Difference between revisions of "YDR172W"
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| − | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl? | + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000002579 YDR172W] |
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''SUP35 '' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name''' ||''SUP35 '' | ||
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Coordinates''' | ||
|nowrap| Chr IV:808321..810378 | |nowrap| Chr IV:808321..810378 | ||
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| + | |valign="top" nowrap bgcolor="{{SGDblue}}"| '''Primary SGDID''' || S000002579 | ||
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<br> | <br> | ||
| − | '''Description of | + | '''Description of YDR172W:''' Translation termination factor eRF3; altered protein conformation creates the [PSI(+)] prion, a dominant cytoplasmically inherited protein aggregate that alters translational fidelity and creates a nonsense suppressor phenotype<ref name='S000080146'>Salnikova AB, et al. (2005) Nonsense suppression in yeast cells overproducing Sup35 (eRF3) is caused by its non-heritable amyloids. J Biol Chem 280(10):8808-12 {{SGDpaper|S000080146}} PMID 15618222</ref><ref name='S000079668'>Derkatch IL, et al. (2004) Effects of Q/N-rich, polyQ, and non-polyQ amyloids on the de novo formation of the [PSI+] prion in yeast and aggregation of Sup35 in vitro. Proc Natl Acad Sci U S A 101(35):12934-9 {{SGDpaper|S000079668}} PMID 15326312</ref><ref name='S000079184'>Lindquist S, et al. (2001) Investigating protein conformation-based inheritance and disease in yeast. Philos Trans R Soc Lond B Biol Sci 356(1406):169-76 |
{{SGDpaper|S000079184}} PMID 11260797</ref> | {{SGDpaper|S000079184}} PMID 11260797</ref> | ||
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J Biol Chem 278(5):3265-74</ref> | J Biol Chem 278(5):3265-74</ref> | ||
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Revision as of 08:46, 27 February 2007
Share your knowledge...Edit this entry! <protect>
| Systematic name | YDR172W |
| Gene name | SUP35 |
| Aliases | GST1, PNM2, SAL3, SUF12, SUP2, SUP36, [PSI(+)], [PSI] |
| Feature type | ORF, Verified |
| Coordinates | Chr IV:808321..810378 |
| Primary SGDID | S000002579 |
Description of YDR172W: Translation termination factor eRF3; altered protein conformation creates the [PSI(+)] prion, a dominant cytoplasmically inherited protein aggregate that alters translational fidelity and creates a nonsense suppressor phenotype[1][2][3]
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Contents
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References
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- Jump up ↑ Salnikova AB, et al. (2005) Nonsense suppression in yeast cells overproducing Sup35 (eRF3) is caused by its non-heritable amyloids. J Biol Chem 280(10):8808-12 SGD PMID 15618222
- Jump up ↑ Derkatch IL, et al. (2004) Effects of Q/N-rich, polyQ, and non-polyQ amyloids on the de novo formation of the [PSI+] prion in yeast and aggregation of Sup35 in vitro. Proc Natl Acad Sci U S A 101(35):12934-9 SGD PMID 15326312
- Jump up ↑ Lindquist S, et al. (2001) Investigating protein conformation-based inheritance and disease in yeast. Philos Trans R Soc Lond B Biol Sci 356(1406):169-76 SGD PMID 11260797
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