PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
20498367-11	2010	EDTA or antibodies against GPIbalpha and alphaIIbbeta3 blocked the effect of the mutant and ristocetin on platelet activation/adhesion.	Ristocetin	92-102	glycoprotein Ib platelet subunit alpha	Homo sapiens	27-36
20231421-0	2010	Common VWF exon 28 polymorphisms in African Americans affecting the VWF activity assay by ristocetin cofactor.	Ristocetin	90-100	von Willebrand factor	Homo sapiens	7-10
20231421-0	2010	Common VWF exon 28 polymorphisms in African Americans affecting the VWF activity assay by ristocetin cofactor.	Ristocetin	90-100	von Willebrand factor	Homo sapiens	68-71
20231421-7	2010	Because the VWF:RCo assay depends on ristocetin binding to VWF, mutations (and polymorphisms) in VWF may affect the measurement of "VWF activity" by this assay and may not reflect a functional defect or true hemorrhagic risk.	Ristocetin	37-47	von Willebrand factor	Homo sapiens	12-15
20216992-6	2010	We conclude that the NTF change induced by 0/37 degrees C incubation reflects clustering of GPIbalpha supports VWF/ristocetin-induced agglutination and spreading and is sufficient to initiate platelet activation in the absence of VWF.	Ristocetin	115-125	glycoprotein Ib platelet subunit alpha	Homo sapiens	92-101
20635317-5	2010	The specific activity for binding to collagen and platelets mediated by ristocetin is higher in rVWF than in commercial plasma-derived VWF-FVIII complex products.	Ristocetin	72-82	von Willebrand factor	Rattus norvegicus	96-100
20635317-5	2010	The specific activity for binding to collagen and platelets mediated by ristocetin is higher in rVWF than in commercial plasma-derived VWF-FVIII complex products.	Ristocetin	72-82	von Willebrand factor	Homo sapiens	97-100
20635317-5	2010	The specific activity for binding to collagen and platelets mediated by ristocetin is higher in rVWF than in commercial plasma-derived VWF-FVIII complex products.	Ristocetin	72-82	coagulation factor VIII	Homo sapiens	139-144
20216992-6	2010	We conclude that the NTF change induced by 0/37 degrees C incubation reflects clustering of GPIbalpha supports VWF/ristocetin-induced agglutination and spreading and is sufficient to initiate platelet activation in the absence of VWF.	Ristocetin	115-125	von Willebrand factor	Homo sapiens	111-114
19932480-6	2010	Aspirin and SC-560, a cyclooxygenase-1 inhibitor, suppressed the ristocetin-induced sCD40L release from platelets in parallel with TXA(2) production.	Ristocetin	65-75	prostaglandin-endoperoxide synthase 1	Homo sapiens	22-38
19633908-5	2010	We measured the plasma concentration of von-Willebrand-factor-antigen (VWF:Ag), the activity of von-Willebrand-factor-Ristocetin-Cofactor (VWF:RiCo) and FVIII at several stress-levels and consecutively split up the different VWF-multimers.	Ristocetin	118-128	von Willebrand factor	Homo sapiens	96-117
20179578-9	2010	Activities determined with HemosIL vWF:activity had good correlation with those determined as ristocetin cofactor, Imubind (vWF:Imubind) and collagen-binding.	Ristocetin	94-104	von Willebrand factor	Homo sapiens	35-38
20179578-11	2010	This automated HemosIL vWF:activity test could be included in routine determination of vWF activity in concentrate samples and supports traditional von Willebrand ristocetin cofactor because it is reliable, reproducible and sensitive.	Ristocetin	163-173	von Willebrand factor	Homo sapiens	23-26
20443704-5	2010	We previously generated a high affinity monoclonal antibody against human platelet GPIbalpha, SZ2, which inhibits both ristocetin- and botrocetin-induced platelet aggregation in vitro.	Ristocetin	119-129	glycoprotein Ib platelet subunit alpha	Homo sapiens	83-92
20443704-9	2010	In vitro functional studies revealed that the chimeric antibody and its Fab fragment prevented platelet adhesion to VWF under high shear stress and inhibited ristocetin-induced platelet aggregation in a dose-dependent manner.	Ristocetin	158-168	FA complementation group B	Homo sapiens	72-75
20443704-9	2010	In vitro functional studies revealed that the chimeric antibody and its Fab fragment prevented platelet adhesion to VWF under high shear stress and inhibited ristocetin-induced platelet aggregation in a dose-dependent manner.	Ristocetin	158-168	von Willebrand factor	Homo sapiens	116-119
19506359-4	2009	There is a good response to desmopressin (DDAVP) followed by rapid clearance of VWF:antigen (Ag), factor VIII coagulant activity (FVIII:C) and VWF:ristocetin cofactor activity (RCo) as the main cause of VWD type 1 or 2 with typical 2E multimeric pattern (VWD type 1/2E).	Ristocetin	147-157	von Willebrand factor	Homo sapiens	143-146
19840363-5	2010	RESULTS: Ristocetin-induced GPIbalpha-VWF interaction elicited apoptotic events in platelets, including phosphatidylserine exposure, elevations of Bax and Bak, gelsolin cleavage, and depolarization of mitochondrial inner transmembrane potential.	Ristocetin	9-19	von Willebrand factor	Cricetulus griseus	38-41
19840363-5	2010	RESULTS: Ristocetin-induced GPIbalpha-VWF interaction elicited apoptotic events in platelets, including phosphatidylserine exposure, elevations of Bax and Bak, gelsolin cleavage, and depolarization of mitochondrial inner transmembrane potential.	Ristocetin	9-19	apoptosis regulator BAX	Cricetulus griseus	147-150
19840363-5	2010	RESULTS: Ristocetin-induced GPIbalpha-VWF interaction elicited apoptotic events in platelets, including phosphatidylserine exposure, elevations of Bax and Bak, gelsolin cleavage, and depolarization of mitochondrial inner transmembrane potential.	Ristocetin	9-19	gelsolin	Cricetulus griseus	160-168
19875727-6	2009	MP-P also promoted GPIb-IX association with the membrane skeleton, and inhibited ristocetin-induced platelet agglutination, VWF binding to platelets and platelet adhesion to immobilized VWF.	Ristocetin	81-91	von Willebrand factor	Homo sapiens	186-189
19875727-7	2009	Furthermore, a GPIb-IX mutant replacing Ser559 of GPIbalpha with alanine showed an enhanced association with the membrane skeleton, reduced ristocetin-induced VWF binding, and diminished ability to mediate cell adhesion to VWF under flow conditions.	Ristocetin	140-150	glycoprotein Ib platelet subunit alpha	Homo sapiens	50-59
19875727-7	2009	Furthermore, a GPIb-IX mutant replacing Ser559 of GPIbalpha with alanine showed an enhanced association with the membrane skeleton, reduced ristocetin-induced VWF binding, and diminished ability to mediate cell adhesion to VWF under flow conditions.	Ristocetin	140-150	von Willebrand factor	Homo sapiens	159-162
19497443-5	2009	RESULTS: The von Willebrand factor (vWF)-dependent ristocetin-induced platelet aggregation was impaired in 11 of the 16 patients, of which 12 had experienced at least 1 minor or major bleeding episode.	Ristocetin	51-61	von Willebrand factor	Homo sapiens	13-34
19497443-5	2009	RESULTS: The von Willebrand factor (vWF)-dependent ristocetin-induced platelet aggregation was impaired in 11 of the 16 patients, of which 12 had experienced at least 1 minor or major bleeding episode.	Ristocetin	51-61	von Willebrand factor	Homo sapiens	36-39
19497443-6	2009	The impaired ristocetin-induced platelet aggregation was associated both with decreased specific activity of plasma vWF, presumably due to lack of high molecular weight vWF multimers, as well as with attenuated function of the platelets themselves.	Ristocetin	13-23	von Willebrand factor	Homo sapiens	116-119
19497443-6	2009	The impaired ristocetin-induced platelet aggregation was associated both with decreased specific activity of plasma vWF, presumably due to lack of high molecular weight vWF multimers, as well as with attenuated function of the platelets themselves.	Ristocetin	13-23	von Willebrand factor	Homo sapiens	169-172
19506360-3	2009	Typical laboratory features of VWD type 2 M are decreased ristocetin-induced platelet aggregation in the presence of a normal or near normal VWF multimeric pattern on a low-resolution agarose gel, a poor response to desmopressin (DDAVP) of VWF:RCo, and a good response of both VWF:CB and VWF:Ag to DDAVP.	Ristocetin	58-68	von Willebrand factor	Homo sapiens	240-243
19506360-3	2009	Typical laboratory features of VWD type 2 M are decreased ristocetin-induced platelet aggregation in the presence of a normal or near normal VWF multimeric pattern on a low-resolution agarose gel, a poor response to desmopressin (DDAVP) of VWF:RCo, and a good response of both VWF:CB and VWF:Ag to DDAVP.	Ristocetin	58-68	von Willebrand factor	Homo sapiens	240-243
19506360-3	2009	Typical laboratory features of VWD type 2 M are decreased ristocetin-induced platelet aggregation in the presence of a normal or near normal VWF multimeric pattern on a low-resolution agarose gel, a poor response to desmopressin (DDAVP) of VWF:RCo, and a good response of both VWF:CB and VWF:Ag to DDAVP.	Ristocetin	58-68	von Willebrand factor	Homo sapiens	240-243
19811543-1	2010	The efficacy of highly purified VWF/FVIII concentrates with standardized ristocetin cofactor content (VWF:RCo) has been already proven in patients with von Willebrand"s disease (VWD).	Ristocetin	73-83	von Willebrand factor	Homo sapiens	32-35
19811543-1	2010	The efficacy of highly purified VWF/FVIII concentrates with standardized ristocetin cofactor content (VWF:RCo) has been already proven in patients with von Willebrand"s disease (VWD).	Ristocetin	73-83	coagulation factor VIII	Homo sapiens	36-41
19811543-1	2010	The efficacy of highly purified VWF/FVIII concentrates with standardized ristocetin cofactor content (VWF:RCo) has been already proven in patients with von Willebrand"s disease (VWD).	Ristocetin	73-83	von Willebrand factor	Homo sapiens	102-105
19694940-0	2009	Limitations of the ristocetin cofactor assay in measurement of von Willebrand factor function.	Ristocetin	19-29	von Willebrand factor	Homo sapiens	63-84
19694940-1	2009	BACKGROUND: Type 2M von Willebrand disease (VWD) is characterized by a qualitative defect in von Willebrand factor (VWF) and diagnosed by a disproportionate decrease in VWF ristocetin cofactor activity (VWF:RCo) as compared with VWF antigen (VWF:Ag).	Ristocetin	173-183	von Willebrand factor	Homo sapiens	169-172
19694940-1	2009	BACKGROUND: Type 2M von Willebrand disease (VWD) is characterized by a qualitative defect in von Willebrand factor (VWF) and diagnosed by a disproportionate decrease in VWF ristocetin cofactor activity (VWF:RCo) as compared with VWF antigen (VWF:Ag).	Ristocetin	173-183	von Willebrand factor	Homo sapiens	169-172
19694940-1	2009	BACKGROUND: Type 2M von Willebrand disease (VWD) is characterized by a qualitative defect in von Willebrand factor (VWF) and diagnosed by a disproportionate decrease in VWF ristocetin cofactor activity (VWF:RCo) as compared with VWF antigen (VWF:Ag).	Ristocetin	173-183	von Willebrand factor	Homo sapiens	169-172
19694940-1	2009	BACKGROUND: Type 2M von Willebrand disease (VWD) is characterized by a qualitative defect in von Willebrand factor (VWF) and diagnosed by a disproportionate decrease in VWF ristocetin cofactor activity (VWF:RCo) as compared with VWF antigen (VWF:Ag).	Ristocetin	173-183	von Willebrand factor	Homo sapiens	169-172
19694940-2	2009	OBJECTIVE: We report here on the spurious diagnosis of VWD in a patient with a sequence variation in the ristocetin-binding domain of VWF.	Ristocetin	105-115	von Willebrand factor	Homo sapiens	134-137
19694940-6	2009	RESULTS: Studies with recombinant VWF showed normal platelet binding with botrocetin, but a significant decrease in binding in response to ristocetin.	Ristocetin	139-149	von Willebrand factor	Homo sapiens	34-37
19694940-9	2009	CONCLUSIONS: The decreased VWF:RCo seen with the P1467S sequence variation likely represents an artifact as a result of the use of ristocetin to measure VWF activity.	Ristocetin	131-141	von Willebrand factor	Homo sapiens	27-30
19694940-9	2009	CONCLUSIONS: The decreased VWF:RCo seen with the P1467S sequence variation likely represents an artifact as a result of the use of ristocetin to measure VWF activity.	Ristocetin	131-141	von Willebrand factor	Homo sapiens	153-156
19647361-0	2009	Kinetic study of von Willebrand factor self-aggregation induced by ristocetin.	Ristocetin	67-77	von Willebrand factor	Homo sapiens	17-38
19647361-3	2009	Likewise, the binding of the glycopeptide antibiotic ristocetin to VWF triggers hemostatically relevant conformational transitions.	Ristocetin	53-63	von Willebrand factor	Homo sapiens	67-70
19647361-5	2009	In this study we investigated by a combined approach of light scattering spectroscopy and turbidimetry the ability of VWF to self-associate in solution in the presence of ristocetin and in the absence of any protein adsorbing surface.	Ristocetin	171-181	von Willebrand factor	Homo sapiens	118-121
18637125-0	2008	N1421K mutation in the glycoprotein Ib binding domain impairs ristocetin- and botrocetin-mediated binding of von Willebrand factor to platelets.	Ristocetin	62-72	von Willebrand factor	Homo sapiens	109-130
19110525-4	2008	Ristocetin-cofactor activity (VWF: RCo) was between 7% and 14% by measurement with von Willebrand reagent (Dade Behring, Marburg, Germany).	Ristocetin	0-10	von Willebrand factor	Homo sapiens	30-33
18637125-5	2008	In vitro mutagenesis and expression in COS-7 cells confirmed the impairment of the mutant in botrocetin- and ristocetin-mediated VWF binding to GPIb.	Ristocetin	109-119	von Willebrand factor	Homo sapiens	129-132
18637125-4	2008	Botrocetin- and ristocetin-mediated binding of plasma VWF to GPIb were reduced in the patients.	Ristocetin	16-26	von Willebrand factor	Homo sapiens	54-57
18485089-8	2008	VWF/ristocetin-mediated activation of the sGC/cGMP signaling pathway may contribute to feedback platelet inhibition.	Ristocetin	4-14	von Willebrand factor	Homo sapiens	0-3
18786009-6	2008	The HMW VWF multimer pattern in Haemate P/Humate-P is more similar to that of normal human plasma (94% for Haemate P/Humate-P vs. 100% for normal human plasma) than that of other VWF/FVIII concentrates and correlates with functional VWF activities including ristocetin cofactor activity (VWF:RCo) and collagen-binding activity.	Ristocetin	258-268	von Willebrand factor	Homo sapiens	8-11
18786010-5	2008	FVIII level and VWF ristocetin cofactor activity may both be used to determine concentrate potency and to monitor treatment.	Ristocetin	20-30	von Willebrand factor	Homo sapiens	16-19
18815197-7	2008	As a consequence, platelet aggregation to 1.2 mg/mL of ristocetin is slightly impaired and flow cytometry reveals a reduced binding of monoclonals directed against N-terminal epitopes of the GPIbalpha.	Ristocetin	55-65	glycoprotein Ib platelet subunit alpha	Homo sapiens	191-200
17786534-3	2008	METHODS: The aim of this study was to explore the correlation between VWF:Ag, VWF ristocetin cofactor activity (VWF:RCo) and FVIII in 213 consecutive patients undergoing screening for VWD.	Ristocetin	82-92	von Willebrand factor	Homo sapiens	78-81
17786534-3	2008	METHODS: The aim of this study was to explore the correlation between VWF:Ag, VWF ristocetin cofactor activity (VWF:RCo) and FVIII in 213 consecutive patients undergoing screening for VWD.	Ristocetin	82-92	von Willebrand factor	Homo sapiens	78-81
17786534-3	2008	METHODS: The aim of this study was to explore the correlation between VWF:Ag, VWF ristocetin cofactor activity (VWF:RCo) and FVIII in 213 consecutive patients undergoing screening for VWD.	Ristocetin	82-92	coagulation factor VIII	Homo sapiens	125-130
18577516-3	2008	GrB delays ristocetin-induced platelet aggregation and inhibits platelet adhesion and spreading on immobilized VWF under static conditions.	Ristocetin	11-21	granzyme B	Homo sapiens	0-3
18845909-3	2008	In this assay, fixed platelets bound to the vWF-R497 mutant, carrying the deletion of Glu497-Tyr508 and the missense mutation of Arg545 to Ala, without binding modulators such as ristocetin.	Ristocetin	179-189	von Willebrand factor	Homo sapiens	44-47
18445014-6	2008	In this group, pre-infusion FVIII:C, VWF:Ag and VWF: ristocetin cofactor (RCoF) level that were 19.5% (1-64), 20 U dL(-1) (0-96) and 12% (0-66) increased to 72% (54-198), 131 U dL(-1) (68-206) and 68% (27-108) postinfusion, respectively.	Ristocetin	53-63	von Willebrand factor	Homo sapiens	48-51
18521510-4	2008	VWF/ristocetin-induced platelet aggregation was delayed after treatment with methyl beta-cyclodextrin (mbCD), but the maximal aggregation response was not affected.	Ristocetin	4-14	von Willebrand factor	Homo sapiens	0-3
18600088-9	2008	Plasma von Willebrand factor levels were measured as ristocetin-cofactor activities.	Ristocetin	53-63	von Willebrand factor	Homo sapiens	7-28
18299448-6	2008	Deleting these, but not upstream sequences of GPIb alpha expressed in CHO cells, inhibited VWF/ristocetin-dependent Akt phosphorylation, relative to wild-type receptor, confirming this region encompassed a functional PI3-kinase-binding site.	Ristocetin	95-105	von Willebrand factor	Cricetulus griseus	91-94
18363340-11	2008	In addition, OS-1 blocked ristocetin-induced platelet agglutination of human platelets in plasma with no influence on platelet aggregation induced by several agonists of alternative platelet aggregation pathways, demonstrating that this peptide specifically disrupted the GPIbalpha-vWF-A1 interaction.	Ristocetin	26-36	glycoprotein Ib platelet subunit alpha	Homo sapiens	272-281
17977030-0	2008	Evidence from limited proteolysis of a ristocetin-induced conformational change in human von Willebrand factor that promotes its binding to platelet glycoprotein Ib-IX-V. von Willebrand factor (VWF) does not normally interact with platelets in the bloodstream.	Ristocetin	39-49	von Willebrand factor	Homo sapiens	89-110
17977030-0	2008	Evidence from limited proteolysis of a ristocetin-induced conformational change in human von Willebrand factor that promotes its binding to platelet glycoprotein Ib-IX-V. von Willebrand factor (VWF) does not normally interact with platelets in the bloodstream.	Ristocetin	39-49	von Willebrand factor	Homo sapiens	171-192
17977030-0	2008	Evidence from limited proteolysis of a ristocetin-induced conformational change in human von Willebrand factor that promotes its binding to platelet glycoprotein Ib-IX-V. von Willebrand factor (VWF) does not normally interact with platelets in the bloodstream.	Ristocetin	39-49	von Willebrand factor	Homo sapiens	194-197
17977030-3	2008	Ristocetin also promotes interaction of VWF with GP Ib-IX-V; it thus provides a model for changes in VWF conformation and function that may occur in vivo.	Ristocetin	0-10	von Willebrand factor	Homo sapiens	40-43
17977030-3	2008	Ristocetin also promotes interaction of VWF with GP Ib-IX-V; it thus provides a model for changes in VWF conformation and function that may occur in vivo.	Ristocetin	0-10	von Willebrand factor	Homo sapiens	101-104
17977030-5	2008	Ristocetin markedly altered the pattern of VWF digestion by trypsin, increasing the prevalence of two major proteolytic fragments (109 and 160 kDa), and decreasing that of four fragments (130, 145, 181 and 199 kDa).	Ristocetin	0-10	von Willebrand factor	Homo sapiens	43-46
17977030-8	2008	Changes in prevalence of five of the tryptic fragments of VWF with ristocetin and vancomycin correlated closely with changes in VWF binding to GP Ib-IX-V. Heparin also partially inhibited the ristocetin-induced changes in tryptic digestion of VWF.	Ristocetin	67-77	von Willebrand factor	Homo sapiens	58-61
17977030-8	2008	Changes in prevalence of five of the tryptic fragments of VWF with ristocetin and vancomycin correlated closely with changes in VWF binding to GP Ib-IX-V. Heparin also partially inhibited the ristocetin-induced changes in tryptic digestion of VWF.	Ristocetin	192-202	von Willebrand factor	Homo sapiens	58-61
17977030-8	2008	Changes in prevalence of five of the tryptic fragments of VWF with ristocetin and vancomycin correlated closely with changes in VWF binding to GP Ib-IX-V. Heparin also partially inhibited the ristocetin-induced changes in tryptic digestion of VWF.	Ristocetin	192-202	von Willebrand factor	Homo sapiens	128-131
17977030-8	2008	Changes in prevalence of five of the tryptic fragments of VWF with ristocetin and vancomycin correlated closely with changes in VWF binding to GP Ib-IX-V. Heparin also partially inhibited the ristocetin-induced changes in tryptic digestion of VWF.	Ristocetin	192-202	von Willebrand factor	Homo sapiens	128-131
17977030-9	2008	These observations suggest that ristocetin may modulate VWF conformation in such a way as to expose its GP Ib-binding domain and enable it to interact with the platelet.	Ristocetin	32-42	von Willebrand factor	Homo sapiens	56-59
18312368-3	2008	Rise in ristocetin cofactor activity (VWF:RCo) > or = 40% at 90-min post-Stimate and 1-2 h after subcutaneous DDAVP was defined as initial response; response longevity was assessed only after subcutaneous dosing by measuring VWF:RCo levels at time-points 1, 2, 4 and 6 h. Eleven patients (five males, six females; age range: 20-56 years) participated in intranasal and 9/11 (four males, five females) in subcutaneous testing.	Ristocetin	8-18	von Willebrand factor	Homo sapiens	38-41
18055988-11	2007	INTERPRETATION AND CONCLUSIONS: The measurement of ristocetin-induced binding of VWF to platelets by flow cytometry is a sensitive, simple and rapid test for the diagnosis of VWD and for the monitoring of the effects of desmopressin therapy.	Ristocetin	51-61	von Willebrand factor	Homo sapiens	81-84
18263586-8	2008	Proteolysis of VWF by InhA impairs its collagen binding activity (VWF:CBA) and ristocetin-induced platelet aggregation activity.	Ristocetin	79-89	Von Willebrand factor	Mus musculus	15-18
18282712-14	2008	Indeed, collagen binding capacity and ristocetin cofactor activity (which measures binding of VWF to platelets) were lower in VAD patients compared to HTX recipients.	Ristocetin	38-48	von Willebrand factor	Homo sapiens	94-97
18327408-10	2008	This effect is likely to be mediated through VWF as Mg(++) partially inhibited ristocetin-induced platelet aggregation and VWF binding to collagen.	Ristocetin	79-89	von Willebrand factor	Homo sapiens	45-48
27263955-9	2007	In comparison with wild types, platelets carrying the PlA1/A2 genotypes showed hyperaggregation measured in whole blood and induced by ristocetin (p< 0.05).	Ristocetin	135-145	POU class 2 homeobox 3	Homo sapiens	54-58
18055988-4	2007	DESIGN AND METHODS: Flow cytometric analysis of ristocetin-induced VWF binding to platelets was performed in platelet-rich plasma (PRP) samples from patients with VWD and from control subjects and in samples of formalin-fixed platelets in the presence of plasma from patients or controls.	Ristocetin	48-58	von Willebrand factor	Homo sapiens	67-70
18055988-7	2007	RESULTS: Ristocetin-induced VWF binding to platelets, evaluated by both flow cytometry-based assays, was significantly reduced in patients with type1, 2A and 2M VWD as compared with that in healthy subjects.	Ristocetin	9-19	von Willebrand factor	Homo sapiens	28-31
18064311-6	2007	Recombinant VWF carrying the I1372S mutation and showing a normal VWF multimer organisation was capable of inducing SPA on normal platelet-rich plasma (unlike wild-type VWF), as well as a hyper-response to ristocetin in the same platelets (0.6 mg/ml ristocetin vs. 1.2 of wild-type VWF).	Ristocetin	206-216	von Willebrand factor	Homo sapiens	12-15
18064311-6	2007	Recombinant VWF carrying the I1372S mutation and showing a normal VWF multimer organisation was capable of inducing SPA on normal platelet-rich plasma (unlike wild-type VWF), as well as a hyper-response to ristocetin in the same platelets (0.6 mg/ml ristocetin vs. 1.2 of wild-type VWF).	Ristocetin	250-260	von Willebrand factor	Homo sapiens	12-15
18064311-7	2007	The new I1372S VWF mutation, characterized by SPA and hyper-responsiveness to ristocetin thus has some of the features of type 2B VWD, but not the lack of large VWF multimers, so we defined this variant as type 2B-like VWD.	Ristocetin	78-88	von Willebrand factor	Homo sapiens	15-18
17655706-2	2007	MATERIALS AND METHODS: We compared agonist (TRAP-6, ADP, Arachidonic acid, Epinephrine, and Ristocetin) -inducible P-selectin expression and PAC-1 binding in 40 patients with cAITP (f/m ratio 23/17) with those in 20 healthy controls.	Ristocetin	92-102	selectin P	Homo sapiens	115-125
18457045-4	2007	Oxidized fibrinogen modified blood clotting parameters and ADP-, ristocetin-, and collagen-induced platelet aggregation in whole blood.	Ristocetin	65-75	fibrinogen beta chain	Homo sapiens	9-19
17439628-6	2007	Median in vivo recovery of VWF ristocetin cofactor (VWF:RCo) was 1.9 IU dL(-1) (IU kg(-1))(-1) with an interquartile range (IQR) of 1.6-2.5 IU dL(-1) (IU kg(-1))(-1).	Ristocetin	31-41	von Willebrand factor	Homo sapiens	27-30
17578514-3	2007	Binding of VWF in solution to immobilized A/C was inhibited by ristocetin and preincubation of platelets with A/C abolished ristocetin/VWF-induced platelet aggregation, indicating that the interaction of A/C with VWF is mediated by the VWA1 domain.	Ristocetin	63-73	von Willebrand factor	Homo sapiens	11-14
17578514-3	2007	Binding of VWF in solution to immobilized A/C was inhibited by ristocetin and preincubation of platelets with A/C abolished ristocetin/VWF-induced platelet aggregation, indicating that the interaction of A/C with VWF is mediated by the VWA1 domain.	Ristocetin	124-134	von Willebrand factor	Homo sapiens	11-14
