The association of α-synuclein with membranes affects bilayer structure, stability, and fibril formation

Journal of Biological Chemistry

Volumn 278, Issue 41, 2003, Pages 40186-40197

  Zhu, Min ^b   Li, Jie ^b   Fink, Anthony L ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

AGGLOMERATION; ATOMIC FORCE MICROSCOPY; DISEASES; FLUORESCENCE; HYDROPHOBICITY; NEUROLOGY; PROBES; PROTEINS;

FIBRIL FORMATION;

BIOCHEMISTRY;

ALPHA SYNUCLEIN; DYE; OLIGOMER;

ARTICLE; ATOMIC FORCE MICROSCOPY; BILAYER MEMBRANE; BINDING AFFINITY; CELL VACUOLE; CORRELATION ANALYSIS; ELECTRICITY; HYDROPHOBICITY; LIPID BILAYER; MEMBRANE DAMAGE; MEMBRANE STABILIZATION; MEMBRANE STRUCTURE; NERVE ENDING; NEUROFILAMENT; NEUROTOXICITY; PARKINSON DISEASE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FUNCTION; PROTEIN INTERACTION;

2-NAPHTHYLAMINE; ALPHA-SYNUCLEIN; FLUORESCENT DYES; HUMANS; KINETICS; LAURATES; LIPID BILAYERS; MICROSCOPY, ATOMIC FORCE; MOLECULAR STRUCTURE; NERVE TISSUE PROTEINS; PARKINSON DISEASE; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SPECTROMETRY, FLUORESCENCE; SYNUCLEINS;

EID: 0141891097     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M305326200     Document Type: Article

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