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Angewandte Chemie - International Edition

Volumn 53, Issue 16, 2014, Pages 4227-4230

Sequestration of a β-hairpin for control of α-synuclein aggregation

(8) Mirecka, Ewa A a Shaykhalishahi, Hamed a Gauhar, Aziz a Akgül, Şerife a Lecher, Justin a,b Willbold, Dieter a,b Stoldt, Matthias a,b Hoyer, Wolfgang a,b

a HEINRICH HEINE UNIVERSITY (Germany)

b FORSCHUNGSZENTRUM JÜLICH (Germany)

Author keywords

aggregation; amyloids; NMR spectroscopy; protein engineering; protein folding

Indexed keywords

AGGLOMERATION; GLYCOPROTEINS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN FOLDING; TOXICITY;

AMYLOID FIBRIL; AMYLOIDS; BINDING PROTEINS; HAIRPIN CONFORMATION; MISFOLDING; NMR STRUCTURES; PARKINSON'S DISEASE; PROTEIN ENGINEERING;

PROTEINS;

ALPHA-SYNUCLEIN;

AMINO ACID SEQUENCE; CHEMISTRY; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; METABOLISM; PARKINSON DISEASE; PROTEIN ENGINEERING; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY;

ALPHA-SYNUCLEIN; AMINO ACID SEQUENCE; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; PARKINSON DISEASE; PROTEIN ENGINEERING; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY;

EID: 84898650496 PISSN: 14337851 EISSN: 15213773 Source Type: Journal
DOI: 10.1002/anie.201309001 Document Type: Article

Times cited : (101)

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