17439628-6	2007	Median in vivo recovery of VWF ristocetin cofactor (VWF:RCo) was 1.9 IU dL(-1) (IU kg(-1))(-1) with an interquartile range (IQR) of 1.6-2.5 IU dL(-1) (IU kg(-1))(-1).	Ristocetin	31-41	von Willebrand factor	Homo sapiens	52-55
17389010-7	2007	The A2 domain polypeptide specifically recognizes the GPIbalpha-binding conformation in the A1 domain, as it only interacted with VWF activated by the modulator ristocetin or immobilized VWF.	Ristocetin	161-171	glycoprotein Ib platelet subunit alpha	Homo sapiens	54-63
17389010-7	2007	The A2 domain polypeptide specifically recognizes the GPIbalpha-binding conformation in the A1 domain, as it only interacted with VWF activated by the modulator ristocetin or immobilized VWF.	Ristocetin	161-171	von Willebrand factor	Homo sapiens	130-133
17701477-4	2007	The ristocetin cofactor activity (VWF:RCo) is the most useful test for VWD diagnosis, because it can mimic the interactions of VWF with its platelet receptor.	Ristocetin	4-14	von Willebrand factor	Homo sapiens	34-37
17549293-6	2007	The subjects received a single infusion of 60 IU/kg ristocetin cofactor activity (VWF:RCo) of either AHF (High Purity) or Biostate, and after a minimum 15-day wash-out period they received the alternative product.	Ristocetin	52-62	von Willebrand factor	Homo sapiens	82-89
17598011-5	2007	Remarkably, when compared to VWF of A/T1381 and A/A1381 individuals, VWF of individuals carrying the T/T1381 variant showed an increased affinity for its platelet receptor GPIbalpha under static conditions, as reflected by an increased sensitivity to low concentrations of ristocetin or botrocetin.	Ristocetin	273-283	von Willebrand factor	Homo sapiens	69-72
17598011-5	2007	Remarkably, when compared to VWF of A/T1381 and A/A1381 individuals, VWF of individuals carrying the T/T1381 variant showed an increased affinity for its platelet receptor GPIbalpha under static conditions, as reflected by an increased sensitivity to low concentrations of ristocetin or botrocetin.	Ristocetin	273-283	glycoprotein Ib platelet subunit alpha	Homo sapiens	172-181
17403090-3	2007	METHODS AND RESULTS: Fifty patients with clinically severe VWD (72% had VWF ristocetin cofactor activity less than 10 IU dL(-1) and 46% had FVIII < 20 IU dL(-1)) were treated with the concentrate as the only therapy, except for clinical situations requiring a priming dose of FVIII to rapidly correct an intrinsic coagulation defect.	Ristocetin	76-86	von Willebrand factor	Homo sapiens	72-75
17296574-1	2007	The aim of this study was to correlate ABO groups with plasma levels of factor VIII (FVIII), von Willebrand factor (VWF:Ag), and ristocetin cofactor (VWF:RCo).	Ristocetin	129-139	ABO, alpha 1-3-N-acetylgalactosaminyltransferase and alpha 1-3-galactosyltransferase	Homo sapiens	39-42
17137472-5	2007	Among the 49 cases who were tested for VWF, low values by three measures were more commonly present than in 166 controls, specifically, ristocetin cofactor (RCo) activity [20.4% vs. 5.4%, odds ratio (OR) 4.5], collagen binding (14.3% vs. 4.2%, OR 3.8), and antigen level (20.4% vs. 6.0%, OR 4.0).	Ristocetin	136-146	von Willebrand factor	Homo sapiens	39-42
17701477-4	2007	The ristocetin cofactor activity (VWF:RCo) is the most useful test for VWD diagnosis, because it can mimic the interactions of VWF with its platelet receptor.	Ristocetin	4-14	von Willebrand factor	Homo sapiens	127-130
16977573-7	2006	The specific vWF activities, as assessed by ristocetin cofactor activity (vWF:RCo) and collagen-binding activity (vWF:CB), correlated well with the HMWvWF content of the products.	Ristocetin	44-54	von Willebrand factor	Homo sapiens	13-16
16978236-8	2006	Chinese hamster ovary cells stably expressing GPIbalpha/Ibbeta Ser122/IX had the ability to bind soluble vWF and to aggregate in the presence of ristocetin.	Ristocetin	145-155	glycoprotein Ib platelet subunit alpha	Homo sapiens	46-55
16977566-5	2006	The ristocetin cofactor activity is the most useful test for VWD screening in the general population because it reproduces in vitro the first VWF interactions with its platelet receptor; however other assays are required to identify and classify VWD types.	Ristocetin	4-14	von Willebrand factor	Homo sapiens	142-145
17200766-7	2007	VWF activity was determined using both the ristocetin cofactor activity (VWF:Rcof) and collagen binding (VWF:CB) assays.	Ristocetin	43-53	von Willebrand factor	Homo sapiens	0-3
16607078-3	2006	In samples from healthy individuals (n=10) and in patients with suspected type 1 VWD (n=10), storage of whole blood on ice caused a drastic time-dependent decrease in von Willebrand factor (VWF):ristocetin cofactor activity, in VWF:antigen activity and factor VIII activity (mean+/-SD) to 35+/-18, 55+/-23 and 53+/-15% of baseline levels after 6 h storage, respectively.	Ristocetin	195-205	von Willebrand factor	Homo sapiens	167-188
16862517-4	2006	In the early 1970s, ristocetin-induced platelet aggregation was described and formed the basis of the first consistent and reliable test that quantified the platelet adhesive function missing in vWD.	Ristocetin	20-30	von Willebrand factor	Homo sapiens	195-198
16862522-6	2006	Several different techniques were used for determination of vWF ristocetin cofactor activity (vWF:RCo), all of which were associated with poor agreement among centers as indicated by CVs of 40 to 50%.	Ristocetin	64-74	von Willebrand factor	Homo sapiens	60-63
16862522-6	2006	Several different techniques were used for determination of vWF ristocetin cofactor activity (vWF:RCo), all of which were associated with poor agreement among centers as indicated by CVs of 40 to 50%.	Ristocetin	64-74	von Willebrand factor	Homo sapiens	94-97
16704443-2	2006	This feature is usually studied in vitro by a ristocetin-dependent VWF platelet-binding assay, which has some limitations as it requires [e.g. (radio)-labelled anti-VWF antibodies and normal formaldehyde-fixed platelets].	Ristocetin	46-56	von Willebrand factor	Homo sapiens	67-70
16704443-3	2006	We, here, extended the applicability of an enzyme-linked immunosorbent assay-based method previously described for the measurement of ristocetin co-factor activity that used a recombinant fragment of GPIb (rfGPIb alpha) and horseradish peroxidase-labelled rabbit anti-human VWF antibodies for measuring the captured ristocetin-VWF complexes on the rfGPIb alpha.	Ristocetin	134-144	von Willebrand factor	Homo sapiens	274-277
16704443-3	2006	We, here, extended the applicability of an enzyme-linked immunosorbent assay-based method previously described for the measurement of ristocetin co-factor activity that used a recombinant fragment of GPIb (rfGPIb alpha) and horseradish peroxidase-labelled rabbit anti-human VWF antibodies for measuring the captured ristocetin-VWF complexes on the rfGPIb alpha.	Ristocetin	134-144	von Willebrand factor	Homo sapiens	327-330
16704443-5	2006	VWF in plasma from 28 of these patients bound better than normal VWF at 0.2 mg/ml ristocetin, with the ratio, optical density (OD) patient/OD normal pool plasma, higher than 1.8.	Ristocetin	82-92	von Willebrand factor	Homo sapiens	0-3
16704443-5	2006	VWF in plasma from 28 of these patients bound better than normal VWF at 0.2 mg/ml ristocetin, with the ratio, optical density (OD) patient/OD normal pool plasma, higher than 1.8.	Ristocetin	82-92	von Willebrand factor	Homo sapiens	65-68
17047284-6	2006	ULVWF is also significantly more potent than P-VWF in mediating both shear-induced platelet aggregation and ristocetin-mediated platelet agglutination.	Ristocetin	108-118	von Willebrand factor	Homo sapiens	2-5
16706984-0	2006	von Willebrand factor mediates platelet spreading through glycoprotein Ib and alpha(IIb)beta3 in the presence of botrocetin and ristocetin, respectively.	Ristocetin	128-138	von Willebrand factor	Homo sapiens	0-21
16706984-3	2006	OBJECTIVE: To evaluate the ability of GPIb and alpha(IIb)beta3 to mediate platelet adhesion and lamellipodia formation on immobilized VWF in the presence of the biochemical modulators, ristocetin and botrocetin.	Ristocetin	185-195	von Willebrand factor	Homo sapiens	134-137
16706984-6	2006	In marked contrast, in the presence of ristocetin, VWF stimulates formation of fully spread lamellipodia through a pathway that is dependent upon alpha(IIb)beta3 and PI3-kinase.	Ristocetin	39-49	von Willebrand factor	Homo sapiens	51-54
16706984-8	2006	The localization of filamentous actin and the Arp2/3 complex in platelets on VWF in the presence of botrocetin and ristocetin are distinct, yielding disparate lamellipodium kinetic signatures.	Ristocetin	115-125	actin related protein 2	Homo sapiens	46-50
16706984-9	2006	Interestingly, botrocetin significantly enhances platelet adhesion to VWF under flow in whole blood in an alpha(IIb)beta3-independent manner, while ristocetin augments washed platelet adhesion and spreading to VWF under flow in an alpha(IIb)beta3-dependent manner.	Ristocetin	148-158	von Willebrand factor	Homo sapiens	210-213
16792915-5	2006	RESULTS: (1) Anti-platelet GPIIb/IIIa and/or GPIb/IX autoantibodies were detected in 34 of 68 (53.6%) ITP patients" plasmas and that from 5 patients significantly inhibited the platelet aggregation induced by ADP or ristocetin.	Ristocetin	216-226	integrin subunit alpha 2b	Homo sapiens	27-32
16420575-4	2006	RESULTS: The A1 domain bound to collagen with K(d) approximately 8.0 nm and this binding was blocked by the mAb 6G1, which blocks the interaction between ristocetin and VWF.	Ristocetin	154-164	von Willebrand factor	Homo sapiens	169-172
16607078-3	2006	In samples from healthy individuals (n=10) and in patients with suspected type 1 VWD (n=10), storage of whole blood on ice caused a drastic time-dependent decrease in von Willebrand factor (VWF):ristocetin cofactor activity, in VWF:antigen activity and factor VIII activity (mean+/-SD) to 35+/-18, 55+/-23 and 53+/-15% of baseline levels after 6 h storage, respectively.	Ristocetin	195-205	von Willebrand factor	Homo sapiens	190-193
16430944-7	2006	The test is based on the measurement of the ristocetin-cofactor activity of purified, urea-denaturated vWF concentrate after incubation with diluted patient plasma that has been preactivated with barium chloride.	Ristocetin	44-54	von Willebrand factor	Homo sapiens	103-106
15809291-7	2005	Ristocetin binding to VWF could reduce the apparent affinity and reverse the inhibitory effect of chloride.	Ristocetin	0-10	von Willebrand factor	Homo sapiens	22-25
16686061-11	2005	The purified IgG and F(ab")2 fragments of 2 patients positive in GP II b/ III a autoantibody out of the 7 patients significantly inhibited the platelet aggregation induced by ADP, the purified IgG and F(ab")2 fragments of 1 patients positive in GP I b/IX out of the 7 patients significantly inhibited the platelet aggregation induced by ristocetin, and the purified IgG and F(ab")2 fragments of 1 patients positive in GP VI out of the 7 patients significantly inhibited the platelet aggregation induced by collagen.	Ristocetin	337-347	integrin subunit alpha 2b	Homo sapiens	65-72
16320153-0	2005	Impact of the Thr789Ala variant of the von Willebrand factor levels, on ristocetin co-factor and collagen binding capacity and its association with coronary heart disease in patients with diabetes mellitus type 2.	Ristocetin	72-82	von Willebrand factor	Homo sapiens	39-60
16320153-7	2005	In addition, ristocetin co-factor was significantly increased in vWF Thr789Ala variant carriers (p < 0.05).	Ristocetin	13-23	von Willebrand factor	Homo sapiens	65-68
16320153-10	2005	In conclusion, although the Thr789Ala vWF gene variant is associated with increased plasma concentrations of vWF, ristocetin co factor levels and collagen binding capacity in patients with type 2 diabetes and CHD, a direct effect of this variant on the occurrence of CHD in patients with type 2 diabetes, could not be detected.	Ristocetin	114-124	von Willebrand factor	Homo sapiens	38-41
16020504-3	2005	Erk2 is activated in platelets on stimulation with VWF/ristocetin in a time-dependent manner.	Ristocetin	55-65	mitogen-activated protein kinase 1	Homo sapiens	0-4
16014562-3	2005	AU/VWFa-11 is unable to bind VWF in solution, but efficiently interacts with ristocetin- or botrocetin-activated VWF, VWF comprising type 2B mutation R1306Q, or immobilized VWF.	Ristocetin	77-87	von Willebrand factor	Homo sapiens	3-6
15933060-3	2005	Substitution of His86 with either Ala or Glu resulted in a gain of VWF-binding function as judged by increased VWF binding in the presence of the modulators ristocetin and botrocetin and by enhanced adhesion of Chinese hamster ovary (CHO) cells expressing the mutant GP Ibalpha to immobilized VWF under conditions of flow.	Ristocetin	157-167	von Willebrand factor	Cricetulus griseus	67-70
15941906-4	2005	MPalphaC also inhibited VWF-dependent platelet agglutination induced by ristocetin.	Ristocetin	72-82	von Willebrand factor	Homo sapiens	24-27
15809291-9	2005	Shear forces, which facilitate GpIbalpha binding (this effect being artificially obtained by ristocetin), can reverse the inhibitory effect of chloride, whose concentration gradient across the cell membrane may represent a simple but efficient strategy to regulate the enzymatic activity of ADAMTS-13.	Ristocetin	93-103	glycoprotein Ib platelet subunit alpha	Homo sapiens	31-40
15809291-9	2005	Shear forces, which facilitate GpIbalpha binding (this effect being artificially obtained by ristocetin), can reverse the inhibitory effect of chloride, whose concentration gradient across the cell membrane may represent a simple but efficient strategy to regulate the enzymatic activity of ADAMTS-13.	Ristocetin	93-103	ADAM metallopeptidase with thrombospondin type 1 motif 13	Homo sapiens	291-300
15946221-0	2005	Endothelial microparticles induce formation of platelet aggregates via a von Willebrand factor/ristocetin dependent pathway, rendering them resistant to dissociation.	Ristocetin	95-105	von Willebrand factor	Homo sapiens	73-94
15705799-7	2005	Analysis of ristocetin-mediated (125)I-VWF binding showed that the Mut receptor binds VWF in the absence of ristocetin and displays an increased sensitivity to lower concentrations of the modulator.	Ristocetin	12-22	von Willebrand factor	Homo sapiens	39-42
15705799-7	2005	Analysis of ristocetin-mediated (125)I-VWF binding showed that the Mut receptor binds VWF in the absence of ristocetin and displays an increased sensitivity to lower concentrations of the modulator.	Ristocetin	12-22	von Willebrand factor	Homo sapiens	86-89
15886805-6	2005	The lambda dimer protein inhibited the binding of platelets to immobilized or ristocetin-treated von Willebrand factor (VWF).	Ristocetin	78-88	von Willebrand factor	Homo sapiens	97-118
15886805-8	2005	To help elucidate the binding site within the A1 domain, binding of ristocetin-treated VWF to the immobilized lambda dimer protein was assayed in the presence of various anti-A1 domain monoclonal antibodies.	Ristocetin	68-78	von Willebrand factor	Homo sapiens	87-90
15886805-6	2005	The lambda dimer protein inhibited the binding of platelets to immobilized or ristocetin-treated von Willebrand factor (VWF).	Ristocetin	78-88	von Willebrand factor	Homo sapiens	120-123
15886805-7	2005	Furthermore, a 39/34 kD fragment of VWF encompassing the A1 domain specifically bound to the immobilized lambda dimer protein in the presence of ristocetin, suggesting that the lambda dimer protein directly binds to the A1 domain of VWF.	Ristocetin	145-155	von Willebrand factor	Homo sapiens	36-39
15849522-5	2005	Study results have shown that the commercially available VWF-containing concentrates are effective in clinical practice (bleeding and surgery), producing responses that may differ depending on the patient"s VWD subtype; infusion results in correction of factor VIII activity (FVIII:C) and ristocetin cofactor activity of VWF (VWF:RCo), whereas bleeding time is not consistently corrected.	Ristocetin	289-299	von Willebrand factor	Homo sapiens	57-60
15459008-3	2005	In the present study, we demonstrated that the addition of VWF/factor VIII complex or purified VWF (> 2 ristocetin cofactor activity units/mL) increased platelet adhesion to the collagen surface in platelet-reduced blood ( approximately 5 x 10(4) platelets/microL) to the normal level.	Ristocetin	107-117	von Willebrand factor	Homo sapiens	59-62
15777951-6	2005	The interaction site of agkicetin-C was further refined: it recognizes a linear sequence in a recombinant GPIbalpha (AA1-289) fragment and inhibited completely the ristocetin-induced VWF binding to this fragment.	Ristocetin	164-174	von Willebrand factor	Rattus norvegicus	183-186
15459008-3	2005	In the present study, we demonstrated that the addition of VWF/factor VIII complex or purified VWF (> 2 ristocetin cofactor activity units/mL) increased platelet adhesion to the collagen surface in platelet-reduced blood ( approximately 5 x 10(4) platelets/microL) to the normal level.	Ristocetin	107-117	von Willebrand factor	Homo sapiens	95-98
15319289-2	2004	Of the many GP Ibalpha monoclonal antibodies described, AP1 is of particular interest because it blocks static VWF binding induced by 2 modulators, ristocetin and botrocetin, and platelet adhesion to VWF surfaces under flow.	Ristocetin	148-158	von Willebrand factor	Cricetulus griseus	111-114
15686464-6	2005	The dissociation constants of ristocetin-induced (125)I-labelled VWF binding to two forms of soluble recombinant GPIb alpha [(1)His-(302)Ala, either (145)Thr (145T) or (145)Met (145M)] were not different.	Ristocetin	30-40	von Willebrand factor	Cricetulus griseus	65-68
16024332-6	2005	On average, type 1 VWD plasma was misidentified as type 2 VWD plasma in 11% of cases, and laboratories that performed the ristocetin cofactor assay for von Willebrand factor (VWF:RCo) without performing the collagen-binding activity assay for VWF (VWF:CB) were 6 times more likely to make such an error than those that did perform the VWF:CB.	Ristocetin	122-132	von Willebrand factor	Homo sapiens	152-173
16024332-6	2005	On average, type 1 VWD plasma was misidentified as type 2 VWD plasma in 11% of cases, and laboratories that performed the ristocetin cofactor assay for von Willebrand factor (VWF:RCo) without performing the collagen-binding activity assay for VWF (VWF:CB) were 6 times more likely to make such an error than those that did perform the VWF:CB.	Ristocetin	122-132	von Willebrand factor	Homo sapiens	175-178
15630508-1	2005	We have previously demonstrated that the von Willebrand factor ristocetin cofactor activity (VWF:RCo), used in the diagnosis of vonWillebrand disease (VWD), can be accurately determined via ELISA by measuring the ristocetin-induced binding of VWF to a captured recombinant fragment of GPIbalpha (rfGPIbalpha, AA 1-289) (Vanhoorelbeke et al., Thromb Haemost 2000; 83: 107-13).	Ristocetin	63-73	von Willebrand factor	Homo sapiens	93-96
15630508-1	2005	We have previously demonstrated that the von Willebrand factor ristocetin cofactor activity (VWF:RCo), used in the diagnosis of vonWillebrand disease (VWD), can be accurately determined via ELISA by measuring the ristocetin-induced binding of VWF to a captured recombinant fragment of GPIbalpha (rfGPIbalpha, AA 1-289) (Vanhoorelbeke et al., Thromb Haemost 2000; 83: 107-13).	Ristocetin	63-73	von Willebrand factor	Homo sapiens	243-246
15630508-1	2005	We have previously demonstrated that the von Willebrand factor ristocetin cofactor activity (VWF:RCo), used in the diagnosis of vonWillebrand disease (VWD), can be accurately determined via ELISA by measuring the ristocetin-induced binding of VWF to a captured recombinant fragment of GPIbalpha (rfGPIbalpha, AA 1-289) (Vanhoorelbeke et al., Thromb Haemost 2000; 83: 107-13).	Ristocetin	63-73	glycoprotein Ib platelet subunit alpha	Homo sapiens	285-294
15493507-2	2004	Data that ristocetin-induced von Willebrand factor (VWF) binding to glycoprotein (Gp) Ibalpha activates proline-rich tyrosine kinase 2 (Pyk2) and extracellular-regulated kinase (ERK) has led to speculation that these events are coupled and that a MAP kinase may activate cytosolic phospholipase A2 (cPLA2)-mediated arachidonic acid (AA) release.	Ristocetin	10-20	von Willebrand factor	Homo sapiens	52-55
15467896-0	2004	Increased shear stress- and ristocetin-induced binding of von Willebrand factor to platelets in cord compared with adult plasma.	Ristocetin	28-38	von Willebrand factor	Homo sapiens	58-79
15467896-5	2004	Subsequently, vWf-platelet interaction was induced by exposing the mixture to shear stress by means of a cone/plate measuring system or by incubating the mixture with ristocetin.	Ristocetin	167-177	von Willebrand factor	Homo sapiens	14-17
15467896-8	2004	We found that significantly higher amounts of neonatal vWf were attached to platelets in the presence of shear stress or ristocetin.	Ristocetin	121-131	von Willebrand factor	Homo sapiens	55-58
15467896-10	2004	Furthermore, decreasing the vWf content in cord plasma to adult level resulted in significantly suppressed vWf-platelet attachment in the presence of ristocetin, indicating that the high neonatal vWf level contributes to the efficient vWf-platelet binding in neonates.	Ristocetin	150-160	von Willebrand factor	Homo sapiens	28-31
15493507-2	2004	Data that ristocetin-induced von Willebrand factor (VWF) binding to glycoprotein (Gp) Ibalpha activates proline-rich tyrosine kinase 2 (Pyk2) and extracellular-regulated kinase (ERK) has led to speculation that these events are coupled and that a MAP kinase may activate cytosolic phospholipase A2 (cPLA2)-mediated arachidonic acid (AA) release.	Ristocetin	10-20	protein tyrosine kinase 2 beta	Homo sapiens	104-134
15493507-2	2004	Data that ristocetin-induced von Willebrand factor (VWF) binding to glycoprotein (Gp) Ibalpha activates proline-rich tyrosine kinase 2 (Pyk2) and extracellular-regulated kinase (ERK) has led to speculation that these events are coupled and that a MAP kinase may activate cytosolic phospholipase A2 (cPLA2)-mediated arachidonic acid (AA) release.	Ristocetin	10-20	protein tyrosine kinase 2 beta	Homo sapiens	136-140
15493507-2	2004	Data that ristocetin-induced von Willebrand factor (VWF) binding to glycoprotein (Gp) Ibalpha activates proline-rich tyrosine kinase 2 (Pyk2) and extracellular-regulated kinase (ERK) has led to speculation that these events are coupled and that a MAP kinase may activate cytosolic phospholipase A2 (cPLA2)-mediated arachidonic acid (AA) release.	Ristocetin	10-20	mitogen-activated protein kinase 3	Homo sapiens	178-181
15493507-2	2004	Data that ristocetin-induced von Willebrand factor (VWF) binding to glycoprotein (Gp) Ibalpha activates proline-rich tyrosine kinase 2 (Pyk2) and extracellular-regulated kinase (ERK) has led to speculation that these events are coupled and that a MAP kinase may activate cytosolic phospholipase A2 (cPLA2)-mediated arachidonic acid (AA) release.	Ristocetin	10-20	phospholipase A2 group IVA	Homo sapiens	271-297
15493507-2	2004	Data that ristocetin-induced von Willebrand factor (VWF) binding to glycoprotein (Gp) Ibalpha activates proline-rich tyrosine kinase 2 (Pyk2) and extracellular-regulated kinase (ERK) has led to speculation that these events are coupled and that a MAP kinase may activate cytosolic phospholipase A2 (cPLA2)-mediated arachidonic acid (AA) release.	Ristocetin	10-20	phospholipase A2 group IVA	Homo sapiens	299-304
14754609-1	2004	BACKGROUND AND OBJECTIVES: The assay of ristocetin co-factor activity of von Willebrand factor (VWF:RCo) is used in the screening of patients with suspected von Willebrand"s disease (VWD), the most frequent inherited bleeding disorder.	Ristocetin	40-50	von Willebrand factor	Homo sapiens	96-99
15311161-1	2004	We have set up a rapid assay for measuring the activity of the von Willebrand factor ristocetin cofactor (VWF : RCo) using an automated coagulometer (ACL 9000; Instrumentation Laboratory, Lexington, Massachusetts, USA) and commercially available lyophilized platelet reagents (Dade-Behring, Marburg, Germany).	Ristocetin	85-95	von Willebrand factor	Homo sapiens	63-84
15311161-1	2004	We have set up a rapid assay for measuring the activity of the von Willebrand factor ristocetin cofactor (VWF : RCo) using an automated coagulometer (ACL 9000; Instrumentation Laboratory, Lexington, Massachusetts, USA) and commercially available lyophilized platelet reagents (Dade-Behring, Marburg, Germany).	Ristocetin	85-95	von Willebrand factor	Homo sapiens	106-109
15333037-15	2004	Overall the best performance was observed for three methods measuring cleaved VWF by ristocetin cofactor, collagen binding, and immunoblotting of degraded multimers of VWF substrate, respectively.	Ristocetin	85-95	von Willebrand factor	Homo sapiens	78-81
15333040-1	2004	We have previously described a monoclonal antibody (mAb), 1C1E7, against von Willebrand factor (VWF), that increases ristocetin-induced platelet aggregation (RIPA) and induces a preferential binding of the high-molecular-weight multimers of VWF to platelet GPIb.	Ristocetin	117-127	von Willebrand factor	Homo sapiens	73-94
15333040-1	2004	We have previously described a monoclonal antibody (mAb), 1C1E7, against von Willebrand factor (VWF), that increases ristocetin-induced platelet aggregation (RIPA) and induces a preferential binding of the high-molecular-weight multimers of VWF to platelet GPIb.	Ristocetin	117-127	von Willebrand factor	Homo sapiens	96-99
