Mechanism of chaperone function in small heat-shock proteins. Phosphorylation-induced activation of two-mode binding in αb-crystallin

Journal of Biological Chemistry

Volumn 278, Issue 12, 2003, Pages 10361-10367

  Koteiche, Hanane A ^b   McHaourab, Hassane S ^a  

^a VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

CRYSTALLIZATION; ISOTHERMS; MUTAGENESIS; SUBSTITUTION REACTIONS;

HEAT-SHOCK PROTEINS;

PROTEINS;

ALPHA CRYSTALLIN; BETA CRYSTALLIN; CHAPERONE; HEAT SHOCK PROTEIN; LYSOZYME;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; COMPLEX FORMATION; ENZYME ACTIVATION; MITOGENICITY; MOLECULAR RECOGNITION; NONHUMAN; OLIGOMERIZATION; PHASE TRANSITION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PHOSPHORYLATION; PROTEIN QUATERNARY STRUCTURE; SIGNAL TRANSDUCTION; ANIMAL; CHEMISTRY; MOUSE; PH; PHOSPHORYLATION; PHYSIOLOGY; PROTEIN CONFORMATION; PROTEIN FOLDING; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION; TEMPERATURE;

ALPHA-CRYSTALLIN B CHAIN; ANIMALS; HEAT-SHOCK PROTEINS; HYDROGEN-ION CONCENTRATION; MICE; MOLECULAR CHAPERONES; MUTAGENESIS, SITE-DIRECTED; PHOSPHORYLATION; PROTEIN CONFORMATION; PROTEIN FOLDING; STRUCTURE-ACTIVITY RELATIONSHIP; TEMPERATURE;

EID: 0038193547     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M211851200     Document Type: Article

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