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In vivo, this reaction may occur primarily on the surfaces of endothelial cells in response to platelet activation (Lin et al. 1997; Motta et al. 1998; Mahdi et al. 2003)."}],"citations":["publicationXrefaa7","publicationXreff84","publicationXrefa08","publicationXrefae0"],"drawAs":"SegmentedLine","zIndex":12288,"borderWidth":1,"points":[{"x":2350,"y":780,"isAttachedTo":"n1386","attachmentDisplay":{"position":[0.5348837209302325,1],"offset":[0,2.9999999999999973]},"orientation":[0,1]},{"x":2359,"y":811,"isAttachedTo":"f7df9","attachmentDisplay":{"position":[0,0],"offset":[],"relativeOffset":[0,0]},"orientation":[]}],"color":"#000000","backgroundColor":"none","dbConventionalName":"Reactome","dbId":"REACT_1335","type":["Interaction","Edge"],"kaavioType":"Edge","gpmlElementName":"Interaction","isAttachedTo":["n1386","e_1385"]},"e_1385_a_i1":{"id":"e_1385_a_i1","comments":[{"source":"Reactome","content":"Prekallikrein (PK) associates specifically with kininogen (HK) on cell surfaces. 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In the body, this reaction appears to occur on the surfaces of endothelial cells and may require the presence of activated platelets. Recent work indicates that the protease that cleaves prekallikrein under these conditions is prolylcarboxypeptidase. Although this enzyme was originally isolated from lysosomes (Odya et al. 1978; Tan et al. 1993), it is associated with plasma membranes of cultured human endothelial cells in vitro (Moreira et al. 2002; Shariat-Madar et al. 2002), and the purified recombinant enzyme efficiently cleaves prekallikrein (Shariat-Madar et al. 2004). In contrast factor XII, despite its activity on prekallikrein in vitro, appears not to be responsible for prekallikrein activation on the cell surface (Rojkjaer et al. 1998)."}],"citations":["publicationXrefeb9","publicationXrefb66","publicationXrefffe","publicationXrefe60","publicationXrefa1a"],"drawAs":"SegmentedLine","zIndex":12288,"borderWidth":1,"points":[{"x":895,"y":789,"isAttachedTo":"n1387","attachmentDisplay":{"position":[0.24242424242424243,1],"offset":[0,3]},"orientation":[0,1]},{"x":820,"y":790,"isAttachedTo":"n1389","attachmentDisplay":{"position":[0.8034188034188035,1],"offset":[0,3.0000000000000036]},"orientation":[0,-1]}],"color":"#000000","backgroundColor":"none","dbConventionalName":"Reactome","dbId":"REACT_6","type":["Interaction","Edge","SBO:0000167","SBO:0000393","SBO:0000394","DirectedInteraction"],"kaavioType":"Edge","gpmlElementName":"Interaction","markerEnd":"Arrow","isAttachedTo":["n1387","n1389"],"burrs":["d1148"]},"d1148":{"attachmentDisplay":{"position":[0.5,0],"offset":[0,0]},"drawAs":"none","id":"d1148","isAttachedTo":"e_1388","borderWidth":0,"height":0,"width":0,"zIndex":12288,"type":["Anchor","Burr"],"kaavioType":"Burr","gpmlElementName":"Anchor"},"e_1388_c_0":{"id":"e_1388_c_0","comments":[{"source":"Reactome","content":"Prekallikrein in a complex with kininogen and C1q binding protein on the plasma membrane is cleaved to generate active kallikrein, which remains bound to the complex. In the body, this reaction appears to occur on the surfaces of endothelial cells and may require the presence of activated platelets. Recent work indicates that the protease that cleaves prekallikrein under these conditions is prolylcarboxypeptidase. Although this enzyme was originally isolated from lysosomes (Odya et al. 1978; Tan et al. 1993), it is associated with plasma membranes of cultured human endothelial cells in vitro (Moreira et al. 2002; Shariat-Madar et al. 2002), and the purified recombinant enzyme efficiently cleaves prekallikrein (Shariat-Madar et al. 2004). In contrast factor XII, despite its activity on prekallikrein in vitro, appears not to be responsible for prekallikrein activation on the cell surface (Rojkjaer et al. 1998)."},{"source":"Reactome","content":"Prekallikrein in a complex with kininogen and C1q binding protein on the plasma membrane is cleaved to generate active kallikrein, which remains bound to the complex. In the body, this reaction appears to occur on the surfaces of endothelial cells and may require the presence of activated platelets. Recent work indicates that the protease that cleaves prekallikrein under these conditions is prolylcarboxypeptidase. Although this enzyme was originally isolated from lysosomes (Odya et al. 1978; Tan et al. 1993), it is associated with plasma membranes of cultured human endothelial cells in vitro (Moreira et al. 2002; Shariat-Madar et al. 2002), and the purified recombinant enzyme efficiently cleaves prekallikrein (Shariat-Madar et al. 2004). In contrast factor XII, despite its activity on prekallikrein in vitro, appears not to be responsible for prekallikrein activation on the cell surface (Rojkjaer et al. 1998)."}],"citations":["publicationXrefeb9","publicationXrefb66","publicationXrefffe","publicationXrefe60","publicationXrefa1a"],"drawAs":"SegmentedLine","zIndex":12288,"borderWidth":1,"points":[{"x":695,"y":784,"isAttachedTo":"n1390","attachmentDisplay":{"position":[0.8818897637795275,1],"offset":[0,3.000000000000001]},"orientation":[0,1]},{"x":859,"y":820,"isAttachedTo":"d1148","attachmentDisplay":{"position":[0.5,0],"offset":[],"relativeOffset":[0.25,14.75]},"orientation":[]}],"color":"#000000","backgroundColor":"none","dbConventionalName":"Reactome","dbId":"REACT_6","type":["Interaction","Edge"],"kaavioType":"Edge","gpmlElementName":"Interaction","markerEnd":"MimCatalysis","isAttachedTo":["n1390","e_1388"]},"e_1391":{"id":"e_1391","comments":[{"source":"Reactome","content":"The cleavage of kininogen (HK, high molecular weight kininogen) yields activated kininogen and the vasoactive peptide bradykinin (Kerbirou and Griffin 1979; Lottspeich et al. 1985; Kellerman et al. 1986). In vivo, this reaction is catalyzed by activated kallikrein, takes places within the kallikrein:kininogen:C1q binding protein tetramer complex on the endothelial cell surface, and results in the release of kallikrein and bradykinin (Motta et al. 1998). The hormonal functions of bradykinin will be annotated in a future version of Reactome."},{"source":"Reactome","content":"The cleavage of kininogen (HK, high molecular weight kininogen) yields activated kininogen and the vasoactive peptide bradykinin (Kerbirou and Griffin 1979; Lottspeich et al. 1985; Kellerman et al. 1986). In vivo, this reaction is catalyzed by activated kallikrein, takes places within the kallikrein:kininogen:C1q binding protein tetramer complex on the endothelial cell surface, and results in the release of kallikrein and bradykinin (Motta et al. 1998). The hormonal functions of bradykinin will be annotated in a future version of Reactome."}],"citations":["publicationXreff42","publicationXrefb5c","publicationXrefd07","publicationXrefa08"],"drawAs":"SegmentedLine","zIndex":12288,"borderWidth":1,"points":[{"x":723,"y":736,"isAttachedTo":"n1389","attachmentDisplay":{"position":[0,0.19047619047619047],"offset":[-3.000000000000002,0]},"orientation":[-1,0]},{"x":511,"y":643}],"color":"#000000","backgroundColor":"none","dbConventionalName":"Reactome","dbId":"REACT_2004","type":["Interaction","Edge"],"kaavioType":"Edge","gpmlElementName":"Interaction","isAttachedTo":["n1389"],"burrs":["dd568","f014d"]},"dd568":{"attachmentDisplay":{"position":[0.99,0],"offset":[0,0]},"drawAs":"none","id":"dd568","isAttachedTo":"e_1391","borderWidth":0,"height":0,"width":0,"zIndex":12288,"type":["Anchor","Burr"],"kaavioType":"Burr","gpmlElementName":"Anchor"},"f014d":{"attachmentDisplay":{"position":[0.5,0],"offset":[0,0]},"drawAs":"none","id":"f014d","isAttachedTo":"e_1391","borderWidth":0,"height":0,"width":0,"zIndex":12288,"type":["Anchor","Burr"],"kaavioType":"Burr","gpmlElementName":"Anchor"},"e_1391_o0":{"id":"e_1391_o0","comments":[{"source":"Reactome","content":"The cleavage of kininogen (HK, high molecular weight kininogen) yields activated kininogen and the vasoactive peptide bradykinin (Kerbirou and Griffin 1979; Lottspeich et al. 1985; Kellerman et al. 1986). In vivo, this reaction is catalyzed by activated kallikrein, takes places within the kallikrein:kininogen:C1q binding protein tetramer complex on the endothelial cell surface, and results in the release of kallikrein and bradykinin (Motta et al. 1998). The hormonal functions of bradykinin will be annotated in a future version of Reactome."},{"source":"Reactome","content":"The cleavage of kininogen (HK, high molecular weight kininogen) yields activated kininogen and the vasoactive peptide bradykinin (Kerbirou and Griffin 1979; Lottspeich et al. 1985; Kellerman et al. 1986). In vivo, this reaction is catalyzed by activated kallikrein, takes places within the kallikrein:kininogen:C1q binding protein tetramer complex on the endothelial cell surface, and results in the release of kallikrein and bradykinin (Motta et al. 1998). The hormonal functions of bradykinin will be annotated in a future version of Reactome."}],"citations":["publicationXreff42","publicationXrefb5c","publicationXrefd07","publicationXrefa08"],"drawAs":"SegmentedLine","zIndex":12288,"borderWidth":1,"points":[{"x":511,"y":643,"isAttachedTo":"dd568","attachmentDisplay":{"position":[0.99,0],"offset":[],"relativeOffset":[-0.5600000000000023,0]},"orientation":[]},{"x":511,"y":729,"isAttachedTo":"n1392","attachmentDisplay":{"position":[0.48717948717948717,0],"offset":[0,-2.999999999999999]},"orientation":[0,1]}],"color":"#000000","backgroundColor":"none","dbConventionalName":"Reactome","dbId":"REACT_2004","type":["Interaction","Edge","SBO:0000167","SBO:0000393","SBO:0000394","DirectedInteraction"],"kaavioType":"Edge","gpmlElementName":"Interaction","markerEnd":"Arrow","isAttachedTo":["e_1391","n1392"]},"e_1391_o1":{"id":"e_1391_o1","comments":[{"source":"Reactome","content":"The cleavage of kininogen (HK, high molecular weight kininogen) yields activated kininogen and the vasoactive peptide bradykinin (Kerbirou and Griffin 1979; Lottspeich et al. 1985; Kellerman et al. 1986). In vivo, this reaction is catalyzed by activated kallikrein, takes places within the kallikrein:kininogen:C1q binding protein tetramer complex on the endothelial cell surface, and results in the release of kallikrein and bradykinin (Motta et al. 1998). The hormonal functions of bradykinin will be annotated in a future version of Reactome."