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:_4 ;
    pav:version "1.4" .
  sub:_3 prov:value "TNF-alpha mediates insulin resistance via serine phosphorylation of insulin receptor substrate (IRS-1) in skeletal muscle, which inhibits the ability of insulin to stimulate GLUT-4 translocation to the cell membrane and therefore reduces glucose uptake (43). Conversely, inhibition of TNF-alpha results in increased insulin-stimulated IRS-1 tyrosine phosphorylation (10, 43). The ability of TNF-alpha to serine phosphorylate IRS-1 may be mediated via diacylglycerol (DAG). Incubating intact rat skeletal muscle strips with TNF-alpha significantly increased palmitate incorporation into DAG (7). This is important because DAGs are known activators of conventional and novel protein kinase C isoforms that serine phosphorylate, and thus inhibit, IRS-1." ;
    prov:wasQuotedFrom pubmed:16020439 .
  sub:_4 rdfs:label "Selventa" .
  sub:assertion prov:hadPrimarySource pubmed:16020439 ;
    prov:wasDerivedFrom beldoc: , sub:_3 .
}