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

M.J. Guerrero-Muñoz, D.L. Castillo-Carranza, R. Kayed

Research output: Contribution to journalReview articlepeer-review

81 Citations (Scopus)

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
Pages (from-to)468-478
Number of pages11
JournalBiochemical Pharmacology
Volume88
Issue number4
DOIs
Publication statusPublished - 15 Apr 2014
Externally publishedYes

Bibliographical note

Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Pharmacology

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