Matches in Nanopublications for { ?s ?p "the association between MEKK3 and 14-3-3 was dependent on Ser526 and prevented dephosphorylation of Ser526. Endogenous MEKK3 was phosphorylated on Ser526 in response to osmotic stress. In addition, phosphorylation of Ser526 was required for MKK6 phosphorylation in vitro, whereas dephosphorylation of Ser526 was mediated by protein phosphatase 2A and sensitive to okadaic acid and sodium fluoride." ?g. }
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- _3 value "the association between MEKK3 and 14-3-3 was dependent on Ser526 and prevented dephosphorylation of Ser526. Endogenous MEKK3 was phosphorylated on Ser526 in response to osmotic stress. In addition, phosphorylation of Ser526 was required for MKK6 phosphorylation in vitro, whereas dephosphorylation of Ser526 was mediated by protein phosphatase 2A and sensitive to okadaic acid and sodium fluoride." provenance.
- _4 value "the association between MEKK3 and 14-3-3 was dependent on Ser526 and prevented dephosphorylation of Ser526. Endogenous MEKK3 was phosphorylated on Ser526 in response to osmotic stress. In addition, phosphorylation of Ser526 was required for MKK6 phosphorylation in vitro, whereas dephosphorylation of Ser526 was mediated by protein phosphatase 2A and sensitive to okadaic acid and sodium fluoride." provenance.
- _4 value "the association between MEKK3 and 14-3-3 was dependent on Ser526 and prevented dephosphorylation of Ser526. Endogenous MEKK3 was phosphorylated on Ser526 in response to osmotic stress. In addition, phosphorylation of Ser526 was required for MKK6 phosphorylation in vitro, whereas dephosphorylation of Ser526 was mediated by protein phosphatase 2A and sensitive to okadaic acid and sodium fluoride." provenance.
- _3 value "the association between MEKK3 and 14-3-3 was dependent on Ser526 and prevented dephosphorylation of Ser526. Endogenous MEKK3 was phosphorylated on Ser526 in response to osmotic stress. In addition, phosphorylation of Ser526 was required for MKK6 phosphorylation in vitro, whereas dephosphorylation of Ser526 was mediated by protein phosphatase 2A and sensitive to okadaic acid and sodium fluoride." provenance.