Structure of β-Amyloid Fibrils and Its Relevance to Their Neurotoxicity : Implications for the Pathogenesis of Alzheimer's Disease

Author(s)

Abstract

Alzheimer's disease and cerebral amyloid angiopathy are characterized by the deposition of β-amyloid fibrils consisting of 40- and 42-mer peptides (Aβ40 and Aβ42). Since the aggregation (fibrilization) of these peptides is closely related to the pathogenesis of these diseases, numerous structural analyses of Aβ40 and Aβ42 fibrils have been carried out. Aβ42 plays a more important role in the pathogenesis of these diseases since its aggregative ability and neurotoxicity are considerably greater than those of Aβ40. This review summarizes mainly our own recent findings from the structural analysis of Aβ42 fibrils and discusses its relevance to their neurotoxicity in vitro.

Journal

  • Journal of bioscience and bioengineering

    Journal of bioscience and bioengineering 99(5), 437-447, 2005-05-25

    The Society for Biotechnology, Japan

References:  95

Cited by:  4

Codes

  • NII Article ID (NAID)
    110002695685
  • NII NACSIS-CAT ID (NCID)
    AA11307678
  • Text Lang
    ENG
  • Article Type
    Journal Article
  • ISSN
    13891723
  • NDL Article ID
    7318456
  • NDL Source Classification
    ZP15(科学技術--化学・化学工業--醗酵・微生物工学)
  • NDL Call No.
    Z53-S65
  • Data Source
    CJP  CJPref  NDL  NII-ELS 
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