Site-directed mutations in the C-terminal extension of human αB-crystallin affect chaperone function and block amyloid fibril formation

PLoS ONE

Volumn 2, Issue 10, 2007, Pages

  Treweek, Teresa M ^a   Ecroyd, Heath ^b   Williams, Danielle M ^b   Meehan, Sarah ^c   Carver, John A ^b   Walker, Mark J ^a  

^a UNIVERSITY OF WOLLONGONG   (Australia)

^b UNIVERSITY OF ADELAIDE   (Australia)

^c UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA CRYSTALLIN; ALPHAB CRYSTALLIN; AMYLOID; CHAPERONE; GLUTAMIC ACID; LYSINE; UNCLASSIFIED DRUG; PROTEIN;

ALZHEIMER DISEASE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; CREUTZFELDT JAKOB DISEASE; DRUG DESIGN; DRUG STRUCTURE; DRUG SYNTHESIS; MUTATIONAL ANALYSIS; PARKINSON DISEASE; PROTEIN AGGREGATION; PROTEIN FUNCTION; PROTEIN QUATERNARY STRUCTURE; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTEIN TARGETING; PROTEIN TERTIARY STRUCTURE; SITE DIRECTED MUTAGENESIS; THERMOSTABILITY; CHEMISTRY; CODON; ELECTROSPRAY MASS SPECTROMETRY; HUMAN; MUTATION; TEMPERATURE;

ALPHA-CRYSTALLIN B CHAIN; AMYLOID; CODON; GLUTAMIC ACID; HUMANS; LYSINE; MOLECULAR CHAPERONES; MUTAGENESIS, SITE-DIRECTED; MUTATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEINS; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; TEMPERATURE;

EID: 42349107955     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0001046     Document Type: Article

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