Nanopublications

Matches in Nanopublications for { ?s ?p ?o <http://www.tkuhn.ch/bel2nanopub/RAdBPS50v1mICbvkZq3Pdd8Zgd59oInE-XfJsNmfxOz20#provenance>. }

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_5 label "Selventa" provenance.
_5 comment "support@belframework.org" provenance.
small_corpus.bel title "BEL Framework Small Corpus Document" provenance.
small_corpus.bel description "Approximately 2000 hand curated statements drawn from 57 PubMeds." provenance.
small_corpus.bel version "1.6" provenance.
small_corpus.bel authoredBy _5 provenance.
assertion wasDerivedFrom _4 provenance.
assertion wasDerivedFrom small_corpus.bel provenance.
assertion hadPrimarySource 11035810 provenance.
_4 wasQuotedFrom 11035810 provenance.
_4 value "In Rat1, NIH 3T3, and HEK293 cells, increases in the intracellular levels of cAMP stimulate phosphorylation of GSK-3α and -β, as demonstrated by immunoblotting with GSK-3 phosphorylation-specific antibodies. As shown in Fig. 1, the cell-permeable cAMP analogue 8-Br-cAMP induced a marked increase in phosphorylation of GSK-3α and - β at serine 21 and 9, respectively, whereas the structurally related cGMP analogue 8-Br-cGMP had little effect. Forskolin, which activates adenyl cyclase thus raising intracellular cAMP levels (15), triggered a similar elevation in GSK-3 phosphorylation at serine 21 and 9. In Rat1 cells, isoproterenol, which activates the b-adrenergic receptor stimulating adenylate cyclase and increasing endogenous cAMP levels (16, 17), also efficiently stimulated GSK-3 phosphorylation at these serine sites. In NIH 3T3 cells that contain few of the β-adrenergic receptors, stimulation with other G-protein-coupled receptor agonists, such as lysophosphatidic acid. also led to GSK-3 phosphorylation (data not shown)" provenance.
small_corpus.bel license "Creative Commons Attribution-Non-Commercial-ShareAlike 3.0 Unported License" provenance.