Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.molcel.2009.02.015
DC FieldValue
dc.titleFrom Promiscuity to Precision: Protein Phosphatases Get a Makeover
dc.contributor.authorVirshup, D.M.
dc.contributor.authorShenolikar, S.
dc.date.accessioned2016-12-13T05:39:15Z
dc.date.available2016-12-13T05:39:15Z
dc.date.issued2009-03-13
dc.identifier.citationVirshup, D.M., Shenolikar, S. (2009-03-13). From Promiscuity to Precision: Protein Phosphatases Get a Makeover. Molecular Cell 33 (5) : 537-545. ScholarBank@NUS Repository. https://doi.org/10.1016/j.molcel.2009.02.015
dc.identifier.issn10972765
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/133023
dc.description.abstractThe control of biological events requires strict regulation using complex protein phosphorylation and dephosphorylation strategies. The bulk of serine-threonine dephosphorylations are catalyzed by a handful of phosphatase catalytic subunits, giving rise to the misconception that these phosphatases are promiscuous and unregulated enzymes in vivo. The reality is much more nuanced: PP1 and PP2A, the most abundant serine-threonine phosphatases, are, in fact, families of hundreds of protein serine/threonine phosphatases, assembled from a few catalytic subunits in combination with a highly diverse array of regulators. As recent publications illustrate, these regulatory subunits confer specificity, selectivity, localization, and regulation on these important enzymes. © 2009 Elsevier Inc. All rights reserved.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/j.molcel.2009.02.015
dc.sourceScopus
dc.typeReview
dc.contributor.departmentDUKE-NUS GRADUATE MEDICAL SCHOOL S'PORE
dc.description.doi10.1016/j.molcel.2009.02.015
dc.description.sourcetitleMolecular Cell
dc.description.volume33
dc.description.issue5
dc.description.page537-545
dc.description.codenMOCEF
dc.identifier.isiut000264237800001
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