The A53T mutation is key in defining the differences in the aggregation kinetics of human and mouse α-synuclein

Journal of the American Chemical Society

Volumn 133, Issue 34, 2011, Pages 13465-13470

  Kang, Lijuan ^a   Wu, Kuen Phon ^a   Vendruscolo, Michele ^c   Baum, Jean ^a,b  

^a RUTGERS UNIVERSITY   (United States)

^b RUTGERS UNIVERSITY   (United States)

^c UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

AGGREGATION KINETICS; ALANINE RESIDUES; CONFORMATIONAL PROPERTIES; DRUG DEVELOPMENT; EVOLUTIONARY ADAPTATION; FLUORESCENCE ANALYSIS; LAG PHASE; LAG TIME; MONOMERIC FORMS; N-TERMINALS; NMR CHEMICAL SHIFTS; PARKINSON'S DISEASE; SECONDARY STRUCTURES; SEQUENCE SIMILARITY; SYNUCLEIN; TRANSGENIC MICE;

AMINO ACIDS; CHEMICAL ANALYSIS; FLUORESCENCE; GROWTH KINETICS; NEURODEGENERATIVE DISEASES;

MAMMALS;

ALANINE; ALPHA SYNUCLEIN;

AGGREGATION KINETICS; AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; CHIMERA; COMPARATIVE STUDY; CONTROLLED STUDY; EVOLUTIONARY ADAPTATION; FLUORESCENCE ANALYSIS; GENE MUTATION; GENETIC VARIABILITY; GROWTH RATE; HUMAN; KINETICS; MOLECULAR EVOLUTION; MOUSE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PARKINSON DISEASE; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; SEQUENCE HOMOLOGY;

ALPHA-SYNUCLEIN; AMINO ACID SEQUENCE; AMYLOID; ANIMALS; HUMANS; KINETICS; MICE; MOLECULAR SEQUENCE DATA; PARKINSON DISEASE; POINT MUTATION; PROTEIN STRUCTURE, SECONDARY; SEQUENCE ALIGNMENT;

EID: 80052087039     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja203979j     Document Type: Article

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