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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. 
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Parkinson Disease ll: Pathophysiology01:24

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Related Experiment Video

Updated: Jul 10, 2026

Exogenous Administration of Microsomes-associated Alpha-synuclein Aggregates to Primary Neurons As a Powerful Cell Model of Fibrils Formation
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Exogenous Administration of Microsomes-associated Alpha-synuclein Aggregates to Primary Neurons As a Powerful Cell Model of Fibrils Formation

Published on: June 26, 2018

Protein aggregation mechanisms in synucleinopathies: commonalities and differences.

Katrin Beyer1, Aurelio Ariza

  • 1Department of Pathology, Hospital Universitari Germans Trias i Pujol, Autonomous University of Barcelona, Badalona, Barcelona, Spain.

Journal of Neuropathology and Experimental Neurology
|November 7, 2007
PubMed
Summary

Synucleinopathies involve alpha-synuclein (AS) aggregation in the brain. Recent research clarifies AS function and aggregation, detailing commonalities and differences in synucleinopathy pathogenesis.

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Sequential Extraction of Soluble and Insoluble Alpha-Synuclein from Parkinsonian Brains
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Exogenous Administration of Microsomes-associated Alpha-synuclein Aggregates to Primary Neurons As a Powerful Cell Model of Fibrils Formation

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Sequential Extraction of Soluble and Insoluble Alpha-Synuclein from Parkinsonian Brains
09:27

Sequential Extraction of Soluble and Insoluble Alpha-Synuclein from Parkinsonian Brains

Published on: January 5, 2016

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Pathology

Background:

  • Synucleinopathies are defined by alpha-synuclein (AS)-positive brain inclusions.
  • Lewy bodies characterize Parkinson disease and dementia with Lewy bodies.
  • Glial and neuronal cytoplasmic inclusions are seen in multiple system atrophy.

Purpose of the Study:

  • To review current knowledge on alpha-synuclein aggregation mechanisms in synucleinopathies.
  • To highlight commonalities and differences in AS aggregation pathways across diseases.
  • To integrate recent findings on AS function and pathogenesis.

Main Methods:

  • Literature review of recent investigations on AS function and aggregation.
  • Analysis of molecular events, including posttranslational modifications and isoform expression.
  • Comparative analysis of protein aggregation mechanisms in different synucleinopathies.

Main Results:

  • Alpha-synuclein aggregation is a key pathogenic event in synucleinopathies.
  • Recent studies have significantly advanced understanding of AS aggregation steps.
  • Differential molecular events contribute to distinct synucleinopathy presentations.

Conclusions:

  • Understanding AS aggregation is crucial for synucleinopathy research.
  • Specific molecular differences underlie the varied pathologies of synucleinopathies.
  • This review consolidates current knowledge on AS aggregation in these neurodegenerative diseases.