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lüll Structure of beta-amyloid fibrils and its relevance to their neurotoxicity: implications for the pathogenesis of Alzheimer s disease Irie K; Murakami K; Masuda Y; Morimoto A; Ohigashi H; Ohashi R; Takegoshi K; Nagao M; Shimizu T; Shirasawa TJ Biosci Bioeng 2005[May]; 99 (5): 437-47Alzheimer's disease and cerebral amyloid angiopathy are characterized by the deposition of beta-amyloid fibrils consisting of 40- and 42-mer peptides (A beta 40 and A beta 42). Since the aggregation (fibrilization) of these peptides is closely related to the pathogenesis of these diseases, numerous structural analyses of A beta 40 and A beta 42 fibrils have been carried out. A beta 42 plays a more important role in the pathogenesis of these diseases since its aggregative ability and neurotoxicity are considerably greater than those of A beta 40. This review summarizes mainly our own recent findings from the structural analysis of A beta 42 fibrils and discusses its relevance to their neurotoxicity in vitro.|Alzheimer Disease/*metabolism[MESH]|Amino Acid Sequence[MESH]|Amyloid beta-Peptides/analysis/*chemistry/*metabolism[MESH]|Animals[MESH]|Humans[MESH]|Models, Biological[MESH]|Models, Chemical[MESH]|Models, Molecular[MESH]|Molecular Sequence Data[MESH]|Neurotoxins/chemistry/metabolism[MESH]|Protein Conformation[MESH]|Structure-Activity Relationship[MESH] |