Distinct cleavage patterns of normal and pathologic forms of α-synuclein by calpain I in vitro

Journal of Neurochemistry

Volumn 86, Issue 4, 2003, Pages 836-847

  Mishizen Eberz, Amanda J ^a   Guttmann, Rodney P ^a,c   Giasson, Benoit I ^a   Day III, George A ^a   Hodara, Roberto ^a   Ischiropoulos, Harry ^a   Lee, Virginia M Y ^a,b   Trojanowski, John Q ^a,b   Lynch, David R ^a,d  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

^c UNIVERSITY OF KENTUCKY   (United States)

^d CHILDREN S HOSPITAL OF PHILADELPHIA   (United States)

Author keywords

synuclein; Calpain I; Fibrillization; Lewy bodies; Parkinson's disease

Indexed keywords

ALPHA SYNUCLEIN; CALPAIN; CALPAIN I; DOPAMINE; MUTANT PROTEIN; PEPTIDE FRAGMENT; UNCLASSIFIED DRUG;

ANIMAL TISSUE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL PROTECTION; DEGENERATIVE DISEASE; FIBRILLIZATION; FIBROGENESIS; IN VITRO STUDY; LEWY BODY; MOUSE; NEUROTOXICITY; NONHUMAN; OXIDATIVE STRESS; PARKINSON DISEASE; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN POLYMERIZATION; PROTEIN STABILITY; TRANSGENIC MOUSE;

ALPHA-SYNUCLEIN; AMINO ACID SUBSTITUTION; ANIMALS; CALPAIN; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; HUMANS; MASS SPECTROMETRY; MICE; MICE, TRANSGENIC; MOLECULAR WEIGHT; MUTATION; NERVE TISSUE PROTEINS; PARKINSON DISEASE; PEPTIDE FRAGMENTS; PEPTIDE MAPPING; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY; SYNUCLEINS;

ANIMALIA; MUS MUSCULUS;

EID: 0043233011     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.2003.01878.x     Document Type: Article

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