Extent of inhibition of α-synuclein aggregation in vitro by SUMOylation is conjugation site- and SUMO isoform-selective

Biochemistry

Volumn 54, Issue 4, 2015, Pages 959-961

  Abeywardana, Tharindumala ^a   Pratt, Matthew R ^a  

^a UNIVERSITY OF SOUTHERN CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY;

IN-VITRO; ISOFORMS; PARKINSONS DISEASE; SEMISYNTHESIS; SMALL PROTEINS; SUMOYLATION; SYNUCLEIN;

PROTEINS;

ALPHA SYNUCLEIN; G PROTEIN COUPLED RECEPTOR KINASE 5; SUMO 3 PROTEIN; SUMO PROTEIN; PROTEIN AGGREGATE; PROTEIN BINDING;

ARTICLE; CELL FUNCTION; CIRCULAR DICHROISM; CONJUGATION; CONTROLLED STUDY; IN VITRO STUDY; LIGHT SCATTERING; MOLECULAR WEIGHT; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN PHOSPHORYLATION; PROTEIN SECONDARY STRUCTURE; PROTEIN SYNTHESIS; SUMOYLATION; TRANSMISSION ELECTRON MICROSCOPY; TURNOVER TIME; UBIQUITINATION; ANTAGONISTS AND INHIBITORS; CHEMISTRY; METABOLISM; PHYSIOLOGY;

ALPHA-SYNUCLEIN; PROTEIN AGGREGATES; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; SUMOYLATION;

EID: 84922198962     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi501512m     Document Type: Article

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