Alpha-synuclein Dysfunction in lewy body diseases
Identifieur interne :
001D69 ( PascalFrancis/Corpus );
précédent :
001D68;
suivant :
001D70
Alpha-synuclein Dysfunction in lewy body diseases
Auteurs : George K. Tofaris ;
Maria Grazia SpillantiniSource :
-
Movement disorders [ 0885-3185 ] ; 2005.
RBID : Pascal:05-0457566
Descripteurs français
English descriptors
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.
Notice en format standard (ISO 2709)
Pour connaître la documentation sur le format Inist Standard.
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| A01 | 01 | 1 | | @0 0885-3185 |
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| A03 | | 1 | | @0 Mov. disord. |
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| A05 | | | | @2 20 |
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| A06 | | | | @3 SUP12 |
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| A08 | 01 | 1 | ENG | @1 Alpha-synuclein Dysfunction in lewy body diseases |
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| A09 | 01 | 1 | ENG | @1 Atypical Parkinsonian Disorders |
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| A11 | 01 | 1 | | @1 TOFARIS (George K.) |
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| A11 | 02 | 1 | | @1 SPILLANTINI (Maria Grazia) |
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| A12 | 01 | 1 | | @1 POEWE (Werner) @9 ed. |
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| A12 | 02 | 1 | | @1 WENNING (Gregor K.) @9 ed. |
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| A14 | 01 | | | @1 Cambridge Centre for Brain Repair, University of Cambridge @2 Cambridge @3 GBR |
|---|
| A14 | 02 | | | @1 Department of Clinical Neurosciences, University of Cambridge @2 Cambridge @3 GBR |
|---|
| A15 | 01 | | | @1 Department of Neurology, Medical University Innsbruck @2 Innsbruck @3 AUT @Z 1 aut. @Z 2 aut. |
|---|
| A20 | | | | @2 S37-S44 |
|---|
| A21 | | | | @1 2005 |
|---|
| A23 | 01 | | | @0 ENG |
|---|
| A43 | 01 | | | @1 INIST @2 20953 @5 354000132714250060 |
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| A44 | | | | @0 0000 @1 © 2005 INIST-CNRS. All rights reserved. |
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| A45 | | | | @0 75 ref. |
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| A47 | 01 | 1 | | @0 05-0457566 |
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| A60 | | | | @1 P @2 C |
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| A61 | | | | @0 A |
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| A64 | 01 | 1 | | @0 Movement disorders |
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| A66 | 01 | | | @0 USA |
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| C01 | 01 | | ENG | @0 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. |
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| C03 | 01 | X | ENG | @0 Nervous system diseases @5 01 |
|---|
| C03 | 01 | X | SPA | @0 Sistema nervioso patología @5 01 |
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| C03 | 02 | X | FRE | @0 Parkinson maladie @5 02 |
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| C03 | 02 | X | ENG | @0 Parkinson disease @5 02 |
|---|
| C03 | 02 | X | SPA | @0 Parkinson enfermedad @5 02 |
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| C03 | 03 | X | FRE | @0 Trouble fonctionnel @5 09 |
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| C03 | 03 | X | ENG | @0 Dysfunction @5 09 |
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| C03 | 03 | X | SPA | @0 Trastorno funcional @5 09 |
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| C03 | 04 | X | FRE | @0 Protéine @5 10 |
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| C03 | 04 | X | ENG | @0 Protein @5 10 |
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| C03 | 04 | X | SPA | @0 Proteína @5 10 |
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| C03 | 05 | X | FRE | @0 Corps Lewy maladie @4 CD @5 96 |
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| C03 | 05 | X | ENG | @0 Lewy body disease @4 CD @5 96 |
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| C03 | 05 | X | SPA | @0 Cuerpo Lewy enfermedad @4 CD @5 96 |
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| C07 | 02 | X | FRE | @0 Extrapyramidal syndrome @5 38 |
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| C07 | 02 | X | ENG | @0 Extrapyramidal syndrome @5 38 |
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| C07 | 02 | X | SPA | @0 Extrapiramidal síndrome @5 38 |
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| C07 | 03 | X | FRE | @0 Maladie dégénérative @5 39 |
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| C07 | 03 | X | ENG | @0 Degenerative disease @5 39 |
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| C07 | 03 | X | SPA | @0 Enfermedad degenerativa @5 39 |
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| C07 | 04 | X | FRE | @0 Système nerveux central pathologie @5 40 |
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| C07 | 04 | X | ENG | @0 Central nervous system disease @5 40 |
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| C07 | 04 | X | SPA | @0 Sistema nervosio central patología @5 40 |
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| N44 | 01 | | | @1 OTO |
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| pR |
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Format Inist (serveur)
| NO : | PASCAL 05-0457566 INIST |
|---|
| ET : | Alpha-synuclein Dysfunction in lewy body diseases |
|---|
| AU : | TOFARIS (George K.); SPILLANTINI (Maria Grazia); POEWE (Werner); WENNING (Gregor K.) |
|---|
| AF : | Cambridge Centre for Brain Repair, University of Cambridge/Cambridge/Royaume-Uni; Department of Clinical Neurosciences, University of Cambridge/Cambridge/Royaume-Uni; Department of Neurology, Medical University Innsbruck/Innsbruck/Autriche (1 aut., 2 aut.) |
|---|
| DT : | Publication en série; Congrès; Niveau analytique |
|---|
| SO : | Movement disorders; ISSN 0885-3185; Etats-Unis; Da. 2005; Vol. 20; No. SUP12; S37-S44; Bibl. 75 ref. |
|---|
| LA : | Anglais |
|---|
| EA : | 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. |
|---|
| CC : | 002B17; 002B17G; 002B17A03 |
|---|
| FD : | Système nerveux pathologie; Parkinson maladie; Trouble fonctionnel; Protéine; Corps Lewy maladie |
|---|
| FG : | Encéphale pathologie; Extrapyramidal syndrome; Maladie dégénérative; Système nerveux central pathologie |
|---|
| ED : | Nervous system diseases; Parkinson disease; Dysfunction; Protein; Lewy body disease |
|---|
| EG : | Cerebral disorder; Extrapyramidal syndrome; Degenerative disease; Central nervous system disease |
|---|
| SD : | Sistema nervioso patología; Parkinson enfermedad; Trastorno funcional; Proteína; Cuerpo Lewy enfermedad |
|---|
| LO : | INIST-20953.354000132714250060 |
|---|
| ID : | 05-0457566 |
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Links to Exploration step
Pascal:05-0457566
Le document en format XML
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