15333040-1	2004	We have previously described a monoclonal antibody (mAb), 1C1E7, against von Willebrand factor (VWF), that increases ristocetin-induced platelet aggregation (RIPA) and induces a preferential binding of the high-molecular-weight multimers of VWF to platelet GPIb.	Ristocetin	117-127	von Willebrand factor	Homo sapiens	241-244
14757772-5	2004	Mutations at Glu128, Glu172, and Asp175 specifically decreased both ristocetin- and botrocetin-induced VWF binding, suggesting that these sites are important for VWF binding of platelet GPIb.	Ristocetin	68-78	von Willebrand factor	Homo sapiens	103-106
14757772-5	2004	Mutations at Glu128, Glu172, and Asp175 specifically decreased both ristocetin- and botrocetin-induced VWF binding, suggesting that these sites are important for VWF binding of platelet GPIb.	Ristocetin	68-78	von Willebrand factor	Homo sapiens	162-165
14757772-6	2004	Monoclonal antibody 6D1 inhibited ristocetin- and botrocetin-induced VWF binding, and a mutation at Glu125 specifically reduced the binding to 6D1.	Ristocetin	34-44	von Willebrand factor	Homo sapiens	69-72
14757772-8	2004	Mutations at His12 and Glu14 decreased the ristocetin-induced VWF binding with normal botrocetin-induced binding.	Ristocetin	43-53	von Willebrand factor	Homo sapiens	62-65
14754609-4	2004	DESIGN AND METHODS: We describe here an ELISA method in which a recombinant fragment of the alpha-subunit of platelet glycoprotein Ib-IX-V complex (rGPIbalpha) is bound to an anti-GPIbalpha monoclonal antibody immobilized onto microtiter plate wells and which captures plasma VWF in the presence of ristocetin.	Ristocetin	299-309	glycoprotein Ib platelet subunit alpha	Homo sapiens	149-158
14962219-2	2004	It has been proposed that VWF:ristocetin cofactor (VWF:RCo) activity may be useful in evaluating the response to VWD treatment in patients who require replacement therapy.	Ristocetin	30-40	von Willebrand factor	Homo sapiens	26-29
14962219-2	2004	It has been proposed that VWF:ristocetin cofactor (VWF:RCo) activity may be useful in evaluating the response to VWD treatment in patients who require replacement therapy.	Ristocetin	30-40	von Willebrand factor	Homo sapiens	51-54
14750934-0	2003	Successful treatment of urgent bleeding in von Willebrand disease with factor VIII/VWF concentrate (Humate-P): use of the ristocetin cofactor assay (VWF:RCo) to measure potency and to guide therapy.	Ristocetin	122-132	von Willebrand factor	Homo sapiens	149-152
14750503-4	2003	These findings indicated that a peptide (Trp-Ile-Arg-Arg-Pro-Phe-Phe-Pro-Phe) from alpha B-crystallin significantly inhibits platelet aggregation induced by thrombin, TRAP (a protease activated receptor-1 agonist) and botrocetin, ristocetin (a stimulator of the platelet glycoprotein Ib/V/IX-von Willebrand factor axis), but not a protease-activated receptor-4 agonist, collagen and ADP.	Ristocetin	230-240	TRAP	Homo sapiens	167-171
14521604-1	2003	Tests based on three different principles are reported to measure the activity of von Willebrand factor (VWF): ristocetin cofactor (VWF:RCo), collagen binding (VWF:CB), and the so-called "activity ELISA" (VWF:MoAb).	Ristocetin	111-121	von Willebrand factor	Homo sapiens	82-103
14521604-1	2003	Tests based on three different principles are reported to measure the activity of von Willebrand factor (VWF): ristocetin cofactor (VWF:RCo), collagen binding (VWF:CB), and the so-called "activity ELISA" (VWF:MoAb).	Ristocetin	111-121	von Willebrand factor	Homo sapiens	105-108
12923581-3	2003	The laboratory features showed a high platelet concentration and a qualitative defect of von Willebrand factor (vWF) with a low normal vWF ristocetin cofactor activity, a normal vWF antigen and a decrease of the larger vWF multimers in plasma.	Ristocetin	139-149	von Willebrand factor	Homo sapiens	89-110
12791664-6	2003	When the A4 peptide was delivered to intact human platelets using a carrier peptide, we observed the dose-dependent inhibition of VWF-induced platelet aggregation in response to both ristocetin and shear stress.	Ristocetin	183-193	von Willebrand factor	Homo sapiens	130-133
12932308-1	2003	Diagnosis of mild forms of type 1 and 2 von Willebrand disease (VWD) may be difficult, especially when the levels of von Willebrand factor (VWF) activities measured as ristocetin cofactor are close to normal (30-60 U/dL) because the laboratory phenotype is highly heterogeneous and confounded by factors outside the VWF gene (eg, blood group) that may influence VWF levels.	Ristocetin	168-178	von Willebrand factor	Homo sapiens	117-138
12932308-1	2003	Diagnosis of mild forms of type 1 and 2 von Willebrand disease (VWD) may be difficult, especially when the levels of von Willebrand factor (VWF) activities measured as ristocetin cofactor are close to normal (30-60 U/dL) because the laboratory phenotype is highly heterogeneous and confounded by factors outside the VWF gene (eg, blood group) that may influence VWF levels.	Ristocetin	168-178	von Willebrand factor	Homo sapiens	140-143
12871509-3	2003	This was accomplished using porcine VWF, which has been shown to interact with human GPIb independently of shear stress or ristocetin.	Ristocetin	123-133	von Willebrand factor	Homo sapiens	36-39
12588351-5	2003	F1285rVWF exhibited a slight decrease of high-molecular-weight multimers and markedly reduced ristocetin- or botrocetin-induced binding of VWF to platelets in association with a decreased binding to botrocetin.	Ristocetin	94-104	von Willebrand factor	Homo sapiens	6-9
12588351-6	2003	The hybrid S/F1285rVWF showed a normal multimeric profile and bound to platelets in a similar way to the patients" plasma VWF, in the presence of ristocetin or botrocetin.	Ristocetin	146-156	von Willebrand factor	Homo sapiens	19-22
12871453-8	2003	Sixteen of 22 women with reduced ristocetin aggregation had von Willebrand ristocetin cofactor (VWF:RCo) and von Willebrand factor antigen (VWF:Ag) > 60%.	Ristocetin	33-43	von Willebrand factor	Homo sapiens	96-99
12871453-8	2003	Sixteen of 22 women with reduced ristocetin aggregation had von Willebrand ristocetin cofactor (VWF:RCo) and von Willebrand factor antigen (VWF:Ag) > 60%.	Ristocetin	33-43	von Willebrand factor	Homo sapiens	140-143
12871537-4	2003	Ristocetin was found to increase the rate of VWF proteolysis approximately two-fold; the differential between blood groups was retained in the presence of ristocetin.	Ristocetin	0-10	von Willebrand factor	Homo sapiens	45-48
12410584-2	2002	Ristocetin cofactor (RCoF) assay is used to evaluate VWF activity, but it does not assess collagen-binding activity.	Ristocetin	0-10	von Willebrand factor	Homo sapiens	53-56
12817908-3	2003	The most widely used method for measurement of VWF activity is the ristocetin cofactor assay (VWF:RCo), which is still crucial for the laboratory diagnosis of von Willebrand"s disease (VWD).	Ristocetin	67-77	von Willebrand factor	Homo sapiens	47-50
12817908-3	2003	The most widely used method for measurement of VWF activity is the ristocetin cofactor assay (VWF:RCo), which is still crucial for the laboratory diagnosis of von Willebrand"s disease (VWD).	Ristocetin	67-77	von Willebrand factor	Homo sapiens	94-97
12817908-10	2003	CONCLUSION: The accuracy and precision of the von Willebrand activity assay may be improved if a flow cytometer is utilized for measurement of the impact of ristocetin on binding of VWF to formalin-fixed platelets instead of measuring agglutination utilizing an aggregometer.	Ristocetin	157-167	von Willebrand factor	Homo sapiens	182-185
11943773-2	2002	In vitro platelet glycoprotein Ib (GPIb) binding of the human von Willebrand factor (VWF) increases markedly by exogenous modulators such as ristocetin or botrocetin, and the binding does not occur in normal circulation.	Ristocetin	141-151	von Willebrand factor	Homo sapiens	62-83
12152679-1	2002	We have evaluated two automated methods for measuring ristocetin cofactor activity (VWF:RCo) on an automated coagulation analyzer (STAR, Diagnostica Stago Inc., Parsippany, NJ).	Ristocetin	54-64	von Willebrand factor	Homo sapiens	84-87
12362242-5	2002	Under static conditions, cells expressing mutant GP Ibalpha bound VWF (binding induced by either botrocetin or ristocetin) in a manner indistinguishable from cells expressing wild-type GP Ibalpha.	Ristocetin	111-121	von Willebrand factor	Cricetulus griseus	66-69
12176890-6	2002	The expressed dimeric VWF displayed a loss of several specific functions: collagen binding, factor VIII binding, and ristocetin-induced platelet binding.	Ristocetin	117-127	von Willebrand factor	Homo sapiens	22-25
12223999-3	2002	We developed a new, rapid, and simple method for measuring VWFcp activity based on the positive correlation between VWF multimeric size and Ristocetin cofactor activity (VWF:RCo).	Ristocetin	140-150	ADAM metallopeptidase with thrombospondin type 1 motif 13	Homo sapiens	59-64
12223999-3	2002	We developed a new, rapid, and simple method for measuring VWFcp activity based on the positive correlation between VWF multimeric size and Ristocetin cofactor activity (VWF:RCo).	Ristocetin	140-150	von Willebrand factor	Homo sapiens	59-62
12223999-3	2002	We developed a new, rapid, and simple method for measuring VWFcp activity based on the positive correlation between VWF multimeric size and Ristocetin cofactor activity (VWF:RCo).	Ristocetin	140-150	von Willebrand factor	Homo sapiens	116-119
11943773-2	2002	In vitro platelet glycoprotein Ib (GPIb) binding of the human von Willebrand factor (VWF) increases markedly by exogenous modulators such as ristocetin or botrocetin, and the binding does not occur in normal circulation.	Ristocetin	141-151	von Willebrand factor	Homo sapiens	85-88
12010796-6	2002	The force required to break the ristocetin- and botrocetin-induced plasma VWF-GP Ib-IX bonds occurred in integer multiples of 6.5 pN and 8.8 pN, respectively, depending on the number of bonds formed.	Ristocetin	32-42	von Willebrand factor	Homo sapiens	74-77
12180497-10	2002	ADP, ristocetin and thrombin induce fibrinogen binding to porcine platelets similarly to human platelets.	Ristocetin	5-15	fibrinogen beta chain	Homo sapiens	36-46
11994985-6	2002	However, ivIG pretreatment improved the VWF ristocetin cofactor (VWF:RCo) half-life from only 1.5 hr to more than 4 hr, allowing desmopressin infusions twice daily to maintain sufficient VWF:RCo levels.	Ristocetin	44-54	von Willebrand factor	Homo sapiens	40-43
11994985-6	2002	However, ivIG pretreatment improved the VWF ristocetin cofactor (VWF:RCo) half-life from only 1.5 hr to more than 4 hr, allowing desmopressin infusions twice daily to maintain sufficient VWF:RCo levels.	Ristocetin	44-54	von Willebrand factor	Homo sapiens	65-68
11994985-6	2002	However, ivIG pretreatment improved the VWF ristocetin cofactor (VWF:RCo) half-life from only 1.5 hr to more than 4 hr, allowing desmopressin infusions twice daily to maintain sufficient VWF:RCo levels.	Ristocetin	44-54	von Willebrand factor	Homo sapiens	65-68
12008954-6	2002	Ristocetin-mediated binding of VWF transiently elevated [Ca2+]i after a lag phase.	Ristocetin	0-10	von Willebrand factor	Homo sapiens	31-34
12038791-7	2002	Ristocetin-induced 125I-vWF binding to L70F, however, did not differ from that to WT.	Ristocetin	0-10	von Willebrand factor	Homo sapiens	24-27
11992238-0	2002	Comparative study on collagen-binding enzyme-linked immunosorbent assay and ristocetin cofactor activity assays for detection of functional activity of von Willebrand factor.	Ristocetin	76-86	von Willebrand factor	Homo sapiens	152-173
11992238-1	2002	For more than two decades, the ristocetin cofactor (RCo) assay, which measures the von Willebrand factor (vWF)-mediated agglutination of platelets in the presence of the antibiotic ristocetin, has been the most common method for measuring the functional activity of vWF.	Ristocetin	31-41	von Willebrand factor	Homo sapiens	83-104
11756169-10	2002	Similar behavior was demonstrated by VWF ristocetin cofactor activity and FVIII.	Ristocetin	41-51	von Willebrand factor	Homo sapiens	37-40
11992238-1	2002	For more than two decades, the ristocetin cofactor (RCo) assay, which measures the von Willebrand factor (vWF)-mediated agglutination of platelets in the presence of the antibiotic ristocetin, has been the most common method for measuring the functional activity of vWF.	Ristocetin	31-41	von Willebrand factor	Homo sapiens	106-109
11992238-1	2002	For more than two decades, the ristocetin cofactor (RCo) assay, which measures the von Willebrand factor (vWF)-mediated agglutination of platelets in the presence of the antibiotic ristocetin, has been the most common method for measuring the functional activity of vWF.	Ristocetin	31-41	von Willebrand factor	Homo sapiens	266-269
11992239-8	2002	The currently used vWF:RCof test is an agglutination test in which patients" plasma is added to washed fixed control platelets in the presence of ristocetin and the extent of agglutination is measured.	Ristocetin	146-156	von Willebrand factor	Homo sapiens	19-22
11788586-6	2002	Btk is also phosphorylated on threonine residues in a PKC-dependent manner and associates with PKCtheta; upon platelet activation by either alboaggregin A or activation of GP Ib-V-IX alone by von Willebrand factor/ristocetin.	Ristocetin	214-224	Bruton tyrosine kinase	Homo sapiens	0-3
11772401-3	2002	In washed platelets, vWF/ristocetin and vWF/botrocetin stimulate weak tyrosine phosphorylation of the FcR gamma-chain, Syk and PLCgamma2, but not the adaptor LAT (linker for activation of T-cells), which is localized to glycolipid-enriched membrane domains.	Ristocetin	25-35	von Willebrand factor	Homo sapiens	21-24
11772401-3	2002	In washed platelets, vWF/ristocetin and vWF/botrocetin stimulate weak tyrosine phosphorylation of the FcR gamma-chain, Syk and PLCgamma2, but not the adaptor LAT (linker for activation of T-cells), which is localized to glycolipid-enriched membrane domains.	Ristocetin	25-35	Fc epsilon receptor Ig	Homo sapiens	102-111
11772401-3	2002	In washed platelets, vWF/ristocetin and vWF/botrocetin stimulate weak tyrosine phosphorylation of the FcR gamma-chain, Syk and PLCgamma2, but not the adaptor LAT (linker for activation of T-cells), which is localized to glycolipid-enriched membrane domains.	Ristocetin	25-35	spleen associated tyrosine kinase	Homo sapiens	119-122
11772401-3	2002	In washed platelets, vWF/ristocetin and vWF/botrocetin stimulate weak tyrosine phosphorylation of the FcR gamma-chain, Syk and PLCgamma2, but not the adaptor LAT (linker for activation of T-cells), which is localized to glycolipid-enriched membrane domains.	Ristocetin	25-35	phospholipase C gamma 2	Homo sapiens	127-136
11772401-6	2002	In contrast, in platelet-rich plasma (PRP), threshold concentrations of ristocetin or asialo-vWF stimulated GPIb-dependent biphasic aggregation, in which the second phase was blocked by PP1.	Ristocetin	72-82	neuropeptide Y receptor Y4	Homo sapiens	186-189
11772401-8	2002	Higher concentrations of ristocetin stimulated GPIIb-IIIa-independent agglutination in PRP.	Ristocetin	25-35	integrin subunit alpha 2b	Homo sapiens	47-52
11981108-3	2001	When com-bined, 1C1E7 and 75H4B12 promoted vWf binding to isolated GPIb under static conditions, even in the absence of ristocetin or botrocetin, and induced platelet aggregation synergistically in the presence of zero to subthreshold ristocetin concentrations.	Ristocetin	235-245	von Willebrand factor	Homo sapiens	43-46
11948601-7	2002	Since vWf does not bind GP Ibalpha without high shear stress, the compounds botrocetin and ristocetin were used to induce binding between human vWf and the chimeras.	Ristocetin	91-101	von Willebrand factor	Homo sapiens	144-147
12372966-9	2002	In CAPD patients treated with rHuEPO serum and dialysate leptin significantly correlated with tissue factor pathway inhibitor, protein C, thrombomodulin, ristocetin-induced platelet aggregation in the whole blood and PRP.	Ristocetin	154-164	leptin	Homo sapiens	57-63
12214161-3	2002	On the 4th day after the infusion, VWF antigen and VWF ristocetin cofactor increased to 40 and 78% of the control, respectively, and dental extractions were performed successfully.	Ristocetin	55-65	von Willebrand factor	Homo sapiens	51-54
11816713-7	2001	In functional assays, RAM.1 had no effect on platelet aggregation induced by ADP, collagen or thrombin, but inhibited ristocetin induced platelet agglutination and botrocetin induced vWF binding.	Ristocetin	118-128	solute carrier family 20 member 2	Homo sapiens	22-27
11810130-7	2001	MEASUREMENT AND RESULTS: The infusion of HES resulted in decreased circulating levels of von Willebrand factor antigen (from 85+/-8% to 59+/-6% after HES vs from 80+/-7% to 69+/-8% after albumin, p<0.05) and ristocetin cofactor activity (from 93+/-4 to 67+/-4% after HES vs from 79+/-5 to 75+/-5% after albumin, p<0.01).	Ristocetin	211-221	ribosome binding protein 1	Homo sapiens	41-44
11535515-7	2001	vWf binding was increased at all concentrations of ristocetin examined, and adhesion on a vWf matrix was enhanced in terms of cell tethering, slower rolling velocity, and decreased detachment with increasing shear rate.	Ristocetin	51-61	von Willebrand factor	Homo sapiens	0-3
11341505-4	2001	Secondly we observed a synergistic activating effect of two anti-von Willebrand factor (vWF) MoAbs IC1E7 and B724, both known to enhance vWF binding to GPIbalpha in the presence of shear or ristocetin.	Ristocetin	190-200	von Willebrand factor	Homo sapiens	60-86
11547362-6	2001	Functional analysis has shown that r-vWF promotes ristocetin cofactor-mediated platelet aggregation, collagen interaction and FVIII binding, and platelet-collagen adhesion under shear stress.	Ristocetin	50-60	von Willebrand factor	Homo sapiens	37-40
11686107-6	2001	The laboratory findings of AVWS associated with systemic lupus erythematosus or IgG benign monoclonal gammopathy are characterized by a prolonged bleeding time and activated partial thromboplastin time, decreased or absent ristocetin-induced platelet activity, low to very low levels of factor VIII coagulant activity (mean 15%), VWF: Ag (mean 10.7%) and VWF: RCo (mean 6.2%), and a type II multimeric pattern of VWF.	Ristocetin	223-233	cytochrome c oxidase subunit 8A	Homo sapiens	294-298
11686107-6	2001	The laboratory findings of AVWS associated with systemic lupus erythematosus or IgG benign monoclonal gammopathy are characterized by a prolonged bleeding time and activated partial thromboplastin time, decreased or absent ristocetin-induced platelet activity, low to very low levels of factor VIII coagulant activity (mean 15%), VWF: Ag (mean 10.7%) and VWF: RCo (mean 6.2%), and a type II multimeric pattern of VWF.	Ristocetin	223-233	von Willebrand factor	Homo sapiens	330-333
11686107-6	2001	The laboratory findings of AVWS associated with systemic lupus erythematosus or IgG benign monoclonal gammopathy are characterized by a prolonged bleeding time and activated partial thromboplastin time, decreased or absent ristocetin-induced platelet activity, low to very low levels of factor VIII coagulant activity (mean 15%), VWF: Ag (mean 10.7%) and VWF: RCo (mean 6.2%), and a type II multimeric pattern of VWF.	Ristocetin	223-233	von Willebrand factor	Homo sapiens	355-358
11686107-6	2001	The laboratory findings of AVWS associated with systemic lupus erythematosus or IgG benign monoclonal gammopathy are characterized by a prolonged bleeding time and activated partial thromboplastin time, decreased or absent ristocetin-induced platelet activity, low to very low levels of factor VIII coagulant activity (mean 15%), VWF: Ag (mean 10.7%) and VWF: RCo (mean 6.2%), and a type II multimeric pattern of VWF.	Ristocetin	223-233	von Willebrand factor	Homo sapiens	355-358
11278380-3	2001	Deletion of the filamin binding site in GPIb(alpha) markedly enhances ristocetin- (or botrocetin)-induced vWF binding and allows GPIb-IX-expressing cells to adhere to immobilized vWF under both static and flow conditions.	Ristocetin	70-80	von Willebrand factor	Homo sapiens	106-109
11292197-5	2001	We found a significant increase in plasma factor VIII (FVIII), vWF:antigen (Ag), and vWF:ristocetin cofactor (Rco) levels, associated with a mean decrease in platelet vWF:Ag.	Ristocetin	89-99	von Willebrand factor	Homo sapiens	85-88
17903829-3	2001	The vWF was measured by the ristocetin cofactor assay.	Ristocetin	28-38	von Willebrand factor	Homo sapiens	4-7
11468163-4	2001	These antibodies, however, had little or no effect (approximately 40% inhibition) on the binding of vWF induced by either botrocetin or ristocetin.	Ristocetin	136-146	von Willebrand factor	Homo sapiens	100-103
11279169-9	2001	Cells expressing the Glu mutant, on the other hand, were normal with respect to ristocetin-induced vWF binding and adhesion to immobilized vWF but were markedly defective in botrocetin-induced vWF binding.	Ristocetin	80-90	von Willebrand factor	Homo sapiens	99-102
11279169-10	2001	These results indicate that GP I(b)alpha tyrosine sulfation influences the interaction of this polypeptide with vWF primarily by contributing negative charges under physiological conditions and when the interaction is induced by ristocetin but contributes a specific structure to the botrocetin-induced interaction.	Ristocetin	229-239	glycoprotein Ib platelet subunit alpha	Homo sapiens	28-40
11279169-10	2001	These results indicate that GP I(b)alpha tyrosine sulfation influences the interaction of this polypeptide with vWF primarily by contributing negative charges under physiological conditions and when the interaction is induced by ristocetin but contributes a specific structure to the botrocetin-induced interaction.	Ristocetin	229-239	von Willebrand factor	Homo sapiens	112-115
11292197-5	2001	We found a significant increase in plasma factor VIII (FVIII), vWF:antigen (Ag), and vWF:ristocetin cofactor (Rco) levels, associated with a mean decrease in platelet vWF:Ag.	Ristocetin	89-99	von Willebrand factor	Homo sapiens	85-88
11341505-4	2001	Secondly we observed a synergistic activating effect of two anti-von Willebrand factor (vWF) MoAbs IC1E7 and B724, both known to enhance vWF binding to GPIbalpha in the presence of shear or ristocetin.	Ristocetin	190-200	von Willebrand factor	Homo sapiens	88-91
11341505-4	2001	Secondly we observed a synergistic activating effect of two anti-von Willebrand factor (vWF) MoAbs IC1E7 and B724, both known to enhance vWF binding to GPIbalpha in the presence of shear or ristocetin.	Ristocetin	190-200	glycoprotein Ib platelet subunit alpha	Homo sapiens	152-161
11680263-6	2001	Platelet aggregation in platelet-rich plasma induced by collagen, ristocetin and serotonin increased significantly after 3 months of erythropoietin therapy when compared to the baseline values.	Ristocetin	66-76	erythropoietin	Homo sapiens	133-147
11181425-5	2001	In vitro, agkistin concentration-dependently inhibited ristocetin-induced human platelet agglutination and aggregation in the presence of vWF.	Ristocetin	55-65	von Willebrand factor	Homo sapiens	138-141
11159522-1	2001	The study identified 10 patients from 6 families with prolonged bleeding time, decreased von Willebrand factor (vWF) ristocetin cofactor activity (RCoF) to vWF:Ag (antigen) ratio, and reduced ristocetin-induced platelet agglutination as well as ristocetin- or botrocetin-induced binding of plasma vWF to platelet glycoprotein Ib (GpIb).	Ristocetin	117-127	von Willebrand factor	Homo sapiens	112-115
11190800-6	2001	Maximal vWF binding induced by botrocetin was only 10% to 15% of that observed with ristocetin.	Ristocetin	84-94	von Willebrand factor	Homo sapiens	8-11
11133756-2	2001	This interaction involves the A1 domain of vWF and the N-terminal extracellular region of GP Ibalpha (His-1-Glu-282), and it can also be induced under static conditions by the modulators ristocetin and botrocetin.	Ristocetin	187-197	von Willebrand factor	Cricetulus griseus	43-46
11133756-4	2001	The combined results suggest that the shear-dependent interactions between vWF and GP Ibalpha closely correlate with ristocetin- rather than botrocetin-dependent binding under static conditions and that certain anti-vWF monoclonal antibodies are able to selectively inhibit shear-dependent platelet aggregation.	Ristocetin	117-127	von Willebrand factor	Cricetulus griseus	75-78
11133756-4	2001	The combined results suggest that the shear-dependent interactions between vWF and GP Ibalpha closely correlate with ristocetin- rather than botrocetin-dependent binding under static conditions and that certain anti-vWF monoclonal antibodies are able to selectively inhibit shear-dependent platelet aggregation.	Ristocetin	117-127	von Willebrand factor	Cricetulus griseus	216-219
11127874-3	2000	TR1-41 also decreased ristocetin-induced platelet agglutination.	Ristocetin	22-32	taste 1 receptor member 1	Homo sapiens	0-3
11150026-1	2001	We describe a von Willebrand disease (VWD) variant characterized by low plasma and platelet von Willebrand factor (VWF), impaired ristocetin-induced VWF binding to platelet glycoprotein Ib (GPIb), and abnormal VWF multimer pattern not associated with the absence of large forms.	Ristocetin	130-140	von Willebrand factor	Homo sapiens	149-152
11150026-1	2001	We describe a von Willebrand disease (VWD) variant characterized by low plasma and platelet von Willebrand factor (VWF), impaired ristocetin-induced VWF binding to platelet glycoprotein Ib (GPIb), and abnormal VWF multimer pattern not associated with the absence of large forms.	Ristocetin	130-140	von Willebrand factor	Homo sapiens	149-152
