Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5504
pubmed:dateCreated
2001-2-22
pubmed:databankReference
pubmed:abstractText
The disulfide reducing enzymes glutathione reductase and thioredoxin reductase are highly conserved among bacteria, fungi, worms, and mammals. These proteins maintain intracellular redox homeostasis to protect the organism from oxidative damage. Here we demonstrate the absence of glutathione reductase in Drosophila melanogaster, identify a new type of thioredoxin reductase, and provide evidence that a thioredoxin system supports GSSG reduction. Our data suggest that antioxidant defense in Drosophila, and probably in related insects, differs fundamentally from that in other organisms.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0036-8075
pubmed:author
pubmed:issnType
Print
pubmed:day
26
pubmed:volume
291
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
643-6
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:11158675-Amino Acid Motifs, pubmed-meshheading:11158675-Amino Acid Sequence, pubmed-meshheading:11158675-Animals, pubmed-meshheading:11158675-Binding Sites, pubmed-meshheading:11158675-Drosophila melanogaster, pubmed-meshheading:11158675-Genes, Insect, pubmed-meshheading:11158675-Glutathione, pubmed-meshheading:11158675-Glutathione Disulfide, pubmed-meshheading:11158675-Glutathione Reductase, pubmed-meshheading:11158675-Humans, pubmed-meshheading:11158675-Kinetics, pubmed-meshheading:11158675-Molecular Sequence Data, pubmed-meshheading:11158675-Mutation, pubmed-meshheading:11158675-NADP, pubmed-meshheading:11158675-Oxidation-Reduction, pubmed-meshheading:11158675-Sequence Alignment, pubmed-meshheading:11158675-Species Specificity, pubmed-meshheading:11158675-Substrate Specificity, pubmed-meshheading:11158675-Thioredoxin-Disulfide Reductase
pubmed:year
2001
pubmed:articleTitle
Substitution of the thioredoxin system for glutathione reductase in Drosophila melanogaster.
pubmed:affiliation
Center of Biochemistry, Im Neuenheimer Feld 328, Heidelberg University, D-69120 Heidelberg, Germany.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't