The small heat-shock protein αB-crystallin uses different mechanisms of chaperone action to prevent the amorphous versus fibrillar aggregation of α-lactalbumin

Biochemical Journal

Volumn 448, Issue 3, 2012, Pages 343-352

  Kulig, Melissa ^a   Ecroyd, Heath ^a  

^a UNIVERSITY OF WOLLONGONG   (Australia)

Author keywords

Amorphous aggregate; Amyloid fibril; Chaperone; Holdase; Protein aggregation; Protein complex

Indexed keywords

ALPHA CRYSTALLIN; ALPHA LACTALBUMIN; AMYLOID; CHAPERONE;

ARTICLE; COMPLEX FORMATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN FUNCTION; REDUCTION;

ALPHA-CRYSTALLIN B CHAIN; ANIMALS; CATTLE; HEAT-SHOCK PROTEINS, SMALL; HUMANS; LACTALBUMIN; MOLECULAR CHAPERONES; PROTEIN CONFORMATION;

BOVINAE;

EID: 84870015466     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20121187     Document Type: Article

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