Role of post-translational modifications in modulating the structure, function and toxicity of α-synuclein. Implications for Parkinson's disease pathogenesis and therapies

Progress in Brain Research

Volumn 183, Issue C, 2010, Pages 115-145

  Oueslati, Abid ^a   Fournier, Margot ^a   Lashuel, Hilal A ^a  

^a EPFL   (Switzerland)

Author keywords

Phosphorylation; Post translationnal modification; Truncation; Ubiquitination; synuclein

Indexed keywords

ALPHA SYNUCLEIN; GUANINE NUCLEOTIDE BINDING PROTEIN; PROTEIN GRRK2; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; GENETIC CONSERVATION; HUMAN; IN VITRO STUDY; IN VIVO STUDY; MOLECULAR MECHANICS; NONHUMAN; PARKINSON DISEASE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN DEPLETION; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; PROTEIN PROCESSING; PROTEIN STRUCTURE; RISK FACTOR; UBIQUITINATION;

EID: 77955366745     PISSN: 00796123     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0079-6123(10)83007-9     Document Type: Chapter

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