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activated factor VIII + H2O
factor VIII
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proteolytic inactivation
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factor VIII + H2O
?
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factor Xa proteolytically activates Factor VIII by cleaving P1 residues Arg372, Arg740, and Arg1689. Factor Xa also catalyzes inactivating cleavages that occur on a slower time scale than the activating ones
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?
factor VIII + H2O
activated factor VIII + B domain
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proteolytic activation by removal of the B domain
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?
protease-activated receptor 1 + H2O
activated protease-activated receptor 1 + ?
protease-activated receptor 2 + H2O
activated protease-activated receptor 2 + ?
prothrombin + H2O
thrombin + ?
prothrombin + H2O
thrombin + propeptide of thrombin
prothrombin + H2O
trhombin + ?
additional information
?
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protease-activated receptor 1 + H2O
activated protease-activated receptor 1 + ?
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PAR-1 activation mediates activation of phospholipase C in endothelial cells
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?
protease-activated receptor 1 + H2O
activated protease-activated receptor 1 + ?
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PAR-1 activation mediates activation of phospholipase C in endothelial cells
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?
protease-activated receptor 1 + H2O
activated protease-activated receptor 1 + ?
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?
protease-activated receptor 2 + H2O
activated protease-activated receptor 2 + ?
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PAR-2 activation mediates activation of phospholipase C in endothelial cells
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?
protease-activated receptor 2 + H2O
activated protease-activated receptor 2 + ?
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PAR-2 activation mediates activation of phospholipase C in endothelial cells
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?
protease-activated receptor 2 + H2O
activated protease-activated receptor 2 + ?
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?
prothrombin + H2O
?
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major role is the activation of prothrombin
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prothrombin + H2O
?
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factor Xaalpha is predominantly responsible for thrombin generation. Slow conversion to factor Xabeta coordinates coagulation and the initiation of fibrinolysis at sites of thrombinase assembly
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?
prothrombin + H2O
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gamma-carboxylation of prothrombin is required for cleavage
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?
prothrombin + H2O
?
gamma-carboxylation of prothrombin is required for cleavage
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?
prothrombin + H2O
thrombin + ?
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?
prothrombin + H2O
thrombin + ?
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?
prothrombin + H2O
thrombin + ?
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crucial step in blood coagulation process
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?
prothrombin + H2O
thrombin + ?
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?
prothrombin + H2O
thrombin + ?
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procoagulant activity
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?
prothrombin + H2O
thrombin + ?
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?
prothrombin + H2O
thrombin + ?
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?
prothrombin + H2O
thrombin + ?
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?
prothrombin + H2O
thrombin + ?
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?
prothrombin + H2O
thrombin + ?
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?
prothrombin + H2O
thrombin + ?
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?
prothrombin + H2O
thrombin + ?
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?
prothrombin + H2O
thrombin + ?
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?
prothrombin + H2O
thrombin + ?
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?
prothrombin + H2O
thrombin + ?
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?
prothrombin + H2O
thrombin + ?
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?
prothrombin + H2O
thrombin + ?
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?
prothrombin + H2O
thrombin + ?
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?
prothrombin + H2O
thrombin + ?
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acts within the prothrombinase complex
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?
prothrombin + H2O
thrombin + ?
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enzyme is involved in thrombotic complications of artherosclerosis and following diseases, overview
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?
prothrombin + H2O
thrombin + ?
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enzyme is responsible for the proteolysis of prothrombin to catalytically active thrombin
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?
prothrombin + H2O
thrombin + ?
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enzyme plays a key role in thrombosis and hemostasis by cleaving prothrombin to thrombin and thereby regulating the generation of this vital procoagulant enzyme, thrombus formation causes diseases like arterial restenosis, induces mitogenic signaling via binding to effector cell protease receptor-1, i.e. EPR-1, on cell surfaces, and via release of platelet-derived growth factor PDGF in aortic smooth-muscle cells
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?
prothrombin + H2O
thrombin + ?
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initial step in thrombus formation
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?
prothrombin + H2O
thrombin + ?
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key enzyme in coagulation cascade responsible for the generation of thrombin by limited proteolysis of its zymogen prothrombin
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?
prothrombin + H2O
thrombin + ?
