Curcumin prevents aggregation in α-synuclein by increasing reconfiguration rate

Journal of Biological Chemistry

Volumn 287, Issue 12, 2012, Pages 9193-9199

  Ahmad, Basir ^a   Lapidus, Lisa J ^a  

^a MICHIGAN STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIMOLECULAR ASSOCIATION; CURCUMIN; HIGH TEMPERATURE; HYDROPHOBIC RESIDUES; IN-VITRO; STRONG BINDING; SYNUCLEIN; TIME-SCALES; UNFOLDED PROTEINS;

HYDROPHOBICITY; OLIGOMERS;

PROTEINS;

ALPHA SYNUCLEIN; CURCUMIN; OLIGOMER;

ARTICLE; CONTROLLED STUDY; DIFFUSION; HIGH TEMPERATURE; HYDROPHOBICITY; INTRAMOLECULAR DIFFUSION; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN MODIFICATION; PROTEIN RECONFIGURATION; PROTEIN UNFOLDING; TEMPERATURE DEPENDENCE;

ALPHA-SYNUCLEIN; CURCUMIN; HOT TEMPERATURE; HUMANS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; KINETICS; PROTEIN BINDING; PROTEIN FOLDING;

CURCUMA LONGA;

EID: 84858595914     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.325548     Document Type: Article

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