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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

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. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid Fibrils03:03

Amyloid Fibrils

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. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...

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Updated: Jun 22, 2026

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

Published on: April 28, 2022

Probing dynamics within amyloid fibrils using a novel capping method

Geoffrey W Platt1, Wei-Feng Xue, Steve W Homans

  • 1Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, LS2 9JT, UK.

Angewandte Chemie (International Ed. in English)
|June 27, 2009
PubMed
Summary

No abstract available in PubMed .

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