Protein degradation, aggregation, and misfolding
Identifieur interne : 001A81 ( Main/Exploration ); précédent : 001A80; suivant : 001A82Protein degradation, aggregation, and misfolding
Auteurs : Ana Maria Cuervo [États-Unis] ; Esther S. P. Wong [États-Unis] ; Marta Martinez-Vicente [États-Unis]Source :
- Movement Disorders [ 0885-3185 ] ; 2010.
Descripteurs français
- Pascal (Inist)
English descriptors
- KwdEn :
- Aggregate, Aggregation, Animals, Autophagy (physiology), Humans, Lysosome, Models, Molecular, Nervous system diseases, Neurons (metabolism), Neurons (pathology), Parkinson Disease (metabolism), Parkinson Disease (pathology), Peptidases, Proteasome Endopeptidase Complex (metabolism), Protein, Protein Conformation, Protein Folding, Proteins (metabolism), Ubiquitin (metabolism), alpha-Synuclein (metabolism), autophagy, lysosomes, neurodegeneration, proteases, protein aggregates.
- MESH :
- chemical , metabolism : Proteasome Endopeptidase Complex, Proteins, Ubiquitin, alpha-Synuclein.
- metabolism : Neurons, Parkinson Disease.
- pathology : Neurons, Parkinson Disease.
- physiology : Autophagy.
- Animals, Humans, Models, Molecular, Protein Conformation, Protein Folding.
Abstract
The cellular surveillance systems guarantee proper removal of altered components from inside cells. Alterations of these systems in neurons have been proposed to be involved in the pathogenesis of different neurodegenerative disorders. In this review, we comment on the advances in our current understanding of how changes in the intracellular proteolytic systems, the main components of the cellular quality control system, contribute to neurodegeneration, with special emphasis on Parkinson's disease. © 2010 Movement Disorder Society
Url:
DOI: 10.1002/mds.22718
Affiliations:
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Le document en format XML
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Disord.</title><idno type="ISSN">0885-3185</idno><idno type="eISSN">1531-8257</idno><imprint><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>Hoboken</pubPlace><date type="published" when="2010">2010</date><biblScope unit="vol">25</biblScope><biblScope unit="issue">S1</biblScope><biblScope unit="page" from="S49">S49</biblScope><biblScope unit="page" to="S54">S54</biblScope></imprint><idno type="ISSN">0885-3185</idno></series><idno type="istex">90F36C78A0579692FD1F510BCED7B24472F0D8C4</idno><idno type="DOI">10.1002/mds.22718</idno><idno type="ArticleID">MDS22718</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0885-3185</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Aggregate</term><term>Aggregation</term><term>Animals</term><term>Autophagy (physiology)</term><term>Humans</term><term>Lysosome</term><term>Models, Molecular</term><term>Nervous system diseases</term><term>Neurons (metabolism)</term><term>Neurons (pathology)</term><term>Parkinson Disease (metabolism)</term><term>Parkinson Disease (pathology)</term><term>Peptidases</term><term>Proteasome Endopeptidase Complex (metabolism)</term><term>Protein</term><term>Protein Conformation</term><term>Protein Folding</term><term>Proteins (metabolism)</term><term>Ubiquitin (metabolism)</term><term>alpha-Synuclein (metabolism)</term><term>autophagy</term><term>lysosomes</term><term>neurodegeneration</term><term>proteases</term><term>protein aggregates</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Proteasome Endopeptidase Complex</term><term>Proteins</term><term>Ubiquitin</term><term>alpha-Synuclein</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Neurons</term><term>Parkinson Disease</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Neurons</term><term>Parkinson Disease</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Autophagy</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Humans</term><term>Models, Molecular</term><term>Protein Conformation</term><term>Protein Folding</term></keywords><keywords scheme="Pascal" xml:lang="fr"><term>Agrégat</term><term>Agrégation</term><term>Lysosome</term><term>Pathologie du système nerveux</term><term>Peptidases</term><term>Protéine</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The cellular surveillance systems guarantee proper removal of altered components from inside cells. Alterations of these systems in neurons have been proposed to be involved in the pathogenesis of different neurodegenerative disorders. In this review, we comment on the advances in our current understanding of how changes in the intracellular proteolytic systems, the main components of the cellular quality control system, contribute to neurodegeneration, with special emphasis on Parkinson's disease. © 2010 Movement Disorder Society</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>État de New York</li></region></list><tree><country name="États-Unis"><region name="État de New York"><name sortKey="Cuervo, Ana Maria" sort="Cuervo, Ana Maria" uniqKey="Cuervo A" first="Ana Maria" last="Cuervo">Ana Maria Cuervo</name></region><name sortKey="Martinez Icente, Marta" sort="Martinez Icente, Marta" uniqKey="Martinez Icente M" first="Marta" last="Martinez-Vicente">Marta Martinez-Vicente</name><name sortKey="Wong, Esther S P" sort="Wong, Esther S P" uniqKey="Wong E" first="Esther S. P." last="Wong">Esther S. P. Wong</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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