The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm

Journal of Biological Chemistry

Volumn 272, Issue 25, 1997, Pages 15661-15667

  Prinz, William A ^a   Åslund, Fredrik ^b   Holmgren, Arne ^b   Beckwith, Jon ^a  

^a HARVARD MEDICAL SCHOOL   (United States)

^b KAROLINSKA INSTITUTE   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN DISULFIDE ISOMERASE; THIOREDOXIN;

ARTICLE; BACTERIAL MEMBRANE; CATALYSIS; CELL MEMBRANE; DISULFIDE BOND; ENZYME ACTIVITY; ENZYME SUBSTRATE; ESCHERICHIA COLI; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN PROTEIN INTERACTION;

BACTERIAL PROTEINS; CYTOPLASM; DIAMIDE; DISULFIDES; ESCHERICHIA COLI; MODELS, CHEMICAL; NADP; OXIDOREDUCTASES; PROTEINS; SULFHYDRYL REAGENTS; THIOREDOXIN; URINARY PLASMINOGEN ACTIVATOR;

EID: 0030941829     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.272.25.15661     Document Type: Article

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