Engineered α-synuclein prevents wild type and familial Parkin variant fibril formation

Biochemical and Biophysical Research Communications

Volumn 335, Issue 2, 2005, Pages 432-436

  Sode, Koji ^a   Usuzaka, Eri ^a   Kobayashi, Natsuki ^a   Ochiai, Sayaka ^a  

^a TOKYO UNIVERSITY OF AGRICULTURE AND TECHNOLOGY   (Japan)

Author keywords

Synuclein; Amyloid fibril; Natively unfolded protein; Parkinson's disease; Site directed mutagenesis

Indexed keywords

ALANINE; ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN; PARKIN; PROLINE; THREONINE; VALINE;

ALZHEIMER DISEASE; ARTICLE; BETA CHAIN; BRAIN PROTECTION; HYDROPHOBICITY; NERVE DEGENERATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ENGINEERING; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; SITE DIRECTED MUTAGENESIS; WILD TYPE;

ALPHA-SYNUCLEIN; ALZHEIMER DISEASE; AMINO ACID SEQUENCE; AMYLOID; BONE MARROW CELLS; CIRCULAR DICHROISM; DNA; DNA, COMPLEMENTARY; GENE LIBRARY; HUMANS; LIGHT; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTATION; NERVE TISSUE PROTEINS; PARKINSON DISEASE; PEPTIDES; POLYMERASE CHAIN REACTION; PROLINE; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN ENGINEERING; PROTEIN STRUCTURE, SECONDARY; SCATTERING, RADIATION; SYNUCLEINS; TIME FACTORS; UBIQUITIN-PROTEIN LIGASES; ULTRAVIOLET RAYS; VALINE;

EID: 23744437433     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.07.100     Document Type: Article

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