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Updated: Feb 10, 2026

Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo

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Published on: June 2, 2019

Alpha-Synuclein: From Early Synaptic Dysfunction to Neurodegeneration.

Veronica Ghiglieri^1,2, Valeria Calabrese², Paolo Calabresi^2,3

¹Dipartimento di Filosofia, Scienze Sociali, Umane e della Formazione, Università degli Studi di Perugia, Perugia, Italy.

Frontiers in Neurology

|May 22, 2018

Summary

Alpha-synuclein (α-syn) protein is linked to Parkinson's disease (PD) pathology. This review covers α-syn's functions, neurodegenerative roles, and early molecular changes in PD pathogenesis.

Keywords:

experimental parkinsonism neurodegeneration protein aggregation synaptic plasticity synucleinopathy

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Published on: October 26, 2010

Area of Science:

Neuroscience
Molecular Biology
Pathology

Background:

Alpha-synuclein (α-syn) is a natively unfolded protein implicated in Parkinson's disease (PD).
Extensive research over two decades links α-syn to PD pathology.
Understanding α-syn's multifaceted roles is crucial for PD research.

Purpose of the Study:

To synthesize seminal and recent findings on alpha-synuclein.
To discuss the physiological and neurodegenerative aspects of α-syn.
To explore the relationship between α-syn and Parkinson's disease pathogenesis.

Main Methods:

Literature review of experimental and clinical studies.
Synopsis of research on α-syn's functions and pathology.
Focus on early cellular and molecular alterations.

Main Results:

Alpha-synuclein aggregation is a key feature in Parkinson's disease.
α-syn exhibits diverse roles, from physiological functions to neurotoxicity.
Early molecular and cellular changes are associated with α-syn aggregates.

Conclusions:

Alpha-synuclein is central to Parkinson's disease pathology.
Further investigation into α-syn's functions and aggregation is warranted.
Understanding α-syn's role may reveal new therapeutic targets for PD.