PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2529923-4 1989 We studied native and ASA-treated platelets for their ability to mobilize and to express platelet-vWF in response to adenosine diphosphate (ADP) or thrombin. Adenosine Diphosphate 117-138 von Willebrand factor Homo sapiens 98-101 2529923-4 1989 We studied native and ASA-treated platelets for their ability to mobilize and to express platelet-vWF in response to adenosine diphosphate (ADP) or thrombin. Adenosine Diphosphate 140-143 von Willebrand factor Homo sapiens 98-101 2529923-7 1989 Measurement of secreted platelet-vWF and beta-thromboglobulin indicated that the increase seen with ADP was largely independent of alpha-granule secretion. Adenosine Diphosphate 100-103 von Willebrand factor Homo sapiens 33-36 2529923-8 1989 Using monoclonal antibodies (MoAbs) against the platelet glycoproteins (GP) IIb/IIIa and Ib (MoAbs 10E5 and 6D1, respectively), we demonstrated that the ADP-induced increase in platelet-vWF expression on control platelets primarily involved the binding of secreted platelet-vWF to the platelet GPIIb/IIIa. Adenosine Diphosphate 153-156 von Willebrand factor Homo sapiens 186-189 2529923-8 1989 Using monoclonal antibodies (MoAbs) against the platelet glycoproteins (GP) IIb/IIIa and Ib (MoAbs 10E5 and 6D1, respectively), we demonstrated that the ADP-induced increase in platelet-vWF expression on control platelets primarily involved the binding of secreted platelet-vWF to the platelet GPIIb/IIIa. Adenosine Diphosphate 153-156 von Willebrand factor Homo sapiens 274-277 2529923-9 1989 In contrast, the increase in platelet-vWF that occurred following ADP stimulation of ASA-treated platelets was largely insensitive to GPIIb/IIIa blockade. Adenosine Diphosphate 66-69 von Willebrand factor Homo sapiens 38-41 2529923-11 1989 When platelet shape change was prevented by the addition of cytochalasin D, ADP-induced platelet-vWf surface expression on ASA-treated platelets was reduced by more than 80%. Adenosine Diphosphate 76-79 von Willebrand factor Homo sapiens 97-100 3140912-6 1988 At a concentration of 10 micrograms IgG/mL, PP3-3A completely inhibited binding either of 125I-fibrinogen or of 125I-vWF to ADP-stimulated platelets. Adenosine Diphosphate 124-127 von Willebrand factor Homo sapiens 117-120 2786916-1 1989 When platelets are stimulated with adenosine diphosphate (ADP), thrombin, or ristocetin, they bind soluble von Willebrand factor (vWF). Adenosine Diphosphate 35-56 von Willebrand factor Homo sapiens 107-128 2786916-1 1989 When platelets are stimulated with adenosine diphosphate (ADP), thrombin, or ristocetin, they bind soluble von Willebrand factor (vWF). Adenosine Diphosphate 35-56 von Willebrand factor Homo sapiens 130-133 2786916-1 1989 When platelets are stimulated with adenosine diphosphate (ADP), thrombin, or ristocetin, they bind soluble von Willebrand factor (vWF). Adenosine Diphosphate 58-61 von Willebrand factor Homo sapiens 107-128 2786916-1 1989 When platelets are stimulated with adenosine diphosphate (ADP), thrombin, or ristocetin, they bind soluble von Willebrand factor (vWF). Adenosine Diphosphate 58-61 von Willebrand factor Homo sapiens 130-133 2786916-11 1989 When used to stimulate the platelets, ADP, thrombin, and ristocetin all increased the platelet adhesion to solid-phase vWF. Adenosine Diphosphate 38-41 von Willebrand factor Homo sapiens 119-122 2786916-16 1989 In addition, these platelets can be stimulated to increase their adherence to vWF by using ADP, thrombin, and ristocetin. Adenosine Diphosphate 91-94 von Willebrand factor Homo sapiens 78-81 2822171-10 1987 Aspirin and prostaglandin E1 also inhibited ADP-induced binding of vWf