Release of long-range tertiary interactions potentiates aggregation of natively unstructured α-synuclein

Proceedings of the National Academy of Sciences of the United States of America

Volumn 102, Issue 5, 2005, Pages 1430-1435

  Bertoncini, Carlos W ^a   Jung, Young Sang ^a   Fernandez, Claudio O ^b   Hoyer, Wolfgang ^a   Griesinger, Christian ^a   Jovin, Thomas M ^a   Zweckstetter, Markus ^a  

^a MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

^b UNIVERSIDAD NACIONAL DE ROSARIO   (Argentina)

Author keywords

Amyloid; Fibrillation; Parkinson's disease

Indexed keywords

ALPHA SYNUCLEIN; POLYAMINE;

ARTICLE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE; TEMPERATURE;

ALPHA-SYNUCLEIN; ANISOTROPY; BINDING SITES; CLONING, MOLECULAR; ESCHERICHIA COLI; HUMANS; MACROMOLECULAR SUBSTANCES; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; NERVE TISSUE PROTEINS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SYNUCLEINS; THERMODYNAMICS;

EID: 13444252277     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0407146102     Document Type: Article

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