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)
 
 
 
 
 

Protein phosphatase-2A modulates the serine and tyrosine phosphorylation of paxillin in Lewis lung carcinoma tumor variants.

Cellular adhesion and motility, processes regulated by focal adhesion assembly and disassembly, can influence a tumor cell's ability to metastasize. Focal adhesion dynamics are, in turn, influenced by the serine and tyrosine phosphorylation state of paxillin. Using Lewis lung carcinoma (LLC) tumor variants, this study shows the importance of the serine/threonine protein phosphatase-2A (PP-2A) in maintaining adherence and restricting tumor cell motility, and modulating the serine and tyrosine phosphorylation of paxillin. Treating non-metastatic LLC-C8 tumor variants with okadaic acid to inhibit PP-2A activity resulted in cell rounding and increased motility. These effects on motility and adherence were accompanied by increased serine and decreased tyrosine phosphorylation of paxillin. These results suggest PP-2A regulation of paxillin phosphorylation may have a role in controlling tumor cell adherence and motility.[1]

References

 
WikiGenes - Universities