in platelet-rich plasma. Adenosine Diphosphate 44-47 von Willebrand factor Homo sapiens 67-70 2822169-1 1987 We used immunoelectron microscopic localization techniques to investigate whether platelets stimulated by ADP or ristocetin in the plasma milieu bind von Willebrand factor (vWF) to their surfaces. Adenosine Diphosphate 106-109 von Willebrand factor Homo sapiens 150-171 2822169-1 1987 We used immunoelectron microscopic localization techniques to investigate whether platelets stimulated by ADP or ristocetin in the plasma milieu bind von Willebrand factor (vWF) to their surfaces. Adenosine Diphosphate 106-109 von Willebrand factor Homo sapiens 173-176 2822169-2 1987 We found by both peroxidase- and ferritin-based methods that unstimulated platelets lack vWF on their surfaces, whereas platelets that are stimulated with ADP or ristocetin have vWF associated with their surfaces. Adenosine Diphosphate 155-158 von Willebrand factor Homo sapiens 178-181 2822169-5 1987 Thus, in the plasma environment, in the presence of fibrinogen, vWF becomes associated with the platelet surface subsequent to stimulation with ADP or ristocetin. Adenosine Diphosphate 144-147 von Willebrand factor Homo sapiens 64-67 2822171-0 1987 von Willebrand factor is present on the surface of platelets stimulated in plasma by ADP. Adenosine Diphosphate 85-88 von Willebrand factor Homo sapiens 0-21 2822171-4 1987 Using this assay, we found vWf on the surface of platelets stimulated in plasma by ADP. Adenosine Diphosphate 83-86 von Willebrand factor Homo sapiens 27-30 2822171-5 1987 The number of platelets that bound vWf increased in proportion to ADP concentration and incubation time. Adenosine Diphosphate 66-69 von Willebrand factor Homo sapiens 35-38 2822171-6 1987 Washed platelets in a protein-free buffer activated by 1 mumol/L calcium ionophore A23187 or 10 mumol/L ADP also bound vWf, suggesting that we were detecting surface binding of alpha-granule-derived vWf. Adenosine Diphosphate 104-107 von Willebrand factor Homo sapiens 119-122 2822171-6 1987 Washed platelets in a protein-free buffer activated by 1 mumol/L calcium ionophore A23187 or 10 mumol/L ADP also bound vWf, suggesting that we were detecting surface binding of alpha-granule-derived vWf. Adenosine Diphosphate 104-107 von Willebrand factor Homo sapiens 199-202 3263711-1 1988 Native von Willebrand factor (N-vWF) binds to platelets activated by thrombin, ADP or ristocetin. Adenosine Diphosphate 79-82 von Willebrand factor Homo sapiens 32-35 3258770-0 1988 Shear-induced platelet aggregation can be mediated by vWF released from platelets, as well as by exogenous large or unusually large vWF multimers, requires adenosine diphosphate, and is resistant to aspirin. Adenosine Diphosphate 156-177 von Willebrand factor Homo sapiens 132-135 2437231-6 1987 As-VWF binding to the GPllb-llla complex appears to be approximately 70% to 80% ADP dependent and approximately 20% to 30% ADP independent. Adenosine Diphosphate 80-83 von Willebrand factor Homo sapiens 3-6 3497679-0 1987 Effect of calcium ion concentration on the ability of fibrinogen and von Willebrand factor to support the ADP-induced aggregation of human platelets. Adenosine Diphosphate 106-109 von Willebrand factor Homo sapiens 69-90 3497679-3 1987 In the low calcium medium, either vWf or fibrinogen supported biphasic aggregation in response to ADP, with thromboxane formation and release of granule contents. Adenosine Diphosphate 98-101 von Willebrand factor Homo sapiens 34-37 3497679-6 1987 Although vWf supports ADP-induced aggregation when the concentration of ionized calcium is in the micromolar range, it does not support ADP-induced aggregation in the