Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Amyloid Fibrils

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,...

Amyloid Fibrils

Amyloid Fibrils

You might also read

Related Articles

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

Sort by

Same author

DNM1-related disorder is characterized by recurrent variants and phenotypic homogeneity.

medRxiv : the preprint server for health sciences·2026

Same author

Copy Number Variant Duplications Associated with Essential Tremor.

Tremor and other hyperkinetic movements (New York, N.Y.)·2026

Same author

Loss-of-function variants in the CAPN1 activator CD99L2 cause X-linked spastic ataxia.

Nature communications·2026

Same author

Diagnostic significance of rhythmicity in postural hand tremor.

Scientific reports·2026

Same author

Immunohistochemistry-guided analyses of steroidogenesis in primary bilateral macronodular adrenal hyperplasia.

The Journal of endocrinology·2025

Same author

Vascular and Neural Transcriptomics Reveal Stage-Dependent Pathways to Inflammation and Cognitive Dysfunction in a Rat Model of Hypertension.

Journal of the American Heart Association·2025

Search research articles

Related Experiment Video

Updated: May 2, 2026

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

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

Published on: January 5, 2016

Differential aggregation properties of alpha-synuclein isoforms.

May Bungeroth¹, Silke Appenzeller¹, Annika Regulin¹

¹Department of Neurology, University of Kiel, Kiel, Germany.

Neurobiology of Aging

|March 18, 2014

Summary

Parkinson's disease involves alpha-synuclein aggregation. Alternative alpha-synuclein isoforms (SNCA126, SNCA112, SNCA98) aggregate less than the canonical SNCA140, with distinct structures and lower brain expression.

Keywords:

Aggregation Alpha-synuclein Isoforms Parkinson

More Related Videos

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

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

Published on: June 23, 2022

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

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

Published on: June 26, 2018

Related Experiment Videos

Last Updated: May 2, 2026

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

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

Published on: January 5, 2016

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

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

Published on: June 23, 2022

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

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

Published on: June 26, 2018

Area of Science:

Neuroscience
Molecular Biology
Biochemistry

Background:

Pathologic alpha-synuclein aggregation drives Parkinson's disease.
The SNCA gene produces four alpha-synuclein isoforms via alternative splicing.
Little is known about the aggregation properties of alternative isoforms compared to SNCA140.

Purpose of the Study:

To investigate and compare the aggregation properties of all four alpha-synuclein isoforms.
To analyze the in vitro fibril formation of three SNCA isoforms.
To examine the expression levels of SNCA isoforms in human brain regions.

Main Methods:

Cellular assays to study aggregation properties of all four isoforms.
In vitro fibril formation analysis of SNCA140, SNCA126, and SNCA98 using electron microscopy.
Quantitative expression analysis of SNCA isoforms in different human brain regions.

Main Results:

All three alternative isoforms (SNCA140, SNCA126, SNCA98) showed significantly reduced aggregation compared to the canonical SNCA140 isoform.
Electron microscopy revealed distinct fibril structures: SNCA140 formed straight fibrils, SNCA126 formed shorter fibrils in bundles, and SNCA98 formed annular structures.
Alternative SNCA isoforms were expressed at low levels in human brain regions compared to SNCA140.

Conclusions:

Alpha-synuclein isoforms exhibit qualitative and quantitative differences in their aggregation behavior.
These isoform-specific properties may influence Parkinson's disease pathogenesis.
Further in vitro and in vivo studies are needed to elucidate the biological consequences of these findings.