Diabetic changes in the redox status of the microsomal protein folding machinery

Biochemical and Biophysical Research Communications

Volumn 334, Issue 3, 2005, Pages 787-795

  Nardai, Gábor ^a   Stadler, Krisztián ^b   Papp, Eszter ^a   Korcsmáros, Tamás ^a   Jakus, Judit ^b   Csermely, Péter ^a  

^a SEMMELWEIS UNIVERSITY   (Hungary)

^b CHEMICAL RESEARCH CENTER   (Hungary)

Author keywords

Diabetes; Endoplasmic reticulum; Ero1 L ; Glucose regulated proteins; Heat shock proteins; Molecular chaperones; Protein disulfide isomerase; Rat liver; Redox status; Streptozotocin

Indexed keywords

CHAPERONE; GLUCOSE REGULATED PROTEIN; OXIDIZING AGENT; PROTEIN; PROTEIN DISULFIDE ISOMERASE; PROTEIN DISULFIDE REDUCTASE (GLUTATHIONE); PROTEIN P57; STREPTOZOCIN; THIOL DERIVATIVE;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; DIABETES MELLITUS; ENDOPLASMIC RETICULUM; ENZYME ACTIVITY; LIVER MICROSOME; MALE; MOLECULAR WEIGHT; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FOLDING; PROTEIN SECRETION; RAT; STATISTICAL SIGNIFICANCE;

ANIMALS; ASCORBIC ACID; DEHYDROASCORBIC ACID; DIABETES MELLITUS, EXPERIMENTAL; FLAVIN-ADENINE DINUCLEOTIDE; GLUTATHIONE DISULFIDE; MALE; MICROSOMES, LIVER; NADH, NADPH OXIDOREDUCTASES; OXIDATION-REDUCTION; PROTEIN DISULFIDE-ISOMERASE; PROTEIN FOLDING; RATS; RATS, WISTAR;

EID: 22744459369     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.06.172     Document Type: Article

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