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Volumn 40, Issue 38, 2001, Pages 11604-11613

Effect of familial Parkinson's disease point mutations A30P and A53T on the structural properties, aggregation, and fibrillation of human α-synuclein

(3) Li, J a Uversky, V N a,b Fink, A L a

a UNIVERSITY OF CALIFORNIA (United States)

b INSTITUTE FOR BIOLOGICAL INSTRUMENTATION (Russian Federation)

Author keywords

[No Author keywords available]

Indexed keywords

MOVEMENT DISORDERS;

AGGLOMERATION; HUMAN ENGINEERING; INCLUSIONS; LIGHT SCATTERING; PATHOLOGY; STRUCTURE (COMPOSITION); X RAY SCATTERING;

DISEASES;

ALPHA SYNUCLEIN; MUTANT PROTEIN; PROTEIN A30P; PROTEIN A53T; UNCLASSIFIED DRUG;

ARTICLE; CELL INCLUSION; CIRCULAR DICHROISM; CORRELATION FUNCTION; DOPAMINERGIC NERVE CELL; FAMILIAL DISEASE; GENE MUTATION; HUMAN; INFRARED SPECTROSCOPY; LEWY BODY; LIGHT SCATTERING; PARKINSON DISEASE; POINT MUTATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE; SUBSTANTIA NIGRA; ULTRAVIOLET RADIATION; X RAY CRYSTALLOGRAPHY;

ALPHA-SYNUCLEIN; AMINO ACID SUBSTITUTION; CIRCULAR DICHROISM; HUMANS; HYDROGEN-ION CONCENTRATION; LIGHT; NERVE TISSUE PROTEINS; PARKINSON DISEASE; PHOSPHOPROTEINS; POINT MUTATION; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT FUSION PROTEINS; SCATTERING, RADIATION; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; SYNUCLEINS; THERMODYNAMICS; X-RAYS;

EID: 0035949542 PISSN: 00062960 EISSN: None Source Type: Journal
DOI: 10.1021/bi010616g Document Type: Article

Times cited : (462)

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