Protein disulfide isomerases from C. elegans are equally efficient at thiol-disulfide exchange in simple peptide-based systems but show differences in reactivity towards protein substrates

Antioxidants and Redox Signaling

Volumn 9, Issue 11, 2007, Pages 1815-1823

  Karala, Anna Riikka ^a   Psarrakos, Panagiotis ^b   Ruddock, Lloyd W ^a   Klappa, Peter ^b  

^a UNIVERSITY OF OULU   (Finland)

^b UNIVERSITY OF KENT   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

DISULFIDE; PROTEIN DISULFIDE ISOMERASE; PROTEIN DISULFIDE ISOMERASE 1; PROTEIN DISULFIDE ISOMERASE 2; PROTEIN DISULFIDE ISOMERASE 3; THIOL; UNCLASSIFIED DRUG;

ANALYTIC METHOD; ARTICLE; CAENORHABDITIS ELEGANS; COMPARATIVE STUDY; CONTROLLED STUDY; ENDOPLASMIC RETICULUM; KINETICS; NEMATODE; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING;

ANIMALS; CAENORHABDITIS ELEGANS; CATALYSIS; CLONING, MOLECULAR; DISULFIDES; DNA, COMPLEMENTARY; GENES, HELMINTH; ISOMERASES; KINETICS; OXIDATION-REDUCTION; PEPTIDES; PROTEIN DISULFIDE-ISOMERASE; PROTEINS; SUBSTRATE SPECIFICITY; SULFHYDRYL COMPOUNDS;

CAENORHABDITIS ELEGANS; EUKARYOTA; MAMMALIA; METAZOA;

EID: 35448949114     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/ars.2007.1624     Document Type: Article

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