Great News, our review on how phosphatase specificity is controlled during mitosis has been re-published in BioEssays and is now Online!
This review was originally published in Inside the Cell, which unfortunately has shut down.
But the good news is that it is still Open Access, so that means its free for everyone to read! And is now also indexed in PubMed
During mitotic exit, phosphatases reverse thousands of phosphorylation events in a specific temporal order to ensure that cell division occurs correctly. This review explores how the physicochemical properties of the phosphosite and surrounding amino acids affect interactions with phosphatase/s and help determine the dephosphorylation of individual phosphorylation sites during mitotic exit.
The Full-text download for the Article can be found here [Link]
Citation: Rogers, S. et al. (2016) Mechanisms regulating phosphatase specificity and the removal of individual phosphorylation sites during mitotic exit. BioEssays, 38, S24–S32.
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This entry was posted in News and tagged amino acid, BioEssays, Cell cycle, cell division, dephosphorylation, Garvan, kinase, metaphase, mitotic exit, Open Access, phosphatase, phosphorylation, phosphosite, PP1, PP2A.