11150026-3	2001	In addition to the decreased factor VIII (FVIII) and VWF levels, ristocetin-induced platelet aggregation (RIPA) was almost absent, and VWF ristocetin cofactor activity (VWF:RCo) was significantly more decreased than VWF antigen.	Ristocetin	139-149	von Willebrand factor	Homo sapiens	135-138
11150026-3	2001	In addition to the decreased factor VIII (FVIII) and VWF levels, ristocetin-induced platelet aggregation (RIPA) was almost absent, and VWF ristocetin cofactor activity (VWF:RCo) was significantly more decreased than VWF antigen.	Ristocetin	139-149	von Willebrand factor	Homo sapiens	135-138
11150026-3	2001	In addition to the decreased factor VIII (FVIII) and VWF levels, ristocetin-induced platelet aggregation (RIPA) was almost absent, and VWF ristocetin cofactor activity (VWF:RCo) was significantly more decreased than VWF antigen.	Ristocetin	139-149	von Willebrand factor	Homo sapiens	135-138
11240613-7	2001	Preliminary results of recent studies support the hypothesis that treatment with factor VIII/vWF concentrates based upon the content of vWF activity as reflected in the ristocetin cofactor assay is practicable, safe and efficacious.	Ristocetin	169-179	von Willebrand factor	Homo sapiens	93-96
11240613-7	2001	Preliminary results of recent studies support the hypothesis that treatment with factor VIII/vWF concentrates based upon the content of vWF activity as reflected in the ristocetin cofactor assay is practicable, safe and efficacious.	Ristocetin	169-179	von Willebrand factor	Homo sapiens	136-139
11127876-2	2000	S-nitroso-AR545C - an S-nitrosoderivative of a recombinant von Willebrand factor fragment AR545C spanning Ala 444 to Asp 730 and containing an Arg 545 Cys mutation, was previously found to inhibit ristocetin- and ADP-induced platelet aggregation and the interaction of platelets with extracellular matrix (ECM).	Ristocetin	197-207	von Willebrand factor	Cavia porcellus	59-80
11026108-3	2000	A monoclonal antibody (MAB)-based enzyme-linked immunosorbent assay (ELISA) system reported to correlate with a standard vWF:ristocetin cofactor (RCof) assay is also commercially available.	Ristocetin	125-135	von Willebrand factor	Equus caballus	121-124
10959711-9	2000	Ristocetin cofactor activity (vWF:RCo) or collagen binding activity (vWF:CBA) were usually low in AvWS (median values 20 U/dL, range 3-150), while factor VIII coagulant activity was sometimes normal (median 25 U/dL, range 3-191).	Ristocetin	0-10	von Willebrand factor	Homo sapiens	30-33
11710113-7	2000	The addition of ristocetin to the rGPIb alpha-AMS in the presence of vWf caused specific aggregation.	Ristocetin	16-26	von Willebrand factor	Homo sapiens	69-72
10959687-5	2000	This elevation of vWf antigen represented functionally normal vWf as evaluated by plasma FVIII, ristocetin cofactor assay and vWf multimer analyses.	Ristocetin	96-106	von Willebrand factor	Homo sapiens	18-21
10959688-4	2000	The patients who have a discrepancy between vWF antigen level and vWF ristocetin cofactor activity exhibited decreased ristocetin-induced binding but only a slight decrease in the percentage of high molecular weight (HMW) multimers in plasma.	Ristocetin	70-80	von Willebrand factor	Homo sapiens	66-69
10959688-4	2000	The patients who have a discrepancy between vWF antigen level and vWF ristocetin cofactor activity exhibited decreased ristocetin-induced binding but only a slight decrease in the percentage of high molecular weight (HMW) multimers in plasma.	Ristocetin	119-129	von Willebrand factor	Homo sapiens	44-47
10959688-4	2000	The patients who have a discrepancy between vWF antigen level and vWF ristocetin cofactor activity exhibited decreased ristocetin-induced binding but only a slight decrease in the percentage of high molecular weight (HMW) multimers in plasma.	Ristocetin	119-129	von Willebrand factor	Homo sapiens	66-69
10845912-2	2000	We report on 9 fully multimerized recombinant vWFs (rvWFs) expressing type 2M or type 2B von Willebrand disease (vWD) mutations, characterized respectively by a decreased or increased binding of vWF to GPIb in the presence of ristocetin.	Ristocetin	226-236	von Willebrand factor	Homo sapiens	46-49
10827132-5	2000	Administration of endotoxin increased the density of periendothelial platelets and reduced the rolling velocities of platelets and leukocytes in venules: All events were attenuated by anti-rat P-selectin monoclonal antibody s789G or by anti-human glycoprotein (GP) Ibalpha monoclonal antibody GUR83/35, which blocks ristocetin-induced aggregation of rat platelets.	Ristocetin	316-326	selectin P	Rattus norvegicus	193-203
11014964-6	2000	In contrast, MoAb 28E6 did abolish both the ristocetin- and botrocetin-induced GPIb-vWF binding, whereas it did not block the shear-induced interaction.	Ristocetin	44-54	von Willebrand factor	Homo sapiens	84-87
11014964-7	2000	Thus, we identify here two anti-GPIb MoAbs 27A10 and 28E6 that either preferentially inhibit the shear-induced or the ristocetin/botrocetin-induced platelet-vWF interaction.	Ristocetin	118-128	von Willebrand factor	Homo sapiens	157-160
10753907-7	2000	Ristocetin and botrocetin actions on VWF were dissociated readily by mutagenesis.	Ristocetin	0-10	von Willebrand factor	Homo sapiens	37-40
10713323-9	2000	Linear regression analysis showed good correlation of results of sulfatide-binding assay for von Willebrand factor with results of the von Willebrand factor antigen, Ristocetin cofactor assay for von Willebrand factor, and collagen-binding assay for von Willebrand factor.	Ristocetin	166-176	von Willebrand factor	Homo sapiens	93-114
10648402-3	2000	We have used mammalian cell expression of canine-human chimeras of GP Ibalpha, corresponding to precise structural boundaries, to demonstrate the first specific requirement for individual leucine-rich repeats for binding of vWf either induced by a modulator, ristocetin, or under hydrodynamic flow.	Ristocetin	259-269	von Willebrand factor	Homo sapiens	224-227
10590063-4	1999	Ristocetin-induced CHO-GPIbalphabeta/IX cell aggregation was completely inhibited by the recombinant VCL fragment of vWF that contains the A1 domain.	Ristocetin	0-10	von Willebrand factor	Homo sapiens	117-120
10739386-9	2000	Patient 1 antibody also blocked vWF binding to platelet GPIb when induced by ristocetin.	Ristocetin	77-87	von Willebrand factor	Homo sapiens	32-35
10739386-11	2000	Our data thus suggest that this inhibitor does not recognize the GPIb-binding site on vWF but the sites of vWF involved in its interaction with ristocetin.	Ristocetin	144-154	von Willebrand factor	Homo sapiens	107-110
10688330-6	2000	Interestingly, ECA-4 monoclonal antibody is able to completely inhibit platelet agglutination induced by ristocetin, suggesting that it binds to von Willebrand Factor close to platelet GPIb binding site.	Ristocetin	105-115	gamma-aminobutyric acid type A receptor subunit alpha1	Homo sapiens	15-20
10739395-6	2000	Addition of protamine sulphate to platelet-rich plasma (PRP), reduced significantly the GPIb-vWF activity as assessed by ristocetin-induced platelet agglutination.	Ristocetin	121-131	von Willebrand factor	Homo sapiens	93-96
10669163-1	2000	The ristocetin induced binding of vWF to GPIb, which is routinely tested in a platelet agglutination assay, can be reproducibly studied in an ELISA where plasma vWF binds to a captured rGPIb alpha-fragment (His1-Val289) in the presence of ristocetin.	Ristocetin	4-14	von Willebrand factor	Homo sapiens	34-37
10669163-1	2000	The ristocetin induced binding of vWF to GPIb, which is routinely tested in a platelet agglutination assay, can be reproducibly studied in an ELISA where plasma vWF binds to a captured rGPIb alpha-fragment (His1-Val289) in the presence of ristocetin.	Ristocetin	4-14	von Willebrand factor	Homo sapiens	161-164
10669163-1	2000	The ristocetin induced binding of vWF to GPIb, which is routinely tested in a platelet agglutination assay, can be reproducibly studied in an ELISA where plasma vWF binds to a captured rGPIb alpha-fragment (His1-Val289) in the presence of ristocetin.	Ristocetin	239-249	von Willebrand factor	Homo sapiens	34-37
10669163-1	2000	The ristocetin induced binding of vWF to GPIb, which is routinely tested in a platelet agglutination assay, can be reproducibly studied in an ELISA where plasma vWF binds to a captured rGPIb alpha-fragment (His1-Val289) in the presence of ristocetin.	Ristocetin	239-249	von Willebrand factor	Homo sapiens	161-164
10669163-2	2000	This binding is specific since the vWF-GPIb interaction could (i) be blocked by inhibitory anti-GPIb or anti-(vWF A1 domain) monoclonal antibodies (mAbs) and (ii) be enhanced by an anti-vWF mAb that also facilitates ristocetin induced platelet agglutination.	Ristocetin	216-226	von Willebrand factor	Homo sapiens	35-38
10590063-6	1999	Using monoclonal antibodies blocking vWF interaction with GPIb/V/IX or mocarhagin, a venom metalloproteinase that removes the amino-terminal fragment of GPIbalpha extending from aa 1 to 282, we demonstrated that both ristocetin- and heparin-induced aggregations involved an interaction between the A1 domain of vWF and the GPIbalpha subunit of the GPIb/V/IX complex.	Ristocetin	217-227	von Willebrand factor	Homo sapiens	37-40
9572997-7	1998	All inhibitors blocked ristocetin-mediated vWF binding to platelets.	Ristocetin	23-33	von Willebrand factor	Homo sapiens	43-46
10339461-9	1999	Also, in patients with vWD type 1 and borderline to normal ristocetin-cofactor (vWF:RCo) activity values, collagen receptor density correlates inversely with closure time in a high shear stress system (platelet function analyzer [PFA-100]).	Ristocetin	59-69	von Willebrand factor	Homo sapiens	80-83
9759623-0	1998	Ristocetin- and thrombin-induced platelet aggregation at physiological shear rates: differential roles for GPIb and GPIIb-IIIa receptor.	Ristocetin	0-10	integrin subunit alpha 2b	Homo sapiens	116-121
9759623-5	1998	The vWF-GPIb interaction was exclusively able to support ristocetin-mediated shear aggregation of metabolically active platelets, with very few vWF monomer equivalents bound per platelet (representing < or = 10 molecules of 10 million Da) required to yield high capture efficiencies (alphaG = 0.38+/-.02; n = 11), suggesting rapid and stable bond formations between vWF and GPIb.	Ristocetin	57-67	von Willebrand factor	Homo sapiens	4-7
9731234-4	1998	Interestingly, binding of von Willebrand Factor (vWF) to purified GPIb in the presence of ristocetin and botrocetin in a standardized microtiter plate assay was not altered by partial or even by total deglycosylation.	Ristocetin	90-100	von Willebrand factor	Homo sapiens	26-47
9731234-4	1998	Interestingly, binding of von Willebrand Factor (vWF) to purified GPIb in the presence of ristocetin and botrocetin in a standardized microtiter plate assay was not altered by partial or even by total deglycosylation.	Ristocetin	90-100	von Willebrand factor	Homo sapiens	49-52
10494765-2	1999	Diagnosis was based on a positive family history and low von Willebrand factor (VWF) ristocetin cofactor activity.	Ristocetin	85-95	von Willebrand factor	Homo sapiens	80-83
10494765-10	1999	The results of this study illustrate that a personal and family bleeding history and persistently low VWF ristocetin cofactor activity, fitting the usual criteria for type 1 VWD, may not cosegregate with genetic markers at the VWF gene locus.	Ristocetin	106-116	von Willebrand factor	Homo sapiens	102-105
10497852-1	1999	Type 2B von Willebrand disease (vWD) is a von Willebrand factor (vWF) subtype with increased binding affinity for platelet glycoprotein (GP) Ib and is characterized by increased ristocetin-induced platelet agglutination at low concentrations of ristocetin.	Ristocetin	178-188	von Willebrand factor	Homo sapiens	42-63
10497852-1	1999	Type 2B von Willebrand disease (vWD) is a von Willebrand factor (vWF) subtype with increased binding affinity for platelet glycoprotein (GP) Ib and is characterized by increased ristocetin-induced platelet agglutination at low concentrations of ristocetin.	Ristocetin	178-188	von Willebrand factor	Homo sapiens	65-68
10497852-1	1999	Type 2B von Willebrand disease (vWD) is a von Willebrand factor (vWF) subtype with increased binding affinity for platelet glycoprotein (GP) Ib and is characterized by increased ristocetin-induced platelet agglutination at low concentrations of ristocetin.	Ristocetin	245-255	von Willebrand factor	Homo sapiens	65-68
10381514-6	1999	Ristocetin-mediated binding of vWF induced a transient platelet [Ca2+]i increase at 37 degrees C, but no response at lower temperatures (20 degrees C to 25 degrees C).	Ristocetin	0-10	von Willebrand factor	Homo sapiens	31-34
10233433-5	1999	In all cases a mixture of patient"s plasma with normal plasma resulted in inhibition of ristocetin-induced binding of VWF to normal platelets.	Ristocetin	88-98	von Willebrand factor	Homo sapiens	118-121
10027712-5	1999	Ristocetin-induced agglutinations of both the thrombin- and TRAP-stimulated platelets were lowered during the decreased surface expressions of GPIbalpha, GPIX and GPV/GPVf2 and then normalized when these GPs were again redistributed onto the surface, indicating that the redistributed GPIb/IX/Vf2 complex on the surface can act as a VWF receptor as efficiently as an intact GPIb/IX/V.	Ristocetin	0-10	coagulation factor II, thrombin	Homo sapiens	46-54
10027712-5	1999	Ristocetin-induced agglutinations of both the thrombin- and TRAP-stimulated platelets were lowered during the decreased surface expressions of GPIbalpha, GPIX and GPV/GPVf2 and then normalized when these GPs were again redistributed onto the surface, indicating that the redistributed GPIb/IX/Vf2 complex on the surface can act as a VWF receptor as efficiently as an intact GPIb/IX/V.	Ristocetin	0-10	TRAP	Homo sapiens	60-64
10027712-5	1999	Ristocetin-induced agglutinations of both the thrombin- and TRAP-stimulated platelets were lowered during the decreased surface expressions of GPIbalpha, GPIX and GPV/GPVf2 and then normalized when these GPs were again redistributed onto the surface, indicating that the redistributed GPIb/IX/Vf2 complex on the surface can act as a VWF receptor as efficiently as an intact GPIb/IX/V.	Ristocetin	0-10	glycoprotein Ib platelet subunit alpha	Homo sapiens	143-152
10027712-5	1999	Ristocetin-induced agglutinations of both the thrombin- and TRAP-stimulated platelets were lowered during the decreased surface expressions of GPIbalpha, GPIX and GPV/GPVf2 and then normalized when these GPs were again redistributed onto the surface, indicating that the redistributed GPIb/IX/Vf2 complex on the surface can act as a VWF receptor as efficiently as an intact GPIb/IX/V.	Ristocetin	0-10	glycoprotein IX platelet	Homo sapiens	154-158
10027712-5	1999	Ristocetin-induced agglutinations of both the thrombin- and TRAP-stimulated platelets were lowered during the decreased surface expressions of GPIbalpha, GPIX and GPV/GPVf2 and then normalized when these GPs were again redistributed onto the surface, indicating that the redistributed GPIb/IX/Vf2 complex on the surface can act as a VWF receptor as efficiently as an intact GPIb/IX/V.	Ristocetin	0-10	glycoprotein V platelet	Homo sapiens	163-166
10027712-5	1999	Ristocetin-induced agglutinations of both the thrombin- and TRAP-stimulated platelets were lowered during the decreased surface expressions of GPIbalpha, GPIX and GPV/GPVf2 and then normalized when these GPs were again redistributed onto the surface, indicating that the redistributed GPIb/IX/Vf2 complex on the surface can act as a VWF receptor as efficiently as an intact GPIb/IX/V.	Ristocetin	0-10	von Willebrand factor	Homo sapiens	333-336
9573016-13	1998	Our results suggested that on binding to a botrocetin-binding site on vWF, MoAb 724 mimics the effect of botrocetin by inducing an active conformation of vWF that is more sensitive to shear stress or to low ristocetin concentration.	Ristocetin	207-217	von Willebrand factor	Homo sapiens	70-73
9573016-13	1998	Our results suggested that on binding to a botrocetin-binding site on vWF, MoAb 724 mimics the effect of botrocetin by inducing an active conformation of vWF that is more sensitive to shear stress or to low ristocetin concentration.	Ristocetin	207-217	von Willebrand factor	Homo sapiens	154-157
9619734-6	1998	Monoclonal antibody directed to the region within the A1 domain of vWF which interacts with the glycoprotein Ib completely inhibited the vWF ristocetin cofactor (vWF:RistCof), while vWF:CBA was not affected.	Ristocetin	141-151	von Willebrand factor	Homo sapiens	67-70
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.	Ristocetin	163-173	integrin subunit alpha 2b	Homo sapiens	115-120
9588391-5	1998	Surprisingly, ristocetin, which "chemically activates" GPIb/vWF to mediate spontaneous binding of the ligand to its receptor, at low concentrations yielding <2000 platelet-bound vWF monomers, gave efficient aggregation even at 1000 sec(-1) (CE = 0.34 +/- 0.02, n = 11) with only GPIb required.	Ristocetin	14-24	von Willebrand factor	Homo sapiens	60-63
9588391-5	1998	Surprisingly, ristocetin, which "chemically activates" GPIb/vWF to mediate spontaneous binding of the ligand to its receptor, at low concentrations yielding <2000 platelet-bound vWF monomers, gave efficient aggregation even at 1000 sec(-1) (CE = 0.34 +/- 0.02, n = 11) with only GPIb required.	Ristocetin	14-24	von Willebrand factor	Homo sapiens	181-184
9531591-7	1998	The low-dose ristocetin aggregation in patient platelet-rich plasma (PRP) was completely blocked by neutralizing antiglycoprotein Ib (GPIb) and anti-vWF antibodies.	Ristocetin	13-23	von Willebrand factor	Homo sapiens	149-152
9531591-8	1998	The monoclonal anti-Fc gamma RII receptor antibody IV.3 inhibited partly, which suggests that PRP aggregation by low-dose ristocetin was elicited by vWF-immunoglobulin (Ig) complexes.	Ristocetin	122-132	von Willebrand factor	Homo sapiens	149-152
9531591-9	1998	Upon addition to washed human platelets, with vWF (10 micrograms/mL), purified patient Igs dose-dependently enhanced ristocetin (0.15 mg/mL)-induced aggregation between 0 and 500 micrograms/mL, an effect that disappeared again above 1 mg/mL.	Ristocetin	117-127	von Willebrand factor	Homo sapiens	46-49
9490688-2	1998	The A1, A2, and A3 domains in vWF mediate binding to glycoprotein Ib, ristocetin, botrocetin, collagen, sulphatides, and heparin and provide a protease cleavage site.	Ristocetin	70-80	von Willebrand factor	Homo sapiens	30-33
9619734-6	1998	Monoclonal antibody directed to the region within the A1 domain of vWF which interacts with the glycoprotein Ib completely inhibited the vWF ristocetin cofactor (vWF:RistCof), while vWF:CBA was not affected.	Ristocetin	141-151	von Willebrand factor	Homo sapiens	137-140
9619734-6	1998	Monoclonal antibody directed to the region within the A1 domain of vWF which interacts with the glycoprotein Ib completely inhibited the vWF ristocetin cofactor (vWF:RistCof), while vWF:CBA was not affected.	Ristocetin	141-151	von Willebrand factor	Homo sapiens	137-140
9619734-6	1998	Monoclonal antibody directed to the region within the A1 domain of vWF which interacts with the glycoprotein Ib completely inhibited the vWF ristocetin cofactor (vWF:RistCof), while vWF:CBA was not affected.	Ristocetin	141-151	von Willebrand factor	Homo sapiens	137-140
9268197-0	1997	Plasma derived von Willebrand factor preparations: collagen binding and ristocetin cofactor activities.	Ristocetin	72-82	von Willebrand factor	Homo sapiens	15-36
9454760-9	1998	We also found that, similar to the signaling mediators phosphatidylinositol 3-kinase and Src, platelet cytoskeletal 14-3-3zeta content is increased following vWF and ristocetin stimulation.	Ristocetin	166-176	SRC proto-oncogene, non-receptor tyrosine kinase	Homo sapiens	89-92
9454760-9	1998	We also found that, similar to the signaling mediators phosphatidylinositol 3-kinase and Src, platelet cytoskeletal 14-3-3zeta content is increased following vWF and ristocetin stimulation.	Ristocetin	166-176	tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein zeta	Homo sapiens	116-126
9473222-3	1998	Whereas ristocetin-induced binding of plasma vWF from affected members of both families to fixed platelets was reduced, botrocetin-induced platelet binding was normal.	Ristocetin	8-18	von Willebrand factor	Homo sapiens	45-48
9473222-7	1998	Expression of recombinant vWF containing either F606I or I662F mutations resulted in mutant recombinant vWF with decreased ristocetin-induced platelet binding, but normal multimer structure, botrocetin-induced platelet binding, collagen binding, and binding to the conformation-sensitive monoclonal antibody, AvW-3.	Ristocetin	123-133	von Willebrand factor	Homo sapiens	26-29
9473222-7	1998	Expression of recombinant vWF containing either F606I or I662F mutations resulted in mutant recombinant vWF with decreased ristocetin-induced platelet binding, but normal multimer structure, botrocetin-induced platelet binding, collagen binding, and binding to the conformation-sensitive monoclonal antibody, AvW-3.	Ristocetin	123-133	von Willebrand factor	Homo sapiens	104-107
9509487-0	1998	Relationship between haemoglobin, ristocetin-induced platelet aggregation and platelet surface glycoproteins GPIb and GPIIb/IIIa in haemodialysis patients under therapy with recombinant human erythropoietin.	Ristocetin	34-44	integrin subunit alpha 2b	Homo sapiens	118-123
9509487-0	1998	Relationship between haemoglobin, ristocetin-induced platelet aggregation and platelet surface glycoproteins GPIb and GPIIb/IIIa in haemodialysis patients under therapy with recombinant human erythropoietin.	Ristocetin	34-44	erythropoietin	Homo sapiens	192-206
9607124-2	1998	Coagulation studies showed a von Willebrand factor (vWF) defect (Duke bleeding time > 20 min; ristocetin cofactor activity [vWF:RC] < 6%; significant reduction of large multimers of vWF.	Ristocetin	97-107	von Willebrand factor	Homo sapiens	29-50
9607124-2	1998	Coagulation studies showed a von Willebrand factor (vWF) defect (Duke bleeding time > 20 min; ristocetin cofactor activity [vWF:RC] < 6%; significant reduction of large multimers of vWF.	Ristocetin	97-107	von Willebrand factor	Homo sapiens	52-55
9607124-5	1998	The inhibitor blocked the interaction of vWF with glycoprotein Ib in the presence of ristocetin, as did the pepsin-digested fragment of the inhibitor [F(ab)2"], but neither blocked botrocetin-mediated interaction of vWF with glycoprotein Ib.	Ristocetin	85-95	von Willebrand factor	Homo sapiens	41-44
9452127-0	1998	Ristocetin-mediated interaction of human von Willebrand factor with platelet glycoprotein lb evokes a transient calcium signal: observations with Fura-PE3.	Ristocetin	0-10	von Willebrand factor	Homo sapiens	41-62
9452127-3	1998	The present study examined the platelet (Ca2+)i signal that arises when ristocetin mediates vWf-GpIb binding.	Ristocetin	72-82	von Willebrand factor	Homo sapiens	92-95
9452127-10	1998	Ristocetin-mediated vWf-GpIb binding induced a transient increase in platelet (Ca2+)i.	Ristocetin	0-10	von Willebrand factor	Homo sapiens	20-23
9459348-3	1998	The first antagonist was the anti-human vWF monoclonal antibody AJvW-2, which inhibits the botrocetin and ristocetin induced aggregation of human blood platelets.	Ristocetin	106-116	von Willebrand factor	Homo sapiens	40-43
9459349-5	1998	Both the binding of mutated rvWFs to platelets and platelet aggregation induced by type 2B rvWFs are inhibited by monoclonal anti-GPIb and anti-vWF antibodies, inhibitors of vWF binding to platelets in the presence of ristocetin, as well as by aurin tricarboxylic acid.	Ristocetin	218-228	von Willebrand factor	Homo sapiens	29-32
9459349-5	1998	Both the binding of mutated rvWFs to platelets and platelet aggregation induced by type 2B rvWFs are inhibited by monoclonal anti-GPIb and anti-vWF antibodies, inhibitors of vWF binding to platelets in the presence of ristocetin, as well as by aurin tricarboxylic acid.	Ristocetin	218-228	von Willebrand factor	Homo sapiens	92-95
9298543-2	1997	A murine anti-human vWF monoclonal antibody, AJvW-2, was developed that inhibited the interaction between platelet glycoprotein Ib (GPIb) and von Willebrand factor (vWF) during the ristocetin- (IC50 = 0.7 +/- 0.1 microgram ml-1) and botrocetin- (IC50 = 1.8 +/- 0.3 microgram ml-1) induced aggregation of human platelets.	Ristocetin	181-191	von Willebrand factor	Homo sapiens	20-23
9298543-2	1997	A murine anti-human vWF monoclonal antibody, AJvW-2, was developed that inhibited the interaction between platelet glycoprotein Ib (GPIb) and von Willebrand factor (vWF) during the ristocetin- (IC50 = 0.7 +/- 0.1 microgram ml-1) and botrocetin- (IC50 = 1.8 +/- 0.3 microgram ml-1) induced aggregation of human platelets.	Ristocetin	181-191	von Willebrand factor	Homo sapiens	142-163
9298543-2	1997	A murine anti-human vWF monoclonal antibody, AJvW-2, was developed that inhibited the interaction between platelet glycoprotein Ib (GPIb) and von Willebrand factor (vWF) during the ristocetin- (IC50 = 0.7 +/- 0.1 microgram ml-1) and botrocetin- (IC50 = 1.8 +/- 0.3 microgram ml-1) induced aggregation of human platelets.	Ristocetin	181-191	von Willebrand factor	Homo sapiens	165-168
9308766-1	1997	Type 2B von Willebrand disease (vWD) is typically characterized by enhanced ristocetin-induced platelet aggregation (RIPA) caused by increased von Willebrand factor (vWF) affinity for platelets.	Ristocetin	76-86	von Willebrand factor	Homo sapiens	143-164
