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)
 
 
 
 
 

Binding specificities of adenosine aminohydrolase from calf intestinal mucosa with dialdehydes derived from hexofuranosyladenine nucleosides.

A series of nucleoside dialdehydes has been prepared as powders after treatment of hexofuranosyladenine nucleosides with paraperiodic acid; thus, periodate oxidation and purification of the products yielded dialdehydes derived from 9-(6-deoxy-beta-D-gulofuranosyl)adenine (1), 9-(6-deoxy-beta-L-gulofuranosyl)adenine (2), 9-(alpha-D-rhamnofuranosyl)adenine (3), 9-(alpha-L-rhamnofuranosyl)adenine (4), 9-(6-deoxy-alpha-L-talofuranosyl)adenine (5), 9-(5,6-dideoxy-beta-L-ribo-hex-5-enofuranosyl)adenine (6), and 9-(5,6-dideoxy-beta-D-ribo-hex-5-enofuranosyl)adenine (7). Nucleoside dialdehydes 1, 4, and 5 were weak substrates for adenosine aminohydrolase from calf intestinal mucosa. Dialdehydes 6 and 7 were not substrates for the enzyme but were rather strong competitive inhibitors, with Ki values of 50 and 7 microM, respectively. Dialdehydes 2 and 3 did not bind to the enzyme at all. The dialdehydes did not exhibit time-dependent inhibition, suggesting that they did not form covalent bonds with the protein.[1]

References

 
WikiGenes - Universities