presence of a concentration of ionized calcium in the physiological range, indicating that vWf probably cannot substitute for fibrinogen in supporting ADP-induced aggregation in vivo. Adenosine Diphosphate 22-25 von Willebrand factor Homo sapiens 9-12 2437231-6 1987 As-VWF binding to the GPllb-llla complex appears to be approximately 70% to 80% ADP dependent and approximately 20% to 30% ADP independent. Adenosine Diphosphate 123-126 von Willebrand factor Homo sapiens 3-6 2827552-3 1987 At least one receptor mechanism for fibrinogen and for vWF is controlled by ADP that is secreted through the known pathways of platelet activation and counterbalanced by cyclic AMP. Adenosine Diphosphate 76-79 von Willebrand factor Homo sapiens 55-58 3804319-4 1987 There are two receptor pathways--classic and alternative--for the binding of vWF to platelets; the latter induced by thrombin, and adenosine diphosphate (ADP) is shared with fibrinogen. Adenosine Diphosphate 131-152 von Willebrand factor Homo sapiens 77-80 3804319-4 1987 There are two receptor pathways--classic and alternative--for the binding of vWF to platelets; the latter induced by thrombin, and adenosine diphosphate (ADP) is shared with fibrinogen. Adenosine Diphosphate 154-157 von Willebrand factor Homo sapiens 77-80 6087354-3 1984 Binding of 125I-labeled vWF to human platelets separated from plasma proteins and treated with ADP was specific, and time and concentration dependent, reaching equilibrium at 20 min and approaching saturation at 12 micrograms/ml. Adenosine Diphosphate 95-98 von Willebrand factor Homo sapiens 24-27 3007578-5 1986 Addition of purified vWF to the afibrinogenemic plasma resulted in marked increase in the rate and extent of aggregation, particularly when platelets were stimulated with ADP. Adenosine Diphosphate 171-174 von Willebrand factor Homo sapiens 21-24 6087354-8 1984 Conversely, unlabeled vWF inhibited ADP-induced binding of 125I-labeled fibrinogen (60 micrograms/ml) with an IC50 of 16 micrograms/ml. Adenosine Diphosphate 36-39 von Willebrand factor Homo sapiens 22-25 6087354-9 1984 A synthetic dodecapeptide (Mr, 1188), analogous with the specific platelet receptor recognition site of human fibrinogen gamma chain (gamma 400-411), inhibited binding of both 125I-labeled vWF and 125I-labeled fibrinogen to ADP-treated platelets, whereas it was without effect on binding of 125I-labeled vWF to ristocetin-treated platelets. Adenosine Diphosphate 224-227 von Willebrand factor Homo sapiens 189-192 6087354-10 1984 These data indicate that vWF and fibrinogen have a common receptor mechanism for their interaction with human platelets that is dependent on ADP occupancy of its binding sites and is recognized by the sequence of 12 amino acid residues at the carboxyl terminus of the human fibrinogen gamma chain. Adenosine Diphosphate 141-144 von Willebrand factor Homo sapiens 25-28 6087354-5 1984 A purine nucleotide affinity analog, 5"-p-fluorosulfonylbenzoyl adenosine (FSBA), which covalently modifies the ADP binding sites on the human platelet membrane, prevented binding of vWF induced with ADP, as well as with human thrombin and with ionophore A23187, agents known to cause platelet ADP secretion. Adenosine Diphosphate 112-115 von Willebrand factor Homo sapiens 183-186 6087354-5 1984 A purine nucleotide affinity analog, 5"-p-fluorosulfonylbenzoyl adenosine (FSBA), which covalently modifies the ADP binding sites on the human platelet membrane, prevented binding of vWF induced with ADP, as well as with human thrombin and with ionophore A23187, agents known to cause platelet ADP secretion. Adenosine Diphosphate 200-203 von Willebrand factor Homo sapiens 183-186 6087354-5 1984 A