},{"source":"Reactome","content":"The cleavage of kininogen (HK, high molecular weight kininogen) yields activated kininogen and the vasoactive peptide bradykinin (Kerbirou and Griffin 1979; Lottspeich et al. 1985; Kellerman et al. 1986). In vivo, this reaction is catalyzed by activated kallikrein, takes places within the kallikrein:kininogen:C1q binding protein tetramer complex on the endothelial cell surface, and results in the release of kallikrein and bradykinin (Motta et al. 1998). The hormonal functions of bradykinin will be annotated in a future version of Reactome."}],"citations":["publicationXreff42","publicationXrefb5c","publicationXrefd07","publicationXrefa08"],"drawAs":"SegmentedLine","zIndex":12288,"borderWidth":1,"points":[{"x":511,"y":643,"isAttachedTo":"dd568","attachmentDisplay":{"position":[0.99,0],"offset":[],"relativeOffset":[-0.5600000000000023,0]},"orientation":[]},{"x":285,"y":530,"isAttachedTo":"n1393","attachmentDisplay":{"position":[0.8412698412698413,1],"offset":[0,3.000000000000003]},"orientation":[0,-1]}],"color":"#000000","backgroundColor":"none","dbConventionalName":"Reactome","dbId":"REACT_2004","type":["Interaction","Edge","SBO:0000167","SBO:0000393","SBO:0000394","DirectedInteraction"],"kaavioType":"Edge","gpmlElementName":"Interaction","markerEnd":"Arrow","isAttachedTo":["e_1391","n1393"]},"e_1391_o2":{"id":"e_1391_o2","comments":[{"source":"Reactome","content":"The cleavage of kininogen (HK, high molecular weight kininogen) yields activated kininogen and the vasoactive peptide bradykinin (Kerbirou and Griffin 1979; Lottspeich et al. 1985; Kellerman et al. 1986). In vivo, this reaction is catalyzed by activated kallikrein, takes places within the kallikrein:kininogen:C1q binding protein tetramer complex on the endothelial cell surface, and results in the release of kallikrein and bradykinin (Motta et al. 1998). The hormonal functions of bradykinin will be annotated in a future version of Reactome."},{"source":"Reactome","content":"The cleavage of kininogen (HK, high molecular weight kininogen) yields activated kininogen and the vasoactive peptide bradykinin (Kerbirou and Griffin 1979; Lottspeich et al. 1985; Kellerman et al. 1986). In vivo, this reaction is catalyzed by activated kallikrein, takes places within the kallikrein:kininogen:C1q binding protein tetramer complex on the endothelial cell surface, and results in the release of kallikrein and bradykinin (Motta et al. 1998). The hormonal functions of bradykinin will be annotated in a future version of Reactome."}],"citations":["publicationXreff42","publicationXrefb5c","publicationXrefd07","publicationXrefa08"],"drawAs":"SegmentedLine","zIndex":12288,"borderWidth":1,"points":[{"x":511,"y":643,"isAttachedTo":"dd568","attachmentDisplay":{"position":[0.99,0],"offset":[],"relativeOffset":[-0.5600000000000023,0]},"orientation":[]},{"x":601,"y":610,"isAttachedTo":"n1394","attachmentDisplay":{"position":[0.11842105263157893,1],"offset":[0,3.000000000000003]},"orientation":[0,-1]}],"color":"#000000","backgroundColor":"none","dbConventionalName":"Reactome","dbId":"REACT_2004","type":["Interaction","Edge","SBO:0000167","SBO:0000393","SBO:0000394","DirectedInteraction"],"kaavioType":"Edge","gpmlElementName":"Interaction","markerEnd":"Arrow","isAttachedTo":["e_1391","n1394"]},"e_1391_c_0":{"id":"e_1391_c_0","comments":[{"source":"Reactome","content":"The cleavage of kininogen (HK, high molecular weight kininogen) yields activated kininogen and the vasoactive peptide bradykinin (Kerbirou and Griffin 1979; Lottspeich et al. 1985; Kellerman et al. 1986). In vivo, this reaction is catalyzed by activated kallikrein, takes places within the kallikrein:kininogen:C1q binding protein tetramer complex on the endothelial cell surface, and results in the release of kallikrein and bradykinin (Motta et al. 1998). The hormonal functions of bradykinin will be annotated in a future version of Reactome."},{"source":"Reactome","content":"The cleavage of kininogen (HK, high molecular weight kininogen) yields activated kininogen and the vasoactive peptide bradykinin (Kerbirou and Griffin 1979; Lottspeich et al. 1985; Kellerman et al. 1986). In vivo, this reaction is catalyzed by activated kallikrein, takes places within the kallikrein:kininogen:C1q binding protein tetramer complex on the endothelial cell surface, and results in the release of kallikrein and bradykinin (Motta et al. 1998). The hormonal functions of bradykinin will be annotated in a future version of Reactome."}],"citations":["publicationXreff42","publicationXrefb5c","publicationXrefd07","publicationXrefa08"],"drawAs":"SegmentedLine","zIndex":12288,"borderWidth":1,"points":[{"x":737,"y":721,"isAttachedTo":"n1389","attachmentDisplay":{"position":[0.09401709401709402,0],"offset":[0,-3.0000000000000036]},"orientation":[0,-1]},{"x":628,"y":698,"isAttachedTo":"f014d","attachmentDisplay":{"position":[0.5,0],"offset":[],"relativeOffset":[5,3.75]},"orientation":[]}],"color":"#000000","backgroundColor":"none","dbConventionalName":"Reactome","dbId":"REACT_2004","type":["Interaction","Edge"],"kaavioType":"Edge","gpmlElementName":"Interaction","markerEnd":"MimCatalysis","isAttachedTo":["n1389","e_1391"]},"e_1395":{"id":"e_1395","comments":[{"source":"Reactome","content":"Cleavage of a single peptide bond converts factor XII to activated factor XII (factor XIIa) (Fujikawa and McMullen 1983; McMullen and Fujikawa 1985). Identification of the catalytic activity or activities responsible for this cleavage has not been straightforward. Studies in vitro have demonstrated the autoactivation of factor XII as well as activation by kallikrein. Both reactions require the presence of negatively charged surfaces and are accelerated in the presence of kininogen (high molecular weight kininogen, HK) (Griffin and Cochrane 1976; Meier et al. 1977; Silverberg et al. 1980). Recent work suggests that factor XII activation in vivo may occur primarily on endothelial cell surfaces and that, as in vitro, association with kininogen may accelerate the reaction (Mahdi et al. 2002; Schmaier 2004), although alternative pathways and alternative mechanisms for associating factor XII with the cell surface have not been excluded (Joseph et al. 2001)."},{"source":"Reactome","content":"Cleavage of a single peptide bond converts factor XII to activated factor XII (factor XIIa) (Fujikawa and McMullen 1983; McMullen and Fujikawa 1985). Identification of the catalytic activity or activities responsible for this cleavage has not been straightforward. Studies in vitro have demonstrated the autoactivation of factor XII as well as activation by kallikrein. Both reactions require the presence of negatively charged surfaces and are accelerated in the presence of kininogen (high molecular weight kininogen, HK) (Griffin and Cochrane 1976; Meier et al. 1977; Silverberg et al. 1980). Recent work suggests that factor XII activation in vivo may occur primarily on endothelial cell surfaces and that, as in vitro, association with kininogen may accelerate the reaction (Mahdi et al. 2002; Schmaier 2004), although alternative pathways and alternative mechanisms for associating factor XII with the cell surface have not been excluded (Joseph et al. 2001)."}],"citations":["publicationXrefca9","publicationXrefcef","publicationXrefb18","publicationXreff54","publicationXreffb9","publicationXreffec","publicationXrefdab","publicationXrefc7a"],"drawAs":"SegmentedLine","zIndex":12288,"borderWidth":1,"points":[{"x":1121,"y":746,"isAttachedTo":"n1396","attachmentDisplay":{"position":[0.3770491803278688,0],"offset":[0,-3.0000000000000004]},"orientation":[0,-1]},{"x":1033,"y":493,"isAttachedTo":"n1397","attachmentDisplay":{"position":[0.47761194029850745,1],"offset":[0,3]},"orientation":[0,-1]}],"color":"#000000","backgroundColor":"none","dbConventionalName":"Reactome","dbId":"REACT_1455","type":["Interaction","Edge","SBO:0000167","SBO:0000393","SBO:0000394","DirectedInteraction"],"kaavioType":"Edge","gpmlElementName":"Interaction","markerEnd":"Arrow","isAttachedTo":["n1396","n1397"],"burrs":["b4a15"]},"b4a15":{"attachmentDisplay":{"position":[0.5,0],"offset":[0,0]},"drawAs":"none","id":"b4a15","isAttachedTo":"e_1395","borderWidth":0,"height":0,"width":0,"zIndex":12288,"type":["Anchor","Burr"],"kaavioType":"Burr","gpmlElementName":"Anchor"},"e_1395_c_0":{"id":"e_1395_c_0","comments":[{"source":"Reactome","content":"Cleavage of a single peptide bond converts factor XII to activated factor XII (factor XIIa) (Fujikawa and McMullen 1983; McMullen and Fujikawa 1985). Identification of the catalytic activity or activities responsible for this cleavage has not been straightforward. Studies in vitro have demonstrated the autoactivation of factor XII as well as activation by kallikrein. Both reactions require the presence of negatively charged surfaces and are accelerated in the presence of kininogen (high molecular weight kininogen, HK) (Griffin and Cochrane 1976; Meier et al. 1977; Silverberg et al. 1980). Recent work suggests that factor XII activation in vivo may occur primarily on endothelial cell surfaces and that, as in vitro, association with kininogen may accelerate the reaction (Mahdi et al. 2002; Schmaier 2004), although alternative pathways and alternative mechanisms for associating factor XII with the cell surface have not been excluded (Joseph et al. 2001)."