Difference between revisions of "YLR364W"
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| − | '''Description of YLR364W:''' Glutaredoxin that employs a dithiol mechanism of catalysis; monomeric; activity is low and null mutation does not affect sensitivity to oxidative stress; GFP-fusion protein localizes to the cytoplasm; expression strongly induced by arsenic<ref name=' | + | '''Description of YLR364W:''' Glutaredoxin that employs a dithiol mechanism of catalysis; monomeric; activity is low and null mutation does not affect sensitivity to oxidative stress; GFP-fusion protein localizes to the cytoplasm; expression strongly induced by arsenic<ref name='S000129092'>Eckers E, et al. (2009) Biochemical characterization of dithiol glutaredoxin 8 from Saccharomyces cerevisiae: the catalytic redox mechanism redux. Biochemistry 48(6):1410-23 {{SGDpaper|S000129092}} PMID 19166312</ref><ref name='S000071347'>Giaever G, et al. (2002) Functional profiling of the Saccharomyces cerevisiae genome. Nature 418(6896):387-91 {{SGDpaper|S000071347}} PMID 12140549</ref><ref name='S000080191'>Haugen AC, et al. (2004) Integrating phenotypic and expression profiles to map arsenic-response networks. Genome Biol 5(12):R95 {{SGDpaper|S000080191}} PMID 15575969</ref><ref name='S000074185'>Huh WK, et al. (2003) Global analysis of protein localization in budding yeast. Nature 425(6959):686-91 {{SGDpaper|S000074185}} PMID 14562095</ref><ref name='S000125083'>Mesecke N, et al. (2008) Two Novel Monothiol Glutaredoxins from Saccharomyces cerevisiae Provide Further Insight into Iron-Sulfur Cluster Binding, Oligomerization, and Enzymatic Activity of Glutaredoxins. Biochemistry 47(5):1452-63 |
| − | + | {{SGDpaper|S000125083}} PMID 18171082</ref> | |
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Revision as of 13:05, 25 February 2010
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| Systematic name | YLR364W |
| Gene name | GRX8 |
| Aliases | |
| Feature type | ORF, Verified |
| Coordinates | Chr XII:854061..854390 |
| Primary SGDID | S000004356 |
Description of YLR364W: Glutaredoxin that employs a dithiol mechanism of catalysis; monomeric; activity is low and null mutation does not affect sensitivity to oxidative stress; GFP-fusion protein localizes to the cytoplasm; expression strongly induced by arsenic[1][2][3][4][5]
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Contents
Community Commentary
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DNA and RNA Details
Other DNA and RNA Details
Other Topic: expression
Specifically higher expression in sulfur limited chemostat cultures versus sulfur excess. [6] [7]
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References
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- ↑ Eckers E, et al. (2009) Biochemical characterization of dithiol glutaredoxin 8 from Saccharomyces cerevisiae: the catalytic redox mechanism redux. Biochemistry 48(6):1410-23 SGD PMID 19166312
- ↑ Giaever G, et al. (2002) Functional profiling of the Saccharomyces cerevisiae genome. Nature 418(6896):387-91 SGD PMID 12140549
- ↑ Haugen AC, et al. (2004) Integrating phenotypic and expression profiles to map arsenic-response networks. Genome Biol 5(12):R95 SGD PMID 15575969
- ↑ Huh WK, et al. (2003) Global analysis of protein localization in budding yeast. Nature 425(6959):686-91 SGD PMID 14562095
- ↑ Mesecke N, et al. (2008) Two Novel Monothiol Glutaredoxins from Saccharomyces cerevisiae Provide Further Insight into Iron-Sulfur Cluster Binding, Oligomerization, and Enzymatic Activity of Glutaredoxins. Biochemistry 47(5):1452-63 SGD PMID 18171082
- ↑ Boer VM, et al. (2003) The genome-wide transcriptional responses of Saccharomyces cerevisiae grown on glucose in aerobic chemostat cultures limited for carbon, nitrogen, phosphorus, or sulfur. J Biol Chem 278(5):3265-74 SGD PMID 12414795
- ↑ submitted by Viktor Boer on 2003-07-25
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