Structural characterization of α-synuclein in an aggregation prone state

Protein Science

Volumn 18, Issue 9, 2009, Pages 1840-1846

  Cho, Min Kyu ^a   Nodet, Gabrielle ^b   Kim, Hai Young ^a   Jensen, Malene R ^b   Bernado, Pau ^c   Fernandez, Claudio O ^d   Becker, Stefan ^a   Blackledge, Martin ^b   Zweckstetter, Markus ^a,e  

^a MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

^b INSTITUT DE BIOLOGIE STRUCTURALE   (France)

^c INSTITUTE FOR RESEARCH IN BIOMEDICINE   (Spain)

^d UNIVERSIDAD NACIONAL DE ROSARIO   (Argentina)

^e Deutsche Forschungsgemeinschaft   (Germany)

Author keywords

Aggregation; Neurodegeneration; Parkinson's disease; Protein structure

Indexed keywords

ALPHA SYNUCLEIN; ASPARTIC ACID; GLUTAMIC ACID;

ACIDITY; ARTICLE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH MEASUREMENT; PRIORITY JOURNAL; PROBABILITY; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE;

ALPHA-SYNUCLEIN; AMINO ACID SEQUENCE; HUMANS; HYDROGEN-ION CONCENTRATION; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PARKINSON DISEASE; PROTEIN CONFORMATION; PROTEIN FOLDING;

EID: 69249094544     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.194     Document Type: Article

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