Related Experiment Video
Updated: May 5, 2026

A Method to Study α-Synuclein Toxicity and Aggregation Using a Humanized Yeast Model
Published on: November 25, 2022
α-Synuclein as a ferrireductase
1*Department of Biology and Biochemistry, University of Bath, Claverton Down, Bath BA2 7AY, U.K.
Abstract:
Many proteins associated with neurodegenerative diseases have poorly defined or unknown functions. α-Synuclein is one such protein which is associated with a range of diseases including Parkinson's disease. Now accepted as a metal-binding protein, α-synuclein's function could possibly be defined in relation to the binding of cofactors. It has been suggested recently that α-synuclein is able to reduce iron using copper as its catalytic centre. The consequence of this is that possibly the function of α-synuclein can now be defined. The evidence for this and the consequences for Parkinson's disease are discussed in the present review.
More Related Videos
09:27Sequential Extraction of Soluble and Insoluble Alpha-Synuclein from Parkinsonian Brains
Published on: January 5, 2016
09:16Exogenous Administration of Microsomes-associated Alpha-synuclein Aggregates to Primary Neurons As a Powerful Cell Model of Fibrils Formation
Published on: June 26, 2018
Related Concept Videos
Amyloid Fibrils
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
Protein Modifications in the RER
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
ATP Synthase: Mechanism
Protein Folding Quality Check in the RER
Neural Regulation
The Early Endosome: Endocytosis of Transferrin