Protein s-glutathionylation in retinal pigment epithelium converts heat shock protein 70 to an active chaperone

Experimental Eye Research

Volumn 78, Issue 6, 2004, Pages 1085-1092

  Hoppe, George ^a   Chai, Yuh Cherng ^a,b   Crabb, John W ^a   Sears, Jonathan ^a  

^a LERNER RESEARCH INSTITUTE   (United States)

^b JOHN CARROLL UNIVERSITY   (United States)

Author keywords

Aggregation; Chaperone activity; Glutathione; Heat shock proteins; Oxidation reduction; Retinal pigment epithelium; Thiols

Indexed keywords

CHAPERONE; GLUTAREDOXIN; GLUTAREDOXIN 1; GLUTATHIONE; HEAT SHOCK PROTEIN 70; PROTEIN S; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CONCENTRATION RESPONSE; CONTROLLED STUDY; ENZYME ACTIVITY; HUMAN; HUMAN CELL; MASS SPECTROMETRY; NUCLEOTIDE SEQUENCE; OXIDATION REDUCTION STATE; PIGMENT EPITHELIUM; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN EXPRESSION;

AMINO ACID SEQUENCE; CELLS, CULTURED; GLUTATHIONE; HSP70 HEAT-SHOCK PROTEINS; HUMANS; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; OXIDATION-REDUCTION; OXIDATIVE STRESS; OXIDOREDUCTASES; PIGMENT EPITHELIUM OF EYE; PROTEINS; RECOMBINANT PROTEINS;

EID: 1942423136     PISSN: 00144835     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.exer.2004.02.001     Document Type: Article

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