9308766-1	1997	Type 2B von Willebrand disease (vWD) is typically characterized by enhanced ristocetin-induced platelet aggregation (RIPA) caused by increased von Willebrand factor (vWF) affinity for platelets.	Ristocetin	76-86	von Willebrand factor	Homo sapiens	166-169
9268197-9	1997	Assignment of potency to vWF containing preparations utilizing the collagen binding activity may be more precise and as accurate as with the traditional ristocetin cofactor assay.	Ristocetin	153-163	von Willebrand factor	Homo sapiens	25-28
9198217-1	1997	During the past 10 years the quality of plasma derived virus inactivated products containing von Willebrand factor (vWF) has improved and the ratios of ristocetin cofactor activity (vWF:RCo) to von Willebrand factor antigen (vWF:Ag) have increased.	Ristocetin	152-162	von Willebrand factor	Homo sapiens	182-185
9226170-1	1997	Platelet-type von Willebrand disease (vWD) is a congenital bleeding disorder characterized by heightened ristocetin-induced platelet aggregation caused by abnormally high affinity between the platelet membrane glycoprotein (GP) Ib/IX complex and von Willebrand factor (vWF).	Ristocetin	105-115	von Willebrand factor	Homo sapiens	246-267
9226170-1	1997	Platelet-type von Willebrand disease (vWD) is a congenital bleeding disorder characterized by heightened ristocetin-induced platelet aggregation caused by abnormally high affinity between the platelet membrane glycoprotein (GP) Ib/IX complex and von Willebrand factor (vWF).	Ristocetin	105-115	von Willebrand factor	Homo sapiens	269-272
9226170-5	1997	The addition of low concentrations of ristocetin (0.2 mg/mL) induced specific 125I-vWF binding to immobilized M239V, but not to WT GPIb alpha.	Ristocetin	38-48	von Willebrand factor	Homo sapiens	83-86
9226170-6	1997	At high concentrations of ristocetin (1.2 mg/mL), both WT GPIb alpha and M239V specifically bound to 125I-vWF.	Ristocetin	26-36	glycoprotein Ib platelet subunit alpha	Homo sapiens	58-68
9226170-6	1997	At high concentrations of ristocetin (1.2 mg/mL), both WT GPIb alpha and M239V specifically bound to 125I-vWF.	Ristocetin	26-36	von Willebrand factor	Homo sapiens	106-109
9198217-1	1997	During the past 10 years the quality of plasma derived virus inactivated products containing von Willebrand factor (vWF) has improved and the ratios of ristocetin cofactor activity (vWF:RCo) to von Willebrand factor antigen (vWF:Ag) have increased.	Ristocetin	152-162	von Willebrand factor	Homo sapiens	182-185
9219327-4	1997	In vitro, soluble vWF is activated to bind to platelets by nonphysiological modulators, such as the bacterial glycopeptide, ristocetin, or the snake venom protein, botrocetin, or by removal of negatively-charged sialic acid residues.	Ristocetin	124-134	von Willebrand factor	Homo sapiens	18-21
9219327-8	1997	Purified soluble histone also bound vWF since, like ristocetin, it induced vWF flocculation.	Ristocetin	52-62	von Willebrand factor	Homo sapiens	36-39
9219327-8	1997	Purified soluble histone also bound vWF since, like ristocetin, it induced vWF flocculation.	Ristocetin	52-62	von Willebrand factor	Homo sapiens	75-78
9219327-11	1997	This implies that specific interactions of the vWF A1 domain with either ristocetin or botrocetin are required for GP Ib-IX-V recognition to occur.	Ristocetin	73-83	von Willebrand factor	Homo sapiens	47-50
9031470-7	1997	The functional analysis of vWF showed a markedly decreased affinity of mutated plasma vWF for platelet GPIb in the presence of ristocetin.	Ristocetin	127-137	von Willebrand factor	Homo sapiens	27-30
9134656-4	1997	The inhibitor inhibited the interaction of vWF in the presence of ristocetin and that of asialo-vWF with GPIb while it partially blocked botrocetin-mediated interaction of vWF to GPIb.	Ristocetin	66-76	von Willebrand factor	Homo sapiens	43-46
27214613-7	1997	Immunoelectron microscopy (IEM) revealed vWF arrangements on platelet surfaces which have been exposed to mixtures of the vWF-rich concentrate plus ristocetin.	Ristocetin	148-158	LOW QUALITY PROTEIN: von Willebrand factor	Oryctolagus cuniculus	41-44
9392827-0	1997	Synthetic peptide from the V3 loop consensus motif with a potent anti-HIV activity inhibits ristocetin-mediated vWF-GPIb interaction.	Ristocetin	92-102	von Willebrand factor	Homo sapiens	112-115
9392827-4	1997	These peptides interact with ristocetin-loaded platelet membrane glycoprotein (GP) Ib and act as inhibitors of von Willebrand factor (vWF)-GPIb interaction by preventing the subsequent formation of ristocetin dimer bridges.	Ristocetin	198-208	von Willebrand factor	Homo sapiens	111-132
9392827-4	1997	These peptides interact with ristocetin-loaded platelet membrane glycoprotein (GP) Ib and act as inhibitors of von Willebrand factor (vWF)-GPIb interaction by preventing the subsequent formation of ristocetin dimer bridges.	Ristocetin	198-208	von Willebrand factor	Homo sapiens	134-137
9031470-7	1997	The functional analysis of vWF showed a markedly decreased affinity of mutated plasma vWF for platelet GPIb in the presence of ristocetin.	Ristocetin	127-137	von Willebrand factor	Homo sapiens	86-89
8826903-3	1996	Each patient was infused with one dose of approximately 50 or 100 iu ristocetin cofactor activity (VWF:RiCoF) per kg body weight.	Ristocetin	69-79	von Willebrand factor	Homo sapiens	99-102
9017620-0	1996	Inverse relationships between haemoglobin and ristocetin-induced platelet aggregation in haemodialysis patients under erythropoietin therapy.	Ristocetin	46-56	erythropoietin	Homo sapiens	118-132
8950788-7	1996	Purified vWF bound to the surface of transfected cells in the presence of ristocetin and botrocetin with a Kd of 52 ng/ml, comparable to the Kd for fixed platelets (65.5 ng/ml).	Ristocetin	74-84	von Willebrand factor	Mesocricetus auratus	9-12
8873615-6	1996	In contrast, only mutants vWF-R524A and vWF-K549A showed significant binding to platelets in the presence of ristocetin.	Ristocetin	109-119	von Willebrand factor	Homo sapiens	26-29
8873615-6	1996	In contrast, only mutants vWF-R524A and vWF-K549A showed significant binding to platelets in the presence of ristocetin.	Ristocetin	109-119	von Willebrand factor	Homo sapiens	40-43
8873615-7	1996	Mutant vWF-K549A showed increased platelet-binding at suboptimal concentrations of both botrocetin and ristocetin.	Ristocetin	103-113	von Willebrand factor	Homo sapiens	7-10
8873615-9	1996	However, the charged amino acids at positions 534, 552, 569-573, and 642-645 do play an important role in the ristocetin-induced binding of vWF to platelets.	Ristocetin	110-120	von Willebrand factor	Homo sapiens	140-143
8839848-4	1996	The secreted mutant vWF showed a normal multimeric profile but did not bind to platelets in the presence of optimal concentrations of either ristocetin or botrocetin.	Ristocetin	141-151	von Willebrand factor	Homo sapiens	20-23
9490916-5	1997	Analysis of the mechanism according to which ristocetin induces vWF binding to GPIb revealed that 2 dimers of ristocetin simultaneously bind to vWF and GPIb, thus forming a quaternary complex in which repulsive negative charges are neutralized by the positively charged ristocetin.	Ristocetin	45-55	von Willebrand factor	Homo sapiens	64-67
9490916-5	1997	Analysis of the mechanism according to which ristocetin induces vWF binding to GPIb revealed that 2 dimers of ristocetin simultaneously bind to vWF and GPIb, thus forming a quaternary complex in which repulsive negative charges are neutralized by the positively charged ristocetin.	Ristocetin	45-55	von Willebrand factor	Homo sapiens	144-147
9490916-5	1997	Analysis of the mechanism according to which ristocetin induces vWF binding to GPIb revealed that 2 dimers of ristocetin simultaneously bind to vWF and GPIb, thus forming a quaternary complex in which repulsive negative charges are neutralized by the positively charged ristocetin.	Ristocetin	110-120	von Willebrand factor	Homo sapiens	64-67
9490916-5	1997	Analysis of the mechanism according to which ristocetin induces vWF binding to GPIb revealed that 2 dimers of ristocetin simultaneously bind to vWF and GPIb, thus forming a quaternary complex in which repulsive negative charges are neutralized by the positively charged ristocetin.	Ristocetin	110-120	von Willebrand factor	Homo sapiens	144-147
9490916-5	1997	Analysis of the mechanism according to which ristocetin induces vWF binding to GPIb revealed that 2 dimers of ristocetin simultaneously bind to vWF and GPIb, thus forming a quaternary complex in which repulsive negative charges are neutralized by the positively charged ristocetin.	Ristocetin	110-120	von Willebrand factor	Homo sapiens	64-67
9490916-5	1997	Analysis of the mechanism according to which ristocetin induces vWF binding to GPIb revealed that 2 dimers of ristocetin simultaneously bind to vWF and GPIb, thus forming a quaternary complex in which repulsive negative charges are neutralized by the positively charged ristocetin.	Ristocetin	110-120	von Willebrand factor	Homo sapiens	144-147
8701941-0	1996	Isolated recombinant domain of von Willebrand factor displaying increased sensitivity to ristocetin.	Ristocetin	89-99	von Willebrand factor	Homo sapiens	31-52
8701941-3	1996	In vitro, the soluble interaction of normal von Willebrand factor with platelets can be initiated with exogenous modulators, the most common being the antibiotic ristocetin.	Ristocetin	162-172	von Willebrand factor	Homo sapiens	44-65
8701941-6	1996	In this study we demonstrate that a recombinant plasmid capable of expressing the isolated GP Ib-IX binding domain of von Willebrand factor, and containing the Arg543-->Trp amino-acid substitution, secretes a dimeric molecule that supports platelet agglutination using subnormal levels of ristocetin.	Ristocetin	292-302	von Willebrand factor	Homo sapiens	118-139
8652394-10	1996	Therefore, when administering very high doses of FVIII concentrates devoid of VWF for prolonged periods of time, ristocetin cofactor and VWF levels should be monitored.	Ristocetin	113-123	coagulation factor VIII	Homo sapiens	49-54
8603015-0	1996	A monoclonal antibody directed against a granule membrane glycoprotein (GMP-140/PADGEM, P-selectin, CD62P) inhibits ristocetin-induced platelet aggregation.	Ristocetin	116-126	selectin P	Homo sapiens	72-79
8664285-12	1996	Four anti-GP Ibalpha monoclonal antibodies (SZ2, ES85, C34 and VM16d) were found to be modulator-specific, strongly inhibiting botrocetin-dependent binding of vWF, but having less or no effect on ristocetin-dependent vWF binding.	Ristocetin	196-206	glycoprotein Ib platelet subunit alpha	Homo sapiens	10-20
8660497-0	1996	Inhibition assay for the binding of biotinylated von Willebrand factor to platelet-bound microtiter wells in the presence of ristocetin or botrocetin.	Ristocetin	125-135	von Willebrand factor	Homo sapiens	49-70
8660497-3	1996	In the presence of an antibiotic ristocetin (1 mg/ml, final) or the snake venom botrocetin (2 micrograms/ml, final), biotinylated vWF bound to the affixed platelets with half-maximal binding occurring at a vWF concentration of approximately 2 micrograms/ml.	Ristocetin	33-43	von Willebrand factor	Homo sapiens	130-133
8645320-7	1996	Human vWF in the presence of ristocetin supported agglutination of transgenic mouse platelets, but not of control mouse platelets.	Ristocetin	29-39	von Willebrand factor	Homo sapiens	6-9
8603015-0	1996	A monoclonal antibody directed against a granule membrane glycoprotein (GMP-140/PADGEM, P-selectin, CD62P) inhibits ristocetin-induced platelet aggregation.	Ristocetin	116-126	selectin P	Homo sapiens	80-86
8603015-0	1996	A monoclonal antibody directed against a granule membrane glycoprotein (GMP-140/PADGEM, P-selectin, CD62P) inhibits ristocetin-induced platelet aggregation.	Ristocetin	116-126	selectin P	Homo sapiens	88-98
8603015-0	1996	A monoclonal antibody directed against a granule membrane glycoprotein (GMP-140/PADGEM, P-selectin, CD62P) inhibits ristocetin-induced platelet aggregation.	Ristocetin	116-126	selectin P	Homo sapiens	100-105
8822132-2	1996	By this mechanism, ATA inhibits shear-induced platelet aggregation as well as ristocetin-induced platelet aggregation/agglutination, both of which require interaction of platelets and vWf.	Ristocetin	78-88	LOW QUALITY PROTEIN: von Willebrand factor	Oryctolagus cuniculus	184-187
8548428-12	1996	Binding studies showed a nonsaturable ristocetin binding of VCL to platelets that was blocked by vWF or inhibitory antibodies against GPIb.	Ristocetin	38-48	vinculin	Homo sapiens	60-63
8548428-12	1996	Binding studies showed a nonsaturable ristocetin binding of VCL to platelets that was blocked by vWF or inhibitory antibodies against GPIb.	Ristocetin	38-48	von Willebrand factor	Homo sapiens	97-100
9075574-5	1996	Ristocetin-mediated binding of vWF to human platelets promoted a slow rise in Fura-2 fluorescence ratio.	Ristocetin	0-10	von Willebrand factor	Homo sapiens	31-34
7539426-7	1995	Substitutions at Glu-626 and in the segment Asp-520-Lys-534 abolished ristocetin-induced binding of VWF to GPIb but did not affect botrocetin-induced binding, suggesting that these regions are required for modulation by ristocetin but not for binding of VWF to GPIb.	Ristocetin	70-80	von Willebrand factor	Homo sapiens	100-103
9112649-4	1996	In the whole blood ristocetin-induced platelet aggregation was significantly diminished following incubation with ET-1 for 5 min, whereas AA-induced platelet aggregation was not significantly changed following preincubation with ET-1.	Ristocetin	19-29	endothelin 1	Homo sapiens	114-118
8713802-13	1996	In the in vitro and ex vivo studies, ristocetin-induced platelet aggregation confirmed that ATA interacts with the vWF-GPIb axis, and suggests that the final common pathway of the aggregation induced by other agents tested consists of fibrinogen binding to the platelet GPIIb/IIIa receptor.	Ristocetin	37-47	von Willebrand factor	Cavia porcellus	115-118
8747526-2	1996	This fragment, VCL, has previously been shown to inhibit vWf-ristocetin, asialo-vWf, and botrocetin-induced vWf binding and aggregation of platelets.	Ristocetin	61-71	vinculin	Homo sapiens	15-18
8747526-2	1996	This fragment, VCL, has previously been shown to inhibit vWf-ristocetin, asialo-vWf, and botrocetin-induced vWf binding and aggregation of platelets.	Ristocetin	61-71	von Willebrand factor	Homo sapiens	57-60
7578899-6	1995	The binding of vWF to GPIb mediated by ristocetin and by botrocetin was inhibited by the patient"s IgG with an IC50s of 0.3 mg/ml and 0.48 mg/ml, respectively.	Ristocetin	39-49	von Willebrand factor	Homo sapiens	15-18
8555986-2	1995	The biological activity of vWF was measured by the ristocetin cofactor assay and its multimeric structure was assessed by Western immunoblotting after SDS-agarose gel electrophoresis.	Ristocetin	51-61	von Willebrand factor	Homo sapiens	27-30
8585016-4	1995	The purified venom protein completely inhibited ristocetin- or botrocetin-induced von Willebrand factor (vWF) binding, and blocked the bovine vWF binding to GPIb, with IC50 values ranging from 28 to 42 nM, without affecting the platelet aggregation induced by ADP or alpha-thrombin.	Ristocetin	48-58	von Willebrand factor	Bos taurus	105-108
21043592-5	1996	Without stirring, preincubation of GFP with plasmin leads to inhibition of platelet aggregation induced by subsequent platelet stimuli (thrombin, collagen, ristocetin or U46619).	Ristocetin	156-166	plasminogen	Homo sapiens	44-51
8572428-3	1995	Direct shear-induced binding to washed platelets (300-360 x 10(3)/microliters) of radiolabeled vWF was maximum at 60-120 dynes/cm2 evaluated at 30 sec and was in extent about one-quarter of the binding stimulated by ristocetin after 3 min of incubation.	Ristocetin	216-226	von Willebrand factor	Homo sapiens	95-98
7559492-3	1995	To validate the methods and reagents used, binding of the same labeled vWF was assessed in the presence of ristocetin or alpha-thrombin and found to be saturable, with a narrow and symmetric distribution on > 90% of the platelets.	Ristocetin	107-117	von Willebrand factor	Homo sapiens	71-74
7559492-4	1995	As expected, essentially all bound ligand interacted exclusively with platelet membrane glycoprotein (GP) Ib alpha in the presence of ristocetin and with GP IIb-IIIa after stimulation with alpha-thrombin.	Ristocetin	134-144	glycoprotein Ib platelet subunit alpha	Homo sapiens	102-114
7577651-3	1995	Thus, when the PMN in PMN/platelet mixtures were stimulated by FMLP, platelets lost GPIb as measured by ristocetin-induced aggregation, flow cytometry and SDS-PAGE analysis.	Ristocetin	104-114	formyl peptide receptor 1	Homo sapiens	63-67
7578895-5	1995	Arabs and Africans had higher levels of FVIII:C and vWF:ristocetin cofactor than Westerners.	Ristocetin	56-66	von Willebrand factor	Homo sapiens	52-55
7539426-7	1995	Substitutions at Glu-626 and in the segment Asp-520-Lys-534 abolished ristocetin-induced binding of VWF to GPIb but did not affect botrocetin-induced binding, suggesting that these regions are required for modulation by ristocetin but not for binding of VWF to GPIb.	Ristocetin	70-80	von Willebrand factor	Homo sapiens	254-257
7539426-7	1995	Substitutions at Glu-626 and in the segment Asp-520-Lys-534 abolished ristocetin-induced binding of VWF to GPIb but did not affect botrocetin-induced binding, suggesting that these regions are required for modulation by ristocetin but not for binding of VWF to GPIb.	Ristocetin	220-230	von Willebrand factor	Homo sapiens	100-103
7720238-0	1995	Four agglutination assays evaluated for measurement of von Willebrand factor (ristocetin cofactor activity) The concentration of von Willebrand factor (vWf) in patients" plasma can be determined by measuring the ristocetin cofactor activity (vWf R:Co).	Ristocetin	78-88	von Willebrand factor	Homo sapiens	129-150
7639074-6	1995	Plasma vWF activity measured as ristocetin cofactor (vWF:RCo) was similar in intercrisis and crisis (100.6 +/- 31 U/dl vs 94.5 +/- 44 U/dl).	Ristocetin	32-42	von Willebrand factor	Homo sapiens	7-10
7639074-6	1995	Plasma vWF activity measured as ristocetin cofactor (vWF:RCo) was similar in intercrisis and crisis (100.6 +/- 31 U/dl vs 94.5 +/- 44 U/dl).	Ristocetin	32-42	von Willebrand factor	Homo sapiens	53-56
7537105-1	1995	The interaction between von Willebrand factor (vWF) and glycoprotein Ib (GPIb) induced by ristocetin or botrocetin resulted in associated platelet aggregation, protein tyrosine phosphorylation (PTP) of a 64 kDa protein, as detected by a monoclonal antibody against phosphotyrosine (PY-20), and intracellular Ca2+ elevation that is largely dependent upon Ca2+ influx in human platelets.	Ristocetin	90-100	von Willebrand factor	Homo sapiens	24-45
7537105-1	1995	The interaction between von Willebrand factor (vWF) and glycoprotein Ib (GPIb) induced by ristocetin or botrocetin resulted in associated platelet aggregation, protein tyrosine phosphorylation (PTP) of a 64 kDa protein, as detected by a monoclonal antibody against phosphotyrosine (PY-20), and intracellular Ca2+ elevation that is largely dependent upon Ca2+ influx in human platelets.	Ristocetin	90-100	von Willebrand factor	Homo sapiens	47-50
7537105-1	1995	The interaction between von Willebrand factor (vWF) and glycoprotein Ib (GPIb) induced by ristocetin or botrocetin resulted in associated platelet aggregation, protein tyrosine phosphorylation (PTP) of a 64 kDa protein, as detected by a monoclonal antibody against phosphotyrosine (PY-20), and intracellular Ca2+ elevation that is largely dependent upon Ca2+ influx in human platelets.	Ristocetin	90-100	protein tyrosine phosphatase receptor type U	Homo sapiens	194-197
7720238-0	1995	Four agglutination assays evaluated for measurement of von Willebrand factor (ristocetin cofactor activity) The concentration of von Willebrand factor (vWf) in patients" plasma can be determined by measuring the ristocetin cofactor activity (vWf R:Co).	Ristocetin	78-88	von Willebrand factor	Homo sapiens	152-155
7495067-6	1995	This mutation which has already been found in several unrelated families with 2B vWD and the increased binding of the patient platelet vWF on normal platelets in the presence of low ristocetin concentrations provide evidence for subtype 2B vWD.	Ristocetin	182-192	von Willebrand factor	Homo sapiens	135-138
7495080-0	1995	Ristocetin-induced platelet agglutination stimulates GPIIb/IIIa-dependent calcium influx.	Ristocetin	0-10	integrin subunit alpha 2b	Homo sapiens	53-58
7887899-0	1995	Promotion of binding of von Willebrand factor to platelet glycoprotein Ib by dimers of ristocetin.	Ristocetin	87-97	von Willebrand factor	Homo sapiens	24-45
7887899-1	1995	In the absence of high shear forces, the in vitro binding of human von Willebrand factor (vWF) to its platelet receptor glycoprotein Ib (GPIb) can be promoted by two well-characterized mediators, botrocetin and ristocetin.	Ristocetin	211-221	von Willebrand factor	Homo sapiens	67-88
7887899-1	1995	In the absence of high shear forces, the in vitro binding of human von Willebrand factor (vWF) to its platelet receptor glycoprotein Ib (GPIb) can be promoted by two well-characterized mediators, botrocetin and ristocetin.	Ristocetin	211-221	von Willebrand factor	Homo sapiens	90-93
7887899-2	1995	Using purified vWF and GPIb, we have investigated the mechanisms by which ristocetin mediates this binding.	Ristocetin	74-84	von Willebrand factor	Homo sapiens	15-18
7887899-5	1995	With increasing ristocetin concentrations, vWF binding depended progressively less on the involvement of its A1 loop, which is compatible with a model in which the two ristocetin dimers bridge the vWF-GPIb complex on secondary sites.	Ristocetin	16-26	von Willebrand factor	Homo sapiens	43-46
7887899-5	1995	With increasing ristocetin concentrations, vWF binding depended progressively less on the involvement of its A1 loop, which is compatible with a model in which the two ristocetin dimers bridge the vWF-GPIb complex on secondary sites.	Ristocetin	168-178	von Willebrand factor	Homo sapiens	43-46
7887899-5	1995	With increasing ristocetin concentrations, vWF binding depended progressively less on the involvement of its A1 loop, which is compatible with a model in which the two ristocetin dimers bridge the vWF-GPIb complex on secondary sites.	Ristocetin	168-178	von Willebrand factor	Homo sapiens	197-200
7887899-6	1995	In agreement with this model, the ristocetin-dimer-promoted stabilization of vWF on GPIb was abolished by low concentrations of poly(Pro-Gly-Pro), which is known to complex ristocetin dimers.	Ristocetin	34-44	von Willebrand factor	Homo sapiens	77-80
7887899-6	1995	In agreement with this model, the ristocetin-dimer-promoted stabilization of vWF on GPIb was abolished by low concentrations of poly(Pro-Gly-Pro), which is known to complex ristocetin dimers.	Ristocetin	173-183	von Willebrand factor	Homo sapiens	77-80
7887899-7	1995	Mechanistic analysis of the inhibition of vWF binding by the recombinant vWF fragment Leu504-Ser728 (VCL), which covers the entire A1 loop, revealed an affinity of VCL for GPIb comparable with that of the botrocetin-vWF complex for GPIb, and identified a specific but 20-fold lower affinity of VCL in the presence of ristocetin.	Ristocetin	317-327	von Willebrand factor	Homo sapiens	42-45
7887899-7	1995	Mechanistic analysis of the inhibition of vWF binding by the recombinant vWF fragment Leu504-Ser728 (VCL), which covers the entire A1 loop, revealed an affinity of VCL for GPIb comparable with that of the botrocetin-vWF complex for GPIb, and identified a specific but 20-fold lower affinity of VCL in the presence of ristocetin.	Ristocetin	317-327	von Willebrand factor	Homo sapiens	73-76
7887899-7	1995	Mechanistic analysis of the inhibition of vWF binding by the recombinant vWF fragment Leu504-Ser728 (VCL), which covers the entire A1 loop, revealed an affinity of VCL for GPIb comparable with that of the botrocetin-vWF complex for GPIb, and identified a specific but 20-fold lower affinity of VCL in the presence of ristocetin.	Ristocetin	317-327	vinculin	Homo sapiens	101-104
7887899-7	1995	Mechanistic analysis of the inhibition of vWF binding by the recombinant vWF fragment Leu504-Ser728 (VCL), which covers the entire A1 loop, revealed an affinity of VCL for GPIb comparable with that of the botrocetin-vWF complex for GPIb, and identified a specific but 20-fold lower affinity of VCL in the presence of ristocetin.	Ristocetin	317-327	von Willebrand factor	Homo sapiens	73-76
7887899-8	1995	The proline-rich peptides flanking the vWF A1 loop, Cys474-Val489 and Leu694-Asp709, inhibited vWF binding semispecifically by competitively interfering with the formation of the GPIb-vWF complex rather than by complexation of free ristocetin dimers.	Ristocetin	232-242	von Willebrand factor	Homo sapiens	39-42
7887899-8	1995	The proline-rich peptides flanking the vWF A1 loop, Cys474-Val489 and Leu694-Asp709, inhibited vWF binding semispecifically by competitively interfering with the formation of the GPIb-vWF complex rather than by complexation of free ristocetin dimers.	Ristocetin	232-242	von Willebrand factor	Homo sapiens	95-98
7887899-8	1995	The proline-rich peptides flanking the vWF A1 loop, Cys474-Val489 and Leu694-Asp709, inhibited vWF binding semispecifically by competitively interfering with the formation of the GPIb-vWF complex rather than by complexation of free ristocetin dimers.	Ristocetin	232-242	von Willebrand factor	Homo sapiens	95-98
7887899-9	1995	In conclusion, ristocetin-promoted binding of vWF to its GPIb receptor results from charge neutralization and interactions involving proline residues in the vicinity of the natural interaction sites present on both GPIb and the A1 domain of vWF.	Ristocetin	15-25	von Willebrand factor	Homo sapiens	46-49
