Difference between revisions of "YDR172W"

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{|{{Prettytable}} align = 'right' width = '200px'
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?locus=YDR172W YDR172W]  
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|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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'''Description of {{PAGENAME}}:''' 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
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'''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

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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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References

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  1. 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
  2. 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
  3. 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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