Nanopublications

Matches in Nanopublications for { ?s ?p ?o <http://www.tkuhn.ch/bel2nanopub/RAP7Ybub14v1iBjxg6ZAvNMAX3N9xXx9F-X2SREH-QiMU#provenance>. }

Showing items 1 to 11 of 11 with 100 items per page.

_6 label "Selventa" provenance.
large_corpus.bel title "BEL Framework Large Corpus Document" provenance.
large_corpus.bel description "Approximately 61,000 statements." provenance.
large_corpus.bel version "20131211" provenance.
large_corpus.bel authoredBy _6 provenance.
assertion wasDerivedFrom large_corpus.bel provenance.
assertion wasDerivedFrom _5 provenance.
assertion hadPrimarySource 11257494 provenance.
_5 wasQuotedFrom 11257494 provenance.
_5 value "In unstimulated cells, GSK3 is active and contributes significantly towards the phosphorylation and inhibition of glycogen synthase [12]. Insulin stimulates glycogen synthesis both by inactivating GSK3 and also by promoting the dephosphorylation of glycogen synthase. The inactivation of GSK3 and GSK3 is achieved through phosphorylation of Ser21 and Ser9, respectively [12], and this is mediated by PKB in a PI3K-dependent fashion. Thus PI3K, PDK, PKB and GSK3 constitute one important arm of the insulin signalling cascade regulating glycogen synthesis. In addition to inducing an increase in glucose transport, over-expression of PKB elicited an inhibition of GSK3 and a concomitant increase in glycogen and protein synthesis a decrease in insulin-stimulated GLUT4 translocation, glucose transport and membrane ruffling, which coincided with reduced phosphorylation of PKB and p70S6K but normal phosphorylation of p42/44 MAPK observed an inhibition of PKB phosphorylation and downstream p70S6K activation, which was attributable to a PP2A-type phosphatase activity Akt phosphorylates and inactivates GSK-3, decreasing the rate of phosphorylation of glycogen synthase" provenance.