},{"source":"Reactome","content":"Cleavage of a single peptide bond converts factor XII to activated factor XII (factor XIIa) (Fujikawa and McMullen 1983; McMullen and Fujikawa 1985). Identification of the catalytic activity or activities responsible for this cleavage has not been straightforward. Studies in vitro have demonstrated the autoactivation of factor XII as well as activation by kallikrein. Both reactions require the presence of negatively charged surfaces and are accelerated in the presence of kininogen (high molecular weight kininogen, HK) (Griffin and Cochrane 1976; Meier et al. 1977; Silverberg et al. 1980). Recent work suggests that factor XII activation in vivo may occur primarily on endothelial cell surfaces and that, as in vitro, association with kininogen may accelerate the reaction (Mahdi et al. 2002; Schmaier 2004), although alternative pathways and alternative mechanisms for associating factor XII with the cell surface have not been excluded (Joseph et al. 2001)."}],"citations":["publicationXrefca9","publicationXrefcef","publicationXrefb18","publicationXreff54","publicationXreffb9","publicationXreffec","publicationXrefdab","publicationXrefc7a"],"drawAs":"SegmentedLine","zIndex":12288,"borderWidth":1,"points":[{"x":828,"y":721,"isAttachedTo":"n1389","attachmentDisplay":{"position":[0.8717948717948718,0],"offset":[0,-3.0000000000000036]},"orientation":[0,-1]},{"x":1033,"y":578,"isAttachedTo":"b4a15","attachmentDisplay":{"position":[0.5,0],"offset":[],"relativeOffset":[-21.5,-20.25]},"orientation":[]}],"color":"#000000","backgroundColor":"none","dbConventionalName":"Reactome","dbId":"REACT_1455","type":["Interaction","Edge"],"kaavioType":"Edge","gpmlElementName":"Interaction","markerEnd":"MimCatalysis","isAttachedTo":["n1389","e_1395"]},"e_1395_a_0":{"id":"e_1395_a_0","comments":[{"source":"Reactome","content":"Cleavage of a single peptide bond converts factor XII to activated factor XII (factor XIIa) (Fujikawa and McMullen 1983; McMullen and Fujikawa 1985). Identification of the catalytic activity or activities responsible for this cleavage has not been straightforward. Studies in vitro have demonstrated the autoactivation of factor XII as well as activation by kallikrein. Both reactions require the presence of negatively charged surfaces and are accelerated in the presence of kininogen (high molecular weight kininogen, HK) (Griffin and Cochrane 1976; Meier et al. 1977; Silverberg et al. 1980). Recent work suggests that factor XII activation in vivo may occur primarily on endothelial cell surfaces and that, as in vitro, association with kininogen may accelerate the reaction (Mahdi et al. 2002; Schmaier 2004), although alternative pathways and alternative mechanisms for associating factor XII with the cell surface have not been excluded (Joseph et al. 2001)."},{"source":"Reactome","content":"Cleavage of a single peptide bond converts factor XII to activated factor XII (factor XIIa) (Fujikawa and McMullen 1983; McMullen and Fujikawa 1985). Identification of the catalytic activity or activities responsible for this cleavage has not been straightforward. Studies in vitro have demonstrated the autoactivation of factor XII as well as activation by kallikrein. Both reactions require the presence of negatively charged surfaces and are accelerated in the presence of kininogen (high molecular weight kininogen, HK) (Griffin and Cochrane 1976; Meier et al. 1977; Silverberg et al. 1980). Recent work suggests that factor XII activation in vivo may occur primarily on endothelial cell surfaces and that, as in vitro, association with kininogen may accelerate the reaction (Mahdi et al. 2002; Schmaier 2004), although alternative pathways and alternative mechanisms for associating factor XII with the cell surface have not been excluded (Joseph et al. 2001)."}],"citations":["publicationXrefca9","publicationXrefcef","publicationXrefb18","publicationXreff54","publicationXreffb9","publicationXreffec","publicationXrefdab","publicationXrefc7a"],"drawAs":"SegmentedLine","zIndex":12288,"borderWidth":1,"points":[{"x":1046,"y":745,"isAttachedTo":"n1398","attachmentDisplay":{"position":[0.47887323943661975,0],"offset":[0,-3]},"orientation":[0,-1]},{"x":1033,"y":578,"isAttachedTo":"b4a15","attachmentDisplay":{"position":[0.5,0],"offset":[],"relativeOffset":[-21.5,-20.25]},"orientation":[]}],"color":"#000000","backgroundColor":"none","dbConventionalName":"Reactome","dbId":"REACT_1455","type":["Interaction","Edge","SBO:0000167","SBO:0000393","SBO:0000394","DirectedInteraction"],"kaavioType":"Edge","gpmlElementName":"Interaction","markerEnd":"Arrow","isAttachedTo":["n1398","e_1395"]},"e_1399":{"id":"e_1399","comments":[{"source":"Reactome","content":"Plasma factor XI binds to the platelet glycoprotein Ib:IX:V complex (Baglia et al. 2002; Greengard et al. 1986). In the body, this reaction occurs specifically on the surfaces of activated platelets, but not on endothelial cells (Baird and Walsh 2002). The stoichiometry of the platelet glycoprotein Ib:IX:V complex has not been established directly, but is inferred from the relative abundances of its components in platelet membranes (Modderman et al. 1992; Shrimpton et al. 2002)."},{"source":"Reactome","content":"Plasma factor XI binds to the platelet glycoprotein Ib:IX:V complex (Baglia et al. 2002; Greengard et al. 1986). In the body, this reaction occurs specifically on the surfaces of activated platelets, but not on endothelial cells (Baird and Walsh 2002). The stoichiometry of the platelet glycoprotein Ib:IX:V complex has not been established directly, but is inferred from the relative abundances of its components in platelet membranes (Modderman et al. 1992; Shrimpton et al. 2002)."}],"citations":["publicationXrefcee","publicationXrefd24","publicationXrefd64","publicationXrefc89"],"drawAs":"SegmentedLine","zIndex":12288,"borderWidth":1,"points":[{"x":2026,"y":703},{"x":1982,"y":738,"isAttachedTo":"n1402","attachmentDisplay":{"position":[0.6610169491525424,0],"offset":[0,-3.000000000000001]},"orientation":[0,1]}],"color":"#000000","backgroundColor":"none","dbConventionalName":"Reactome","dbId":"REACT_177","type":["Interaction","Edge","SBO:0000167","SBO:0000393","SBO:0000394","DirectedInteraction"],"kaavioType":"Edge","gpmlElementName":"Interaction","markerEnd":"Arrow","isAttachedTo":["n1402"],"burrs":["ba321"]},"ba321":{"attachmentDisplay":{"position":[0,0],"offset":[0,0]},"drawAs":"none","id":"ba321","isAttachedTo":"e_1399","borderWidth":0,"height":0,"width":0,"zIndex":12288,"type":["Anchor","Burr"],"kaavioType":"Burr","gpmlElementName":"Anchor"},"e_1399_a_i0":{"id":"e_1399_a_i0","comments":[{"source":"Reactome","content":"Plasma factor XI binds to the platelet glycoprotein Ib:IX:V complex (Baglia et al. 2002; Greengard et al. 1986). In the body, this reaction occurs specifically on the surfaces of activated platelets, but not on endothelial cells (Baird and Walsh 2002). The stoichiometry of the platelet glycoprotein Ib:IX:V complex has not been established directly, but is inferred from the relative abundances of its components in platelet membranes (Modderman et al. 1992; Shrimpton et al. 2002)."},{"source":"Reactome","content":"Plasma factor XI binds to the platelet glycoprotein Ib:IX:V complex (Baglia et al. 2002; Greengard et al. 1986). In the body, this reaction occurs specifically on the surfaces of activated platelets, but not on endothelial cells (Baird and Walsh 2002). The stoichiometry of the platelet glycoprotein Ib:IX:V complex has not been established directly, but is inferred from the relative abundances of its components in platelet membranes (Modderman et al. 1992; Shrimpton et al. 2002)."}],"citations":["publicationXrefcee","publicationXrefd24","publicationXrefd64","publicationXrefc89"],"drawAs":"SegmentedLine","zIndex":12288,"borderWidth":1,"points":[{"x":2046,"y":687,"isAttachedTo":"n1401","attachmentDisplay":{"position":[0.1923076923076923,1],"offset":[0,2.9999999999999973]},"orientation":[0,1]},{"x":2026,"y":703,"isAttachedTo":"ba321","attachmentDisplay":{"position":[0,0],"offset":[],"relativeOffset":[0,0]},"orientation":[]}],"color":"#000000","backgroundColor":"none","dbConventionalName":"Reactome","dbId":"REACT_177","type":["Interaction","Edge"],"kaavioType":"Edge","gpmlElementName":"Interaction","isAttachedTo":["n1401","e_1399"]},"e_1399_a_i1":{"id":"e_1399_a_i1","comments":[{"source":"Reactome","content":"Plasma factor XI binds to the platelet glycoprotein Ib:IX:V complex (Baglia et al. 2002; Greengard et al. 1986). In the body, this reaction occurs specifically on the surfaces of activated platelets, but not on endothelial cells (Baird and Walsh 2002). The stoichiometry of the platelet glycoprotein Ib:IX:V complex has not been established directly, but is inferred from the relative abundances of its components in platelet membranes (Modderman et al. 1992; Shrimpton et al. 2002)."},{"source":"Reactome","content":"Plasma factor XI binds to the platelet glycoprotein Ib:IX:V complex (Baglia et al. 2002; Greengard et al. 1986). In the body, this reaction occurs specifically on the surfaces of activated platelets, but not on endothelial cells (Baird and Walsh 2002). The stoichiometry of the platelet glycoprotein Ib:IX:V complex has not been established directly, but is inferred from the relative abundances of its components in platelet membranes (Modderman et al. 1992; Shrimpton et al. 2002)."}],"citations":["publicationXrefcee","publicationXrefd24","publicationXrefd64","publicationXrefc89"],"drawAs":"SegmentedLine","zIndex":12288,"borderWidth":1,"points":[{"x":2066,"y":739,"isAttachedTo":"n1841","attachmentDisplay":{"position":[0.25316455696202533,0],"offset":[0,-3.0000000000000013]},"orientation":[0,-1]},{"x":2026,"y":703,"isAttachedTo":"ba321","attachmentDisplay":{"position":[0,0],"offset":[],"relativeOffset":[0,0]},"orientation":[]}],"color":"#000000","backgroundColor":"none","dbConventionalName":"Reactome","dbId":"REACT_177","type":["Interaction","Edge"],"kaavioType":"Edge","gpmlElementName":"Interaction","isAttachedTo":["n1841","e_1399"]},"e_1403":{"id":"e_1403","comments":[{"source":"Reactome","content":"Factor XI, bound to the cell surface, is converted to activated factor XI (factor XIa). Chemically, this reaction involves the cleavage of a single peptide bond in each subunit of the factor XI homodimer; intra- and inter-chain disulfide bonds hold the resulting four polypeptides together (Bouma and Griffin 1977; Kurachi and Davie 1977; McMullen et al. 1991). In the body, this reaction occurs on the surfaces of activated platelets (Greengard et al. 1986; Baglia et al. 2002; Baird and Walsh 2002); when this reaction occurs as a step in the intrinsic (\"contact\") pathway of blood coagulation, it is catalyzed by activated factor XIIa (Kurachi and Davie 1977, Baglia and Walsh 2000) which in turn is generated through the interactions of factor XII, kallikrein, and kininogen on endothelial cell surfaces (Schmaier 2004)."