Difference between revisions of "YDR513W"
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| − | '''Description of YDR513W:''' Cytoplasmic glutaredoxin, thioltransferase, glutathione-dependent disulfide oxidoreductase involved in maintaining redox state of target proteins, also exhibits glutathione peroxidase activity, expression induced in response to stress<ref name=' | + | '''Description of YDR513W:''' Cytoplasmic glutaredoxin, thioltransferase, glutathione-dependent disulfide oxidoreductase involved in maintaining redox state of target proteins, also exhibits glutathione peroxidase activity, expression induced in response to stress<ref name='S000069834'>Collinson EJ, et al. (2002) The yeast glutaredoxins are active as glutathione peroxidases. J Biol Chem 277(19):16712-7 {{SGDpaper|S000069834}} PMID 11875065</ref><ref name='S000056789'>Gan ZR, et al. (1990) Complete amino acid sequence of yeast thioltransferase (glutaredoxin). Biochem Biophys Res Commun 168(3):944-51 {{SGDpaper|S000056789}} PMID 2189409</ref><ref name='S000054906'>Draculic T, et al. (2000) A single glutaredoxin or thioredoxin gene is essential for viability in the yeast Saccharomyces cerevisiae. Mol Microbiol 36(5):1167-74 {{SGDpaper|S000054906}} PMID 10844700</ref><ref name='S000053996'>Luikenhuis S, et al. (1998) The yeast Saccharomyces cerevisiae contains two glutaredoxin genes that are required for protection against reactive oxygen species. Mol Biol Cell 9(5):1081-91 {{SGDpaper|S000053996}} PMID 9571241</ref><ref name='S000048888'>Rodriguez-Manzaneque MT, et al. (1999) Grx5 glutaredoxin plays a central role in protection against protein oxidative damage in Saccharomyces cerevisiae. Mol Cell Biol 19(12):8180-90 {{SGDpaper|S000048888}} PMID 10567543</ref><ref name='S000048077'>Grant CM, et al. (2000) Differential regulation of glutaredoxin gene expression in response to stress conditions in the yeast Saccharomyces cerevisiae. Biochim Biophys Acta 1490(1-2):33-42 |
| − | {{SGDpaper| | + | {{SGDpaper|S000048077}} PMID 10786615</ref> |
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Revision as of 13:05, 16 January 2009
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| Systematic name | YDR513W |
| Gene name | GRX2 |
| Aliases | TTR1 |
| Feature type | ORF, Verified |
| Coordinates | Chr IV:1471010..1471441 |
| Primary SGDID | S000002921 |
Description of YDR513W: Cytoplasmic glutaredoxin, thioltransferase, glutathione-dependent disulfide oxidoreductase involved in maintaining redox state of target proteins, also exhibits glutathione peroxidase activity, expression induced in response to stress[1][2][3][4][5][6]
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References
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- ↑ Collinson EJ, et al. (2002) The yeast glutaredoxins are active as glutathione peroxidases. J Biol Chem 277(19):16712-7 SGD PMID 11875065
- ↑ Gan ZR, et al. (1990) Complete amino acid sequence of yeast thioltransferase (glutaredoxin). Biochem Biophys Res Commun 168(3):944-51 SGD PMID 2189409
- ↑ Draculic T, et al. (2000) A single glutaredoxin or thioredoxin gene is essential for viability in the yeast Saccharomyces cerevisiae. Mol Microbiol 36(5):1167-74 SGD PMID 10844700
- ↑ Luikenhuis S, et al. (1998) The yeast Saccharomyces cerevisiae contains two glutaredoxin genes that are required for protection against reactive oxygen species. Mol Biol Cell 9(5):1081-91 SGD PMID 9571241
- ↑ Rodriguez-Manzaneque MT, et al. (1999) Grx5 glutaredoxin plays a central role in protection against protein oxidative damage in Saccharomyces cerevisiae. Mol Cell Biol 19(12):8180-90 SGD PMID 10567543
- ↑ Grant CM, et al. (2000) Differential regulation of glutaredoxin gene expression in response to stress conditions in the yeast Saccharomyces cerevisiae. Biochim Biophys Acta 1490(1-2):33-42 SGD PMID 10786615
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