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Updated: Mar 11, 2026

Detection of Disease-associated α-synuclein by Enhanced ELISA in the Brain of Transgenic Mice Overexpressing Human A53T Mutated α-synuclein
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Exploiting the aggregation properties of alpha-synuclein for diagnostic purposes

David P Breen1, Lorraine V Kalia1

  • 1Morton and Gloria Shulman Movement Disorders Clinic and Edmond J. Safra Program in Parkinson's Disease, Toronto Western Hospital, Toronto, Canada.

Movement Disorders : Official Journal of the Movement Disorder Society
|November 30, 2016
PubMed
Summary

No abstract available in PubMed .

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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
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