Related Experiment Video
Updated: Jul 1, 2026

09:16
Exogenous Administration of Microsomes-associated Alpha-synuclein Aggregates to Primary Neurons As a Powerful Cell Model of Fibrils Formation
Published on: June 26, 2018
Correction to: Induction of CNS α-synuclein pathology by fibrillar and non-amyloidogenic recombinant α-synuclein
Amanda N Sacino1, Mieu Brooks1, Nicholas H McGarvey1
1Center for Translational Research in Neurodegenerative Disease, Department of Neuroscience, BMS Building J-483, University of Florida College of Medicine, 1275 Center Drive, PO Box 100159, Gainesville, FL, 32610, USA.
Acta Neuropathologica Communications
|June 30, 2026
Abstract
No abstract available in PubMed .
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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 deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
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 deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...