purine nucleotide affinity analog, 5"-p-fluorosulfonylbenzoyl adenosine (FSBA), which covalently modifies the ADP binding sites on the human platelet membrane, prevented binding of vWF induced with ADP, as well as with human thrombin and with ionophore A23187, agents known to cause platelet ADP secretion. Adenosine Diphosphate 200-203 von Willebrand factor Homo sapiens 183-186 6087354-7 1984 Human fibrinogen inhibited in a competitive manner the ADP-induced binding of 125I-labeled vWF (9 micrograms/ml) with an IC50 of 25 micrograms/ml. Adenosine Diphosphate 55-58 von Willebrand factor Homo sapiens 91-94 6324004-3 1984 Two apparently distinct mechanisms have now been identified for enhancing 125I-vWF interaction with stimulated platelets: one is induced by ristocetin and apparently mediated by platelet membrane glycoprotein Ib (GPIb); a second mechanism has been identified more recently and is induced by the physiological stimuli ADP and thrombin. Adenosine Diphosphate 317-320 von Willebrand factor Homo sapiens 79-82 6324004-5 1984 As ADP and thrombin are released at sites of platelet accumulation, it is possible that these agonists regulate the vWF-platelet interactions in vivo. Adenosine Diphosphate 3-6 von Willebrand factor Homo sapiens 116-119 6324004-7 1984 Thus, in addition to its role in coagulation and platelet aggregation, fibrinogen influences the binding of vWF to thrombin- and ADP-stimulated platelets. Adenosine Diphosphate 129-132 von Willebrand factor Homo sapiens 108-111 6223940-1 1983 The binding of 125I-von Willebrand factor (125I-vWF) to platelets stimulated by thrombin, ADP, and a combination of ADP + epinephrine (EPI) is specific, saturable, and reversible. Adenosine Diphosphate 90-93 von Willebrand factor Homo sapiens 20-41 6230372-2 1984 Plasma proteins specifically inhibited the thrombin- and ADP/epinephrine-induced vWf binding to activated platelets but did not inhibit the ristocetin-induced vWf binding. Adenosine Diphosphate 57-60 von Willebrand factor Homo sapiens 81-84 6230372-3 1984 When normal plasma was heat defibrinated, monoclonal-labeled vWf was bound to platelets following thrombin or ADP/epinephrine stimulation. Adenosine Diphosphate 110-113 von Willebrand factor Homo sapiens 61-64 6230372-8 1984 These studies show that thrombin-induced and ADP/epinephrine-induced vWf binding to platelets does not occur in the plasma milieu, although at reduced levels of fibrinogen, vWf binding to stimulated platelets can be demonstrated. Adenosine Diphosphate 45-48 von Willebrand factor Homo sapiens 69-72 6419373-1 1983 Human Factor VIII associated von Willebrand factor (VIII:vWF) binds to human platelets in vitro only in the presence of a mediator such as ristocetin, thrombin or ADP. Adenosine Diphosphate 163-166 von Willebrand factor Homo sapiens 57-60 6223940-1 1983 The binding of 125I-von Willebrand factor (125I-vWF) to platelets stimulated by thrombin, ADP, and a combination of ADP + epinephrine (EPI) is specific, saturable, and reversible. Adenosine Diphosphate 90-93 von Willebrand factor Homo sapiens 48-51 6281653-0 1982 Adenosine diphosphate induces binding of von Willebrand factor to human platelets. Adenosine Diphosphate 0-21 von Willebrand factor Homo sapiens 41-62 6419355-0 1983 [Multimeric structure of factor VIII/von Willebrand factor released from human platelets by ADP, collagen and thrombin]. Adenosine Diphosphate 92-95 von Willebrand factor Homo sapiens 37-58 16706984-4 2006 RESULTS: In the presence of botrocetin and inhibitors of adenosine diphosphate (ADP) and thromboxane A2 (TxA2), VWF is able to support formation of lamellipodia through a GPIb-dependent mechanism that is independent of alpha(IIb)beta3 