},{"source":"Reactome","content":"Factor XI, bound to the cell surface, is converted to activated factor XI (factor XIa). Chemically, this reaction involves the cleavage of a single peptide bond in each subunit of the factor XI homodimer; intra- and inter-chain disulfide bonds hold the resulting four polypeptides together (Bouma and Griffin 1977; Kurachi and Davie 1977; McMullen et al. 1991). In the body, this reaction occurs on the surfaces of activated platelets (Greengard et al. 1986; Baglia et al. 2002; Baird and Walsh 2002); when this reaction occurs as a step in the intrinsic (\"contact\") pathway of blood coagulation, it is catalyzed by activated factor XIIa (Kurachi and Davie 1977, Baglia and Walsh 2000) which in turn is generated through the interactions of factor XII, kallikrein, and kininogen on endothelial cell surfaces (Schmaier 2004)."}],"citations":["publicationXrefb7a","publicationXrefbee","publicationXrefd85","publicationXrefb17"],"drawAs":"SegmentedLine","zIndex":12288,"borderWidth":1,"points":[{"x":1944,"y":738,"isAttachedTo":"n1402","attachmentDisplay":{"position":[0.3389830508474576,0],"offset":[0,-3.000000000000001]},"orientation":[0,-1]},{"x":1820,"y":738,"isAttachedTo":"n1404","attachmentDisplay":{"position":[0.5080645161290323,0],"offset":[0,-3.000000000000001]},"orientation":[0,1]}],"color":"#000000","backgroundColor":"none","dbConventionalName":"Reactome","dbId":"REACT_905","type":["Interaction","Edge","SBO:0000167","SBO:0000393","SBO:0000394","DirectedInteraction"],"kaavioType":"Edge","gpmlElementName":"Interaction","markerEnd":"Arrow","isAttachedTo":["n1402","n1404"],"burrs":["aac22"]},"aac22":{"attachmentDisplay":{"position":[0.5,0],"offset":[0,0]},"drawAs":"none","id":"aac22","isAttachedTo":"e_1403","borderWidth":0,"height":0,"width":0,"zIndex":12288,"type":["Anchor","Burr"],"kaavioType":"Burr","gpmlElementName":"Anchor"},"e_1403_c_0":{"id":"e_1403_c_0","comments":[{"source":"Reactome","content":"Factor XI, bound to the cell surface, is converted to activated factor XI (factor XIa). Chemically, this reaction involves the cleavage of a single peptide bond in each subunit of the factor XI homodimer; intra- and inter-chain disulfide bonds hold the resulting four polypeptides together (Bouma and Griffin 1977; Kurachi and Davie 1977; McMullen et al. 1991). In the body, this reaction occurs on the surfaces of activated platelets (Greengard et al. 1986; Baglia et al. 2002; Baird and Walsh 2002); when this reaction occurs as a step in the intrinsic (\"contact\") pathway of blood coagulation, it is catalyzed by activated factor XIIa (Kurachi and Davie 1977, Baglia and Walsh 2000) which in turn is generated through the interactions of factor XII, kallikrein, and kininogen on endothelial cell surfaces (Schmaier 2004)."},{"source":"Reactome","content":"Factor XI, bound to the cell surface, is converted to activated factor XI (factor XIa). Chemically, this reaction involves the cleavage of a single peptide bond in each subunit of the factor XI homodimer; intra- and inter-chain disulfide bonds hold the resulting four polypeptides together (Bouma and Griffin 1977; Kurachi and Davie 1977; McMullen et al. 1991). In the body, this reaction occurs on the surfaces of activated platelets (Greengard et al. 1986; Baglia et al. 2002; Baird and Walsh 2002); when this reaction occurs as a step in the intrinsic (\"contact\") pathway of blood coagulation, it is catalyzed by activated factor XIIa (Kurachi and Davie 1977, Baglia and Walsh 2000) which in turn is generated through the interactions of factor XII, kallikrein, and kininogen on endothelial cell surfaces (Schmaier 2004)."}],"citations":["publicationXrefb7a","publicationXrefbee","publicationXrefd85","publicationXrefb17"],"drawAs":"SegmentedLine","zIndex":12288,"borderWidth":1,"points":[{"x":1071,"y":477,"isAttachedTo":"n1397","attachmentDisplay":{"position":[1,0.4583333333333333],"offset":[2.999999999999994,0]},"orientation":[1,0]},{"x":1827,"y":624,"isAttachedTo":"aac22","attachmentDisplay":{"position":[0.5,0],"offset":[],"relativeOffset":[-27,-56.5]},"orientation":[]}],"color":"#000000","backgroundColor":"none","dbConventionalName":"Reactome","dbId":"REACT_905","type":["Interaction","Edge"],"kaavioType":"Edge","gpmlElementName":"Interaction","markerEnd":"MimCatalysis","isAttachedTo":["n1397","e_1403"]},"e_1405":{"id":"e_1405","comments":[{"source":"Reactome","content":"Factor XI, bound to the cell surface, is converted to activated factor XI (factor XIa). In the body, this reaction occurs on the surfaces of activated platelets (Baglia et al. 2002). Small quantities of factor XI can be activated in a reaction catalyzed by factor XIIa, to initiate formation of a fibrin clot. However, the efficient activation of larger quantities of factor XI, needed to propagate the blood clotting process, appears to be mediated by thrombin (Baglia and Walsh 2000; Gailani and Broze 1993; Naito and Fujikawa 1991; Oliver et al. 1999; Monroe et al. 2002)."},{"source":"Reactome","content":"Factor XI, bound to the cell surface, is converted to activated factor XI (factor XIa). In the body, this reaction occurs on the surfaces of activated platelets (Baglia et al. 2002). Small quantities of factor XI can be activated in a reaction catalyzed by factor XIIa, to initiate formation of a fibrin clot. However, the efficient activation of larger quantities of factor XI, needed to propagate the blood clotting process, appears to be mediated by thrombin (Baglia and Walsh 2000; Gailani and Broze 1993; Naito and Fujikawa 1991; Oliver et al. 1999; Monroe et al. 2002)."}],"citations":["publicationXrefb7a","publicationXrefc3f","publicationXreff30","publicationXrefd32"],"drawAs":"SegmentedLine","zIndex":12288,"borderWidth":1,"points":[{"x":1956,"y":738,"isAttachedTo":"n1402","attachmentDisplay":{"position":[0.4406779661016949,0],"offset":[0,-3.000000000000001]},"orientation":[0,-1]},{"x":1832,"y":738,"isAttachedTo":"n1404","attachmentDisplay":{"position":[0.6048387096774194,0],"offset":[0,-3.000000000000001]},"orientation":[0,1]}],"color":"#000000","backgroundColor":"none","dbConventionalName":"Reactome","dbId":"REACT_1581","type":["Interaction","Edge","SBO:0000167","SBO:0000393","SBO:0000394","DirectedInteraction"],"kaavioType":"Edge","gpmlElementName":"Interaction","markerEnd":"Arrow","isAttachedTo":["n1402","n1404"],"burrs":["a790c"]},"a790c":{"attachmentDisplay":{"position":[0.5,0],"offset":[0,0]},"drawAs":"none","id":"a790c","isAttachedTo":"e_1405","borderWidth":0,"height":0,"width":0,"zIndex":12288,"type":["Anchor","Burr"],"kaavioType":"Burr","gpmlElementName":"Anchor"},"e_1405_c_0":{"id":"e_1405_c_0","comments":[{"source":"Reactome","content":"Factor XI, bound to the cell surface, is converted to activated factor XI (factor XIa). In the body, this reaction occurs on the surfaces of activated platelets (Baglia et al. 2002). Small quantities of factor XI can be activated in a reaction catalyzed by factor XIIa, to initiate formation of a fibrin clot. However, the efficient activation of larger quantities of factor XI, needed to propagate the blood clotting process, appears to be mediated by thrombin (Baglia and Walsh 2000; Gailani and Broze 1993; Naito and Fujikawa 1991; Oliver et al. 1999; Monroe et al. 2002)."},{"source":"Reactome","content":"Factor XI, bound to the cell surface, is converted to activated factor XI (factor XIa). In the body, this reaction occurs on the surfaces of activated platelets (Baglia et al. 2002). Small quantities of factor XI can be activated in a reaction catalyzed by factor XIIa, to initiate formation of a fibrin clot. However, the efficient activation of larger quantities of factor XI, needed to propagate the blood clotting process, appears to be mediated by thrombin (Baglia and Walsh 2000; Gailani and Broze 1993; Naito and Fujikawa 1991; Oliver et al. 1999; Monroe et al. 2002)."}],"citations":["publicationXrefb7a","publicationXrefc3f","publicationXreff30","publicationXrefd32"],"drawAs":"SegmentedLine","zIndex":12288,"borderWidth":1,"points":[{"x":1804,"y":180,"isAttachedTo":"n1406","attachmentDisplay":{"position":[0.6216216216216216,1],"offset":[0,2.999999999999993]},"orientation":[0,1]},{"x":1916,"y":623,"isAttachedTo":"a790c","attachmentDisplay":{"position":[0.5,0],"offset":[],"relativeOffset":[10.5,-57]},"orientation":[]}],"color":"#000000","backgroundColor":"none","dbConventionalName":"Reactome","dbId":"REACT_1581","type":["Interaction","Edge"],"kaavioType":"Edge","gpmlElementName":"Interaction","markerEnd":"MimCatalysis","isAttachedTo":["n1406","e_1405"]},"e_1407":{"id":"e_1407","comments":[{"source":"Reactome","content":"Factor XIa, bound to platelet glycoprotein (GP) Ib:IX:V on the platelet cell surface, catalyzes the formation of activated factor IX with high efficiency in a reaction that requires Ca++. The amino terminal part of the heavy chain of factor IX, the factor IX activation peptide, is released. (This peptide has no known function.)"},{"source":"Reactome","content":"Factor XIa, bound to platelet glycoprotein (GP) Ib:IX:V on the platelet cell surface, catalyzes the formation of activated factor IX with high efficiency in a reaction that requires Ca++. The amino terminal part of the heavy chain of factor IX, the factor IX activation peptide, is released. (This peptide has no known function.)"