Effects of the mutations Ala30 to Pro and Ala53 to Thr on the physical and morphological properties of α-synuclein protein implicated in Parkinson's disease

FEBS Letters

Volumn 440, Issue 1-2, 1998, Pages 67-70

  El Agnaf, Omar M A ^a   Jakes, Ross ^b   Curran, Martin D ^c   Wallace, Andrew ^a  

^a QUEEN'S UNIVERSITY BELFAST   (United Kingdom)

^b Med Res Cncl of Molecular Biology   (United Kingdom)

^c BELFAST CITY HOSPITAL   (United Kingdom)

Author keywords

Synuclein; Amyloid; Lewy body; Neurodegenerative disease; Parkinson's disease; Self aggregation

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID; BIOPOLYMER; NERVE PROTEIN; RECOMBINANT PROTEIN; SNCA PROTEIN, HUMAN; SYNUCLEIN; THIAZOLE DERIVATIVE; THIOFLAVINE;

ARTICLE; CONTROLLED STUDY; GENE MUTATION; HUMAN; LEWY BODY; NERVE DEGENERATION; PARKINSON DISEASE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN STRUCTURE, FUNCTION AND VARIABILITY; AMINO ACID SUBSTITUTION; CHEMISTRY; CIRCULAR DICHROISM; DIMERIZATION; ELECTRON MICROSCOPY; GENETICS; METABOLISM; MUTATION; PH; PROTEIN SECONDARY STRUCTURE; ULTRASTRUCTURE;

ALPHA-SYNUCLEIN; AMINO ACID SUBSTITUTION; AMYLOID; BIOPOLYMERS; CIRCULAR DICHROISM; DIMERIZATION; HUMANS; HYDROGEN-ION CONCENTRATION; LEWY BODIES; MICROSCOPY, ELECTRON; MUTATION; NERVE TISSUE PROTEINS; PARKINSON DISEASE; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SYNUCLEINS; THIAZOLES;

EID: 0032573289     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(98)01419-7     Document Type: Article

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