Therapeutic approaches against common structural features of toxic oligomers shared by multiple amyloidogenic proteins

Marcos J. Guerrero-Muñoz, Diana L. Castillo-Carranza, Rakez Kayed

Research output: Contribution to journalReview article

71 Scopus citations

Abstract

Impaired proteostasis is one of the main features of all amyloid diseases, which are associated with the formation of insoluble aggregates from amyloidogenic proteins. The aggregation process can be caused by overproduction or poor clearance of these proteins. However, numerous reports suggest that amyloid oligomers are the most toxic species, rather than insoluble fibrillar material, in Alzheimer's, Parkinson's, and Prion diseases, among others. Although the exact protein that aggregates varies between amyloid disorders, they all share common structural features that can be used as therapeutic targets. In this review, we focus on therapeutic approaches against shared features of toxic oligomeric structures and future directions.

Original languageEnglish (US)
Pages (from-to)468-478
Number of pages11
JournalBiochemical Pharmacology
Volume88
Issue number4
DOIs
StatePublished - Apr 15 2014

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Keywords

  • Amyloid oligomers
  • Anti-amyloid small molecules
  • Immunotherapy

ASJC Scopus subject areas

  • Biochemistry
  • Pharmacology

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