and PI3-kinase. Adenosine Diphosphate 57-78 von Willebrand factor Homo sapiens 112-115 818909-0 1976 ADP-induced inhibition of von Willebrand factor-mediated platelet agglutination. Adenosine Diphosphate 0-3 von Willebrand factor Homo sapiens 26-47 818909-2 1976 The prior addition of 1-10 muM ADP, which causes platelet shape change but not aggregation under these conditions, inhibited vWF-mediated agglutination. Adenosine Diphosphate 31-34 von Willebrand factor Homo sapiens 125-128 818909-4 1976 Addition of ADP caused prompt reversal of established vWF-mediated agglutination, which resumed when the ADP was enzymatically removed. Adenosine Diphosphate 12-15 von Willebrand factor Homo sapiens 54-57 818909-4 1976 Addition of ADP caused prompt reversal of established vWF-mediated agglutination, which resumed when the ADP was enzymatically removed. Adenosine Diphosphate 105-108 von Willebrand factor Homo sapiens 54-57 818909-10 1976 It concluded that ADP causes a reversible decrease in the accessibility of the membrane receptor to vWF. Adenosine Diphosphate 18-21 von Willebrand factor Homo sapiens 100-103 24270421-6 2013 Further, alphaIIbbeta3 activation and activation of the small GTPase Rap1 were impaired by vWF/p.V1316M following exposure to platelet agonists (thrombin, ADP, or convulxin). Adenosine Diphosphate 155-158 von Willebrand factor Homo sapiens 91-94 28567087-8 2017 Irrespective of regimen, the changes in fibrinogen and vWF:Ag levels were mainly associated with the change in ADP-mediated PR (r=0.339, p=0.008 and r=0.322, p=0.012, respectively). Adenosine Diphosphate 111-114 von Willebrand factor Homo sapiens 55-58 28567087-9 2017 CONCLUSION: In patients with NVAF, combination antiplatelet therapy showed reductions for vWF:Ag and fibrinogen levels, which may be associated with the inhibitory levels of ADP-mediated PR. Adenosine Diphosphate 174-177 von Willebrand factor Homo sapiens 90-93 20024494-11 2010 We conclude that reduced levels of large VWF multimers associated with aortic stenosis lead to impairment of both adhesion and, especially, ADP-inducible platelet aggregation. Adenosine Diphosphate 140-143 von Willebrand factor Homo sapiens 41-44 18987357-6 2009 Thus, human von Willebrand factor contains an RGD motif and binds equally well to adenosine diphosphate-stimulated human and rodent platelets, implying that other motifs are responsible for maintaining ligand binding affinity. Adenosine Diphosphate 82-103 von Willebrand factor Homo sapiens 12-33 17100655-10 2006 CONCLUSIONS: We demonstrate that VWF activates eNOS through a specific Ca2+-dependent GPIb receptor-signaling cascade that relies on the generation of platelet-derived ADP and TxA2. Adenosine Diphosphate 168-171 von Willebrand factor Homo sapiens 33-36 16706984-4 2006 RESULTS: In the presence of botrocetin and inhibitors of adenosine diphosphate (ADP) and thromboxane A2 (TxA2), VWF is able to support formation of lamellipodia through a GPIb-dependent mechanism that is independent of alpha(IIb)beta3 and PI3-kinase. Adenosine Diphosphate 80-83 von Willebrand factor Homo sapiens 112-115 15284110-6 2004 Our results demonstrate that, under elevated shear stress conditions, ADP signaling through P2Y(1) may contribute to the initial stages of platelet adhesion and activation mediated by immobilized VWF, and through P2Y(12) to sustained thrombus formation. Adenosine Diphosphate 70-73 von Willebrand factor Homo sapiens 196-199 15821821-11 2005 vWF and diastolic blood pressure were significant predictors for adenosine diphosphate-induced platelet aggregability. Adenosine Diphosphate 65-86 von Willebrand factor Homo sapiens 0-3 9588391-1 1998 This article addresses the