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Correlative cryo-soft X-ray tomography and cryo-structured illumination microscopy reveal changes to lysosomes in

Karen E Marshall1, Kurtis Mengham1, Matthew C Spink2

  • 1Sussex Neuroscience, School of Life Sciences, University of Sussex, Falmer, BN1 9QG Brighton, UK.

Structure (London, England : 1993)
|March 12, 2024
PubMed

Keywords:
Alzheimer'sdiseaseamyloidcorrelative imagingcryo-soft X-ray tomographylysosomesneuronsoligomersultrastructure

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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. 
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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...