Cataract-linked γd-crystallin mutants have weak affinity to lens chaperones α-crystallins

FEBS Letters

Volumn 586, Issue 4, 2012, Pages 330-336

  Mishra, Sanjay ^a   Stein, Richard A ^a   McHaourab, Hassane S ^a  

^a VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Crystallin; B crystallin phosphorylation; Crystallin; D crystallin; Bimane fluorescence; Cataract; Chaperone; Denaturant unfolding; Small heat shock protein

Indexed keywords

ALPHA CRYSTALLIN; CHAPERONE; GAMMA CRYSTALLIN; MUTANT PROTEIN;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; CATARACT; CONCENTRATION RESPONSE; CONTROLLED STUDY; HUMAN; LENS; LENS TRANSPARENCY; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN PURIFICATION; PROTEIN STABILITY; QUALITY CONTROL;

ALPHA-CRYSTALLINS; ANIMALS; CATARACT; GAMMA-CRYSTALLINS; HUMANS; LENS, CRYSTALLINE; MICE; MODELS, MOLECULAR; MUTANT PROTEINS; PROTEIN BINDING; RECOMBINANT PROTEINS; THERMODYNAMICS; UNFOLDED PROTEIN RESPONSE;

EID: 84857048837     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2012.01.019     Document Type: Article

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