flow-dependent differential roles of the platelet receptors, glycoprotein (GP) GPIb and GPIIb-IIIa, in platelet aggregation mediated by ristocetin and soluble von Willebrand factor (vWF), by adenosine diphosphate (ADP) and soluble fibrinogen (Fg), and by thrombin and ADP in absence of exogenous ligands. Adenosine Diphosphate 218-239 von Willebrand factor Homo sapiens 209-212 10539883-9 1999 All samples from patients confirmed to have VWD following specific VWF studies [N = 9; 3 x Type 1, 1 x Type 3, 1 x Type 2A, 4 x Type 2B] gave prolonged CTs (>/= 200 s) for both C/ADP and C/Epi membranes; in contrast, all patients yielding normal CT values were found to yield normal VWF results (i.e., were found not to suffer from VWD). Adenosine Diphosphate 182-185 von Willebrand factor Homo sapiens 67-70 9588391-6 1998 The physiologic activators ADP and thrombin both supported efficient aggregation of washed platelets with no exogenous ligands at 1000 sec(-1) by surface-secreted vWF (CE = 0.08 +/- 0.01, n = 6), in contrast to poorer ADP and soluble Fg-mediated aggregation in the absence of secretion (CE = 0.05). Adenosine Diphosphate 27-30 von Willebrand factor Homo sapiens 163-166 9588391-6 1998 The physiologic activators ADP and thrombin both supported efficient aggregation of washed platelets with no exogenous ligands at 1000 sec(-1) by surface-secreted vWF (CE = 0.08 +/- 0.01, n = 6), in contrast to poorer ADP and soluble Fg-mediated aggregation in the absence of secretion (CE = 0.05). Adenosine Diphosphate 218-221 von Willebrand factor Homo sapiens 163-166 14675082-6 2003 Treatment of cells with agonists of platelet activation (ADP, epinephrine, and thrombin receptor-activating peptide) resulted in the release of VWF antigen and active FVIII into the supernatant from transduced cells. Adenosine Diphosphate 57-60 von Willebrand factor Homo sapiens 144-147 9588391-1 1998 This article addresses the flow-dependent differential roles of the platelet receptors, glycoprotein (GP) GPIb and GPIIb-IIIa, in platelet aggregation mediated by ristocetin and soluble von Willebrand factor (vWF), by adenosine diphosphate (ADP) and soluble fibrinogen (Fg), and by thrombin and ADP in absence of exogenous ligands. Adenosine Diphosphate 241-244 von Willebrand factor Homo sapiens 209-212 8772218-4 1995 Thus, after induction of vWF release from platelets by polybrene or ADP, platelet function was normal. Adenosine Diphosphate 68-71 von Willebrand factor Homo sapiens 25-28 9435321-5 1998 In contrast, platelets exposed to high shear rate after activation by exogenous agonists such as ADP and epinephrine can aggregate when fibrinogen is the alphaIIbbeta3 adhesive ligand, yet only if vWf binding to glycoprotein Ibalpha can also occur. Adenosine Diphosphate 97-100 von Willebrand factor Homo sapiens 197-200 9414275-14 1998 Our results suggest that ATP/ADP can induce vWF release from endothelial cells via dual activation of P2y and adenosine A2 receptors. Adenosine Diphosphate 29-32 von Willebrand factor Homo sapiens 44-47 9168979-3 1997 This antibody inhibited high shear-induced platelet aggregation and blocked adhesion of ADP plus epinephrine-stimulated platelets to vWf, indicating that it interferes with the interaction with alpha IIb beta 3. Adenosine Diphosphate 88-91 von Willebrand factor Homo sapiens 133-136 9066012-0 1997 Surface-secreted von Willebrand factor mediates aggregation of ADP-activated platelets at moderate shear stress: facilitated by GPIb but controlled by GPIIb-IIIa. Adenosine Diphosphate 63-66 von Willebrand factor Homo sapiens 17-38 9066012-7 1997 We showed that mAbs 6D1 and NMC4, respectively blocking the adhesive domains on the GPIb receptor