The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Editor

Share

Personal info

View

Links

About

Terms

 

 
 
 Bouton,  
 

Nitrosative and oxidative modulation of iron regulatory proteins.

Cytokine-driven nitric oxide (NO) synthase II provides cells with effectors for reactions at redox-sensitive site(s) of proteins. Iron regulatory proteins (IRP1 and IRP2), two post-transcriptional regulators of gene expression, are particularly sensitive to NO synthesis and to oxidative stress. IRP1 possesses a redox-active Fe-S cluster and can also exhibit aconitase activity. IRP2 has no Fe-S cluster but exhibits several redox-sensitive cysteine residues. Under proper redox conditions, both IRPs bind to iron-responsive elements in the untranslated region of mRNAs encoding proteins involved in iron metabolism and energy production. This review describes and compares the effects of NO, peroxynitrite, and reactive oxygen species on these two chemosensitive proteins.[1]

References

  1. Nitrosative and oxidative modulation of iron regulatory proteins. Bouton, C. Cell. Mol. Life Sci. (1999) [Pubmed]
Annotations and hyperlinks in this abstract are from individual authors of WikiGenes or automatically generated by the WikiGenes Data Mining Engine. The abstract is from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenesOpen Access LicencePrivacy PolicyTerms of Useapsburg
 
WikiGenes - Universities