Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide

Nat Rev Mol Cell Biol. 2007 Feb;8(2):101-12. doi: 10.1038/nrm2101.


The distinct protein aggregates that are found in Alzheimer's, Parkinson's, Huntington's and prion diseases seem to cause these disorders. Small intermediates - soluble oligomers - in the aggregation process can confer synaptic dysfunction, whereas large, insoluble deposits might function as reservoirs of the bioactive oligomers. These emerging concepts are exemplified by Alzheimer's disease, in which amyloid beta-protein oligomers adversely affect synaptic structure and plasticity. Findings in other neurodegenerative diseases indicate that a broadly similar process of neuronal dysfunction is induced by diffusible oligomers of misfolded proteins.

Publication types

  • Review

MeSH terms

  • Alzheimer Disease / etiology
  • Alzheimer Disease / metabolism*
  • Alzheimer Disease / pathology
  • Alzheimer Disease / therapy
  • Amyloid beta-Peptides / metabolism*
  • Cell Membrane / metabolism
  • Humans
  • Memory Disorders / etiology
  • Models, Biological
  • Nerve Degeneration / etiology
  • Nerve Degeneration / metabolism*
  • Nerve Degeneration / therapy
  • Protein Folding
  • Signal Transduction
  • Solubility
  • Synapses / pathology


  • Amyloid beta-Peptides