}],"citations":["publicationXrefe03","publicationXrefd59"],"drawAs":"SegmentedLine","zIndex":12288,"borderWidth":1,"points":[{"x":2373,"y":257,"isAttachedTo":"n1374","attachmentDisplay":{"position":[0.2151898734177215,1],"offset":[0,2.9999999999999982]},"orientation":[0,1]},{"x":2316,"y":395}],"color":"#000000","backgroundColor":"none","dbConventionalName":"Reactome","dbId":"REACT_2073","type":["Interaction","Edge"],"kaavioType":"Edge","gpmlElementName":"Interaction","isAttachedTo":["n1374"],"burrs":["d1ef5","fad13"]},"d1ef5":{"attachmentDisplay":{"position":[0.99,0],"offset":[0,0]},"drawAs":"none","id":"d1ef5","isAttachedTo":"e_1407","borderWidth":0,"height":0,"width":0,"zIndex":12288,"type":["Anchor","Burr"],"kaavioType":"Burr","gpmlElementName":"Anchor"},"fad13":{"attachmentDisplay":{"position":[0.5,0],"offset":[0,0]},"drawAs":"none","id":"fad13","isAttachedTo":"e_1407","borderWidth":0,"height":0,"width":0,"zIndex":12288,"type":["Anchor","Burr"],"kaavioType":"Burr","gpmlElementName":"Anchor"},"e_1407_o0":{"id":"e_1407_o0","comments":[{"source":"Reactome","content":"Factor XIa, bound to platelet glycoprotein (GP) Ib:IX:V on the platelet cell surface, catalyzes the formation of activated factor IX with high efficiency in a reaction that requires Ca++. The amino terminal part of the heavy chain of factor IX, the factor IX activation peptide, is released. (This peptide has no known function.)"},{"source":"Reactome","content":"Factor XIa, bound to platelet glycoprotein (GP) Ib:IX:V on the platelet cell surface, catalyzes the formation of activated factor IX with high efficiency in a reaction that requires Ca++. The amino terminal part of the heavy chain of factor IX, the factor IX activation peptide, is released. (This peptide has no known function.)"}],"citations":["publicationXrefe03","publicationXrefd59"],"drawAs":"SegmentedLine","zIndex":12288,"borderWidth":1,"points":[{"x":2316,"y":395,"isAttachedTo":"d1ef5","attachmentDisplay":{"position":[0.99,0],"offset":[],"relativeOffset":[0,0.18999999999999773]},"orientation":[]},{"x":2371,"y":345,"isAttachedTo":"n1375","attachmentDisplay":{"position":[0.3097345132743363,1],"offset":[0,3.000000000000001]},"orientation":[0,-1]}],"color":"#000000","backgroundColor":"none","dbConventionalName":"Reactome","dbId":"REACT_2073","type":["Interaction","Edge","SBO:0000167","SBO:0000393","SBO:0000394","DirectedInteraction"],"kaavioType":"Edge","gpmlElementName":"Interaction","markerEnd":"Arrow","isAttachedTo":["e_1407","n1375"]},"e_1407_o1":{"id":"e_1407_o1","comments":[{"source":"Reactome","content":"Factor XIa, bound to platelet glycoprotein (GP) Ib:IX:V on the platelet cell surface, catalyzes the formation of activated factor IX with high efficiency in a reaction that requires Ca++. The amino terminal part of the heavy chain of factor IX, the factor IX activation peptide, is released. (This peptide has no known function.)"},{"source":"Reactome","content":"Factor XIa, bound to platelet glycoprotein (GP) Ib:IX:V on the platelet cell surface, catalyzes the formation of activated factor IX with high efficiency in a reaction that requires Ca++. The amino terminal part of the heavy chain of factor IX, the factor IX activation peptide, is released. (This peptide has no known function.)"}],"citations":["publicationXrefe03","publicationXrefd59"],"drawAs":"SegmentedLine","zIndex":12288,"borderWidth":1,"points":[{"x":2316,"y":395,"isAttachedTo":"d1ef5","attachmentDisplay":{"position":[0.99,0],"offset":[],"relativeOffset":[0,0.18999999999999773]},"orientation":[]},{"x":2380,"y":430,"isAttachedTo":"n1376","attachmentDisplay":{"position":[0.16666666666666669,0],"offset":[0,-3.000000000000001]},"orientation":[0,1]}],"color":"#000000","backgroundColor":"none","dbConventionalName":"Reactome","dbId":"REACT_2073","type":["Interaction","Edge","SBO:0000167","SBO:0000393","SBO:0000394","DirectedInteraction"],"kaavioType":"Edge","gpmlElementName":"Interaction","markerEnd":"Arrow","isAttachedTo":["e_1407","n1376"]},"e_1407_c_0":{"id":"e_1407_c_0","comments":[{"source":"Reactome","content":"Factor XIa, bound to platelet glycoprotein (GP) Ib:IX:V on the platelet cell surface, catalyzes the formation of activated factor IX with high efficiency in a reaction that requires Ca++. The amino terminal part of the heavy chain of factor IX, the factor IX activation peptide, is released. (This peptide has no known function.)"},{"source":"Reactome","content":"Factor XIa, bound to platelet glycoprotein (GP) Ib:IX:V on the platelet cell surface, catalyzes the formation of activated factor IX with high efficiency in a reaction that requires Ca++. The amino terminal part of the heavy chain of factor IX, the factor IX activation peptide, is released. (This peptide has no known function.)"}],"citations":["publicationXrefe03","publicationXrefd59"],"drawAs":"SegmentedLine","zIndex":12288,"borderWidth":1,"points":[{"x":1839,"y":738,"isAttachedTo":"n1404","attachmentDisplay":{"position":[0.6612903225806451,0],"offset":[0,-3.000000000000001]},"orientation":[0,-1]},{"x":2270,"y":348,"isAttachedTo":"fad13","attachmentDisplay":{"position":[0.5,0],"offset":[],"relativeOffset":[-36.75,10.5]},"orientation":[]}],"color":"#000000","backgroundColor":"none","dbConventionalName":"Reactome","dbId":"REACT_2073","type":["Interaction","Edge"],"kaavioType":"Edge","gpmlElementName":"Interaction","markerEnd":"MimCatalysis","isAttachedTo":["n1404","e_1407"]},"e_1407_a_0":{"id":"e_1407_a_0","comments":[{"source":"Reactome","content":"Factor XIa, bound to platelet glycoprotein (GP) Ib:IX:V on the platelet cell surface, catalyzes the formation of activated factor IX with high efficiency in a reaction that requires Ca++. The amino terminal part of the heavy chain of factor IX, the factor IX activation peptide, is released. (This peptide has no known function.)"},{"source":"Reactome","content":"Factor XIa, bound to platelet glycoprotein (GP) Ib:IX:V on the platelet cell surface, catalyzes the formation of activated factor IX with high efficiency in a reaction that requires Ca++. The amino terminal part of the heavy chain of factor IX, the factor IX activation peptide, is released. (This peptide has no known function.)"}],"citations":["publicationXrefe03","publicationXrefd59"],"drawAs":"SegmentedLine","zIndex":12288,"borderWidth":1,"points":[{"x":2234,"y":317,"isAttachedTo":"n1840","attachmentDisplay":{"position":[0.7377049180327868,1],"offset":[0,2.9999999999999973]},"orientation":[0,1]},{"x":2270,"y":348,"isAttachedTo":"fad13","attachmentDisplay":{"position":[0.5,0],"offset":[],"relativeOffset":[-36.75,10.5]},"orientation":[]}],"color":"#000000","backgroundColor":"none","dbConventionalName":"Reactome","dbId":"REACT_2073","type":["Interaction","Edge","SBO:0000167","SBO:0000393","SBO:0000394","DirectedInteraction"],"kaavioType":"Edge","gpmlElementName":"Interaction","markerEnd":"Arrow","isAttachedTo":["n1840","e_1407"]},"e_1408":{"id":"e_1408","comments":[{"source":"Reactome","content":"Factor VIII binds to von Willebrand factor to form a complex. This complex stabilizes factor VIII, which otherwise has a very short half-life in the blood.<P>Factor VIII (Vehar et al. 1984) is a heterodimer containing a heavy and a light polypeptide chain, generated by the proteolytic cleavage of a single large precursor polypeptide. Several forms of the heavy chain are found in vivo, all functionally the same but differing in the amount of the B domain removed by proteolysis. The single form annotated here is the shortest one (Eaton et al. 1986; Hill-Eubanks et al. 1989).<P>In vitro, von Willebrand factor (Titani et al. 1986) can form complexes with factor VIII with a 1:1 stoichiometry. The complexes that form in vivo, however, involve large multimers of von Willebrand factor and varied, but always low, proportions of factor VIII (Vlot et al. 1995). A stoichiometry of one molecule of factor VIII associated with 50 of von Willebrand factor is typical in vivo, and is used here to annotate the factor VIII:von Willebrand factor complex."},{"source":"Reactome","content":"Factor VIII binds to von Willebrand factor to form a complex. This complex stabilizes factor VIII, which otherwise has a very short half-life in the blood.<P>Factor VIII (Vehar et al. 1984) is a heterodimer containing a heavy and a light polypeptide chain, generated by the proteolytic cleavage of a single large precursor polypeptide. Several forms of the heavy chain are found in vivo, all functionally the same but differing in the amount of the B domain removed by proteolysis. The single form annotated here is the shortest one (Eaton et al. 1986; Hill-Eubanks et al. 1989).<P>In vitro, von Willebrand factor (Titani et al. 1986) can form complexes with factor VIII with a 1:1 stoichiometry. The complexes that form in vivo, however, involve large multimers of von Willebrand factor and varied, but always low, proportions of factor VIII (Vlot et al. 1995). A stoichiometry of one molecule of factor VIII associated with 50 of von Willebrand factor is typical in vivo, and is used here to annotate the factor VIII:von Willebrand factor complex."}],"citations":["publicationXrefb26","publicationXrefa34","publicationXrefaea","publicationXrefb4d","publicationXrefc95","publicationXrefcf8"],"drawAs":"SegmentedLine","zIndex":12288,"borderWidth":1,"points":[{"x":2029,"y":81},{"x":1968,"y":82,"isAttachedTo":"n1411","attachmentDisplay":{"position":[1,0.39622641509433965],"offset":[2.9999999999999987,0]},"orientation":[-1,0]}],"color":"#000000","backgroundColor":"none","dbConventionalName":"Reactome","dbId":"REACT_531","type":["Interaction","Edge","SBO:0000167","SBO:0000393","SBO:0000394","DirectedInteraction"],"kaavioType":"Edge","gpmlElementName":"Interaction","markerEnd":"Arrow","isAttachedTo":["n1411"],"burrs":["bf641"]},"bf641":{"attachmentDisplay":{"position":[0,0],"offset":[0,0]},"drawAs":"none","id":"bf641","isAttachedTo":"e_1408","borderWidth":0,"height":0,"width":0,"zIndex":12288,"type":["Anchor","Burr"],"kaavioType":"Burr","gpmlElementName":"Anchor"},"e_1408_a_i0":{"id":"e_1408_a_i0","comments":[{"source":"Reactome","content":"Factor VIII binds to von Willebrand factor to form a complex. This complex stabilizes factor VIII, which otherwise has a very short half-life in the blood.