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Volumn 19, Issue 10, 2005, Pages 1377-1379
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Dopamine promotes α-synuclein aggregation into SDS-resistant soluble oligomers via a distinct folding pathway
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Author keywords
[No Author keywords available]
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Indexed keywords
ALPHA SYNUCLEIN;
AMYLOID;
DODECYL SULFATE SODIUM;
DOPAMINE;
IRON;
OLIGOMER;
THIOFLAVINE;
ALPHA HELIX;
ARTICLE;
BETA SHEET;
CIRCULAR DICHROISM;
CONCENTRATION RESPONSE;
CONTROLLED STUDY;
DOPAMINERGIC NERVE CELL;
ELECTRON MICROSCOPY;
FLUORESCENCE;
HUMAN;
HUMAN CELL;
LEWY BODY;
NERVE DEGENERATION;
OLIGOMERIZATION;
PARKINSON DISEASE;
POLYACRYLAMIDE GEL ELECTROPHORESIS;
PRIORITY JOURNAL;
PROTEIN AGGREGATION;
PROTEIN FOLDING;
PROTEIN SECONDARY STRUCTURE;
SIGNAL TRANSDUCTION;
STOICHIOMETRY;
WILD TYPE;
ALPHA-SYNUCLEIN;
AMYLOID;
CIRCULAR DICHROISM;
DOPAMINE;
FERRIC COMPOUNDS;
HUMANS;
PARKINSON DISEASE;
PROTEIN FOLDING;
PROTEIN STRUCTURE, SECONDARY;
SODIUM DODECYL SULFATE;
THIAZOLES;
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EID: 23444455247
PISSN: 08926638
EISSN: None
Source Type: Journal
DOI: 10.1096/fj.04-3437fje Document Type: Article |
Times cited : (241)
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References (0)
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