Matches in Nanopublications for { ?s ?p "The repression of MEF2 transcriptional activation by class II HDACs is regulated by the phosphorylation status of HDAC in a variety of cell types. Dephosphorylated HDAC remains within the nucleus and represses MEF2 activity. In response to activation of calmodulin-dependent protein kinase (CaMK), HDAC becomes phosphorylated (Kao et al., 2001). Phosphorylated HDAC binds to the chaperone protein 14-3-3 (Van Hemert et al., 2001) within the nucleus and moves out of the nucleus via the nuclear export protein CRM1 in complex with 14-3-3 (Grozinger and Schreiber, 2000; McKinsey et al., 2001)." ?g. }
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- _10 value "The repression of MEF2 transcriptional activation by class II HDACs is regulated by the phosphorylation status of HDAC in a variety of cell types. Dephosphorylated HDAC remains within the nucleus and represses MEF2 activity. In response to activation of calmodulin-dependent protein kinase (CaMK), HDAC becomes phosphorylated (Kao et al., 2001). Phosphorylated HDAC binds to the chaperone protein 14-3-3 (Van Hemert et al., 2001) within the nucleus and moves out of the nucleus via the nuclear export protein CRM1 in complex with 14-3-3 (Grozinger and Schreiber, 2000; McKinsey et al., 2001)." provenance.
- _10 value "The repression of MEF2 transcriptional activation by class II HDACs is regulated by the phosphorylation status of HDAC in a variety of cell types. Dephosphorylated HDAC remains within the nucleus and represses MEF2 activity. In response to activation of calmodulin-dependent protein kinase (CaMK), HDAC becomes phosphorylated (Kao et al., 2001). Phosphorylated HDAC binds to the chaperone protein 14-3-3 (Van Hemert et al., 2001) within the nucleus and moves out of the nucleus via the nuclear export protein CRM1 in complex with 14-3-3 (Grozinger and Schreiber, 2000; McKinsey et al., 2001)." provenance.