Matches in Nanopublications for { ?s ?p "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 [" ?g. }
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- _6 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 [" provenance.
- _6 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 [" provenance.