7887899-9	1995	In conclusion, ristocetin-promoted binding of vWF to its GPIb receptor results from charge neutralization and interactions involving proline residues in the vicinity of the natural interaction sites present on both GPIb and the A1 domain of vWF.	Ristocetin	15-25	von Willebrand factor	Homo sapiens	241-244
7792749-2	1995	The inhibitory effect of this peptide, named VCL, was tested in vitro on ristocetin- and botrocetin-induced platelet aggregation and compared to the ADP-induced platelet aggregation.	Ristocetin	73-83	vinculin	Cavia porcellus	45-48
7792749-3	1995	In vivo, the antithrombotic effect of VCL was tested in a model of laser-injured mesentery small arteries and correlated to the ex vivo ristocetin-induced platelet aggregation.	Ristocetin	136-146	vinculin	Cavia porcellus	38-41
7792749-5	1995	In vitro, VCL totally abolished ristocetin- and botrocetin-induced platelet aggregation, but had no effect on ADP-induced platelet aggregation.	Ristocetin	32-42	vinculin	Cavia porcellus	10-13
21043709-9	1995	Thirdly, many of the compounds tested that inhibited binding of vWF to heparin also effectively inhibited both ristocetin- and botrocetin-dependent binding of vWF to the GP Ib-IX complex on platelets, whereas none of the compounds tested blocked vWF binding to sulfatides and GP Ib-IX but not heparin.	Ristocetin	111-121	von Willebrand factor	Homo sapiens	64-67
21043709-4	1995	Binding of vWF to the GP Ib-IX complex involves the vWF A1 internal repeat domain, which also contains distinct binding sites for sulfatides, heparin, and the non-physiological modulators of the vWF-GP Ib-IX interaction, ristocetin and botrocetin.	Ristocetin	221-231	von Willebrand factor	Homo sapiens	11-14
21043709-9	1995	Thirdly, many of the compounds tested that inhibited binding of vWF to heparin also effectively inhibited both ristocetin- and botrocetin-dependent binding of vWF to the GP Ib-IX complex on platelets, whereas none of the compounds tested blocked vWF binding to sulfatides and GP Ib-IX but not heparin.	Ristocetin	111-121	von Willebrand factor	Homo sapiens	159-162
21043709-4	1995	Binding of vWF to the GP Ib-IX complex involves the vWF A1 internal repeat domain, which also contains distinct binding sites for sulfatides, heparin, and the non-physiological modulators of the vWF-GP Ib-IX interaction, ristocetin and botrocetin.	Ristocetin	221-231	von Willebrand factor	Homo sapiens	52-55
21043709-9	1995	Thirdly, many of the compounds tested that inhibited binding of vWF to heparin also effectively inhibited both ristocetin- and botrocetin-dependent binding of vWF to the GP Ib-IX complex on platelets, whereas none of the compounds tested blocked vWF binding to sulfatides and GP Ib-IX but not heparin.	Ristocetin	111-121	von Willebrand factor	Homo sapiens	159-162
21043709-4	1995	Binding of vWF to the GP Ib-IX complex involves the vWF A1 internal repeat domain, which also contains distinct binding sites for sulfatides, heparin, and the non-physiological modulators of the vWF-GP Ib-IX interaction, ristocetin and botrocetin.	Ristocetin	221-231	von Willebrand factor	Homo sapiens	52-55
21043709-10	1995	The majority of compounds tested inhibited the vWF-platelet interaction to a comparable degree in the presence of ristocetin or botrocetin, suggesting a similar mechanism for inhibition irrespective of the modulator used.	Ristocetin	114-124	von Willebrand factor	Homo sapiens	47-50
7949092-2	1994	Coagulation studies showed a von Willebrand factor (vWF) defect (Ivy bleeding time, > 15 minutes; vWF antigen [vWF:Ag], 0.08 U/mL; ristocetin cofactor activity [vWF:RCoF], < 0.05 U/mL; collagen binding activity [vWF:CBA], 0.01 U/mL; absence of the high molecular weight multimers of vWF on multimeric analysis).	Ristocetin	134-144	von Willebrand factor	Homo sapiens	52-55
7947801-9	1994	Nevertheless, inhibiting sulfation of GP Ib alpha reduced the binding of 125I-labeled vWf in the presence of ristocetin by up to 37%.	Ristocetin	109-119	von Willebrand factor	Cricetulus griseus	86-89
7900092-7	1994	Ristocetin stimulation of the patients" platelets in the presence of plasma resulted in a low binding of vWF, about 30% of healthy controls.	Ristocetin	0-10	von Willebrand factor	Homo sapiens	105-108
7871492-3	1994	The ristocetin-induced agglutination was inhibited in a TMS concentration-dependent manner, which suggests that TMS may interact with the vWF receptor on platelets.	Ristocetin	4-14	von Willebrand factor	Homo sapiens	138-141
7997978-1	1994	The quantitative determinations of von Willebrand Factor (vWF)-Ristocetin cofactor (vWF:RCof) and the Botrocetin cofactor (vWF:BCof) are important parameters for the diagnosis of von Willebrand"s disease.	Ristocetin	63-73	von Willebrand factor	Homo sapiens	58-61
7532923-4	1994	Furthermore, incubation of PRP with a recombinant fragment of von Willebrand factor (vWF) that abolishes ristocetin-induced platelet agglutination significantly inhibited but did not eliminate SIPA.	Ristocetin	105-115	complement component 4 binding protein alpha	Homo sapiens	27-30
7532923-4	1994	Furthermore, incubation of PRP with a recombinant fragment of von Willebrand factor (vWF) that abolishes ristocetin-induced platelet agglutination significantly inhibited but did not eliminate SIPA.	Ristocetin	105-115	von Willebrand factor	Homo sapiens	62-83
7532923-4	1994	Furthermore, incubation of PRP with a recombinant fragment of von Willebrand factor (vWF) that abolishes ristocetin-induced platelet agglutination significantly inhibited but did not eliminate SIPA.	Ristocetin	105-115	von Willebrand factor	Homo sapiens	85-88
7803236-5	1994	The only way to cause GPIb/IX to move was to add anti-vWF to thrombin-activated platelets allowed to spread on formvar grids and covered with multimers of ristocetin-activated human or bovine vWF.	Ristocetin	155-165	von Willebrand factor	Homo sapiens	54-57
7803236-5	1994	The only way to cause GPIb/IX to move was to add anti-vWF to thrombin-activated platelets allowed to spread on formvar grids and covered with multimers of ristocetin-activated human or bovine vWF.	Ristocetin	155-165	coagulation factor II, thrombin	Homo sapiens	61-69
7803236-5	1994	The only way to cause GPIb/IX to move was to add anti-vWF to thrombin-activated platelets allowed to spread on formvar grids and covered with multimers of ristocetin-activated human or bovine vWF.	Ristocetin	155-165	von Willebrand factor	Bos taurus	192-195
7819071-5	1994	In concentration dependent binding to botrocetin- or ristocetin-stimulated platelets, 125I-plasma vWf bound with a higher affinity than platelet.	Ristocetin	53-63	von Willebrand factor	Homo sapiens	98-101
7819071-6	1994	The ristocetin cofactor activity per mg of purified plasma vWf was 5-fold greater than the platelet vWf activity.	Ristocetin	4-14	von Willebrand factor	Homo sapiens	59-62
7777905-9	1994	Defective aggregation to ristocetin would indicate abnormal von Willebrand"s factor (vWF).	Ristocetin	25-35	von Willebrand factor	Homo sapiens	60-83
7777905-9	1994	Defective aggregation to ristocetin would indicate abnormal von Willebrand"s factor (vWF).	Ristocetin	25-35	von Willebrand factor	Homo sapiens	85-88
7997978-1	1994	The quantitative determinations of von Willebrand Factor (vWF)-Ristocetin cofactor (vWF:RCof) and the Botrocetin cofactor (vWF:BCof) are important parameters for the diagnosis of von Willebrand"s disease.	Ristocetin	63-73	von Willebrand factor	Homo sapiens	84-87
7997978-1	1994	The quantitative determinations of von Willebrand Factor (vWF)-Ristocetin cofactor (vWF:RCof) and the Botrocetin cofactor (vWF:BCof) are important parameters for the diagnosis of von Willebrand"s disease.	Ristocetin	63-73	von Willebrand factor	Homo sapiens	84-87
7517206-2	1994	Cathepsin G resulted in a concentration- and time-dependent decrease in the platelet surface GPIb-IX complex, as determined by flow cytometry, binding of exogenous von Willebrand factor (vWF) in the presence of ristocetin, and ristocetin-induced platelet agglutination.	Ristocetin	211-221	cathepsin G	Homo sapiens	0-11
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).	Ristocetin	132-142	integrin subunit alpha 2b	Homo sapiens	56-61
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).	Ristocetin	132-142	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).	Ristocetin	132-142	von Willebrand factor	Homo sapiens	104-107
7993797-3	1994	Out of 30 monoclonal antibodies reacting with GPIIb/IIIa, one, MA-16N7C2, potently inhibited platelet aggregation induced by ADP, thrombin, arachidonic acid, collagen, U46619, adrenaline and platelet-activating factor, whereas ristocetin-induced aggregation was unaffected.	Ristocetin	227-237	integrin subunit alpha 2b	Homo sapiens	46-51
7517206-2	1994	Cathepsin G resulted in a concentration- and time-dependent decrease in the platelet surface GPIb-IX complex, as determined by flow cytometry, binding of exogenous von Willebrand factor (vWF) in the presence of ristocetin, and ristocetin-induced platelet agglutination.	Ristocetin	227-237	cathepsin G	Homo sapiens	0-11
8141116-2	1994	After 5 days of storage, 82 +/- 9% of basal levels of ristocetin cofactor activity (vWF:RCo) remained in PCs.	Ristocetin	54-64	von Willebrand factor	Homo sapiens	84-87
8204881-3	1994	Functions of vWF were analyzed by binding assays to platelets in the presence of ristocetin or botrocetin.	Ristocetin	81-91	von Willebrand factor	Homo sapiens	13-16
8204881-5	1994	We found that ristocetin- or botrocetin-induced binding to platelets was correlated in all cases with the size of vWF multimers.	Ristocetin	14-24	von Willebrand factor	Homo sapiens	114-117
8120035-8	1994	Furthermore, recombinant vWF with Gly or Ala at all three positions induces platelet aggregation in the presence of ristocetin and binds to platelet glycoprotein Ib, factor VIII, and collagen in a manner similar to wild-type recombinant vWF.	Ristocetin	116-126	von Willebrand factor	Homo sapiens	25-28
8250006-3	1994	Interestingly, we found a significant decrease of immunoreactive GP Ib molecules (9,978 +/- 1,534 vs. 17,064 +/- 404 molecules per platelet) and ristocetin-dependent binding of vWF (9,113 +/- 1,338 vs. 13,992 +/- 1,968 molecules per platelet) (P < 0.01) in comparison to the levels found in a control group of healthy subjects.	Ristocetin	145-155	von Willebrand factor	Homo sapiens	177-180
8250006-5	1994	The ristocetin-induced platelet agglutination (light transmission %) was also significantly lower in patients with cirrhosis (48 +/- 7.6 vs. 92 +/- 3.6, P < 0.01), and correlated with the binding of normal vWF (r = 0.863, P = 0.0013).	Ristocetin	4-14	von Willebrand factor	Homo sapiens	209-212
8229521-3	1993	METHODS: Von Willebrand factor (vWF) was measured by the ristocetin cofactor method in 600 healthy children, aged 2 to 18 years, seen for routine school physical examinations in a three-state region.	Ristocetin	57-67	von Willebrand factor	Homo sapiens	9-30
7511534-5	1993	Here, we demonstrate that neutralization of plasmin by its inhibitors, aprotinin or tripeptide Val-Phe-Lys-CH2Cl, permits a time dependent recovery (within 30 min) of ristocetin-induced agglutination in the platelets which were stimulated by plasmin at < 1 CU ml-1.	Ristocetin	167-177	plasminogen	Homo sapiens	44-51
7511534-5	1993	Here, we demonstrate that neutralization of plasmin by its inhibitors, aprotinin or tripeptide Val-Phe-Lys-CH2Cl, permits a time dependent recovery (within 30 min) of ristocetin-induced agglutination in the platelets which were stimulated by plasmin at < 1 CU ml-1.	Ristocetin	167-177	plasminogen	Homo sapiens	242-249
8229521-3	1993	METHODS: Von Willebrand factor (vWF) was measured by the ristocetin cofactor method in 600 healthy children, aged 2 to 18 years, seen for routine school physical examinations in a three-state region.	Ristocetin	57-67	von Willebrand factor	Homo sapiens	32-35
7691402-7	1993	MG-63 and HOS cells induced biphasic platelet aggregation both before and after deamino-D-arginine vasopressin treatment, while the ristocetin-dependent binding of von Willebrand factor to platelets only occurred after deamino-D-arginine vasopressin treatment.	Ristocetin	132-142	arginine vasopressin	Homo sapiens	238-249
8246533-8	1993	Tissue-type plasminogen activator and fibrin monomers (tissue-type plasminogen activator stimulator) together induced severe platelet damage, resulting in a decreased ristocetin agglutination response.	Ristocetin	167-177	plasminogen activator, tissue type	Homo sapiens	0-33
8246533-8	1993	Tissue-type plasminogen activator and fibrin monomers (tissue-type plasminogen activator stimulator) together induced severe platelet damage, resulting in a decreased ristocetin agglutination response.	Ristocetin	167-177	plasminogen activator, tissue type	Homo sapiens	55-88
8376405-7	1993	Relative to wild type vWF, the mutant vWF exhibited markedly increased binding to platelets at low concentrations of ristocetin, confirming the association between the His-505-->Asp substitution and the type IIB vWD phenotype.	Ristocetin	117-127	von Willebrand factor	Homo sapiens	38-41
8251378-4	1993	Moreover, we show that when adding thrombin inhibitors to the platelets preincubated with < 0.04 U/ml thrombin for 5 min, their agglutinability by ristocetin was gradually recovered within 30 min, indicating that in these conditions the decrease in platelet adhesiveness is reversible.	Ristocetin	150-160	coagulation factor II, thrombin	Homo sapiens	35-43
8251378-4	1993	Moreover, we show that when adding thrombin inhibitors to the platelets preincubated with < 0.04 U/ml thrombin for 5 min, their agglutinability by ristocetin was gradually recovered within 30 min, indicating that in these conditions the decrease in platelet adhesiveness is reversible.	Ristocetin	150-160	coagulation factor II, thrombin	Homo sapiens	105-113
8376606-7	1993	Here we report that vWF-dependent aggregation occurs under low shear stress in citrated platelet-rich plasma (PRP) from two types of congenital bleeding disorders, platelet-type von Willebrand disease (vWD) and type IIB vWD, in both of which ristocetin-induced aggregation is known to be heightened.	Ristocetin	242-252	von Willebrand factor	Homo sapiens	20-23
8376606-7	1993	Here we report that vWF-dependent aggregation occurs under low shear stress in citrated platelet-rich plasma (PRP) from two types of congenital bleeding disorders, platelet-type von Willebrand disease (vWD) and type IIB vWD, in both of which ristocetin-induced aggregation is known to be heightened.	Ristocetin	242-252	complement component 4 binding protein alpha	Homo sapiens	110-113
8463345-4	1993	In contrast, the receptor function of GP Ib exhibited restricted species specificity, since only the chimeric complex containing human GP Ib alpha bound human von Willebrand factor and supported platelet aggregation mediated by ristocetin.	Ristocetin	228-238	glycoprotein Ib platelet subunit alpha	Homo sapiens	135-146
7686594-3	1993	In vitro research confirmed that the addition of urokinase (40 U/ml) to platelet-rich plasma and the addition of plasmin (0.3 U/ml) to washed platelets made ristocetin-induced agglutination decline to 31.6% and 38.5% of control values, respectively.	Ristocetin	157-167	plasminogen	Homo sapiens	113-120
8367835-3	1993	GPIb function, as evaluated by measuring vWF-dependent, ristocetin-induced platelet agglutination in human platelet rich plasma (PRP) was significantly impaired following incubation with plasmin (60 +/- 14% inhibition, p < 0.01).	Ristocetin	56-66	von Willebrand factor	Homo sapiens	41-44
8367835-3	1993	GPIb function, as evaluated by measuring vWF-dependent, ristocetin-induced platelet agglutination in human platelet rich plasma (PRP) was significantly impaired following incubation with plasmin (60 +/- 14% inhibition, p < 0.01).	Ristocetin	56-66	plasminogen	Homo sapiens	187-194
8438875-2	1993	Individuals with type I von Willebrand"s disease (vWd) with prolonged bleeding times are best discriminated from those who have normal bleeding times by the normal level of platelet vWf ristocetin cofactor activity (vWf activity) and, to a lesser extent, by their platelet vWf antigen content.	Ristocetin	186-196	von Willebrand factor	Homo sapiens	182-185
8483792-1	1993	We synthesized peptides of the general formula Argn, Lysn, and (Lys-Arg)n. These agents inhibited the ristocetin-mediated binding of vWF to GPIb and the binding of asialo-vWF to platelets.	Ristocetin	102-112	von Willebrand factor	Homo sapiens	133-136
8483792-1	1993	We synthesized peptides of the general formula Argn, Lysn, and (Lys-Arg)n. These agents inhibited the ristocetin-mediated binding of vWF to GPIb and the binding of asialo-vWF to platelets.	Ristocetin	102-112	von Willebrand factor	Homo sapiens	171-174
8400294-8	1993	Moreover, platelet incubation with cathepsin G resulted in the loss of ristocetin-induced agglutination in the presence of the von Willebrand factor and in the appearance of Gp Ib-derived proteolytic products in supernatants.	Ristocetin	71-81	cathepsin G	Homo sapiens	35-46
8423224-1	1993	We developed a monoclonal antibody, 1C1E7, against vWf that increases ristocetin-induced platelet aggregation in a dose-dependent manner and lowers the threshold concentration of ristocetin needed to obtain a full aggregatory response.	Ristocetin	70-80	von Willebrand factor	Homo sapiens	51-54
8457648-4	1993	Type I vWd was diagnosed because of a concomitant decrease of von Willebrand factor antigen (vWf:Ag) and vWf ristocetin-cofactor activity (vWf:RCoF), associated with the presence of vWf multimers of all sizes in plasma and platelets.	Ristocetin	109-119	von Willebrand factor	Homo sapiens	105-108
8457648-4	1993	Type I vWd was diagnosed because of a concomitant decrease of von Willebrand factor antigen (vWf:Ag) and vWf ristocetin-cofactor activity (vWf:RCoF), associated with the presence of vWf multimers of all sizes in plasma and platelets.	Ristocetin	109-119	von Willebrand factor	Homo sapiens	105-108
8457648-4	1993	Type I vWd was diagnosed because of a concomitant decrease of von Willebrand factor antigen (vWf:Ag) and vWf ristocetin-cofactor activity (vWf:RCoF), associated with the presence of vWf multimers of all sizes in plasma and platelets.	Ristocetin	109-119	von Willebrand factor	Homo sapiens	105-108
8456433-0	1993	A role for von Willebrand factor proline residues 702-704 in ristocetin-mediated binding to platelet glycoprotein Ib.	Ristocetin	61-71	von Willebrand factor	Cricetulus griseus	11-32
8456433-6	1993	The results demonstrate that vWF proline702-704 are important for the ristocetin-mediated interaction between vWF and GP Ib, but are not essential residues of the GP Ib binding site within vWF.	Ristocetin	70-80	von Willebrand factor	Cricetulus griseus	29-32
8456433-6	1993	The results demonstrate that vWF proline702-704 are important for the ristocetin-mediated interaction between vWF and GP Ib, but are not essential residues of the GP Ib binding site within vWF.	Ristocetin	70-80	von Willebrand factor	Cricetulus griseus	110-113
8456433-6	1993	The results demonstrate that vWF proline702-704 are important for the ristocetin-mediated interaction between vWF and GP Ib, but are not essential residues of the GP Ib binding site within vWF.	Ristocetin	70-80	von Willebrand factor	Cricetulus griseus	110-113
8426951-1	1993	We report two cases of von Willebrand (type I) disease with vWF antigen levels of 21 and 25%, vWF ristocetin cofactor concentrations of 32 and 30%, and coagulation FVIII levels of 10 and 50% respectively.	Ristocetin	98-108	von Willebrand factor	Homo sapiens	94-97
8423224-1	1993	We developed a monoclonal antibody, 1C1E7, against vWf that increases ristocetin-induced platelet aggregation in a dose-dependent manner and lowers the threshold concentration of ristocetin needed to obtain a full aggregatory response.	Ristocetin	179-189	von Willebrand factor	Homo sapiens	51-54
8423224-3	1993	In the presence of ristocetin, both intact 1C1E7 and its Fab fragments enhance specific binding of 125I-vWf to platelets.	Ristocetin	19-29	FA complementation group B	Homo sapiens	57-60
8423224-3	1993	In the presence of ristocetin, both intact 1C1E7 and its Fab fragments enhance specific binding of 125I-vWf to platelets.	Ristocetin	19-29	von Willebrand factor	Homo sapiens	104-107
21043845-4	1993	Binding assays and flow cytometry with antibodies against GPs Ib/IX and IIb/IIIa, the study of the ristocetin-dependent vWF binding, and immunoblotting with an anti-GPIb/IX antibody, demonstrated no quantitative or functional changes of these complexes after the infusion of DDAVP.	Ristocetin	99-109	von Willebrand factor	Homo sapiens	120-123
21043859-7	1993	Contact with collagen fibrils causing adhesion to this matrix, or aggregate formation induced by ristocetin or by certain lectins also caused an increase in [cyclic-3",5"-GMP].	Ristocetin	97-107	5'-nucleotidase, cytosolic II	Homo sapiens	171-174
1287886-5	1992	ATA completely abolished vWF-dependent platelet agglutination induced by ristocetin, botrocetin and asialo-vWF, respectively.	Ristocetin	73-83	von Willebrand factor	Homo sapiens	25-28
1287886-6	1992	125I-vWF binding to ristocetin- and botrocetin-treated platelets, to heparin and to sulfatides as well as 125I-botrocetin binding to vWF was competitively inhibited by ATA.	Ristocetin	20-30	von Willebrand factor	Homo sapiens	5-8
1469086-0	1992	O-linked carbohydrate of recombinant von Willebrand factor influences ristocetin-induced binding to platelet glycoprotein 1b.	Ristocetin	70-80	von Willebrand factor	Homo sapiens	37-58
1469086-7	1992	These data indicate a possible role for O-linked carbohydrates in the vWf-glycoprotein 1b interaction promoted by ristocetin and suggest that abnormalities in carbohydrate modification might contribute to the altered ristocetin-dependent reactivity between vWf and platelets described for some variant forms of von Willebrand disease.	Ristocetin	114-124	von Willebrand factor	Homo sapiens	70-73
1280375-5	1992	Among several anti-vWF monoclonal antibodies (MoAbs) which inhibit ristocetin-induced platelet aggregation and/or vWF binding to GP Ib, only two MoAbs (NMC-4 and RFF-VIII RAG:1) abolished direct binding between purified botrocetin and vWF.	Ristocetin	67-77	von Willebrand factor	Homo sapiens	19-22
1359905-1	1992	Mechanism of modulation of von Willebrand factor by ristocetin and botrocetin.	Ristocetin	52-62	von Willebrand factor	Bos taurus	27-48
1359905-8	1992	This peptide inhibited both the ristocetin- and botrocetin-mediated binding of vWF to either platelets or purified GP Ib-IX complex (IC50 approximately 50-200 microM) as well as the asialo-vWF- and bovine vWF-dependent agglutination of platelets.	Ristocetin	32-42	von Willebrand factor	Bos taurus	79-82
1409710-0	1992	von Willebrand disease type B: a missense mutation selectively abolishes ristocetin-induced von Willebrand factor binding to platelet glycoprotein Ib.	Ristocetin	73-83	von Willebrand factor	Homo sapiens	92-113
1409710-2	1992	For human vWF, this interaction can be induced in vitro by the antibiotic ristocetin or the snake venom protein botrocetin.	Ristocetin	74-84	von Willebrand factor	Homo sapiens	10-13
1409710-3	1992	A missense mutation, Gly-561-->Ser, was identified within the proposed glycoprotein Ib binding domain of vWF in the proband with von Willebrand disease type B, a unique variant characterized by no ristocetin-induced, but normal botrocetin-induced, binding to glycoprotein Ib.	Ristocetin	200-210	von Willebrand factor	Homo sapiens	108-111
1518808-4	1992	This recombinant fragment, named VCL, inhibits ristocetin-induced, botrocetin-induced, and asialo-von Willebrand factor-induced platelet aggregation and binding to platelets at an IC50 = 0.011-0.260 microM, significantly lower than the IC50 of peptide 153 or 154, IC50 = 86-700 microM.	Ristocetin	47-57	vinculin	Homo sapiens	33-36
1409710-5	1992	These data show that botrocetin and ristocetin cofactor activities of vWF can be dissociated by a point mutation and confirm that these mediators promote vWF binding to platelets by different mechanisms.	Ristocetin	36-46	von Willebrand factor	Homo sapiens	70-73
1409710-6	1992	The normal botrocetin-induced binding and the defective ristocetin-induced binding of rvWF(G561S) suggest that the primary defect in von Willebrand disease type B may be a failure of normal allosteric regulation of the glycoprotein Ib binding function of vWF.	Ristocetin	56-66	von Willebrand factor	Homo sapiens	87-90
1295515-1	1992	Ristocetin induces a conformational change on von Willebrand Factor (vWF) similar to that due to the interaction with the subendothelium, by which the former can interact with the Glycoprotein-1 B (GPIB) of the platelet membrane and trigger aggregation and granule content secretion.	Ristocetin	0-10	von Willebrand factor	Homo sapiens	46-67
1295515-1	1992	Ristocetin induces a conformational change on von Willebrand Factor (vWF) similar to that due to the interaction with the subendothelium, by which the former can interact with the Glycoprotein-1 B (GPIB) of the platelet membrane and trigger aggregation and granule content secretion.	Ristocetin	0-10	von Willebrand factor	Homo sapiens	69-72
1609773-4	1992	In the presence of ristocetin, binding of the patient"s plasma vWF to normal platelets was increased but binding of normal vWF to his platelets was normal.	Ristocetin	19-29	von Willebrand factor	Homo sapiens	63-66
