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 Dipartimento di Biochimica, Università di Pavia, Pavia, 27100, 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 Riferimenti: 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.
Recombinant amyloidogenic domain of ApoA-I: analysis of its fibrillogenic potential
Petraglia F, Singh AA, Carafa V, Nebbioso A, Conte M, Scisciola L, Valente S, Baldi A, Mandoli A, Petrizzi VB, Ingenito C, De Falco S, Cicatiello V, Apicella I, Janssen-megens EM, Kim B, Yi G, Logie C, Heath S, Ruvo M, Wierenga ATJ, Flicek P, Yaspo ML, Della Valle V, Bernard O, Tomassi S, Novellino E, Feoli A, Sbardella G, Gut I, Vellenga E, Stunnenberg HG, Mai A, Martens JHA, Altucci L * Combined HAT/EZH2 modulation leads to cancer-selective cell death(206 visite) Oncotarget (ISSN: 1949-2553electronic, 1949-2553linking), 2018 May 22; 9(39): 25630-25646. Impact Factor:5.008 DettagliEsporta in BibTeXEsporta in EndNote
Santulli G, Cipolletta E, Sorriento D, Del Giudice C, Anastasio A, Monaco S, Maione AS, Condorelli G, Puca A, Trimarco B, Illario M, Iaccarino G * CaMK4 gene deletion induces hypertension(284 visite) J Am Heart Assoc Journal Of The American Heart Association (ISSN: 2047-9980), 2012; 1(4): N/D-N/D. Impact Factor:2.882 DettagliEsporta in BibTeXEsporta in EndNote
Antonini A, Vitale C, Barone P, Cilia R, Righini A, Bonuccelli U, Abbruzzese G, Ramat S, Petrone A, Quatrale R, Marconi R, Ceravolo R, Stefani A, Lopiano L, Zappia M, Capus L, Morgante L, Tamma F, Tinazzi M, Colosimo C, Guerra UP, Valzania F, Fagioli G, Distefano A, Bagnato A, Feggi L, Anna S, Maria Teresa Rosaria De Cr, Nobili F, Mazzuca N, Baldari S, Eleopra R, Bestetti A, Benti R, Varrone A, Volterrani D, Massa R, Stocchi F, Schillaci O, Dore F, Zibetti M, Castellano G, Battista SG, Giorgetti G * The relationship between cerebral vascular disease and parkinsonism: The VADO study(422 visite) Parkinsonism Relat D (ISSN: 1353-8020, 1873-5126, 1873-5126electronic), 2012; 18(6): 775-780. Impact Factor:3.274 DettagliEsporta in BibTeXEsporta in EndNote
Malvindi MA, Greco A, Conversano F, Figuerola A, Corti M, Bonora M, Lascialfari A, Doumari HA, Moscardini M, Cingolani R, Gigli G, Casciaro S, Pellegrino T, Ragusa A * MR Contrast Agents(230 visite) Small Animal Imaging, 2011 Jul 8; 21(13): 2548-2555. Impact Factor:1.784 DettagliEsporta in BibTeXEsporta in EndNote
Bruni AC, Bernardi L, Colao R, Rubino E, Smirne N, Frangipane F, Terni B, Curcio SA, Mirabelli M, Clodomiro A, Di Lorenzo R, Maletta R, Anfossi M, Gallo M, Geracitano S, Tomaino C, Muraca MG, Leotta A, Lio SG, Pinessi L, Rainero I, Sorbi S, Nee L, Milan G, Pappata S, Postiglione A, Abbamondi N, Forloni G, St George Hyslop P, Rogaeva E, Bugiani O, Giaccone G, Foncin JF, Spillantini MG, Puccio G * Worldwide distribution of PSEN1 Met146Leu mutation: A large variability for a founder mutation(409 visite) Neurology (ISSN: 0028-3878, 1526-632x, 1526-632xelectronic), 2010 Mar 9; 74(10): 798-806. Impact Factor:8.017 DettagliEsporta in BibTeXEsporta in EndNote