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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. 
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Amyloid Fibrils03:03

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Parkinson Disease ll: Pathophysiology01:24

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Related Experiment Video

Updated: May 7, 2026

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

The function of α-synuclein.

Jacob T Bendor1, Todd P Logan, Robert H Edwards

  • 1Departments of Neurology and Physiology, Graduate Programs in Biomedical Sciences, Cell Biology and Neuroscience, UCSF School of Medicine, San Francisco, CA 94158-2517, USA.

Neuron
|September 21, 2013
PubMed
Summary
This summary is machine-generated.

Alpha-synuclein protein aggregation causes Parkinson's disease (PD) and other neurodegenerative disorders. Its normal function at nerve terminals and role in disease spread are reviewed.

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Studying Pre-formed Fibril Induced α-Synuclein Accumulation in Primary Embryonic Mouse Midbrain Dopamine Neurons
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Studying Pre-formed Fibril Induced α-Synuclein Accumulation in Primary Embryonic Mouse Midbrain Dopamine Neurons

Published on: August 16, 2020

Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays
09:36

Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays

Published on: August 13, 2017

Related Experiment Videos

Last Updated: May 7, 2026

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

Studying Pre-formed Fibril Induced α-Synuclein Accumulation in Primary Embryonic Mouse Midbrain Dopamine Neurons
10:03

Studying Pre-formed Fibril Induced α-Synuclein Accumulation in Primary Embryonic Mouse Midbrain Dopamine Neurons

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Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays
09:36

Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays

Published on: August 13, 2017

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Genetics

Background:

  • Alpha-synuclein's causal role in familial Parkinson's disease (PD) is established.
  • Synuclein aggregation is a hallmark of sporadic PD and other neurodegenerative diseases.
  • The normal function of alpha-synuclein remains largely unknown.

Purpose of the Study:

  • To review the role of alpha-synuclein in nerve terminal function.
  • To explore alpha-synuclein's involvement in membrane remodeling.
  • To discuss the prion-like propagation of misfolded alpha-synuclein in neurodegeneration.

Main Methods:

  • Literature review of existing research on alpha-synuclein.
  • Analysis of genetic data linking alpha-synuclein to PD.
  • Examination of studies on protein aggregation and neurodegeneration.

Main Results:

  • Alpha-synuclein aggregation is central to PD pathogenesis.
  • Misfolded alpha-synuclein accumulation defines multiple neurodegenerative conditions.
  • The protein's normal function is poorly understood despite its pathological significance.

Conclusions:

  • Alpha-synuclein plays a critical role in nerve terminal function and membrane remodeling.
  • Prion-like spread of misfolded alpha-synuclein contributes to neurodegeneration progression.
  • Further research into alpha-synuclein's normal function is crucial for understanding and treating PD.