1412167-4	1992	Soluble rGpIb alpha L318 harvested from COS cell-conditioned medium inhibited ristocetin-dependent binding of [125I]-vWF to fixed washed human platelets (IC50 20 nM).	Ristocetin	78-88	von Willebrand factor	Homo sapiens	117-120
1420815-5	1992	After cryoprecipitation the supernatant, which contained predominantly low-molecular-weight vWF multimers, was effective with ristocetin only after prior incubation of the platelets with dibucaine.	Ristocetin	126-136	von Willebrand factor	Homo sapiens	92-95
1420815-6	1992	This indicates that low-molecular-weight vWF multimers can also support ristocetin-induced aggregation when the membrane fluidity is increased.	Ristocetin	72-82	von Willebrand factor	Homo sapiens	41-44
1562727-4	1992	When unstirred platelet-rich plasma was incubated with ristocetin, bound vWF was located by Au-EM as discrete masses regularly distributed over the cell surface.	Ristocetin	55-65	von Willebrand factor	Homo sapiens	73-76
1643023-6	1992	In all cases, fetal vWF was able to interact with factor VIII and to bind to GP Ib platelet receptor in the presence of ristocetin and to types I and III collagen.	Ristocetin	120-130	von Willebrand factor	Homo sapiens	20-23
1513036-4	1992	All synthetic peptides inhibited both vWf binding to GPIb, ristocetin-induced platelet aggregation and asialo vWf-induced platelet aggregation.	Ristocetin	59-69	von Willebrand factor	Homo sapiens	38-41
1562727-8	1992	Under these conditions, platelets were treated with ristocetin for 5 minutes at 37 degrees C in the presence of increasing amounts of purified vWF.	Ristocetin	52-62	von Willebrand factor	Homo sapiens	143-146
1737795-4	1992	High molecular weight RADS-vWF and RGES-vWF multimers inhibited binding of 125I-vWF to a mixture of insolubilized native type I and III collagen and competed effectively with 125I-vWF for binding to formalin-fixed platelets in the presence of ristocetin, indicating functional collagen and platelet glycoprotein Ib binding.	Ristocetin	243-253	von Willebrand factor	Homo sapiens	27-30
1557393-4	1992	vWF from a human umbilical vein endothelial cell culture heterozygous for the vWF R543W mutation showed markedly increased binding of large vWF multimers to platelets in the presence of a low dose of ristocetin compared to vWF from a normal control culture.	Ristocetin	200-210	von Willebrand factor	Homo sapiens	0-3
1557393-4	1992	vWF from a human umbilical vein endothelial cell culture heterozygous for the vWF R543W mutation showed markedly increased binding of large vWF multimers to platelets in the presence of a low dose of ristocetin compared to vWF from a normal control culture.	Ristocetin	200-210	von Willebrand factor	Homo sapiens	78-81
1557393-4	1992	vWF from a human umbilical vein endothelial cell culture heterozygous for the vWF R543W mutation showed markedly increased binding of large vWF multimers to platelets in the presence of a low dose of ristocetin compared to vWF from a normal control culture.	Ristocetin	200-210	von Willebrand factor	Homo sapiens	78-81
1557393-4	1992	vWF from a human umbilical vein endothelial cell culture heterozygous for the vWF R543W mutation showed markedly increased binding of large vWF multimers to platelets in the presence of a low dose of ristocetin compared to vWF from a normal control culture.	Ristocetin	200-210	von Willebrand factor	Homo sapiens	78-81
1737795-4	1992	High molecular weight RADS-vWF and RGES-vWF multimers inhibited binding of 125I-vWF to a mixture of insolubilized native type I and III collagen and competed effectively with 125I-vWF for binding to formalin-fixed platelets in the presence of ristocetin, indicating functional collagen and platelet glycoprotein Ib binding.	Ristocetin	243-253	von Willebrand factor	Homo sapiens	40-43
1737795-4	1992	High molecular weight RADS-vWF and RGES-vWF multimers inhibited binding of 125I-vWF to a mixture of insolubilized native type I and III collagen and competed effectively with 125I-vWF for binding to formalin-fixed platelets in the presence of ristocetin, indicating functional collagen and platelet glycoprotein Ib binding.	Ristocetin	243-253	von Willebrand factor	Homo sapiens	40-43
1737795-4	1992	High molecular weight RADS-vWF and RGES-vWF multimers inhibited binding of 125I-vWF to a mixture of insolubilized native type I and III collagen and competed effectively with 125I-vWF for binding to formalin-fixed platelets in the presence of ristocetin, indicating functional collagen and platelet glycoprotein Ib binding.	Ristocetin	243-253	von Willebrand factor	Homo sapiens	40-43
1579897-1	1992	Von Willebrand"s disease (vWD) "Vicenza" is characterized by low plasma von Willebrand Factor antigen (vWF:Ag) and very low levels of Ristocetin Cofactor activity (RiCof).	Ristocetin	134-144	von Willebrand factor	Homo sapiens	26-29
1730088-6	1992	The kd for 125I-vWF binding to patients platelets was significantly increased over control values at 0.5 mg/mL ristocetin, but was normal at 1.0 or 1.5 mg/mL ristocetin.	Ristocetin	111-121	von Willebrand factor	Homo sapiens	16-19
1730088-6	1992	The kd for 125I-vWF binding to patients platelets was significantly increased over control values at 0.5 mg/mL ristocetin, but was normal at 1.0 or 1.5 mg/mL ristocetin.	Ristocetin	158-168	von Willebrand factor	Homo sapiens	16-19
1585777-2	1992	The profile of plasma von Willebrand factor (vWF) revealed decreased ristocetin cofactor activity and diminished large multimers of vWF in spite of a normal vWF antigen level.	Ristocetin	69-79	von Willebrand factor	Homo sapiens	22-43
1585777-2	1992	The profile of plasma von Willebrand factor (vWF) revealed decreased ristocetin cofactor activity and diminished large multimers of vWF in spite of a normal vWF antigen level.	Ristocetin	69-79	von Willebrand factor	Homo sapiens	45-48
1530813-3	1992	The ristocetin cofactor (RiCof) activity of vWF, high before therapy, tended to decrease soon after therapy.	Ristocetin	4-14	von Willebrand factor	Homo sapiens	44-47
1651333-3	1991	After insolubilization on nitrocellulose membrane, the recombinant GP Ib alpha fragment bound soluble vWF in the presence of ristocetin or botrocetin with a dissociation constant similar to that exhibited by GP Ib.IX complex on platelets.	Ristocetin	125-135	glycoprotein Ib platelet subunit alpha	Homo sapiens	67-78
1733754-3	1992	A decrease in factor VIII:C was noted in 33%, a decrease in von Willebrand factor (vWF:Ag) was noted in 83% and a decrease in ristocetin-cofactor activity (vWF:Rcof) was noted in 66% of the children.	Ristocetin	126-136	von Willebrand factor	Homo sapiens	156-159
1724577-4	1991	A marked reduction in the placebo group of ristocetin-induced platelet agglutination (binding of von Willebrand factor [vWF] to platelet glycoprotein [GP] Ib) was shown during ECC and at the end of surgery, but not in the aprotinin group.	Ristocetin	43-53	von Willebrand factor	Homo sapiens	97-118
1724577-4	1991	A marked reduction in the placebo group of ristocetin-induced platelet agglutination (binding of von Willebrand factor [vWF] to platelet glycoprotein [GP] Ib) was shown during ECC and at the end of surgery, but not in the aprotinin group.	Ristocetin	43-53	von Willebrand factor	Homo sapiens	120-123
1939217-5	1991	The mutant vWF molecules were also assayed for their function in ristocetin-induced platelet agglutination mediated through the platelet receptor GPIb.	Ristocetin	65-75	von Willebrand factor	Homo sapiens	11-14
1932745-2	1991	Solutions of commercial aurintricarboxylic acid (ATA) inhibit ristocetin- or shear stress-induced, von Willebrand factor (vWF)-mediated platelet aggregation by interacting with vWF and blocking its attachment to platelet membrane glycoprotein Ib.	Ristocetin	62-72	von Willebrand factor	Canis lupus familiaris	99-120
1932745-2	1991	Solutions of commercial aurintricarboxylic acid (ATA) inhibit ristocetin- or shear stress-induced, von Willebrand factor (vWF)-mediated platelet aggregation by interacting with vWF and blocking its attachment to platelet membrane glycoprotein Ib.	Ristocetin	62-72	von Willebrand factor	Canis lupus familiaris	122-125
1932745-5	1991	ATA polymers larger than Mr 700 inhibited ristocetin-induced, vWF-mediated platelet aggregation more effectively than smaller ATA polymers, whereas shear-induced, vWF-mediated platelet aggregation was optimally inhibited by ATA polymers of Mr greater than or equal to 2,500.	Ristocetin	42-52	von Willebrand factor	Canis lupus familiaris	62-65
1932745-7	1991	Polyanionic, polysulfonated aromatic polymers (polystyrene sulfonate) of Mr 35, 17.4, 8, and 4.6 x 10(3) inhibited ristocetin- and shear-induced, vWF-mediated aggregation with less potency on a mass/volume basis than large polymers of ATA.	Ristocetin	115-125	von Willebrand factor	Canis lupus familiaris	146-149
1932745-8	1991	We conclude that a polyanionic, polycarboxylated, polyphenolic ATA polymer of Mr 2,500 is optimally potent as an inhibitor of shear- and ristocetin-induced, vWF-mediated platelet aggregation and is likely to be more effective than solutions of commercial ATA as an anti-arterial thrombotic agent.	Ristocetin	137-147	von Willebrand factor	Canis lupus familiaris	157-160
1939645-4	1991	PA production, PKC activation, and the rise of [Ca2+]i stimulated by the ristocetin-induced binding of vWF multimers to platelets are inhibited by an anti-GpIb monoclonal antibody, but are unaffected by anti-GpIIb-IIIa monoclonal antibodies.	Ristocetin	73-83	von Willebrand factor	Homo sapiens	103-106
1939645-4	1991	PA production, PKC activation, and the rise of [Ca2+]i stimulated by the ristocetin-induced binding of vWF multimers to platelets are inhibited by an anti-GpIb monoclonal antibody, but are unaffected by anti-GpIIb-IIIa monoclonal antibodies.	Ristocetin	73-83	integrin subunit alpha 2b	Homo sapiens	208-213
2011604-6	1991	In contrast, mammalian cell expression of the same segment of sequence yielded molecules that, when containing the normal Trp550, did not bind to GP Ib directly but, like native vWF, bound in the presence of ristocetin.	Ristocetin	208-218	von Willebrand factor	Homo sapiens	178-181
1768767-4	1991	RIPA was completely inhibited by an anti-glycoprotein (GP) Ib monoclonal antibody that recognizes the ristocetin-induced vWf binding site.	Ristocetin	102-112	von Willebrand factor	Homo sapiens	121-124
1906179-3	1991	The corresponding mutant recombinant vWF(T28M) formed normal multimers and had normal ristocetin cofactor activity.	Ristocetin	86-96	von Willebrand factor	Homo sapiens	37-40
2022745-4	1991	Heparin also inhibited platelet agglutination induced by bovine vWF and inhibited the binding of human asialo-vWF to platelets in ristocetin-free systems.	Ristocetin	130-140	von Willebrand factor	Homo sapiens	110-113
1870263-5	1991	In vitro, an antibiotic ristocetin or the snake venom botrocetin isolated from Bothrops jararaca mimics the active component of subendothelial matrix and causes the binding of vWF to GP Ib.	Ristocetin	24-34	von Willebrand factor	Homo sapiens	176-179
2011604-7	1991	However, molecules containing the point mutation (Cys550) behaved like type IIB vWF--namely, bound to GP Ib even without ristocetin modulation and, in the presence of ristocetin, had 10-fold higher affinity than molecules with normal sequence.	Ristocetin	121-131	von Willebrand factor	Homo sapiens	80-83
2011604-7	1991	However, molecules containing the point mutation (Cys550) behaved like type IIB vWF--namely, bound to GP Ib even without ristocetin modulation and, in the presence of ristocetin, had 10-fold higher affinity than molecules with normal sequence.	Ristocetin	167-177	von Willebrand factor	Homo sapiens	80-83
1825180-3	1991	Previous studies demonstrated that plasmin can induce platelet stimulation and also decrease ristocetin-induced platelet aggregation; it was suggested that this was because of GPIb degradation by plasmin.	Ristocetin	93-103	plasminogen	Homo sapiens	35-42
1825180-3	1991	Previous studies demonstrated that plasmin can induce platelet stimulation and also decrease ristocetin-induced platelet aggregation; it was suggested that this was because of GPIb degradation by plasmin.	Ristocetin	93-103	plasminogen	Homo sapiens	196-203
1772996-11	1991	In contrast, a MAb against ristocetin-induced vWf binding site on GPIb did not affect SPA.	Ristocetin	27-37	von Willebrand factor	Homo sapiens	46-49
1984791-0	1991	Studies on anti-von Willebrand factor (vWF) monoclonal antibody NMC-4, which inhibits both ristocetin- and botrocetin-induced vWF binding to platelet glycoprotein Ib.	Ristocetin	91-101	von Willebrand factor	Homo sapiens	11-37
1984791-0	1991	Studies on anti-von Willebrand factor (vWF) monoclonal antibody NMC-4, which inhibits both ristocetin- and botrocetin-induced vWF binding to platelet glycoprotein Ib.	Ristocetin	91-101	von Willebrand factor	Homo sapiens	39-42
1984791-1	1991	Anti-von Willebrand factor (vWF) monoclonal antibody NMC-4 completely inhibited vWF binding to platelet glycoprotein (GP) lb induced by either ristocetin or botrocetin at an IgG concentration of approximately 10 micrograms/mL, and also blocked binding of asialo-vWF to GP lb.	Ristocetin	143-153	von Willebrand factor	Homo sapiens	0-26
1984791-1	1991	Anti-von Willebrand factor (vWF) monoclonal antibody NMC-4 completely inhibited vWF binding to platelet glycoprotein (GP) lb induced by either ristocetin or botrocetin at an IgG concentration of approximately 10 micrograms/mL, and also blocked binding of asialo-vWF to GP lb.	Ristocetin	143-153	von Willebrand factor	Homo sapiens	28-31
1984791-1	1991	Anti-von Willebrand factor (vWF) monoclonal antibody NMC-4 completely inhibited vWF binding to platelet glycoprotein (GP) lb induced by either ristocetin or botrocetin at an IgG concentration of approximately 10 micrograms/mL, and also blocked binding of asialo-vWF to GP lb.	Ristocetin	143-153	von Willebrand factor	Homo sapiens	80-83
1984791-1	1991	Anti-von Willebrand factor (vWF) monoclonal antibody NMC-4 completely inhibited vWF binding to platelet glycoprotein (GP) lb induced by either ristocetin or botrocetin at an IgG concentration of approximately 10 micrograms/mL, and also blocked binding of asialo-vWF to GP lb.	Ristocetin	143-153	von Willebrand factor	Homo sapiens	80-83
1984791-6	1991	Fr III-T2 completely inhibited ristocetin-induced vWF binding at a concentration of 100 mumol/L but had no effect on botrocetin-induced binding.	Ristocetin	31-41	von Willebrand factor	Homo sapiens	50-53
1823880-2	1991	Both OP-F1 and a well-characterized anti-GPIb MoAb, AP-1, totally abolished ristocetin-induced von Willebrand factor (vWF) binding to platelets and desialylated vWF binding to platelets at an IgG concentration of 2-8 micrograms/ml.	Ristocetin	76-86	von Willebrand factor	Homo sapiens	118-121
1949703-2	1991	The functional activity of vWF assessed by its ristocetin cofactor activity (vWF:RCo) correlated with the level of vWF antigen (vWF:Ag), with the vWF:RCo/vWF:Ag ratios ranging from 0.56 to 1.02, and the specific activity being always greater than 50 IU vWF:RCo/mg protein.	Ristocetin	47-57	von Willebrand factor	Homo sapiens	27-30
1949703-2	1991	The functional activity of vWF assessed by its ristocetin cofactor activity (vWF:RCo) correlated with the level of vWF antigen (vWF:Ag), with the vWF:RCo/vWF:Ag ratios ranging from 0.56 to 1.02, and the specific activity being always greater than 50 IU vWF:RCo/mg protein.	Ristocetin	47-57	von Willebrand factor	Homo sapiens	77-80
1949703-2	1991	The functional activity of vWF assessed by its ristocetin cofactor activity (vWF:RCo) correlated with the level of vWF antigen (vWF:Ag), with the vWF:RCo/vWF:Ag ratios ranging from 0.56 to 1.02, and the specific activity being always greater than 50 IU vWF:RCo/mg protein.	Ristocetin	47-57	von Willebrand factor	Homo sapiens	77-80
1949703-2	1991	The functional activity of vWF assessed by its ristocetin cofactor activity (vWF:RCo) correlated with the level of vWF antigen (vWF:Ag), with the vWF:RCo/vWF:Ag ratios ranging from 0.56 to 1.02, and the specific activity being always greater than 50 IU vWF:RCo/mg protein.	Ristocetin	47-57	von Willebrand factor	Homo sapiens	77-80
1949703-2	1991	The functional activity of vWF assessed by its ristocetin cofactor activity (vWF:RCo) correlated with the level of vWF antigen (vWF:Ag), with the vWF:RCo/vWF:Ag ratios ranging from 0.56 to 1.02, and the specific activity being always greater than 50 IU vWF:RCo/mg protein.	Ristocetin	47-57	von Willebrand factor	Homo sapiens	77-80
1949703-2	1991	The functional activity of vWF assessed by its ristocetin cofactor activity (vWF:RCo) correlated with the level of vWF antigen (vWF:Ag), with the vWF:RCo/vWF:Ag ratios ranging from 0.56 to 1.02, and the specific activity being always greater than 50 IU vWF:RCo/mg protein.	Ristocetin	47-57	von Willebrand factor	Homo sapiens	77-80
1949703-2	1991	The functional activity of vWF assessed by its ristocetin cofactor activity (vWF:RCo) correlated with the level of vWF antigen (vWF:Ag), with the vWF:RCo/vWF:Ag ratios ranging from 0.56 to 1.02, and the specific activity being always greater than 50 IU vWF:RCo/mg protein.	Ristocetin	47-57	von Willebrand factor	Homo sapiens	77-80
1949703-4	1991	The biological activity of vWF was also evaluated by studying its ability to bind to collagen and to platelet receptors in the presence of either ristocetin or thrombin.	Ristocetin	146-156	von Willebrand factor	Homo sapiens	27-30
2245394-5	1990	Levels of von Willebrand factor (vWF), both antigenic and functional (ristocetin cofactor), were elevated.	Ristocetin	70-80	von Willebrand factor	Homo sapiens	10-31
2245394-5	1990	Levels of von Willebrand factor (vWF), both antigenic and functional (ristocetin cofactor), were elevated.	Ristocetin	70-80	von Willebrand factor	Homo sapiens	33-36
2401846-4	1990	Equal amounts of vWf were eluted from ristocetin/vWf-treated platelets when they were resuspended without ristocetin, whether or not the platelets had been exposed to ADP, and the vWf recovered in either case was composed only of large multimers.	Ristocetin	38-48	von Willebrand factor	Homo sapiens	17-20
2246822-5	1990	In vitro, the patient"s plasma exhibited inhibitory activity against vWF: ristocetin cofactor activity (vWF: Rco) but had no effect on RIPA.	Ristocetin	74-84	von Willebrand factor	Homo sapiens	69-72
2246822-5	1990	In vitro, the patient"s plasma exhibited inhibitory activity against vWF: ristocetin cofactor activity (vWF: Rco) but had no effect on RIPA.	Ristocetin	74-84	von Willebrand factor	Homo sapiens	104-107
2214316-3	1990	Ristocetin-induced vWF:Ag binding to platelets by using 125I-vWF was significantly increased.	Ristocetin	0-10	von Willebrand factor	Homo sapiens	19-22
2214316-3	1990	Ristocetin-induced vWF:Ag binding to platelets by using 125I-vWF was significantly increased.	Ristocetin	0-10	von Willebrand factor	Homo sapiens	61-64
2214174-6	1990	The analysis of plasma von Willebrand factor (vWF) revealed the decrease of ristocetin cofactor activity and the lack of large multimeric components of vWF.	Ristocetin	76-86	von Willebrand factor	Homo sapiens	23-44
2214174-6	1990	The analysis of plasma von Willebrand factor (vWF) revealed the decrease of ristocetin cofactor activity and the lack of large multimeric components of vWF.	Ristocetin	76-86	von Willebrand factor	Homo sapiens	46-49
1702906-0	1990	Ristocetin and botrocetin involve two distinct domains of von Willebrand factor for binding to platelet membrane glycoprotein Ib.	Ristocetin	0-10	von Willebrand factor	Homo sapiens	58-79
1702906-1	1990	We have evidence that ristocetin and botrocetin mediate binding of von Willebrand Factor (vWF) to platelet glycoprotein Ib (GPIb) through two distinct domains on the vWF molecule.	Ristocetin	22-32	von Willebrand factor	Homo sapiens	67-88
1702906-1	1990	We have evidence that ristocetin and botrocetin mediate binding of von Willebrand Factor (vWF) to platelet glycoprotein Ib (GPIb) through two distinct domains on the vWF molecule.	Ristocetin	22-32	von Willebrand factor	Homo sapiens	90-93
1702906-1	1990	We have evidence that ristocetin and botrocetin mediate binding of von Willebrand Factor (vWF) to platelet glycoprotein Ib (GPIb) through two distinct domains on the vWF molecule.	Ristocetin	22-32	von Willebrand factor	Homo sapiens	166-169
1702906-5	1990	Both MAbs inhibit 125I-vWF binding to platelet membrane GPIb and vWF-dependent platelet agglutination induced by ristocetin.	Ristocetin	113-123	von Willebrand factor	Homo sapiens	23-26
1702906-5	1990	Both MAbs inhibit 125I-vWF binding to platelet membrane GPIb and vWF-dependent platelet agglutination induced by ristocetin.	Ristocetin	113-123	von Willebrand factor	Homo sapiens	65-68
1702906-7	1990	The involvement of two distinct domains of vWF for binding to GPIb in the presence of ristocetin or botrocetin was confirmed in experiments of binding of 125I-vWF to platelets using a competitor synthetic peptides corresponding to the GPIb binding domain of vWF (Cys 474 to Pro 488 and Ser 692 to Pro 708).	Ristocetin	86-96	von Willebrand factor	Homo sapiens	43-46
1702906-8	1990	At a final concentration of 2.5 mM both peptides inhibit more than 90% of the binding of vWF to ristocetin-treated platelets but are unable to modify this binding in the presence of botrocetin.	Ristocetin	96-106	von Willebrand factor	Homo sapiens	89-92
1702906-9	1990	In conclusion our data suggest that botrocetin and ristocetin involve distinct sites on vWF for binding to GPIb.	Ristocetin	51-61	von Willebrand factor	Homo sapiens	88-91
2401564-14	1990	YopM-containing supernatant proteins of Y. pestis inhibited thrombin- or ristocetin-induced platelet aggregation, whereas there was no inhibition by supernatant proteins from the YopM- Y. pestis mutant.	Ristocetin	73-83	outer membrane protein YopM	Yersinia pestis	0-4
2394830-8	1990	Thus, IIB vWF binds to GP Ib-IX with high affinity and induces platelet aggregation, whether with or without ristocetin, in spite of the absence of larger multimers.	Ristocetin	109-119	von Willebrand factor	Homo sapiens	10-13
2375928-6	1990	Aggregation induced by patient plasma could also be blocked either by two monoclonal antibodies raised against vWF or by a fragment derived from trypsin digestion of normal vWF which blocks the ristocetin-induced binding of normal vWF to platelets.	Ristocetin	194-204	von Willebrand factor	Homo sapiens	173-176
2375928-6	1990	Aggregation induced by patient plasma could also be blocked either by two monoclonal antibodies raised against vWF or by a fragment derived from trypsin digestion of normal vWF which blocks the ristocetin-induced binding of normal vWF to platelets.	Ristocetin	194-204	von Willebrand factor	Homo sapiens	173-176
2339348-1	1990	Platelet membrane glycoprotein Ib (GPIb) functions as receptors for thrombin and von Willebrand factor (vWF) in the presence of ristocetin.	Ristocetin	128-138	coagulation factor II, thrombin	Homo sapiens	68-102
2316510-1	1990	Botrocetin, a protein isolated from the venom of the snake Bothrops jararaca, induces platelet aggregation/agglutination by von Willebrand factor (vWF) binding to the membrane glycoprotein (GP) Ib, an action resembling that of ristocetin.	Ristocetin	227-237	von Willebrand factor	Homo sapiens	147-150
2196663-3	1990	The first is based on the interaction between vWf and Gp Ib of the platelet membrane in presence of ristocetin (ristocetin cofactor activity, RiCof) and depends not only on the amount of the factor but also on its ability to bring about this interaction, large multimers being more active.	Ristocetin	100-110	von Willebrand factor	Homo sapiens	46-49
2196663-3	1990	The first is based on the interaction between vWf and Gp Ib of the platelet membrane in presence of ristocetin (ristocetin cofactor activity, RiCof) and depends not only on the amount of the factor but also on its ability to bring about this interaction, large multimers being more active.	Ristocetin	112-122	von Willebrand factor	Homo sapiens	46-49
2339348-1	1990	Platelet membrane glycoprotein Ib (GPIb) functions as receptors for thrombin and von Willebrand factor (vWF) in the presence of ristocetin.	Ristocetin	128-138	von Willebrand factor	Homo sapiens	104-107
2339348-2	1990	To precisely locate the domains on GPIb interacting with vWF and thrombin, we prepared several peptides that have amino acid sequences analogous to that of the GPIb alpha-chain and examined their effects on ristocetin-induced (vWF-dependent) and thrombin-induced platelet aggregations.	Ristocetin	207-217	von Willebrand factor	Homo sapiens	227-230
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.	Ristocetin	106-116	von Willebrand factor	Homo sapiens	83-86
2300925-1	1990	The ability of von Willebrand factor protein (vWF) to agglutinate platelets with ristocetin depends upon the presence of its highest molecular weight multimers (HMWM) and its intact carbohydrate structure.	Ristocetin	81-91	von Willebrand factor	Homo sapiens	15-36
2104618-3	1990	Initial studies suggested that the modality of vWF interaction with GP Ib depended on the conditions used for induction of binding, either in the presence of ristocetin, or botrocetin, or with asialo-vWF.	Ristocetin	158-168	von Willebrand factor	Homo sapiens	47-50
2104618-7	1990	This led to the identification of a linear GP Ib alpha sequence (residues Ser251-Tyr279) that effectively inhibited platelet interaction with vWF mediated by ristocetin and, at higher concentration, also by botrocetin.	Ristocetin	158-168	glycoprotein Ib platelet subunit alpha	Homo sapiens	43-54