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procoagulant activity
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?
prothrombin + H2O
thrombin + ?
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prothrombin activation requires proteolysis of 2 bonds and thus involves 2 possible activation pathways, parallel-sequential activation model
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?
prothrombin + H2O
thrombin + ?
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cleavage at Arg320 followed by cleavage at Arg271
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?
prothrombin + H2O
thrombin + ?
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the interaction of factor Xa with factor Va on membranes to form prothrombinase profoundly increases the rate of the proteolytic conversion of prothrombin to thrombin
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?
prothrombin + H2O
thrombin + ?
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activation, a first cleavage of prothrombin by prothrombinase at Arg320 produces the active intermediate meizothrombin, while the second cleavage at Arg271 produces thrombin
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?
prothrombin + H2O
thrombin + ?
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activation, interaction of factor Xa with factor Va promotes prothrombin activation
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?
prothrombin + H2O
thrombin + ?
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prothrombinase cleaves prothrombin at two cleavage positions Arg-271-Thr-272 and Arg-320-Ile-321
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?
prothrombin + H2O
thrombin + ?
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?
prothrombin + H2O
thrombin + ?
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?
prothrombin + H2O
thrombin + ?
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?
prothrombin + H2O
thrombin + ?
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enzyme plays a key role in thrombosis and hemostasis by cleaving prothrombin to thrombin and thereby regulating the generation of this vital procoagulant enzyme, thrombus formation causes diseases like arterial restenosis, induces mitogenic signaling via binding to effector cell protease receptor-1, i.e. EPR-1, on cell surfaces
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?
prothrombin + H2O
thrombin + ?
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?
prothrombin + H2O
thrombin + ?
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?
prothrombin + H2O
thrombin + ?
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enzyme plays a key role in thrombosis and hemostasis by cleaving prothrombin to thrombin and thereby regulating the generation of this vital procoagulant enzyme, thrombus formation causes diseases like arterial restenosis, induces mitogenic signaling via binding to effector cell protease receptor-1, i.e. EPR-1, on cell surfaces, and via release of platelet-derived growth factor PDGF in aortic smooth-muscle cells
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?
prothrombin + H2O
thrombin + ?
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initial step in thrombus formation
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?
prothrombin + H2O
thrombin + ?
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enzyme plays a key role in thrombosis and hemostasis by cleaving prothrombin to thrombin and thereby regulating the generation of this vital procoagulant enzyme, thrombus formation causes diseases like arterial restenosis, induces mitogenic signaling via binding to effector cell protease receptor-1, i.e. EPR-1, on cell surfaces
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?
prothrombin + H2O
thrombin + propeptide of thrombin
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proteolytic activation
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?
prothrombin + H2O
thrombin + propeptide of thrombin
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?
prothrombin + H2O
trhombin + ?
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?
prothrombin + H2O
trhombin + ?
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?
prothrombin + H2O
trhombin + ?
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?
additional information
?
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factor Xa and thrombin evoke additive calcium and proinflammatory responses in endothelial cells subjected to coagulation, overview
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additional information
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the enzyme is responsible for clot-associated procoagulant activity
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?
additional information
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enzyme is involved in the coagulation cascade
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?
additional information
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enzyme is involved in the coagulation cascade
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?
additional information
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enzyme link between cancer and thrombosis appears to be a bidirectional relationship, physiological role of factor Xa, involvement in inflammation and diseases, physiological interactions, regulation, overview
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additional information
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properties of and indications for different enzyme inhibitors, overview, the enzyme is responsible for clot-associated procoagulant activity, enzyme inhibition lead to reduced platelet deposition and aggregation at thrombic sites
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additional information
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the enzyme is regulated by sequential occupancy of a pair of linked lipid binding sites, each of which have different minimum ligand structural requirements to induce structural changes
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?
additional information
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factor Xa can induce mesangial cell proliferation through the activation of extracellular regulated kinase via protease-activated receptor 2 in mesangial cells. Protease-activated receptor 2 may play a crucial role in the cell proliferation induced by factor Xa
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additional information
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blood clot elongation is regulated by factor Xa formation by intrinsic tenase, i.e. factor VIIa and tissue factor complex, coagulation factors from plasma bind to tissue factor TF-expressing cells, become activated, dissociate, and diffuse into plasma to form enzymatic complexes on the membranes of activated platelets, overview
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?