<P>Factor VIII (Vehar et al. 1984) is a heterodimer containing a heavy and a light polypeptide chain, generated by the proteolytic cleavage of a single large precursor polypeptide. Several forms of the heavy chain are found in vivo, all functionally the same but differing in the amount of the B domain removed by proteolysis. The single form annotated here is the shortest one (Eaton et al. 1986; Hill-Eubanks et al. 1989).<P>In vitro, von Willebrand factor (Titani et al. 1986) can form complexes with factor VIII with a 1:1 stoichiometry. The complexes that form in vivo, however, involve large multimers of von Willebrand factor and varied, but always low, proportions of factor VIII (Vlot et al. 1995). A stoichiometry of one molecule of factor VIII associated with 50 of von Willebrand factor is typical in vivo, and is used here to annotate the factor VIII:von Willebrand factor complex."},{"source":"Reactome","content":"Factor VIII binds to von Willebrand factor to form a complex. This complex stabilizes factor VIII, which otherwise has a very short half-life in the blood.<P>Factor VIII (Vehar et al. 1984) is a heterodimer containing a heavy and a light polypeptide chain, generated by the proteolytic cleavage of a single large precursor polypeptide. Several forms of the heavy chain are found in vivo, all functionally the same but differing in the amount of the B domain removed by proteolysis. The single form annotated here is the shortest one (Eaton et al. 1986; Hill-Eubanks et al. 1989).<P>In vitro, von Willebrand factor (Titani et al. 1986) can form complexes with factor VIII with a 1:1 stoichiometry. The complexes that form in vivo, however, involve large multimers of von Willebrand factor and varied, but always low, proportions of factor VIII (Vlot et al. 1995). A stoichiometry of one molecule of factor VIII associated with 50 of von Willebrand factor is typical in vivo, and is used here to annotate the factor VIII:von Willebrand factor complex."}],"citations":["publicationXrefb26","publicationXrefa34","publicationXrefaea","publicationXrefb4d","publicationXrefc95","publicationXrefcf8"],"drawAs":"SegmentedLine","zIndex":12288,"borderWidth":1,"points":[{"x":2060,"y":66,"isAttachedTo":"n1409","attachmentDisplay":{"position":[0.08695652173913043,1],"offset":[0,2.9999999999999973]},"orientation":[0,1]},{"x":2029,"y":81,"isAttachedTo":"bf641","attachmentDisplay":{"position":[0,0],"offset":[],"relativeOffset":[0,0]},"orientation":[]}],"color":"#000000","backgroundColor":"none","dbConventionalName":"Reactome","dbId":"REACT_531","type":["Interaction","Edge"],"kaavioType":"Edge","gpmlElementName":"Interaction","isAttachedTo":["n1409","e_1408"]},"e_1408_a_i1":{"id":"e_1408_a_i1","comments":[{"source":"Reactome","content":"Factor VIII binds to von Willebrand factor to form a complex. This complex stabilizes factor VIII, which otherwise has a very short half-life in the blood.<P>Factor VIII (Vehar et al. 1984) is a heterodimer containing a heavy and a light polypeptide chain, generated by the proteolytic cleavage of a single large precursor polypeptide. Several forms of the heavy chain are found in vivo, all functionally the same but differing in the amount of the B domain removed by proteolysis. The single form annotated here is the shortest one (Eaton et al. 1986; Hill-Eubanks et al. 1989).<P>In vitro, von Willebrand factor (Titani et al. 1986) can form complexes with factor VIII with a 1:1 stoichiometry. The complexes that form in vivo, however, involve large multimers of von Willebrand factor and varied, but always low, proportions of factor VIII (Vlot et al. 1995). A stoichiometry of one molecule of factor VIII associated with 50 of von Willebrand factor is typical in vivo, and is used here to annotate the factor VIII:von Willebrand factor complex."},{"source":"Reactome","content":"Factor VIII binds to von Willebrand factor to form a complex. This complex stabilizes factor VIII, which otherwise has a very short half-life in the blood.<P>Factor VIII (Vehar et al. 1984) is a heterodimer containing a heavy and a light polypeptide chain, generated by the proteolytic cleavage of a single large precursor polypeptide. Several forms of the heavy chain are found in vivo, all functionally the same but differing in the amount of the B domain removed by proteolysis. The single form annotated here is the shortest one (Eaton et al. 1986; Hill-Eubanks et al. 1989).<P>In vitro, von Willebrand factor (Titani et al. 1986) can form complexes with factor VIII with a 1:1 stoichiometry. The complexes that form in vivo, however, involve large multimers of von Willebrand factor and varied, but always low, proportions of factor VIII (Vlot et al. 1995). A stoichiometry of one molecule of factor VIII associated with 50 of von Willebrand factor is typical in vivo, and is used here to annotate the factor VIII:von Willebrand factor complex."}],"citations":["publicationXrefb26","publicationXrefa34","publicationXrefaea","publicationXrefb4d","publicationXrefc95","publicationXrefcf8"],"drawAs":"SegmentedLine","zIndex":12288,"borderWidth":1,"points":[{"x":2060,"y":100,"isAttachedTo":"n1410","attachmentDisplay":{"position":[0.2786885245901639,0],"offset":[0,-3.000000000000001]},"orientation":[0,-1]},{"x":2029,"y":81,"isAttachedTo":"bf641","attachmentDisplay":{"position":[0,0],"offset":[],"relativeOffset":[0,0]},"orientation":[]}],"color":"#000000","backgroundColor":"none","dbConventionalName":"Reactome","dbId":"REACT_531","type":["Interaction","Edge"],"kaavioType":"Edge","gpmlElementName":"Interaction","isAttachedTo":["n1410","e_1408"]},"e_1412":{"id":"e_1412","comments":[{"source":"Reactome","content":"Factor VIII complexed to von Willibrand factor in the blood is cleaved into several smaller polypeptides that remain associated. The acidic polypeptide on the aminoterminal side of the A3 domain of the light chain is released, however, and as this polypeptide mediates the association of factor VIII with von Willibrand factor, the activated factor VIII is released. While several proteases are capable of catalyzing these cleavages in vitro, only thrombin is active on factor VIII:von Willibrand factor complexes under physiological conditions (Eaton et al. 1986; Hill-Eubanks et al. 1989; Lollar et al. 1988; Pieters et al. 1989)"},{"source":"Reactome","content":"Factor VIII complexed to von Willibrand factor in the blood is cleaved into several smaller polypeptides that remain associated. The acidic polypeptide on the aminoterminal side of the A3 domain of the light chain is released, however, and as this polypeptide mediates the association of factor VIII with von Willibrand factor, the activated factor VIII is released. While several proteases are capable of catalyzing these cleavages in vitro, only thrombin is active on factor VIII:von Willibrand factor complexes under physiological conditions (Eaton et al. 1986; Hill-Eubanks et al. 1989; Lollar et al. 1988; Pieters et al. 1989)"}],"citations":["publicationXrefb26","publicationXrefa34","publicationXrefc95","publicationXreff70"],"drawAs":"SegmentedLine","zIndex":12288,"borderWidth":1,"points":[{"x":1913,"y":117,"isAttachedTo":"n1411","attachmentDisplay":{"position":[0.49514563106796117,1],"offset":[0,2.999999999999999]},"orientation":[0,1]},{"x":1947,"y":170}],"color":"#000000","backgroundColor":"none","dbConventionalName":"Reactome","dbId":"REACT_217","type":["Interaction","Edge"],"kaavioType":"Edge","gpmlElementName":"Interaction","isAttachedTo":["n1411"],"burrs":["a5159","f51e7"]},"a5159":{"attachmentDisplay":{"position":[0.99,0],"offset":[0,0]},"drawAs":"none","id":"a5159","isAttachedTo":"e_1412","borderWidth":0,"height":0,"width":0,"zIndex":12288,"type":["Anchor","Burr"],"kaavioType":"Burr","gpmlElementName":"Anchor"},"f51e7":{"attachmentDisplay":{"position":[0.5,0],"offset":[0,0]},"drawAs":"none","id":"f51e7","isAttachedTo":"e_1412","borderWidth":0,"height":0,"width":0,"zIndex":12288,"type":["Anchor","Burr"],"kaavioType":"Burr","gpmlElementName":"Anchor"},"e_1412_o0":{"id":"e_1412_o0","comments":[{"source":"Reactome","content":"Factor VIII complexed to von Willibrand factor in the blood is cleaved into several smaller polypeptides that remain associated. The acidic polypeptide on the aminoterminal side of the A3 domain of the light chain is released, however, and as this polypeptide mediates the association of factor VIII with von Willibrand factor, the activated factor VIII is released. While several proteases are capable of catalyzing these cleavages in vitro, only thrombin is active on factor VIII:von Willibrand factor complexes under physiological conditions (Eaton et al. 1986; Hill-Eubanks et al. 1989; Lollar et al. 1988; Pieters et al. 1989)"},{"source":"Reactome","content":"Factor VIII complexed to von Willibrand factor in the blood is cleaved into several smaller polypeptides that remain associated. The acidic polypeptide on the aminoterminal side of the A3 domain of the light chain is released, however, and as this polypeptide mediates the association of factor VIII with von Willibrand factor, the activated factor VIII is released. While several proteases are capable of catalyzing these cleavages in vitro, only thrombin is active on factor VIII:von Willibrand factor complexes under physiological conditions (Eaton et al. 1986; Hill-Eubanks et al. 1989; Lollar et al. 1988; Pieters et al. 1989)"}],"citations":["publicationXrefb26","publicationXrefa34","publicationXrefc95","publicationXreff70"],"drawAs":"SegmentedLine","zIndex":12288,"borderWidth":1,"points":[{"x":1947,"y":170,"isAttachedTo":"a5159","attachmentDisplay":{"position":[0.99,0],"offset":[],"relativeOffset":[0,0]},"orientation":[]},{"x":1968,"y":242,"isAttachedTo":"n1413","attachmentDisplay":{"position":[0.40909090909090906,0],"offset":[0,-2.9999999999999982]},"orientation":[0,1]}],"color":"#000000","backgroundColor":"none","dbConventionalName":"Reactome","dbId":"REACT_217","type":["Interaction","Edge","SBO:0000167","SBO:0000393","SBO:0000394","DirectedInteraction"],"kaavioType":"Edge","gpmlElementName":"Interaction","markerEnd":"Arrow","isAttachedTo":["e_1412","n1413"]},"e_1412_o1":{"id":"e_1412_o1","comments":[{"source":"Reactome","content":"Factor VIII complexed