Amyloid growth and membrane damage: Current themes and emerging perspectives from theory and experiments on Abeta and hIAPP(31 visite)(PDF pubblico15 visite) Sciacca MFM, Tempra C, Scollo F, Milardi D, La Rosa C
Impact factor: 4.647, Impact factor a 5 anni: 4.494
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Parole chiave: Abeta, Alzheimer, Amylin, Amyloid, Model Membrane, Type Ii Diabetes Mellitus,
Affiliazioni:
*** IBB - CNR *** Istituto CNR di Biostrutture e Bioimmagini- Sede Secondaria di Catania, Via Paolo Gaifami 18, 95126 Catania, Italy., Universita degli Studi di Catania, Dipartimento di Scienze Chimiche, Viale Andrea Doria 6, 95125 Catania, Italy., Universita degli Studi di Catania, Dipartimento di Scienze Chimiche, Viale Andrea Doria 6, 95125 Catania, Italy. Electronic address: clarosa@unict.it.,
Riferimenti:
Non disponibile.
Alzheimer's Disease (AD) and Type 2 diabetes mellitus (T2DM) are two incurable diseases both hallmarked by an abnormal deposition of the amyloidogenic peptides Abeta and Islet Amyloid Polypeptide (IAPP) in affected tissues. Epidemiological data demonstrate that patients suffering from diabetes are at high risk of developing AD, thus making the search for factors common to the two pathologies of special interest for the design of new therapies. Accumulating evidence suggests that the toxic properties of both Abeta or IAPP are ascribable to their ability to damage the cell membrane. However, the molecular details describing Abeta or IAPP interaction with membranes are poorly understood. This review focuses on biophysical and in silico studies addressing these topics. Effects of calcium, cholesterol and membrane lipid composition in driving aberrant Abeta or IAPP interaction with the membrane will be specifically considered. The cross correlation of all these factors appears to be a key issue not only to shed light in the countless and often controversial reports relative to this area but also to gain valuable insights into the central events leading to membrane damage caused by amyloidogenic peptides. This article is part of a Special Issue entitled: Protein Aggregation and Misfolding at the Cell Membrane Interface edited by Ayyalusamy Ramamoorthy.
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(132 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
104 Records (92 escludendo Abstract e Conferenze). Impact factor totale: 429.515 (392.989 escludendo Abstract e Conferenze). Impact factor a 5 anni totale: 455.526 (413.178 escludendo Abstract e Conferenze).
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