Journal of Molecular Medicine

, Volume 91, Issue 6, pp 653–664 | Cite as

The role of amyloidogenic protein oligomerization in neurodegenerative disease



A common pathological hallmark in many neurodegenerative diseases, including Alzheimer’s disease, Parkinson’s disease, and Huntington’s disease, is the formation of fibrillar protein aggregates referred to as amyloids. The amyloidogenic aggregates were long thought to be toxic, but mounting evidence supports the notion that a variety of amyloid aggregate intermediates to fibril formation, termed oligomers, may in fact be the primary culprit leading to neuronal dysfunction and cell death. While amyloid formation is a complex, heterogeneous process, aggregates formed by diverse, diseases-related proteins share many conformational similarities, suggesting common toxic mechanisms among these diseases. Ideally, similar therapeutic strategies may be applicable. This review focuses on the potential role of amyloidogenic oligomers in neurodegenerative disease, highlighting some promising therapeutic strategies.


Amyloidogenic oligomers Neurodegenerative disease Alzheimer’s disease Parkinson’s disease Huntington’s disease Therapeutic strategies 



JL is supported by the National Science Foundation (Grant 1054211), and the Alzheimer’s Association (NIRG-11-203834).


The authors declare that they have no conflict of interests.


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Copyright information

© Springer-Verlag Berlin Heidelberg 2013

Authors and Affiliations

  1. 1.Novartis Institutes for Biomedical Research Novartis Pharma AGBaselSwitzerland
  2. 2.The C. Eugene Bennett Department of Chemistry, Center for Neuroscience, Robert C. Byrd Health Sciences CenterWest Virginia UniversityMorgantownUSA

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