recognizing vWF, and on the vWF molecule recognizing the GPIb receptor, partially inhibited ADP-induced aggregation under shear in Couette flow, the degree of inhibition increasing with increasing shear stress. Adenosine Diphosphate 190-193 von Willebrand factor Homo sapiens 110-113 9066012-7 1997 We showed that mAbs 6D1 and NMC4, respectively blocking the adhesive domains on the GPIb receptor recognizing vWF, and on the vWF molecule recognizing the GPIb receptor, partially inhibited ADP-induced aggregation under shear in Couette flow, the degree of inhibition increasing with increasing shear stress. Adenosine Diphosphate 190-193 von Willebrand factor Homo sapiens 126-129 9066012-9 1997 We conclude that vWF, expressed on ADP-activated platelets, is at least the predominant cross-bridging molecule mediating aggregation at moderate shear stress. Adenosine Diphosphate 35-38 von Willebrand factor Homo sapiens 17-20 7974361-4 1994 We have examined the effects of the platelet secretagogues ADP, AMP, ATP and serotonin on the release of vWf from ECs and demonstrated enhanced release in all cases. Adenosine Diphosphate 59-62 von Willebrand factor Homo sapiens 105-108 7669029-5 1995 The IIB vWF-evoked (3 micrograms/ml) cytosolic Ca2+ increase was negligibly affected by ADP scavengers or protein kinase C inhibitors; it was drastically reduced by EGTA, La3+, Ni2+ or acetylsalicylate and abolished by the phospholipase A2 inhibitors ONO-RS-082 or oleolyloxyethyl-phosphocholine. Adenosine Diphosphate 88-91 von Willebrand factor Homo sapiens 8-11 21043735-4 1995 There are now at least two systems of platelet activation under intensive study: (a) agonist (e.g. ADP and thrombin) induced platelet activation when fibrinogen is the ligand; this process occurs at low shear forces and is aspirin sensitive; (b) secondly, in marked contrast, at high shear forces, shear itself activates the platelets and von Willebrand"s factor (vWf) is the ligand, and this process is aspirin insensitive. Adenosine Diphosphate 99-102 von Willebrand factor Homo sapiens 339-362 21043735-4 1995 There are now at least two systems of platelet activation under intensive study: (a) agonist (e.g. ADP and thrombin) induced platelet activation when fibrinogen is the ligand; this process occurs at low shear forces and is aspirin sensitive; (b) secondly, in marked contrast, at high shear forces, shear itself activates the platelets and von Willebrand"s factor (vWf) is the ligand, and this process is aspirin insensitive. Adenosine Diphosphate 99-102 von Willebrand factor Homo sapiens 364-367 7660157-9 1995 In addition, the IVBT with ADP showed a close correlation to the vWF:RCo activity (r2 = 0.73). Adenosine Diphosphate 27-30 von Willebrand factor Homo sapiens 65-68 7529494-11 1994 In contrast with the behaviour of these venom proteins, the adhesion of ADP-treated platelets to immobilized fibrinogen, fibronectin and vWF was inhibited non-selectively by a range of monoclonal antibodies with specificity for the alpha IIb beta 3 complex. Adenosine Diphosphate 72-75 von Willebrand factor Homo sapiens 137-140 8051492-1 1994 Platelet membrane glycoproteins Ib (GPIb) and IIb/IIIa (GPIIb/IIIa) bind soluble von Willebrand factor (vWf) after stimulation with ristocetin (GPIb) or with thrombin or ADP (GPIIb/IIIa). Adenosine Diphosphate 170-173 von Willebrand factor Homo sapiens 81-102 8051492-1 1994 Platelet membrane glycoproteins Ib (GPIb) and IIb/IIIa (GPIIb/IIIa) bind soluble von Willebrand factor (vWf) after stimulation with ristocetin (GPIb) or with thrombin or ADP (GPIIb/IIIa). Adenosine Diphosphate 170-173 von Willebrand factor Homo sapiens 104-107 2401846-6 1990 We conclude that inhibition of