additional information
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coagulation factor Xa is a serine protease that plays a crucial role during blood coagulation by converting prothrombin into thrombin, it drives tumor cells of epithelial, but not endothelial, origin into apoptosis through BH3-only protein Bim up-regulation, and enhances fibroblast survival, overview, signaling through protease-activated receptor 1, PAR-1, with rapid and transient desensitization of PAR-1 signaling, signaling pathway, overview
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additional information
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different anticoagulant mechanisms, overview
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additional information
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different anticoagulant mechanisms, overview
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additional information
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factor Xa and thrombin evoke additive calcium and proinflammatory responses in endothelial cells subjected to coagulation, overview
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additional information
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factor Xa inhibits the inhibition of the procoagulant function of activated factor V by activated protein C through proteolytic cleavages at Arg506, with a half-maximum inhibition of 2 nM, while the cleavage at Arg306, and Arg679 is not protected, protein S counteracted the inhibition by FXa of the Arg506 cleavage, whereas protein S and FXa yielded additive stimulatory effect of the cleavage at Arg306, activity with recombinant FVa Q306/Q679 and FVa Q506/Q679 variants, interaction analysis with 1.5-dansyl-Glu-Gly-Arg-inhibited factor Xa, overview
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additional information
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PD0313052 and argatroban, inhibitors of blood coagulation factors Xa and IIa, synergize to reduce thrombus weight and thrombin generation in vivo and in vitro
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additional information
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annexin 2 acts as a receptor for factor Xa on the cell surface. It facilitates factor Xa activation of receptor PAR-1 but does not enhance coagulant function of factor Xa. Overexpression of tissue factor abolishes annexin 2 dependence on factor Xa signaling and diminishes binding to cell surface annexin 2, whereas selectively abolishing tissue factor promotes the annexin 2/factor Xa interaction
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additional information
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treatment with factor Xa markedly diminishes the migration of different cancer cell lines from breast, lung and colon. Factor Xa mediates inhibition of cancer cell migration specifically and dose dependently. It acts via protease-activated receptor-1 dependent signaling. The G protein alpha 1 pathway is not involved in signaling
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additional information
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coagulation factor Xa inhibits cancer cell migration via LIMK1-mediated cofilin inactivation through induction of myosin light chain phosphorylation and LIMK1 activation, overview
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additional information
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effects of factor X on the respiratory function and asthmatic response in mice, factor X transcript levels and factor Xa activity are increased in lungs of asthmatic mice leading to a significant decrease in the thickness of the mucosal layer and in lung collagen deposition, factor Xa modulates airway remodeling, overview
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?
additional information
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enzyme elicits a signaling response in C2C12 and NIH-3T3 fibroblast cells. ERK1/2 phosphorylation by factor Xa is dependent on protease-activated receptor PAR-2 cleavage and leads to fibroblast proliferation, migration, and differentiation into myofibroblasts
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additional information
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enzyme link between cancer and thrombosis appears to be a bidirectional relationship, physiological role of factor Xa, involvement in inflammation and diseases, physiological interactions, regulation, overview
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?
additional information
?
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enzyme link between cancer and thrombosis appears to be a bidirectional relationship, physiological role of factor Xa, involvement in inflammation and diseases, physiological interactions, regulation, overview
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?
additional information
?
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roles of coagulation pathway and factor Xa in rat mesangioproliferative glomerulonephritis, initiation of the extrinsic coagulation pathway by activating coagulation factor X to factor Xa, factor Xa promote the proliferation of mesangial cells in culture, enzyme inhibitor DX-9065a treatment significantly ameliorated proteinuria in vivo in rats with a a significant reduction in the size of glomeruli, the total number of glomerular cells, and crescent formation, as well as abolishing phosphorylation of p44/42 MAP kinase on day 8, overview
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additional information
?
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enzyme link between cancer and thrombosis appears to be a bidirectional relationship, physiological role of factor Xa, involvement in inflammation and diseases, physiological interactions, regulation, overview
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?