Aggregation promoting C-terminal truncation of α-synuclein is a normal cellular process and is enhanced by the familial Parkinson's disease-linked mutations

Proceedings of the National Academy of Sciences of the United States of America

Volumn 102, Issue 6, 2005, Pages 2162-2167

  Li, Wenxue ^a   West, Neva ^a   Colla, Emanuela ^a   Pletnikova, Olga ^a   Troncoso, Juan C ^a   Marsh, Laura ^a   Dawson, Ted M ^a   Jäkälä, Pekka ^b   Hartmann, Tobias ^c   Price, Donald L ^a   Lee, Michael K ^a  

^a JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b KUOPIO UNIVERSITY HOSPITAL   (Finland)

^c UNIVERSITY OF HEIDELBERG   (Germany)

Author keywords

synucleinopathy; Lewy body; Mass spectrometry; Proteolysis

Indexed keywords

ALPHA SYNUCLEIN;

ALPHA SYNUCLEINOPATHY; ANIMAL CELL; ANIMAL EXPERIMENT; ARTICLE; BRAIN DISEASE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; FAMILIAL DISEASE; GENE MUTATION; LEWY BODY; MOUSE; NERVE CELL; NONHUMAN; PARKINSON DISEASE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DEGRADATION; PROTEIN EXPRESSION; STOICHIOMETRY;

ALPHA-SYNUCLEIN; ANIMALS; BRAIN; CELL LINE; CELLS, CULTURED; EPITOPE MAPPING; HUMANS; MASS SPECTROMETRY; MICE; MICE, TRANSGENIC; MUTATION; NERVE TISSUE PROTEINS; NEURONS; PARKINSON DISEASE; PEPTIDE FRAGMENTS; PROTEIN ISOFORMS; SYNUCLEINS;

ANIMALIA;

EID: 13844320376     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0406976102     Document Type: Article

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