691.
Impact Factor: 4.773
View Export to BibTeX Export to EndNote
Mazzaglia A, Micali N, Scolaro LM, Attanasio F, Magrí A, Pappalardo G, Villari V
* Aggregation properties of the peptide fragments derived from the 17-29 region of the human and rat IAPP: A comparative study with two PEG-conjugated variants of the human sequence (440 views)
J Phys Chem B (ISSN: 1520-6106, 1520-5207, 1520-5207electronic), 2010 Jan 21; 114(2): 705-713.
Impact Factor: 3.603
View Export to BibTeX Export to EndNote
De Bona P, Giuffrida ML, Caraci F, Copani A, Pignataro B, Attanasio F, Cataldo S, Pappalardo G, Rizzarelli E
* Design And Synthesis Of New Trehalose-Conjugated Pentapeptides As Inhibitors Of Abeta (1-42) Fibrillogenesis And Toxicity (688 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2009 Mar; 15(3): 220-228.
Impact Factor: 1.807
View Export to BibTeX Export to EndNote
Calvanese L, Saporito A, Oliva R, D'Auria G, Pedone C, Paolillo L, Ruvo M, Marasco D, Falcigno L
* Structural insights into the interaction between the Cripto CFC domain and the ALK4 receptor (456 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2009 Mar; 15(3): 175-183.
Impact Factor: 1.807
View Export to BibTeX Export to EndNote
Kaczmarek K, Farina B, Zubrzak P, Jankowski S, Zimecki M, Suder P, Benedetti E, Fattorusso R, Saviano M, Zabrocki J
* Synthesis, conformational analysis and immunological activity of β3Phe-substituted Cyclolinopeptide A analogues (460 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2009 Mar; 15(3): 166-174.
Impact Factor: 1.807
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Merlino A, Vergara A, Sica F, Mazzarella L
* The bis-histidyl complex in hemoproteins: A detailed conformational analysis of database protein structures and the case of Antarctic fish hemoglobins (331 views)
Marine Genomics (ISSN: 1874-7787), 2009 Mar; 2(1): 51-56.
Impact Factor: 1.2
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Cigliano L, D'Andrea LD, Maresca B, Serino M, Carlucci A, Salvatore A, Spagnuolo MS, Scigliuolo G, Pedone C, Abrescia P
* Relevance of the amino acid conversions L144R (Zaragoza) and L159P (Zavalla) in the apolipoprotein A-I binding site for haptoglobin (393 views)
Biol Chem Biological Chemistry (ISSN: 1431-6730, 1437-4315), 2008 Nov; 389(11): 1421-1426.
Impact Factor: 3.035
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Salvatore A, Cigliano L, Bucci EM, Corpillo D, Velasco S, Carlucci A, Pedone C, Abrescia P
* Haptoglobin binding to apolipoprotein A-I prevents damage from hydroxyl radicals on its stimulatory activity of the enzyme lecithin-cholesterol acyl-transferase (407 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2007 Oct 2; 46(39): 11158-11168.
Impact Factor: 3.368
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Vacatello M, D'Auria G, Falcigno L, Dettin M, Gambaretto R, Di Bello C, Paolillo L
* Conformational Analysis Of Novel Heparin Binding Peptides (618 views)
Biomaterials (ISSN: 0142-9612, 1878-5905electronic, 0142-9612linking), 2005 Jun; 26(16): 3207-3214.
Impact Factor: 4.698
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Saviano M, Isernia C, Bassarello C, Di Lello P, Galdiero S, Mierke DF, Benedetti E, Pedone C
* Conformational analysis by NMR and distance geometry techniques of a peptide mimetic of the third helix of the Antennapedia homeodomain (436 views)
J Pept Res (ISSN: 1397-002x), 2005 Feb; 65(2): 200-208.
Impact Factor: 1.741
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Spagnuolo MS, Cigliano L, D'Andrea LD, Pedone C, Abrescia P
* Assignment of the binding site for haptoglobin on apolipoprotein A-I (479 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2005 Jan 14; 280(2): 1193-1198.
Impact Factor: 5.854
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Giacco R, Clemente G, Luongo D, Lasorella G, Fiume I, Brouns F, Bornet F, Patti L, Cipriano P, Rivellese AA, Riccardi G
* Effects of short-chain fructo-oligosaccharides on glucose and lipid metabolism in mild hypercholesterolaemic individuals (486 views)
Clin Nutr (ISSN: 0261-5614, 0261-5614linking), 2004 Jun; 23(3): 331-340.
Impact Factor: 2.019
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Peggion C, Formaggio F, Crisma M, Toniolo C, Jimenez AI, Cativiela C, Kaptein B, Broxterman QB, Saviano M, Benedetti E
* Folding of peptides characterized by c3Val, a highly constrained analogue of valine (413 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2003; 68(2): 178-191.
Impact Factor: 2.733
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Langella E, Rega N, Improta R, Crescenzi O, Barone V
* Conformational analysis of the tyrosine dipeptide analogue in the gas phase and in aqueous solution by a density functional/continuum solvent model (292 views)
J Comput Chem (ISSN: 0192-8651, 1096-987xelectronic), 2002 Apr 30; 23(6): 650-661.
Impact Factor: 2.931
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Zanotti G, Maione A, Rossi F, Saviano M, Pedone C, Tancredi T
BIOACTIVE PEPTIDES - CONFORMATIONAL STUDY OF A CYSTINYL CYCLOHEPTAPEPTIDE IN ITS FREE AND CALCIUM COMPLEXED FORMS (581 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1993 Jul; 33(7): 1083-1091.
Impact Factor: 2.425
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23 Records (23 excluding Abstracts).
Total impact factor: 73.554 (73.554 excluding Abstracts).
Total 5 year impact factor: 78.291 (78.291 excluding Abstracts).
Total impact factor: 73.554 (73.554 excluding Abstracts).
Total 5 year impact factor: 78.291 (78.291 excluding Abstracts).
365 views. Last view on Monday 13 February 2023, 12:56:48
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