Semisynthetic, site-specific ubiquitin modification of α-synuclein reveals differential effects on aggregation

Journal of the American Chemical Society

Volumn 134, Issue 12, 2012, Pages 5468-5471

  Meier, Franziska ^a   Abeywardana, Tharindumala ^a   Dhall, Abhinav ^b   Marotta, Nicholas P ^a   Varkey, Jobin ^a   Langen, Ralf ^a   Chatterjee, Champak ^b   Pratt, Matthew R ^a  

^a UNIVERSITY OF SOUTHERN CALIFORNIA   (United States)

^b UNIVERSITY OF WASHINGTON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DIFFERENTIAL EFFECT; LYSINE RESIDUES; NEURODEGENERATION; PARKINSON'S DISEASE; PROTEIN AGGREGATES; SEMISYNTHESIS; SITE-SPECIFIC; SYNUCLEIN; UBIQUITIN; UBIQUITINATION;

AMINO ACIDS; OLIGOMERS;

PROTEINS;

ALPHA SYNUCLEIN; UBIQUITIN;

ARTICLE; PROTEIN AGGREGATION; PROTEIN SYNTHESIS; UBIQUITINATION;

ALPHA-SYNUCLEIN; AMINO ACID SEQUENCE; DISULFIDES; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PARKINSON DISEASE; PROTEIN CONFORMATION; UBIQUITIN; UBIQUITINATION;

EID: 84859142134     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja300094r     Document Type: Article

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