The A53E α-synuclein pathological mutation demonstrates reduced aggregation propensity in vitro and in cell culture

Neuroscience Letters

Volumn 597, Issue , 2015, Pages 43-48

  Rutherford, Nicola J ^a   Giasson, Benoit I ^a  

^a UNIVERSITY OF FLORIDA COLLEGE OF MEDICINE   (United States)

Author keywords

Fibrillization kinetics; Inclusion formation; Parkinson's disease; SNCA mutation; Synuclein

Indexed keywords

A53E ALPHA SYNUCLEIN; ALPHA SYNUCLEIN; AMYLOID PROTEIN; MUTANT PROTEIN; THINNER; UNCLASSIFIED DRUG; 1,3-BIS(4-HYDROXYPHENYL)-4-METHYL-5-(4-(2-PIPERIDINYLETHOXY)PHENOL)-1H-PYRAZOLE; AMYLOID; PIPERIDINE DERIVATIVE; PROTEIN AGGREGATE; PYRAZOLE DERIVATIVE;

ARTICLE; CELL AGGREGATION; CELL CULTURE; CELL STRESS; CELL STRUCTURE; COMPARATIVE STUDY; CONTROLLED STUDY; CYTOTOXICITY; DEGENERATIVE DISEASE; GENE MUTATION; IN VITRO STUDY; MITOCHONDRION; MUTAGENESIS; NEUROPATHOLOGY; NONHUMAN; PARKINSONISM; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN EXPRESSION; PROTEIN STRUCTURE; WILD TYPE; ANIMAL; CELL SURVIVAL; CHEMISTRY; DRUG EFFECTS; GENETICS; METABOLISM; MOUSE; MUTATION; TUMOR CELL LINE;

ALPHA-SYNUCLEIN; AMYLOID; ANIMALS; CELL LINE, TUMOR; CELL SURVIVAL; MICE; MITOCHONDRIA; MUTATION; PIPERIDINES; PROTEIN AGGREGATES; PYRAZOLES;

EID: 84928227099     PISSN: 03043940     EISSN: 18727972     Source Type: Journal    
DOI: 10.1016/j.neulet.2015.04.022     Document Type: Article

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