sub:provenance {
  beldoc: dce:description "Approximately 61,000 statements." ;
    dce:rights "Copyright (c) 2011-2012, Selventa. All rights reserved." ;
    dce:title "BEL Framework Large Corpus Document" ;
    pav:authoredBy sub:_7 ;
    pav:version "1.4" .
  sub:_5 dce:identifier "Biochemistry of Lipids, Lipoproteins and Membranes 2002 - Chapter 10" ;
    dce:title "Biochemistry of Lipids, Lipoproteins and Membranes 2002 - Chapter 10" ;
    dce:type "Book" .
  sub:_6 prov:value "The insulin receptor tyrosine kinase is capable of inducing phosphorylation and activation of the cGMP-inhibited phosphodiesterase and several protein serine phosphatases (most likely protein phosphatases 1, 2A, and 2C). Phosphatidyl inositol 3-kinase A has been demonstrated as an essential component in the insulin-stimulated activation of the cGMP-inhibited phosphodiesterase but, as previously mentioned, Protein kinase A can also fullfill this this role in the absence of insulin.  Thus, insulin inhibits the cAMP cascade (including the activation of hormone senstive lipase) through cleavage of cAMP and direct dephosphorlyation of protein kinase A-activated substrates Dephosphrylation also activates acetyl-CoA carboxylase, the enzyment that catalyzes the first committed step in de novo fatty acid synthesis, and fatty acyl-CoA synthetase, the first enzyme in the triacylglycerol synthetic pathway." ;
    prov:wasQuotedFrom sub:_5 .
  sub:_7 rdfs:label "Selventa" .
  sub:assertion prov:hadPrimarySource sub:_5 ;
    prov:wasDerivedFrom beldoc: , sub:_6 .
}