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Properties And Biological Activities Of Thioredoxins.
G. Powis, W. Montfort
Published 2001 · Chemistry, Medicine, Biology
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The mammalian thioredoxins are a family of small (approximately 12 kDa) redox proteins that undergo NADPH-dependent reduction by thioredoxin reductase and in turn reduce oxidized cysteine groups on proteins. The two main thioredoxins are thioredoxin-1, a cytosolic and nuclear form, and thioredoxin-2, a mitochondrial form. Thioredoxin-1 has been studied more. It performs many biological actions including the supply of reducing equivalents to thioredoxin peroxidases and ribonucleotide reductase, the regulation of transcription factor activity, and the regulation of enzyme activity by heterodimer formation. Thioredoxin-1 stimulates cell growth and is an inhibitor of apoptosis. Thioredoxins may play a role in a variety of human diseases including cancer. An increased level of thioredoxin-1 is found in many human tumors, where it is associated with aggressive tumor growth. Drugs are being developed that inhibit thioredoxin and that have antitumor activity.
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An association between manganese superoxide dismutase polymorphism and outcome of chemotherapy in acute myeloid leukemia.
P. Koistinen (2006)
Cloning, expression and characterization of mouse spermatid specific thioredoxin-1 gene and protein.
A. Jiménez (2002)
Identification of potential biomarkers for giant cell tumor of bone using comparative proteomics analysis.
A. Conti (2011)
Oxidative stress and diabetes: what can we learn about insulin resistance from antioxidant mutant mouse models?
Jennalynn Styskal (2012)
TRX-1 Regulates SKN-1 Nuclear Localization Cell Non-Autonomously in Caenorhabditis 1 elegans 2 3
K. McCallum (2016)
Escherichia coli thioredoxin inhibition by cadmium
Françoise Rollin-Genetet (2004)
Title Thiol redox homeostasis in neurodegenerative disease
G. McBean (2018)
Sulfhydryl oxidases: emerging catalysts of protein disulfide bond formation in eukaryotes.
C. Thorpe (2002)See more