Matches in Nanopublications for { ?s ?p "Insulin action on Na+, K+-ATPase was dependent on ERK1/2 in HSMCs. Insulin also increased phosphorylation and plasma membrane content of the Na+,K+-ATPase alpha1- and alpha2-subunits. The insulin induced phosphorylation at threonine and proline motif of alpha subunits inhibited by ERK1/2 inhibitors and its upstream kinase inhibitors. Results of in-vitro assay showed that ERK1/2 phosphorylated alpha subunits of Na+, K+-ATPase." ?g. }
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- _4 value "Insulin action on Na+, K+-ATPase was dependent on ERK1/2 in HSMCs. Insulin also increased phosphorylation and plasma membrane content of the Na+,K+-ATPase alpha1- and alpha2-subunits. The insulin induced phosphorylation at threonine and proline motif of alpha subunits inhibited by ERK1/2 inhibitors and its upstream kinase inhibitors. Results of in-vitro assay showed that ERK1/2 phosphorylated alpha subunits of Na+, K+-ATPase." provenance.
- _4 value "Insulin action on Na+, K+-ATPase was dependent on ERK1/2 in HSMCs. Insulin also increased phosphorylation and plasma membrane content of the Na+,K+-ATPase alpha1- and alpha2-subunits. The insulin induced phosphorylation at threonine and proline motif of alpha subunits inhibited by ERK1/2 inhibitors and its upstream kinase inhibitors. Results of in-vitro assay showed that ERK1/2 phosphorylated alpha subunits of Na+, K+-ATPase." provenance.
- _4 value "Insulin action on Na+, K+-ATPase was dependent on ERK1/2 in HSMCs. Insulin also increased phosphorylation and plasma membrane content of the Na+,K+-ATPase alpha1- and alpha2-subunits. The insulin induced phosphorylation at threonine and proline motif of alpha subunits inhibited by ERK1/2 inhibitors and its upstream kinase inhibitors. Results of in-vitro assay showed that ERK1/2 phosphorylated alpha subunits of Na+, K+-ATPase." provenance.
- _4 value "Insulin action on Na+, K+-ATPase was dependent on ERK1/2 in HSMCs. Insulin also increased phosphorylation and plasma membrane content of the Na+,K+-ATPase alpha1- and alpha2-subunits. The insulin induced phosphorylation at threonine and proline motif of alpha subunits inhibited by ERK1/2 inhibitors and its upstream kinase inhibitors. Results of in-vitro assay showed that ERK1/2 phosphorylated alpha subunits of Na+, K+-ATPase." provenance.
- _4 value "Insulin action on Na+, K+-ATPase was dependent on ERK1/2 in HSMCs. Insulin also increased phosphorylation and plasma membrane content of the Na+,K+-ATPase alpha1- and alpha2-subunits. The insulin induced phosphorylation at threonine and proline motif of alpha subunits inhibited by ERK1/2 inhibitors and its upstream kinase inhibitors. Results of in-vitro assay showed that ERK1/2 phosphorylated alpha subunits of Na+, K+-ATPase." provenance.
- _4 value "Insulin action on Na+, K+-ATPase was dependent on ERK1/2 in HSMCs. Insulin also increased phosphorylation and plasma membrane content of the Na+,K+-ATPase alpha1- and alpha2-subunits. The insulin induced phosphorylation at threonine and proline motif of alpha subunits inhibited by ERK1/2 inhibitors and its upstream kinase inhibitors. Results of in-vitro assay showed that ERK1/2 phosphorylated alpha subunits of Na+, K+-ATPase." provenance.
- _4 value "Insulin action on Na+, K+-ATPase was dependent on ERK1/2 in HSMCs. Insulin also increased phosphorylation and plasma membrane content of the Na+,K+-ATPase alpha1- and alpha2-subunits. The insulin induced phosphorylation at threonine and proline motif of alpha subunits inhibited by ERK1/2 inhibitors and its upstream kinase inhibitors. Results of in-vitro assay showed that ERK1/2 phosphorylated alpha subunits of Na+, K+-ATPase." provenance.
- _4 value "Insulin action on Na+, K+-ATPase was dependent on ERK1/2 in HSMCs. Insulin also increased phosphorylation and plasma membrane content of the Na+,K+-ATPase alpha1- and alpha2-subunits. The insulin induced phosphorylation at threonine and proline motif of alpha subunits inhibited by ERK1/2 inhibitors and its upstream kinase inhibitors. Results of in-vitro assay showed that ERK1/2 phosphorylated alpha subunits of Na+, K+-ATPase." provenance.
- _4 value "Insulin action on Na+, K+-ATPase was dependent on ERK1/2 in HSMCs. Insulin also increased phosphorylation and plasma membrane content of the Na+,K+-ATPase alpha1- and alpha2-subunits. The insulin induced phosphorylation at threonine and proline motif of alpha subunits inhibited by ERK1/2 inhibitors and its upstream kinase inhibitors. Results of in-vitro assay showed that ERK1/2 phosphorylated alpha subunits of Na+, K+-ATPase." provenance.
- _4 value "Insulin action on Na+, K+-ATPase was dependent on ERK1/2 in HSMCs. Insulin also increased phosphorylation and plasma membrane content of the Na+,K+-ATPase alpha1- and alpha2-subunits. The insulin induced phosphorylation at threonine and proline motif of alpha subunits inhibited by ERK1/2 inhibitors and its upstream kinase inhibitors. Results of in-vitro assay showed that ERK1/2 phosphorylated alpha subunits of Na+, K+-ATPase." provenance.