Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

10.4K
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,...
10.4K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

The Cytosolic Zinc Finger Domain Structure of the CCHFV Glycoprotein n Is Maintained in Its Membrane-Bound Form.

Journal of the American Chemical Society·2026
Same author

ATP-driven membrane binding and polymerization of bacterial actin MreB promotes local membrane fluidization.

Biophysical journal·2026
Same author

An engineered closed-shell, two-component, 480-subunit nucleocapsid.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Adaptive PEG Bis-dendron Hydrogels with Tunable Mechanics and Bioactivity.

Chemistry of materials : a publication of the American Chemical Society·2026
Same author

Matrix plasticity and the molecular basis of extracellular filament assembly in <i>Bacillus cereus</i>.

Science advances·2026
Same author

Structural Basis of the Membrane Association by the Conserved RocS Membrane-Targeting Sequence in Streptococcus.

Advanced science (Weinheim, Baden-Wurttemberg, Germany)·2026

Related Experiment Video

Updated: May 7, 2026

Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions
08:40

Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions

Published on: June 23, 2022

2.6K

Structural and functional characterization of two alpha-synuclein strains.

Luc Bousset1, Laura Pieri, Gemma Ruiz-Arlandis

  • 1Laboratoire d'Enzymologie et Biochimie Structurales, CNRS, Avenue de la Terrasse, 91198 Gif-sur-Yvette, France.

Nature Communications
|October 11, 2013
PubMed
Summary

Two distinct strains of alpha-synuclein (α-synuclein) exhibit different structures and behaviors. These alpha-synuclein strains may explain varied disease progression in synucleinopathies like Parkinson's disease.

More Related Videos

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

19.1K
Recombinant &#945;- &#946;- and &#947;-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

8.1K

Related Experiment Videos

Last Updated: May 7, 2026

Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions
08:40

Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions

Published on: June 23, 2022

2.6K
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

19.1K
Recombinant &#945;- &#946;- and &#947;-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

8.1K

Area of Science:

  • Neuroscience
  • Biochemistry
  • Molecular Biology

Background:

  • Alpha-synuclein (α-synuclein) aggregation is a hallmark of neurodegenerative synucleinopathies, including Parkinson's disease.
  • Different clinical presentations in synucleinopathies suggest underlying molecular variations, analogous to prion strains.

Purpose of the Study:

  • To structurally and functionally characterize distinct polymorphs of α-synuclein.
  • To determine if these polymorphs meet the criteria for distinct α-synuclein strains.

Main Methods:

  • Structural analysis of α-synuclein polymorphs.
  • Functional assays assessing toxicity, seeding, and propagation in vitro and in vivo.

Main Results:

  • Two distinct α-synuclein polymorphs were identified.
  • These polymorphs demonstrated differences in structure, toxicity, and seeding/propagation capabilities.
  • Evidence supports classifying these polymorphs as distinct α-synuclein strains.

Conclusions:

  • The existence of α-synuclein strains provides a molecular basis for the diverse phenotypes observed in synucleinopathies.
  • Strain-specific properties may influence disease progression and cell-type tropism in conditions like Parkinson's disease.