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:_6 prov:value "Several types of proteolytic enzymes have been identified to specifically degrade the proteins of the extracellular matrix: matrix metalloproteinases (MMPs) [5], cysteine proteases [6], and serine proteases [7]. Serine protease urokinase-type plasminogen activator (uPA) is a protease that cleaves the extracellular matrix and stimulates the conversion of plasminogen to plasmin [8]. Plasmin mediates invasion directly, by degrading matrix proteins such as collagen IV, fibronectin, and laminin, or indirectly, by activating matrix metalloproteinases MMP-2, -3, and -9 and serine protease uPA [9-12]. uPA exerts its nonproteolytic activity through its interaction with uPA receptor (uPAR), which forms the complex with integrins and controls cell adhesion and cell migration [" ;
    prov:wasQuotedFrom pubmed:15180498 .
  sub:_7 rdfs:label "Selventa" .
  sub:assertion prov:hadPrimarySource pubmed:15180498 ;
    prov:wasDerivedFrom beldoc: , sub:_6 .
}