Difference between revisions of "YBR014C"

From SGD-Wiki
Jump to: navigation, search
(Automated import of articles)
(Automated import of articles)
Line 18: Line 18:
 
|}
 
|}
 
<br>
 
<br>
'''Description of YBR014C:''' Monothiol glutaredoxin; more similar in activity to dithiol than other monothiol glutaredoxins; membrane localized; forms homodimers; does not bind metal ions<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><ref name='S000123913'>Herrero E and Izquierdo A (2007)    {{SGDpaper|S000123913}} PMID </ref><ref name='S000075303'>Terashima H, et al. (2002) Sequence-based approach for identification of cell wall proteins in Saccharomyces cerevisiae. Curr Genet 40(5):311-6 {{SGDpaper|S000075303}} PMID 11935221</ref><ref name='S000060381'>Fetrow JS, et al. (2001) Genomic-scale comparison of sequence- and structure-based methods of function prediction: does structure provide additional insight? Protein Sci 10(5):1005-14
+
'''Description of YBR014C:''' Cis-golgi localized monothiol glutaredoxin; more similar in activity to dithiol than other monothiol glutaredoxins; involved in the oxidative stress response; does not bind metal ions; functional overlap with GRX6<ref name='S000126041'>Mesecke N, et al. (2008) A Novel Group of Glutaredoxins in the cis-Golgi Critical for Oxidative Stress Resistance. Mol Biol Cell  {{SGDpaper|S000126041}} PMID 18400945</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><ref name='S000123913'>Herrero E and Izquierdo A (2007)    {{SGDpaper|S000123913}} PMID </ref><ref name='S000075303'>Terashima H, et al. (2002) Sequence-based approach for identification of cell wall proteins in Saccharomyces cerevisiae. Curr Genet 40(5):311-6 {{SGDpaper|S000075303}} PMID 11935221</ref><ref name='S000060381'>Fetrow JS, et al. (2001) Genomic-scale comparison of sequence- and structure-based methods of function prediction: does structure provide additional insight? Protein Sci 10(5):1005-14
 
  {{SGDpaper|S000060381}} PMID 11316881</ref>
 
  {{SGDpaper|S000060381}} PMID 11316881</ref>
 
<br>
 
<br>

Revision as of 14:05, 14 April 2008

Share your knowledge...Edit this entry! <protect>

Systematic name YBR014C
Gene name GRX7
Aliases
Feature type ORF, Verified
Coordinates Chr II:267336..266725
Primary SGDID S000000218


Description of YBR014C: Cis-golgi localized monothiol glutaredoxin; more similar in activity to dithiol than other monothiol glutaredoxins; involved in the oxidative stress response; does not bind metal ions; functional overlap with GRX6[1][2][3][4][5]




</protect>

Community Commentary

About Community Commentary. Please share your knowledge!




<protect>

References

See Help:References on how to add references

  1. Mesecke N, et al. (2008) A Novel Group of Glutaredoxins in the cis-Golgi Critical for Oxidative Stress Resistance. Mol Biol Cell SGD PMID 18400945
  2. 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
  3. Herrero E and Izquierdo A (2007) SGD PMID
  4. Terashima H, et al. (2002) Sequence-based approach for identification of cell wall proteins in Saccharomyces cerevisiae. Curr Genet 40(5):311-6 SGD PMID 11935221
  5. Fetrow JS, et al. (2001) Genomic-scale comparison of sequence- and structure-based methods of function prediction: does structure provide additional insight? Protein Sci 10(5):1005-14 SGD PMID 11316881

See Help:Categories on how to add the wiki page for this gene to a Category </protect>