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:_6 ;
    pav:version "1.4" .
  sub:_5 prov:value "Activation of PKC-a mediated the sustained decrease in mitochondrial membrane hyperpolarisation and oxidative phosphorylation but not the decrease in electron transfer rate. Sustained mitochondrial dysfunction was also affected by ERK1/2, through a PKC-independent pathway. These findings suggest that activation of PKC-a and/or ERK1/2 lead to decreased activity of ATP synthase, rather than affecting OXPHOS system complexes [40]. Indeed, the a, b, and e subunits of F(1)F(0)- ATPase have PKC consensus motifs [41]. PKC-a phosphorylated the b subunit of F(1)F(0)-ATPase on a serine residue and decreased F(0)F(1)-ATPase activity, oxidative phosphorylation and ATP production [41]." ;
    prov:wasQuotedFrom pubmed:16568236 .
  sub:_6 rdfs:label "Selventa" .
  sub:assertion prov:hadPrimarySource pubmed:16568236 ;
    prov:wasDerivedFrom beldoc: , sub:_5 .
}