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)

[search][options]

Editor

Personal info

View

About

Terms

Javascript disabled

Please enable Javascript support in your browser to use this application.

Instructions on how to enable JavaScript on different browsers can be found here: http://www.google.com/support/bin/answer.py?answer=23852.

[edit this page]

Neckameyer, W.S. et al.

Neckameyer, Holt, Paradowski,

Biochemical conservation of recombinant Drosophila tyrosine hydroxylase with its mammalian cognates.

Dopamine modulates several behavioral and developmental events; in the fruit fly Drosophila melanogaster, dopamine is a neurotransmitter, a neuromodulator, and a developmental signal. Studies in mammals suggest that these diverse roles for dopamine have been evolutionarily conserved. Fundamental regulation of dopamine occurs via tyrosine hydroxylase (TH), the first and rate-limiting enzyme in the catecholamine biosynthetic pathway. Mammalian TH is acutely regulated via phosphorylation-dephosphorylation mechanisms, which occur as a direct consequence of nerve stimulation. We have shown that the Drosophila homolog of TH, DTH, shares over 50% sequence identity with mammalian TH, and the serine residue corresponding to the major site of phosphorylation is conserved. We demonstrate using recombinant DTH protein generated in E. coli that its regulatory biochemical mechanisms closely parallel those from mammals. Drosophila thus provides a highly conserved and tractable model system in which to test the functional consequences of perturbing TH activity by acute regulatory mechanisms.[1]

References

Biochemical conservation of recombinant Drosophila tyrosine hydroxylase with its mammalian cognates. Neckameyer, W.S., Holt, B., Paradowski, T.J. Biochem. Genet. (2005) [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 WikiGenes Open Access Licence Privacy Policy Terms of Use apsburg