Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Editor

Personal info

View

About

Terms

Javascript disabled

Please enable Javascript support in your browser to use this application.

Instructions on how to enable JavaScript on different browsers can be found here: http://www.google.com/support/bin/answer.py?answer=23852.

[edit this page]

Gene Review:

TXNRD1 - thioredoxin reductase 1

Sus scrofa

Moon, S. et al., Patel, J.M. et al., Kahlos, K. et al., Bodenstein, J. et al.

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

High impact information on TRXR1

CONCLUSIONS: The data show that TTase, Trx, and TR activity and expression are induced in lens cells under oxidative stress, probably to protect and maintain the health of the lens [1].
Under mild H(2)O(2) stress, a slow and transient activation of TTase, Trx, and TR was observed [1].
Similarly, enzymatic reduction by thioredoxin/thioredoxin reductase, but not by glutaredoxin, reversed the inhibition of membrane fraction and purified NO synthase isolated from diamide-treated cells [2].
Heart extracts were also shown to contain a NADPH-specific thioredoxin reductase of the known mammalian type [3].

Associations of TRXR1 with chemical compounds

NO-induced loss of the catalytic activity of PKC-zeta was restored by incubation with the disulfide reducing agent dithiothreitol (DTT) as well as by purified thioredoxin or thioredoxin reductase [4].

References

Induction of thioltransferase and thioredoxin/thioredoxin reductase systems in cultured porcine lenses under oxidative stress. Moon, S., Fernando, M.R., Lou, M.F. Invest. Ophthalmol. Vis. Sci. (2005) [Pubmed]
Sulfhydryl-disulfide modulation and the role of disulfide oxidoreductases in regulation of the catalytic activity of nitric oxide synthase in pulmonary artery endothelial cells. Patel, J.M., Block, E.R. Am. J. Respir. Cell Mol. Biol. (1995) [Pubmed]
Characterization of two thioredoxins in pig heart including a new mitochondrial protein. Bodenstein, J., Follmann, H. Z. Naturforsch., C, J. Biosci. (1991) [Pubmed]
Thioredoxin restores nitric oxide-induced inhibition of protein kinase C activity in lung endothelial cells. Kahlos, K., Zhang, J., Block, E.R., Patel, J.M. Mol. Cell. Biochem. (2003) [Pubmed]

Contributions to this collaborative article are from individual authors of WikiGenes or mined by the WikiGenes Data Mining Engine from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenes Open Access Licence Privacy Policy Terms of Use apsburg

The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.