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Volumn 53, Issue 41, 2014, Pages 6419-6421
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The newly discovered Parkinsons disease associated finnish mutation (A53E) attenuates α-synuclein aggregation and membrane binding
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Author keywords
[No Author keywords available]
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Indexed keywords
FINNISH;
MEMBRANE BINDING;
PARKINSONS DISEASE;
SYNUCLEIN;
ALPHA SYNUCLEIN;
AMYLOID A PROTEIN;
MUTANT PROTEIN;
AMYLOID;
FLUORESCENT DYE;
LIPID BILAYER;
PHOSPHATIDYLCHOLINE;
PHOSPHATIDYLETHANOLAMINE;
RECOMBINANT PROTEIN;
SNCA PROTEIN, HUMAN;
ARTICLE;
BINDING AFFINITY;
FINN (CITIZEN);
GENE MUTATION;
IN VITRO STUDY;
MEMBRANE BINDING;
OLIGOMERIZATION;
PARKINSON DISEASE;
PATHOGENESIS;
PROTEIN AGGREGATION;
PROTEIN SECONDARY STRUCTURE;
AMINO ACID SUBSTITUTION;
ATOMIC FORCE MICROSCOPY;
CHEMISTRY;
CIRCULAR DICHROISM;
COMPARATIVE STUDY;
FINLAND;
GENETICS;
HUMAN;
KINETICS;
LIPID BILAYER;
METABOLISM;
MUTATION;
PROTEINOSIS;
SPECTROFLUOROMETRY;
SURFACE PLASMON RESONANCE;
SURFACE PROPERTY;
ALPHA-SYNUCLEIN;
AMINO ACID SUBSTITUTION;
AMYLOID;
CIRCULAR DICHROISM;
FINLAND;
FLUORESCENT DYES;
HUMANS;
KINETICS;
LIPID BILAYERS;
MICROSCOPY, ATOMIC FORCE;
MUTATION;
PARKINSON DISEASE;
PHOSPHATIDYLCHOLINES;
PHOSPHATIDYLETHANOLAMINES;
PROTEIN AGGREGATION, PATHOLOGICAL;
PROTEIN STRUCTURE, SECONDARY;
RECOMBINANT PROTEINS;
SPECTROMETRY, FLUORESCENCE;
SURFACE PLASMON RESONANCE;
SURFACE PROPERTIES;
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EID: 84908204323
PISSN: 00062960
EISSN: 15204995
Source Type: Journal
DOI: 10.1021/bi5010365 Document Type: Article |
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Times cited : (126)
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References (14)
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