to von Willibrand factor in the blood is cleaved into several smaller polypeptides that remain associated. The acidic polypeptide on the aminoterminal side of the A3 domain of the light chain is released, however, and as this polypeptide mediates the association of factor VIII with von Willibrand factor, the activated factor VIII is released. While several proteases are capable of catalyzing these cleavages in vitro, only thrombin is active on factor VIII:von Willibrand factor complexes under physiological conditions (Eaton et al. 1986; Hill-Eubanks et al. 1989; Lollar et al. 1988; Pieters et al. 1989)"},{"source":"Reactome","content":"Factor VIII complexed to von Willibrand factor in the blood is cleaved into several smaller polypeptides that remain associated. The acidic polypeptide on the aminoterminal side of the A3 domain of the light chain is released, however, and as this polypeptide mediates the association of factor VIII with von Willibrand factor, the activated factor VIII is released. While several proteases are capable of catalyzing these cleavages in vitro, only thrombin is active on factor VIII:von Willibrand factor complexes under physiological conditions (Eaton et al. 1986; Hill-Eubanks et al. 1989; Lollar et al. 1988; Pieters et al. 1989)"}],"citations":["publicationXrefb26","publicationXrefa34","publicationXrefc95","publicationXreff70"],"drawAs":"SegmentedLine","zIndex":12288,"borderWidth":1,"points":[{"x":1947,"y":170,"isAttachedTo":"a5159","attachmentDisplay":{"position":[0.99,0],"offset":[],"relativeOffset":[0,0]},"orientation":[]},{"x":2008,"y":192,"isAttachedTo":"n1414","attachmentDisplay":{"position":[0.04672897196261683,0],"offset":[0,-3.000000000000001]},"orientation":[0,1]}],"color":"#000000","backgroundColor":"none","dbConventionalName":"Reactome","dbId":"REACT_217","type":["Interaction","Edge","SBO:0000167","SBO:0000393","SBO:0000394","DirectedInteraction"],"kaavioType":"Edge","gpmlElementName":"Interaction","markerEnd":"Arrow","isAttachedTo":["e_1412","n1414"]},"e_1412_o2":{"id":"e_1412_o2","comments":[{"source":"Reactome","content":"Factor VIII complexed to von Willibrand factor in the blood is cleaved into several smaller polypeptides that remain associated. The acidic polypeptide on the aminoterminal side of the A3 domain of the light chain is released, however, and as this polypeptide mediates the association of factor VIII with von Willibrand factor, the activated factor VIII is released. While several proteases are capable of catalyzing these cleavages in vitro, only thrombin is active on factor VIII:von Willibrand factor complexes under physiological conditions (Eaton et al. 1986; Hill-Eubanks et al. 1989; Lollar et al. 1988; Pieters et al. 1989)"},{"source":"Reactome","content":"Factor VIII complexed to von Willibrand factor in the blood is cleaved into several smaller polypeptides that remain associated. The acidic polypeptide on the aminoterminal side of the A3 domain of the light chain is released, however, and as this polypeptide mediates the association of factor VIII with von Willibrand factor, the activated factor VIII is released. While several proteases are capable of catalyzing these cleavages in vitro, only thrombin is active on factor VIII:von Willibrand factor complexes under physiological conditions (Eaton et al. 1986; Hill-Eubanks et al. 1989; Lollar et al. 1988; Pieters et al. 1989)"}],"citations":["publicationXrefb26","publicationXrefa34","publicationXrefc95","publicationXreff70"],"drawAs":"SegmentedLine","zIndex":12288,"borderWidth":1,"points":[{"x":1947,"y":170,"isAttachedTo":"a5159","attachmentDisplay":{"position":[0.99,0],"offset":[],"relativeOffset":[0,0]},"orientation":[]},{"x":2031,"y":144,"isAttachedTo":"n1410","attachmentDisplay":{"position":[0.04098360655737704,1],"offset":[0,3.000000000000001]},"orientation":[0,-1]}],"color":"#000000","backgroundColor":"none","dbConventionalName":"Reactome","dbId":"REACT_217","type":["Interaction","Edge","SBO:0000167","SBO:0000393","SBO:0000394","DirectedInteraction"],"kaavioType":"Edge","gpmlElementName":"Interaction","markerEnd":"Arrow","isAttachedTo":["e_1412","n1410"]},"e_1412_c_0":{"id":"e_1412_c_0","comments":[{"source":"Reactome","content":"Factor VIII complexed to von Willibrand factor in the blood is cleaved into several smaller polypeptides that remain associated. The acidic polypeptide on the aminoterminal side of the A3 domain of the light chain is released, however, and as this polypeptide mediates the association of factor VIII with von Willibrand factor, the activated factor VIII is released. While several proteases are capable of catalyzing these cleavages in vitro, only thrombin is active on factor VIII:von Willibrand factor complexes under physiological conditions (Eaton et al. 1986; Hill-Eubanks et al. 1989; Lollar et al. 1988; Pieters et al. 1989)"},{"source":"Reactome","content":"Factor VIII complexed to von Willibrand factor in the blood is cleaved into several smaller polypeptides that remain associated. The acidic polypeptide on the aminoterminal side of the A3 domain of the light chain is released, however, and as this polypeptide mediates the association of factor VIII with von Willibrand factor, the activated factor VIII is released. While several proteases are capable of catalyzing these cleavages in vitro, only thrombin is active on factor VIII:von Willibrand factor complexes under physiological conditions (Eaton et al. 1986; Hill-Eubanks et al. 1989; Lollar et al. 1988; Pieters et al. 1989)"}],"citations":["publicationXrefb26","publicationXrefa34","publicationXrefc95","publicationXreff70"],"drawAs":"SegmentedLine","zIndex":12288,"borderWidth":1,"points":[{"x":1849,"y":154,"isAttachedTo":"n1406","attachmentDisplay":{"position":[1,0.5],"offset":[2.999999999999994,0]},"orientation":[1,0]},{"x":1913,"y":155,"isAttachedTo":"f51e7","attachmentDisplay":{"position":[0.5,0],"offset":[],"relativeOffset":[-8,5.25]},"orientation":[]}],"color":"#000000","backgroundColor":"none","dbConventionalName":"Reactome","dbId":"REACT_217","type":["Interaction","Edge"],"kaavioType":"Edge","gpmlElementName":"Interaction","markerEnd":"MimCatalysis","isAttachedTo":["n1406","e_1412"]},"e_1415":{"id":"e_1415","comments":[{"source":"Reactome","content":"The activated forms of factors VIII and IX associate on a cell surface to form a complex that very efficiently catalyzes the activation of factor X, the so-called \"intrinsic tenase complex\". In vitro, negatively charged phospholipids can provide an appropriate surface. In the body, the surface is provided by the plasma membranes of activated platelets (Gilbert and Arena 1996)."},{"source":"Reactome","content":"The activated forms of factors VIII and IX associate on a cell surface to form a complex that very efficiently catalyzes the activation of factor X, the so-called \"intrinsic tenase complex\". In vitro, negatively charged phospholipids can provide an appropriate surface. In the body, the surface is provided by the plasma membranes of activated platelets (Gilbert and Arena 1996)."}],"citations":["publicationXrefcc1"],"drawAs":"SegmentedLine","zIndex":12288,"borderWidth":1,"points":[{"x":2374,"y":497},{"x":2715,"y":739,"isAttachedTo":"n1416","attachmentDisplay":{"position":[0.32380952380952377,0],"offset":[0,-3.000000000000001]},"orientation":[0,1]}],"color":"#000000","backgroundColor":"none","dbConventionalName":"Reactome","dbId":"REACT_112","type":["Interaction","Edge","SBO:0000167","SBO:0000393","SBO:0000394","DirectedInteraction"],"kaavioType":"Edge","gpmlElementName":"Interaction","markerEnd":"Arrow","isAttachedTo":["n1416"],"burrs":["f9ac2"]},"f9ac2":{"attachmentDisplay":{"position":[0,0],"offset":[0,0]},"drawAs":"none","id":"f9ac2","isAttachedTo":"e_1415","borderWidth":0,"height":0,"width":0,"zIndex":12288,"type":["Anchor","Burr"],"kaavioType":"Burr","gpmlElementName":"Anchor"},"e_1415_a_i0":{"id":"e_1415_a_i0","comments":[{"source":"Reactome","content":"The activated forms of factors VIII and IX associate on a cell surface to form a complex that very efficiently catalyzes the activation of factor X, the so-called \"intrinsic tenase complex\". In vitro, negatively charged phospholipids can provide an appropriate surface. In the body, the surface is provided by the plasma membranes of activated platelets (Gilbert and Arena 1996)."},{"source":"Reactome","content":"The activated forms of factors VIII and IX associate on a cell surface to form a complex that very efficiently catalyzes the activation of factor X, the so-called \"intrinsic tenase complex\". In vitro, negatively charged phospholipids can provide an appropriate surface. In the body, the surface is provided by the plasma membranes of activated platelets (Gilbert and Arena 1996)."}],"citations":["publicationXrefcc1"],"drawAs":"SegmentedLine","zIndex":12288,"borderWidth":1,"points":[{"x":2005,"y":285,"isAttachedTo":"n1413","attachmentDisplay":{"position":[0.9696969696969697,1],"offset":[0,3.000000000000002]},"orientation":[0,1]},{"x":2374,"y":497,"isAttachedTo":"f9ac2","attachmentDisplay":{"position":[0,0],"offset":[],"relativeOffset":[0,0]},"orientation":[]}],"color":"#000000","backgroundColor":"none","dbConventionalName":"Reactome","dbId":"REACT_112","type":["Interaction","Edge"],"kaavioType":"Edge","gpmlElementName":"Interaction","isAttachedTo":["n1413","e_1415"]},"e_1415_a_i1":{"id":"e_1415_a_i1","comments":[{"source":"Reactome","content":"The activated forms of factors VIII and IX associate on a cell surface to form a complex that very efficiently catalyzes the activation of factor X, the so-called \"intrinsic tenase complex\". In vitro, negatively charged phospholipids can provide an appropriate surface. In the body, the surface is provided by the plasma membranes of activated platelets (Gilbert and Arena 1996)."},{"source":"Reactome","content":"The activated forms of factors VIII and IX associate on a cell surface to form a complex that very efficiently catalyzes the activation of factor X, the so-called \"intrinsic tenase complex\". In vitro, negatively charged phospholipids can provide an appropriate surface. In the body, the surface is provided by the plasma membranes of activated platelets (Gilbert and Arena 1996)."