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Alpha‐synuclein dysfunction in Lewy body diseases

Identifieur interne : 003A31 ( Main/Exploration ); précédent : 003A30; suivant : 003A32

Alpha‐synuclein dysfunction in Lewy body diseases

Auteurs : George K. Tofaris [Royaume-Uni] ; Maria Grazia Spillantini [Royaume-Uni]

Source :

Movement Disorders [ 0885-3185 ] ; 2005-08.

RBID : ISTEX:AC41B1C282777141A6B56DC13BCAC7DFF3BF7D24

Descripteurs français

Pascal (Inist)
- Corps Lewy maladie, Parkinson maladie, Protéine, Système nerveux pathologie, Trouble fonctionnel.

English descriptors

KwdEn :
- Animals, Chromosomes, Human, Pair 6 (genetics), Cytoskeleton (metabolism), Drosophila, Dysfunction, Humans, In Vitro Techniques, Lewy Body Disease (genetics), Lewy Body Disease (metabolism), Lewy Body Disease (physiopathology), Lewy body disease, Lewy body diseases, Mice, Nervous system diseases, Parkinson Disease (genetics), Parkinson Disease (physiopathology), Parkinson disease, Parkinson's disease, Phenotype, Phosphorylation, Point Mutation (genetics), Protein, alpha-Synuclein (genetics), alpha-Synuclein (metabolism), neurodegeneration, protein folding, synuclein.
MESH :
- chemical , genetics : alpha-Synuclein.
- genetics : Chromosomes, Human, Pair 6, Lewy Body Disease, Parkinson Disease, Point Mutation.
- metabolism : Cytoskeleton, Lewy Body Disease, alpha-Synuclein.
- physiopathology : Lewy Body Disease, Parkinson Disease.
- Animals, Drosophila, Humans, In Vitro Techniques, Mice, Phenotype, Phosphorylation.

Abstract

α‐Synuclein belongs to a small group of natively unfolded proteins that can transiently bind to lipid membranes and acquire a partial α‐helical conformation. Its relevance to Parkinson's disease (PD) is based on mutations found in familial cases of the disease and its presence in filaments of Lewy bodies (LB) and Lewy neurites (LN) in sporadic cases where it is packed in a β‐sheet configuration. This structural plasticity of α‐synuclein has raised the possibility that neurodegeneration may be a consequence of abnormal protein folding. The extent to which abnormal folding and aggregation of neuronal proteins is directly toxic to the cell, an inert biochemical marker of an underlying harmful metabolic defect, or a protective reaction remains to be seen. We review the function of α‐synuclein and recent studies that have shed light on the mechanisms by which it aggregates. © 2005 Movement Disorder Society

Url:

https://api.istex.fr/document/AC41B1C282777141A6B56DC13BCAC7DFF3BF7D24/fulltext/pdf

DOI: 10.1002/mds.20538

Affiliations:

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Movement Disorders (revue)

Alpha‐synuclein dysfunction in Lewy body diseases

Alpha‐synuclein dysfunction in Lewy body diseases

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

	Movement Disorders (revue)
	Attention, ce site est en cours de développement ! Attention, site généré par des moyens informatiques à partir de corpus bruts. Les informations ne sont donc pas validées.