agglutination by ADP must involve the way in which vWf is bound, because it does not result from a decreased amount or from a difference in multimer size of bound vWf. Adenosine Diphosphate 48-51 von Willebrand factor Homo sapiens 82-85 8238012-5 1993 Activation-dependent receptor function of the GP IIb-IIIa complex was studied with 125I-fibrinogen and 125I-vWF binding to washed platelets stimulated with adenosine diphosphate plus epinephrine (10 mumol/L each). Adenosine Diphosphate 156-177 von Willebrand factor Homo sapiens 108-111 2046403-6 1991 Aspirin inhibits 80% of the adenosine diphosphate-induced platelet vWF surface expression, and the platelet vWF surface expression that is not inhibited by aspirin can be almost totally inhibited by disruption of the platelet cytoskeleton. Adenosine Diphosphate 28-49 von Willebrand factor Homo sapiens 67-70 1499407-7 1992 It was found that the plasma vWF correlated with platelet aggregation induced by ADP constantly, but not with other risk factors. Adenosine Diphosphate 81-84 von Willebrand factor Homo sapiens 29-32 2401846-0 1990 Inhibition of von Willebrand factor-induced platelet agglutination by ADP does not result from reduced binding of total von Willebrand factor or its larger multimers. Adenosine Diphosphate 70-73 von Willebrand factor Homo sapiens 14-35 2401846-1 1990 Earlier experiments showed that platelet agglutination induced by von Willebrand factor (vWf) plus ristocetin was greatly diminished if adenosine diphosphate (ADP) was added first in the presence of ethylenediaminetetraacetic acid (to prevent aggregation). Adenosine Diphosphate 136-157 von Willebrand factor Homo sapiens 66-87 2401846-1 1990 Earlier experiments showed that platelet agglutination induced by von Willebrand factor (vWf) plus ristocetin was greatly diminished if adenosine diphosphate (ADP) was added first in the presence of ethylenediaminetetraacetic acid (to prevent aggregation). Adenosine Diphosphate 136-157 von Willebrand factor Homo sapiens 89-92 2401846-1 1990 Earlier experiments showed that platelet agglutination induced by von Willebrand factor (vWf) plus ristocetin was greatly diminished if adenosine diphosphate (ADP) was added first in the presence of ethylenediaminetetraacetic acid (to prevent aggregation). Adenosine Diphosphate 159-162 von Willebrand factor Homo sapiens 66-87 2401846-1 1990 Earlier experiments showed that platelet agglutination induced by von Willebrand factor (vWf) plus ristocetin was greatly diminished if adenosine diphosphate (ADP) was added first in the presence of ethylenediaminetetraacetic acid (to prevent aggregation). Adenosine Diphosphate 159-162 von Willebrand factor Homo sapiens 89-92 2346725-8 1990 Calpain proteolysis of vWF changed the binding characteristics of the vWF so that it had greatly increased binding to both ADP and calpain activated platelets. Adenosine Diphosphate 123-126 von Willebrand factor Homo sapiens 23-26 2346725-8 1990 Calpain proteolysis of vWF changed the binding characteristics of the vWF so that it had greatly increased binding to both ADP and calpain activated platelets. Adenosine Diphosphate 123-126 von Willebrand factor Homo sapiens 70-73 2154674-1 1990 Agglutination of human platelets by bovine von Willebrand factor (vWF) or by human vWF in the presence of ristocetin is inhibited by ADP and by several other platelet agonists but not by epinephrine. Adenosine Diphosphate 133-136 von Willebrand factor Homo sapiens 83-86 2154674-5 1990 ADP caused a small decrease in the number and affinity of binding sites for vWF on platelets, too small to explain the inhibition of agglutination. Adenosine Diphosphate 0-3 von Willebrand factor Homo sapiens 76-79