}],"citations":["publicationXrefcc1"],"drawAs":"SegmentedLine","zIndex":12288,"borderWidth":1,"points":[{"x":2394,"y":462,"isAttachedTo":"n1376","attachmentDisplay":{"position":[0.3787878787878788,1],"offset":[0,3.000000000000001]},"orientation":[0,1]},{"x":2374,"y":497,"isAttachedTo":"f9ac2","attachmentDisplay":{"position":[0,0],"offset":[],"relativeOffset":[0,0]},"orientation":[]}],"color":"#000000","backgroundColor":"none","dbConventionalName":"Reactome","dbId":"REACT_112","type":["Interaction","Edge"],"kaavioType":"Edge","gpmlElementName":"Interaction","isAttachedTo":["n1376","e_1415"]},"e_1415_a_0":{"id":"e_1415_a_0","comments":[{"source":"Reactome","content":"The activated forms of factors VIII and IX associate on a cell surface to form a complex that very efficiently catalyzes the activation of factor X, the so-called \"intrinsic tenase complex\". In vitro, negatively charged phospholipids can provide an appropriate surface. In the body, the surface is provided by the plasma membranes of activated platelets (Gilbert and Arena 1996)."},{"source":"Reactome","content":"The activated forms of factors VIII and IX associate on a cell surface to form a complex that very efficiently catalyzes the activation of factor X, the so-called \"intrinsic tenase complex\". In vitro, negatively charged phospholipids can provide an appropriate surface. In the body, the surface is provided by the plasma membranes of activated platelets (Gilbert and Arena 1996)."}],"citations":["publicationXrefcc1"],"drawAs":"SegmentedLine","zIndex":12288,"borderWidth":1,"points":[{"x":2631,"y":614,"isAttachedTo":"n1332","attachmentDisplay":{"position":[0.4918032786885246,1],"offset":[0,2.9999999999999973]},"orientation":[0,1]},{"x":2633,"y":660,"isAttachedTo":"f51e7","attachmentDisplay":{"position":[0.5,0],"offset":[],"relativeOffset":[351,257.75]},"orientation":[]}],"color":"#000000","backgroundColor":"none","dbConventionalName":"Reactome","dbId":"REACT_112","type":["Interaction","Edge","SBO:0000167","SBO:0000393","SBO:0000394","DirectedInteraction"],"kaavioType":"Edge","gpmlElementName":"Interaction","markerEnd":"Arrow","isAttachedTo":["n1332","e_1412"]},"e_1457":{"id":"e_1457","comments":[{"source":"Reactome","content":"Factor IXa, in a complex with factor VIIIa on the surfaces of activated platelets (the \"intrinsic tenase complex\"), catalyzes the formation of activated factor X with high efficiency. The amino terminal part of the heavy chain of factor X, the factor X activation peptide, is released. (This peptide has no known function.)"},{"source":"Reactome","content":"Factor IXa, in a complex with factor VIIIa on the surfaces of activated platelets (the \"intrinsic tenase complex\"), catalyzes the formation of activated factor X with high efficiency. The amino terminal part of the heavy chain of factor X, the factor X activation peptide, is released. (This peptide has no known function.)"}],"citations":["publicationXrefbeb"],"drawAs":"SegmentedLine","zIndex":12288,"borderWidth":1,"points":[{"x":2734,"y":422},{"x":2853,"y":422}],"color":"#000000","backgroundColor":"none","dbConventionalName":"Reactome","dbId":"REACT_1668","type":["Interaction","Edge"],"kaavioType":"Edge","gpmlElementName":"Interaction","burrs":["db48d","eb2ab","f5c72"]},"db48d":{"attachmentDisplay":{"position":[0,0],"offset":[0,0]},"drawAs":"none","id":"db48d","isAttachedTo":"e_1457","borderWidth":0,"height":0,"width":0,"zIndex":12288,"type":["Anchor","Burr"],"kaavioType":"Burr","gpmlElementName":"Anchor"},"eb2ab":{"attachmentDisplay":{"position":[0.99,0],"offset":[0,0]},"drawAs":"none","id":"eb2ab","isAttachedTo":"e_1457","borderWidth":0,"height":0,"width":0,"zIndex":12288,"type":["Anchor","Burr"],"kaavioType":"Burr","gpmlElementName":"Anchor"},"f5c72":{"attachmentDisplay":{"position":[0.5,0],"offset":[0,0]},"drawAs":"none","id":"f5c72","isAttachedTo":"e_1457","borderWidth":0,"height":0,"width":0,"zIndex":12288,"type":["Anchor","Burr"],"kaavioType":"Burr","gpmlElementName":"Anchor"},"e_1457_a_i0":{"id":"e_1457_a_i0","comments":[{"source":"Reactome","content":"Factor IXa, in a complex with factor VIIIa on the surfaces of activated platelets (the \"intrinsic tenase complex\"), catalyzes the formation of activated factor X with high efficiency. The amino terminal part of the heavy chain of factor X, the factor X activation peptide, is released. (This peptide has no known function.)"},{"source":"Reactome","content":"Factor IXa, in a complex with factor VIIIa on the surfaces of activated platelets (the \"intrinsic tenase complex\"), catalyzes the formation of activated factor X with high efficiency. The amino terminal part of the heavy chain of factor X, the factor X activation peptide, is released. (This peptide has no known function.)"}],"citations":["publicationXrefbeb"],"drawAs":"SegmentedLine","zIndex":12288,"borderWidth":1,"points":[{"x":2714,"y":468,"isAttachedTo":"n1324","attachmentDisplay":{"position":[0.5740740740740741,0],"offset":[0,-3]},"orientation":[0,-1]},{"x":2734,"y":422,"isAttachedTo":"db48d","attachmentDisplay":{"position":[0,0],"offset":[],"relativeOffset":[0,0]},"orientation":[]}],"color":"#000000","backgroundColor":"none","dbConventionalName":"Reactome","dbId":"REACT_1668","type":["Interaction","Edge"],"kaavioType":"Edge","gpmlElementName":"Interaction","isAttachedTo":["n1324","e_1457"]},"e_1457_a_i1":{"id":"e_1457_a_i1","comments":[{"source":"Reactome","content":"Factor IXa, in a complex with factor VIIIa on the surfaces of activated platelets (the \"intrinsic tenase complex\"), catalyzes the formation of activated factor X with high efficiency. The amino terminal part of the heavy chain of factor X, the factor X activation peptide, is released. (This peptide has no known function.)"},{"source":"Reactome","content":"Factor IXa, in a complex with factor VIIIa on the surfaces of activated platelets (the \"intrinsic tenase complex\"), catalyzes the formation of activated factor X with high efficiency. The amino terminal part of the heavy chain of factor X, the factor X activation peptide, is released. (This peptide has no known function.)"}],"citations":["publicationXrefbeb"],"drawAs":"SegmentedLine","zIndex":12288,"borderWidth":1,"points":[{"x":2675,"y":345,"isAttachedTo":"n1838","attachmentDisplay":{"position":[0.6721311475409836,1],"offset":[0,2.9999999999999973]},"orientation":[0,1]},{"x":2734,"y":422,"isAttachedTo":"db48d","attachmentDisplay":{"position":[0,0],"offset":[],"relativeOffset":[0,0]},"orientation":[]}],"color":"#000000","backgroundColor":"none","dbConventionalName":"Reactome","dbId":"REACT_1668","type":["Interaction","Edge"],"kaavioType":"Edge","gpmlElementName":"Interaction","isAttachedTo":["n1838","e_1457"]},"e_1457_o0":{"id":"e_1457_o0","comments":[{"source":"Reactome","content":"Factor IXa, in a complex with factor VIIIa on the surfaces of activated platelets (the \"intrinsic tenase complex\"), catalyzes the formation of activated factor X with high efficiency. The amino terminal part of the heavy chain of factor X, the factor X activation peptide, is released. (This peptide has no known function.)"},{"source":"Reactome","content":"Factor IXa, in a complex with factor VIIIa on the surfaces of activated platelets (the \"intrinsic tenase complex\"), catalyzes the formation of activated factor X with high efficiency. The amino terminal part of the heavy chain of factor X, the factor X activation peptide, is released. (This peptide has no known function.)"}],"citations":["publicationXrefbeb"],"drawAs":"SegmentedLine","zIndex":12288,"borderWidth":1,"points":[{"x":2853,"y":422,"isAttachedTo":"eb2ab","attachmentDisplay":{"position":[0.99,0],"offset":[],"relativeOffset":[0.09500000000002728,0]},"orientation":[]},{"x":2921,"y":336,"isAttachedTo":"n1325","attachmentDisplay":{"position":[0.23214285714285715,1],"offset":[0,2.9999999999999982]},"orientation":[0,-1]}],"color":"#000000","backgroundColor":"none","dbConventionalName":"Reactome","dbId":"REACT_1668","type":["Interaction","Edge","SBO:0000167","SBO:0000393","SBO:0000394","DirectedInteraction"],"kaavioType":"Edge","gpmlElementName":"Interaction","markerEnd":"Arrow","isAttachedTo":["e_1457","n1325"]},"e_1457_o1":{"id":"e_1457_o1","comments":[{"source":"Reactome","content":"Factor IXa, in a complex with factor VIIIa on the surfaces of activated platelets (the \"intrinsic tenase complex\"), catalyzes the formation of activated factor X with high efficiency. The amino terminal part of the heavy chain of factor X, the factor X activation peptide, is released. (This peptide has no known function.)"},{"source":"Reactome","content":"Factor IXa, in a complex with factor VIIIa on the surfaces of activated platelets (the \"intrinsic tenase complex\"), catalyzes the formation of activated factor X with high efficiency. The amino terminal part of the heavy chain of factor X, the factor X activation peptide, is released. (This peptide has no known function.)"}],"citations":["publicationXrefbeb"],"drawAs":"SegmentedLine","zIndex":12288,"borderWidth":1,"points":[{"x":2853,"y":422,"isAttachedTo":"eb2ab","attachmentDisplay":{"position":[0.99,0],"offset":[],"relativeOffset":[0.09500000000002728,0]},"orientation":[]},{"x":2930,"y":478,"isAttachedTo":"n1326","attachmentDisplay":{"position":[0.08139534883720928,0],"offset":[0,-2.999999999999999]},"orientation":[0,1]}],"color":"#000000","backgroundColor":"none","dbConventionalName":"Reactome","dbId":"REACT_1668","type":["Interaction","Edge","SBO:0000167","SBO:0000393","SBO:0000394","DirectedInteraction"],"kaavioType":"Edge","gpmlElementName":"Interaction","markerEnd":"Arrow","isAttachedTo":["e_1457","n1326"]},"e_1457_c_0":{"id":"e_1457_c_0","comments":[{"source":"Reactome","content":"Factor IXa, in a complex with factor VIIIa on the surfaces of activated platelets (the \"intrinsic tenase complex\"), catalyzes the formation of activated factor X with high efficiency. 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