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Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain
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Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain

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A report from the European Proteomics Amyloid Network (EPAN)

Diana Canetti1, Graham W Taylor1, Francesca Lavatelli2

  • 1Centre for Amyloidosis, Division of Medicine, Royal Free Campus, University College London, London, UK.

Amyloid : the International Journal of Experimental and Clinical Investigation : the Official Journal of the International Society of Amyloidosis
|August 23, 2024
PubMed
Abstract

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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