Small molecule-mediated stabilization of vesicle-associated helical α-synuclein inhibits pathogenic misfolding and aggregation

Nature communications

Volumn 5, Issue , 2014, Pages 5857-

  Fonseca Ornelas, Luis ^a   Eisbach, Sybille E ^a   Paulat, Maria ^a   Giller, Karin ^a   Fernández, Claudio O ^a   Outeiro, Tiago F ^a   Becker, Stefan ^a   Zweckstetter, Markus ^a  

^a MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; ANTIPARKINSON AGENT; INDOLE DERIVATIVE; SELEGILINE; TETRASULFOPHTHALOCYANINE;

CHEMISTRY; GENETICS; HUMAN; METABOLISM; PARKINSON DISEASE; PATHOPHYSIOLOGY; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEINOSIS; SYNAPSE VESICLE;

ALPHA-SYNUCLEIN; ANTIPARKINSON AGENTS; HUMANS; INDOLES; PARKINSON DISEASE; PROTEIN AGGREGATION, PATHOLOGICAL; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE, SECONDARY; SELEGILINE; SYNAPTIC VESICLES;

EID: 84930230633     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms6857     Document Type: Article

References (0)