Dependence of α-synuclein aggregate morphology on solution conditions

Journal of Molecular Biology

Volumn 322, Issue 2, 2002, Pages 383-393

  Hoyer, Wolfgang ^a   Antony, Thomas ^a   Cherny, Dmitry ^a,b   Heim, Gudrun ^a   Jovin, Thomas M ^a   Subramaniam, Vinod ^a  

^a MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

^b INSTITUTE OF MOLECULAR GENETICS   (Russian Federation)

Author keywords

Electron microscopy; Protein aggregation; Scanning force microscopy; Thioflavin T; synuclein

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; ALPHA SYNUCLEIN; THIOFLAVINE;

ARTICLE; ELECTRON MICROSCOPY; IN VITRO STUDY; INCUBATION TIME; MICROSCOPY; PH; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN STRUCTURE; SCANNING FORCE MICROSCOPY; WILD TYPE;

EID: 0036386364     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)00775-1     Document Type: Article

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