作者: Fiorella Malchiodi-Albedi , Silvia Paradisi , Andrea Matteucci , Claudio Frank , Marco Diociaiuti
DOI: 10.4061/2011/906964
关键词:
摘要: Amyloid proteins constitute a chemically heterogeneous group of proteins, which share some biophysical and biological characteristics, the principal are high propensity to acquire an incorrect folding tendency aggregate. A number diseases associated with misfolding aggregation although only in them—most notably Alzheimer's disease (AD) transmissible spongiform encephalopathies (TSEs)—a pathogenetic link misfolded is now widely recognized. Lipid rafts (LRs) have been involved pathophysiology protein at several levels, including amyloidogenic processing, neurotoxicity. Among pathogenic AD-related amyloid β (Aβ) by far most studied protein, large body evidence has gathered on role played LRs Aβ pathogenicity. However, significant amount data also collected for other so that their ability interact can be considered additional, shared feature characterizing family. In this paper, we will review neurotoxicity huntingtin, α-synuclein, prion calcitonin.