α-Crystallin prevents irreversible protein denaturation and acts cooperatively with other heat-shock proteins to renature the stabilized partially denatured protein in an ATP-dependent manner

European Journal of Biochemistry

Volumn 267, Issue 15, 2000, Pages 4705-4712

  Wang, Keyang ^a   Spector, Abraham ^a  

^a Och Spine at New York Presbyterian Hospitals   (United States)

Author keywords

Crystallin; Heat shock protein; Molecular chaperone; Re activation

Indexed keywords

ADENOSINE TRIPHOSPHATE; ALPHA CRYSTALLIN; CHAPERONE; CITRATE SYNTHASE; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 60; HEAT SHOCK PROTEIN 70; LUCIFERASE;

ARTICLE; ENZYME BINDING; PRIORITY JOURNAL; PROTEIN DENATURATION; RETICULOCYTE LYSATE;

ADENOSINE TRIPHOSPHATE; ANIMALS; BLOTTING, WESTERN; CATTLE; CHAPERONIN 60; CITRATE (SI)-SYNTHASE; CRYSTALLINS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENZYME ACTIVATION; HEAT-SHOCK PROTEINS; HSP40 HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; LENS, CRYSTALLINE; LUCIFERASES; PHOSPHORYLATION; PROTEIN DENATURATION; PROTEIN RENATURATION; RABBITS; RETICULOCYTES; SWINE; TEMPERATURE; TIME FACTORS; ULTRAFILTRATION;

EID: 0033863553     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2000.01521.x     Document Type: Article

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4. 2 but phosphorylation has no effect on chaperone activity
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