2104618-7	1990	This led to the identification of a linear GP Ib alpha sequence (residues Ser251-Tyr279) that effectively inhibited platelet interaction with vWF mediated by ristocetin and, at higher concentration, also by botrocetin.	Ristocetin	158-168	von Willebrand factor	Homo sapiens	142-145
2300925-1	1990	The ability of von Willebrand factor protein (vWF) to agglutinate platelets with ristocetin depends upon the presence of its highest molecular weight multimers (HMWM) and its intact carbohydrate structure.	Ristocetin	81-91	von Willebrand factor	Homo sapiens	46-49
33663351-8	2021	We detected elevated VWF antigen and decreased VWF ristocetin cofactor activity.	Ristocetin	51-61	von Willebrand factor	Homo sapiens	47-50
2242824-4	1990	The amount of ristocetin-induced normal vWF binding to nephrotic washed platelets, when ristocetin was used at concentrations of 0.5, 0.75, and 1.0 mg/ml, was 152-163% above the binding to normal platelets.	Ristocetin	14-24	von Willebrand factor	Homo sapiens	40-43
2242824-4	1990	The amount of ristocetin-induced normal vWF binding to nephrotic washed platelets, when ristocetin was used at concentrations of 0.5, 0.75, and 1.0 mg/ml, was 152-163% above the binding to normal platelets.	Ristocetin	88-98	von Willebrand factor	Homo sapiens	40-43
2242824-7	1990	These results appear to indicate that the plasma vWF level and the altered surface-negative charge in platelets both contribute to heightened vWF binding to GPIb, thus lowering the ristocetin concentration required for RIPA in SRNS.	Ristocetin	181-191	von Willebrand factor	Homo sapiens	49-52
2242824-7	1990	These results appear to indicate that the plasma vWF level and the altered surface-negative charge in platelets both contribute to heightened vWF binding to GPIb, thus lowering the ristocetin concentration required for RIPA in SRNS.	Ristocetin	181-191	von Willebrand factor	Homo sapiens	142-145
34741678-13	2021	Levels of VWF: Ag, VWF: activity, VWF: ristocetin, and factor VIII are increased in patients with COVID-19.	Ristocetin	39-49	von Willebrand factor	Homo sapiens	34-37
34619770-6	2022	CHO cells expressing p.Arg127Gln GPIbalpha showed increased binding of VWF induced by ristocetin and enhanced tethering on immobilized VWF as compared with cells expressing wild-type (WT) GPIbalpha.	Ristocetin	86-96	glycoprotein Ib platelet subunit alpha	Homo sapiens	33-42
34619770-6	2022	CHO cells expressing p.Arg127Gln GPIbalpha showed increased binding of VWF induced by ristocetin and enhanced tethering on immobilized VWF as compared with cells expressing wild-type (WT) GPIbalpha.	Ristocetin	86-96	von Willebrand factor	Cricetulus griseus	71-74
34089550-1	2021	BACKGROUND: Antibodies inhibiting von Willebrand factor (VWF) develop in a subset of patients with type 3 von Willebrand disease (VWD3) and may be detected by their inhibition of ristocetin cofactor activity (VWF:RCo).	Ristocetin	179-189	von Willebrand factor	Homo sapiens	34-55
34089550-1	2021	BACKGROUND: Antibodies inhibiting von Willebrand factor (VWF) develop in a subset of patients with type 3 von Willebrand disease (VWD3) and may be detected by their inhibition of ristocetin cofactor activity (VWF:RCo).	Ristocetin	179-189	von Willebrand factor	Homo sapiens	57-60
34089550-1	2021	BACKGROUND: Antibodies inhibiting von Willebrand factor (VWF) develop in a subset of patients with type 3 von Willebrand disease (VWD3) and may be detected by their inhibition of ristocetin cofactor activity (VWF:RCo).	Ristocetin	179-189	von Willebrand factor	Homo sapiens	209-212
2533412-4	1989	We conclude that in acquired hypothyroidism the lowering of factor VIII:C and vWf:Ag (acquired von Willebrand disease) is associated with impaired platelet reactivity not only to ristocetin but also to collagen and especially adrenalin.	Ristocetin	179-189	cytochrome c oxidase subunit 8A	Homo sapiens	67-71
34269797-8	2021	This report illustrates that continuous-infusion VWF concentrate administration with or without intravenous immunoglobulin rapidly achieves target ristocetin cofactor activity and provides adequate hemostasis in aVWD associated with immunoglobulin G MGUS.	Ristocetin	147-157	von Willebrand factor	Homo sapiens	49-52
34497208-6	2021	Since ristocetin cofactor activity (vWF:RCo) and VWF antigen levels (vWF:Ag) are not routinely measured in clinical laboratories, the actual diagnosis is often determined by a mild prolongation of the activated partial thromboplastic time (APTT) associated with a relative decrease in factor VIII activity.	Ristocetin	6-16	von Willebrand factor	Homo sapiens	36-39
34269464-8	2021	Ristocetin cofactor assay quantified von Willebrand factor (vWF) activity.	Ristocetin	0-10	von Willebrand factor	Homo sapiens	37-58
34269464-8	2021	Ristocetin cofactor assay quantified von Willebrand factor (vWF) activity.	Ristocetin	0-10	von Willebrand factor	Homo sapiens	60-63
35075935-9	2022	VWF antigen (VWF-Ag) and VWF ristocetin cofactor activity (VWF-Rico) on these topographic surfaces were quantified by enzyme-linked immunosorbent assay (ELISA), the loss of HMWM-VWF was quantified by immunoblotting.	Ristocetin	29-39	von Willebrand factor	Homo sapiens	59-62
2533412-4	1989	We conclude that in acquired hypothyroidism the lowering of factor VIII:C and vWf:Ag (acquired von Willebrand disease) is associated with impaired platelet reactivity not only to ristocetin but also to collagen and especially adrenalin.	Ristocetin	179-189	von Willebrand factor	Homo sapiens	78-81
2621801-8	1989	These studies suggest that the abnormality of ristocetin-induced vWF-platelet interaction by IgA RIPA inhibitor and the reduction of all vWF multimers (like type IA von Willebrand disease) may have a relationship with the pathogenesis of bleeding diathesis in this case.	Ristocetin	46-56	von Willebrand factor	Homo sapiens	65-68
2804346-10	1989	The amount of radiolabeled vWF bound to platelets in the presence of either low concentration of ristocetin or asialo vWF was increased 30% compared with normal.	Ristocetin	97-107	von Willebrand factor	Homo sapiens	27-30
2557900-2	1989	Interaction of von Willebrand factor (vWF) with its platelet receptor only occurs in vitro in the presence of a modulator such as ristocetin.	Ristocetin	130-140	von Willebrand factor	Homo sapiens	15-36
2557900-2	1989	Interaction of von Willebrand factor (vWF) with its platelet receptor only occurs in vitro in the presence of a modulator such as ristocetin.	Ristocetin	130-140	von Willebrand factor	Homo sapiens	38-41
2557900-3	1989	We have recently confirmed that the human platelet membrane glycoprotein (GP) Ib-IX complex is the receptor involved in the ristocetin-dependent binding of vWF by reconstitution with the purified components [Berndt, M.C., Du, X., & Booth, W.J.	Ristocetin	124-134	von Willebrand factor	Homo sapiens	156-159
2557900-10	1989	Botrocetin-dependent binding of vWF was specific, saturable, and comparable to that observed with ristocetin.	Ristocetin	98-108	von Willebrand factor	Homo sapiens	32-35
2557900-11	1989	An anti-vWF monoclonal antibody, 3F8, inhibited ristocetin- but not botrocetin-dependent binding of vWF, suggesting the presence of distinct ristocetin and botrocetin modulator sites on vWF.	Ristocetin	48-58	von Willebrand factor	Homo sapiens	8-11
2557900-11	1989	An anti-vWF monoclonal antibody, 3F8, inhibited ristocetin- but not botrocetin-dependent binding of vWF, suggesting the presence of distinct ristocetin and botrocetin modulator sites on vWF.	Ristocetin	141-151	von Willebrand factor	Homo sapiens	8-11
2508742-4	1989	The functional activity of vWf was assessed by either Ristocetin Cofactor (vWf:RCo) or collagen binding methods (vWf:CBA) with typical vWf:RCo/vWf:Ag ratios ranging from 0.08 to 0.94.	Ristocetin	54-64	von Willebrand factor	Homo sapiens	27-30
2803984-3	1989	The pool was labelled with 125I and used for inhibition binding studies with individual fractions to calculate the dissociation constants (Kd values expressed in mol/l) of the individual fractions for ristocetin-dependent binding to GP Ib and thrombin-induced binding to GP IIb/IIIa.	Ristocetin	201-211	coagulation factor II, thrombin	Homo sapiens	243-251
2803984-3	1989	The pool was labelled with 125I and used for inhibition binding studies with individual fractions to calculate the dissociation constants (Kd values expressed in mol/l) of the individual fractions for ristocetin-dependent binding to GP Ib and thrombin-induced binding to GP IIb/IIIa.	Ristocetin	201-211	integrin subunit alpha 2b	Homo sapiens	271-277
2787678-5	1989	More than 50% of the ristocetin cofactor activity was lost during a five-minute incubation of vWF with 0.56 U/mL porcine elastase when no detectable structural changes in the vWF molecule had occurred.	Ristocetin	21-31	von Willebrand factor	Homo sapiens	94-97
2787678-5	1989	More than 50% of the ristocetin cofactor activity was lost during a five-minute incubation of vWF with 0.56 U/mL porcine elastase when no detectable structural changes in the vWF molecule had occurred.	Ristocetin	21-31	von Willebrand factor	Homo sapiens	175-178
2659619-8	1989	The mean plasma vWF value also was significantly elevated initially [vWF antigen, 1.8 +/- 0.7; normal group, 0.9 +/- 0.1 x 10(3) U/L (P less than 0.01); vWF ristocetin cofactor activity, 1.9 +/- 0.9; normal group, 1.0 +/- 0.3 x 10(3) U/L (P less than 0.001)] and decreased significantly after only 1 week of therapy.	Ristocetin	157-167	von Willebrand factor	Homo sapiens	16-19
3264111-7	1988	In eight cases, the platelets of uremic patients were purified, and the thrombin- and ristocetin-induced binding of normal von Willebrand factor to these platelets was examined.	Ristocetin	86-96	von Willebrand factor	Homo sapiens	123-144
3263968-4	1988	Glycocalicin, as well as the 45- and 84-kDa fragments, inhibited the ristocetin-dependent binding of native vWF to platelet GP Ib.	Ristocetin	69-79	von Willebrand factor	Homo sapiens	108-111
2786916-1	1989	When platelets are stimulated with adenosine diphosphate (ADP), thrombin, or ristocetin, they bind soluble von Willebrand factor (vWF).	Ristocetin	77-87	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).	Ristocetin	77-87	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.	Ristocetin	57-67	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.	Ristocetin	110-120	von Willebrand factor	Homo sapiens	78-81
2657729-4	1989	vWF secreted constitutively by IIB cells into the culture medium bound to platelets at concentrations of ristocetin lower than those necessary for vWF from normal cells.	Ristocetin	105-115	von Willebrand factor	Homo sapiens	0-3
2657729-5	1989	vWF stored in the Weibel-Palade bodies of type IIB cells was released upon stimulation with phorbol ester and bound almost completely to platelets even in the absence of ristocetin.	Ristocetin	170-180	von Willebrand factor	Homo sapiens	0-3
2591151-4	1989	Platelet/vWF interaction induced by ristocetin is not enhanced in these cases and the platelet vWF shows the same aberrant multimer pattern as plasma vWF.	Ristocetin	36-46	von Willebrand factor	Homo sapiens	9-12
3263968-6	1988	In contrast, the binding of asialo-vWF to platelet GP Ib, measured directly in the absence of ristocetin, was blocked by glycocalicin and the 45-kDa fragment with a similar IC50, but not by the 84-kDa fragment.	Ristocetin	94-104	von Willebrand factor	Homo sapiens	35-38
3263968-7	1988	Both glycocalicin and the 45-kDa fragment bound to purified surface-bound vWF in a ristocetin-dependent manner and with similar affinities.	Ristocetin	83-93	von Willebrand factor	Homo sapiens	74-77
3264111-8	1988	RESULTS: The mean plasma von Willebrand factor antigen and activity (ristocetin cofactor assay) were elevated 2.77 mu/ml and 1.88 mu/ml, respectively (normal, 1.01 mu/ml and 1.07 mu/ml, respectively).	Ristocetin	69-79	von Willebrand factor	Homo sapiens	25-46
3263968-10	1988	Whereas the ristocetin-dependent binding of vWF may involve also other domains in the macroglycopeptide region, the direct vWF-GP Ib interaction appears to be mediated only by a domain in the amino-terminal region of GP Ib alpha.	Ristocetin	12-22	von Willebrand factor	Homo sapiens	44-47
3264111-15	1988	Thrombin and ristocetin-induced binding of normal von Willebrand factor to uremic patients" platelets was indistinguishable from the binding to normal platelets.	Ristocetin	13-23	von Willebrand factor	Homo sapiens	50-71
2903069-1	1988	Very low concentrations of somatostatin (S-14) strongly potentiate the in vitro aggregation induced by collagen, ristocetin and arachidonic acid, but not that induced by ADP or epinephrine, in both human platelet rich plasmas and gel-filtered platelet preparations.	Ristocetin	113-123	thyroid hormone responsive	Homo sapiens	41-45
3264193-4	1988	In a concentration-dependent manner, ATA also inhibits ristocetin-induced, vWF-mediated platelet clumping in both fresh and formaldehyde-fixed platelet suspensions.	Ristocetin	55-65	von Willebrand factor	Homo sapiens	75-78
3140912-2	1988	One monoclonal antibody, designated PP3-4C, blocked Ristocetin-induced platelet agglutination and caused 80% inhibition of Ristocetin-induced 125I-von Willebrand factor (vWF) binding to porcine platelets at a concentration of greater than or equal to 12 micrograms IgG/mL.	Ristocetin	123-133	von Willebrand factor	Homo sapiens	142-168
3140912-2	1988	One monoclonal antibody, designated PP3-4C, blocked Ristocetin-induced platelet agglutination and caused 80% inhibition of Ristocetin-induced 125I-von Willebrand factor (vWF) binding to porcine platelets at a concentration of greater than or equal to 12 micrograms IgG/mL.	Ristocetin	123-133	von Willebrand factor	Homo sapiens	170-173
3064358-8	1988	A MAb to vWF (CLB-RAg 35), that inhibits ristocetin induced binding of vWF to platelets, decreased the CCo of normal plasma by 70%.	Ristocetin	41-51	von Willebrand factor	Homo sapiens	9-12
3064358-8	1988	A MAb to vWF (CLB-RAg 35), that inhibits ristocetin induced binding of vWF to platelets, decreased the CCo of normal plasma by 70%.	Ristocetin	41-51	von Willebrand factor	Homo sapiens	71-74
3413736-5	1988	Furthermore, the von Willebrand factor (vWF) dependent platelet aggregation induced by 0.6 and 1.0 mg/ml ristocetin was clearly diminished after ASA.	Ristocetin	105-115	von Willebrand factor	Homo sapiens	17-38
3263711-1	1988	Native von Willebrand factor (N-vWF) binds to platelets activated by thrombin, ADP or ristocetin.	Ristocetin	86-96	von Willebrand factor	Homo sapiens	32-35
3413736-5	1988	Furthermore, the von Willebrand factor (vWF) dependent platelet aggregation induced by 0.6 and 1.0 mg/ml ristocetin was clearly diminished after ASA.	Ristocetin	105-115	von Willebrand factor	Homo sapiens	40-43
3258766-3	1988	Platelet stimulation by thrombin decreased the binding of von Willebrand factor (vWF) to glycoprotein (GP) Ib and decreased ristocetin-induced agglutination, in vitro reactions that correlate with initial platelet adhesion to the vessel wall.	Ristocetin	124-134	coagulation factor II, thrombin	Homo sapiens	24-32
3284916-7	1988	Endothelial cells as well as smooth muscle cells bound 125I-labeled vWF in a ristocetin-dependent manner, with a Kd of 7.9 nM.	Ristocetin	77-87	von Willebrand factor	Homo sapiens	68-71
3258474-2	1988	Findings typical of type IIB vWD included enhanced ristocetin-induced binding of patient von Willebrand factor (vWF) to platelets of patients and normal individuals in association with the absence of larger multimers from plasma.	Ristocetin	51-61	von Willebrand factor	Homo sapiens	89-110
3258474-2	1988	Findings typical of type IIB vWD included enhanced ristocetin-induced binding of patient von Willebrand factor (vWF) to platelets of patients and normal individuals in association with the absence of larger multimers from plasma.	Ristocetin	51-61	von Willebrand factor	Homo sapiens	112-115
3128354-3	1988	In 4 patients with type I vWF who were given a Ristocetin cofactor (Rcof) dose of 42-78 U/kg, there was a clear reduction of the bleeding time and an increase of F VIII: C, F VIII: Ag, Rcof and vWF: Ag for several hours.	Ristocetin	47-57	von Willebrand factor	Homo sapiens	26-29
3128354-3	1988	In 4 patients with type I vWF who were given a Ristocetin cofactor (Rcof) dose of 42-78 U/kg, there was a clear reduction of the bleeding time and an increase of F VIII: C, F VIII: Ag, Rcof and vWF: Ag for several hours.	Ristocetin	47-57	coagulation factor VIII	Homo sapiens	162-168
3128354-3	1988	In 4 patients with type I vWF who were given a Ristocetin cofactor (Rcof) dose of 42-78 U/kg, there was a clear reduction of the bleeding time and an increase of F VIII: C, F VIII: Ag, Rcof and vWF: Ag for several hours.	Ristocetin	47-57	coagulation factor VIII	Homo sapiens	173-179
3128354-3	1988	In 4 patients with type I vWF who were given a Ristocetin cofactor (Rcof) dose of 42-78 U/kg, there was a clear reduction of the bleeding time and an increase of F VIII: C, F VIII: Ag, Rcof and vWF: Ag for several hours.	Ristocetin	47-57	von Willebrand factor	Homo sapiens	194-197
3126793-4	1988	The inhibitor was able to inhibit the binding of 125I-vWf to platelets in the presence of ristocetin in both cases and to thrombin-stimulated platelets in one case.	Ristocetin	90-100	von Willebrand factor	Homo sapiens	54-57
3126081-3	1988	In 14 patients with type I vWd characterized by very low plasma levels of factor VIII coagulant activity (VIII:C) and vWf, measured as ristocetin cofactor activity (lower than 20% and 3% of normal respectively), but with a normal intraplatelet content of vWf, a test infusion of DDAVP (0.4 microgram/kg) elicited a very marked increase of VIII:C and vWf and normalized the bleeding time.	Ristocetin	135-145	von Willebrand factor	Homo sapiens	118-121
2450575-0	1988	Ristocetin-dependent reconstitution of binding of von Willebrand factor to purified human platelet membrane glycoprotein Ib-IX complex.	Ristocetin	0-10	von Willebrand factor	Homo sapiens	50-71
2450575-1	1988	Whether the human platelet membrane glycoprotein (GP) Ib-IX complex is the receptor for ristocetin-dependent binding of von Willebrand factor (vWF) has been examined by reconstitution with the purified components using a solid-phase bead assay.	Ristocetin	88-98	von Willebrand factor	Homo sapiens	120-141
2450575-1	1988	Whether the human platelet membrane glycoprotein (GP) Ib-IX complex is the receptor for ristocetin-dependent binding of von Willebrand factor (vWF) has been examined by reconstitution with the purified components using a solid-phase bead assay.	Ristocetin	88-98	von Willebrand factor	Homo sapiens	143-146
2450575-3	1988	Specific binding of 125I-labeled vWF to the GP Ib-IX complex coated beads was strictly ristocetin dependent with maximal binding occurring at ristocetin concentrations greater than or equal to 1 mg/mL.	Ristocetin	87-97	von Willebrand factor	Homo sapiens	33-36
2450575-3	1988	Specific binding of 125I-labeled vWF to the GP Ib-IX complex coated beads was strictly ristocetin dependent with maximal binding occurring at ristocetin concentrations greater than or equal to 1 mg/mL.	Ristocetin	142-152	von Willebrand factor	Homo sapiens	33-36
2450575-4	1988	Ristocetin-dependent specific binding of 125I-labeled vWF was saturable.	Ristocetin	0-10	von Willebrand factor	Homo sapiens	54-57
2450575-7	1988	Ristocetin-dependent binding of vWF to platelets and to GP Ib-IX complex coated beads was inhibited by monoclonal antibodies against a 45,000 molecular weight N-terminal region of GP Ib but not by monoclonal antibodies directed against other regions of the GP Ib-IX complex.	Ristocetin	0-10	von Willebrand factor	Homo sapiens	32-35
2450575-8	1988	Similar correspondence between platelets and purified GP Ib-IX complex with respect to the ristocetin-dependent binding of vWF was obtained with anti-vWF monoclonal antibodies.	Ristocetin	91-101	von Willebrand factor	Homo sapiens	123-126
2450575-8	1988	Similar correspondence between platelets and purified GP Ib-IX complex with respect to the ristocetin-dependent binding of vWF was obtained with anti-vWF monoclonal antibodies.	Ristocetin	91-101	von Willebrand factor	Homo sapiens	150-153
3069641-10	1988	The storage vesicles contain von Willebrand factor that supports ristocetin-induced platelet aggregation.	Ristocetin	65-75	von Willebrand factor	Homo sapiens	29-50
3142084-7	1988	Furthermore, the partial inhibition of CCo by monoclonal antibody CLB-RAg 35 that inhibits the binding of vWF to platelet in the presence of ristocetin, suggests that CCo is partly mediated through platelet membrane glycoprotein Ib.	Ristocetin	141-151	von Willebrand factor	Homo sapiens	106-109
3500868-2	1987	Ristocetin promotes the binding of vWf to platelet membrane glycoprotein lb, whereas platelet activation by thrombin supports binding to the glycoprotein IIb/IIIa complex.	Ristocetin	0-10	von Willebrand factor	Homo sapiens	35-38
3502200-0	1987	Calibration of lyophilized standards for ristocetin cofactor activity of von Willebrand Factor (vWF) requires vWF-deficient plasma as diluent for dose-response curves.	Ristocetin	41-51	von Willebrand factor	Homo sapiens	96-99
3502200-1	1987	Calibration of local standards for ristocetin cofactor activity of von Willebrand"s factor (vWF:Rcof) against reference preparations is required to achieve a better standardization of this measurement.	Ristocetin	35-45	von Willebrand factor	Homo sapiens	92-95
3501312-10	1987	Thus, we deduce that vWF can spontaneously re-multimerize from its reduced subunits and regain a small but measurable quantity of ristocetin co-factor activity.	Ristocetin	130-140	von Willebrand factor	Homo sapiens	21-24
3500868-6	1987	Modification of vWf amino groups markedly impaired the ability of the protein to support ristocetin-dependent adhesion but did not alter its ability to support thrombin-enhanced adhesion.	Ristocetin	89-99	von Willebrand factor	Homo sapiens	16-19
2966106-5	1987	However, platelet CR3 does not merely bind C3bi, but the binding of the OKM1 antibody to platelet CR3 selectively blocks platelet functions of aggregation and serotonin release induced by arachadonic acid but not by other ligands (ristocetin, ADP, L-epinephrine, collagen and thrombin).	Ristocetin	231-241	teratocarcinoma-derived growth factor 1 pseudogene 3	Homo sapiens	98-101
3500868-7	1987	Reduction and carboxymethylation nearly abolished the ability of vWf to support adhesion via the ristocetin-dependent mechanism, but did not substantially impair its ability to support thrombin-enhanced adhesion.	Ristocetin	97-107	von Willebrand factor	Homo sapiens	65-68
2822171-8	1987	Ristocetin-induced binding of vWf was inhibited by 6D1, and ADP-induced binding of fibrinogen was inhibited by LJ-CP8.	Ristocetin	0-10	von Willebrand factor	Homo sapiens	30-33
3122318-9	1987	Aggregation of washed fixed platelets in the presence of ristocetin or collagen is used for assessment of vWF"s biological activity.	Ristocetin	57-67	von Willebrand factor	Homo sapiens	106-109
3127926-4	1987	The PT-PAF activity was dependent on the multimer size of vWf, like in the case of ristocetin cofactor (RCof) activity.	Ristocetin	83-93	von Willebrand factor	Homo sapiens	58-61
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.	Ristocetin	113-123	von Willebrand factor	Homo sapiens	150-171
2822176-6	1987	We confirmed that a calcium-dependent cysteine protease (CDP) was present in the sera of each of the 15 patients when we used an assay based on the ability of CDP to proteolyse platelet membrane glycoprotein 1b (GP1b) and hence to abolish the ability of CDP-treated normal platelets to agglutinate in the presence of ristocetin and von Willebrand factor.	Ristocetin	317-327	glycoprotein Ib platelet subunit alpha	Homo sapiens	212-216
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.	Ristocetin	113-123	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.	Ristocetin	162-172	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.	Ristocetin	151-161	fibrinogen beta chain	Homo sapiens	52-62
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.	Ristocetin	151-161	von Willebrand factor	Homo sapiens	64-67
3115333-0	1987	Asialo-von Willebrand factor inhibits platelet adherence to human arterial subendothelium: discrepancy between ristocetin cofactor activity and primary hemostatic function.	Ristocetin	111-121	von Willebrand factor	Homo sapiens	7-28
3116841-6	1987	The ratio of vWF:Ag to ristocetin cofactor was elevated in these patients.	Ristocetin	23-33	von Willebrand factor	Homo sapiens	13-16
3115333-2	1987	Clinically, the ristocetin cofactor (RCof) activity is the only widely available assay for vWF function.	Ristocetin	16-26	von Willebrand factor	Homo sapiens	91-94
3499929-7	1987	Released vWF contained the higher molecular weight multimers observed in normal endothelial cells, and it possessed ristocetin cofactor activity.	Ristocetin	116-126	von Willebrand factor	Homo sapiens	9-12
3492062-0	1986	A paradoxical effect of antibody concentration on vWF-dependent platelet agglutination distinguishes between botrocetin and ristocetin-induced agglutination.	Ristocetin	124-134	von Willebrand factor	Homo sapiens	50-53
3659809-1	1987	Both von Willebrand factor antigen and activity tested as ristocetin cofactor, were found to be increased in the 20 patients with hyperthyroidism, while changes detected on the 10 hypothyroid patients did not significantly differ from the mean values recorded in 19 healthy control subjects.	Ristocetin	58-68	von Willebrand factor	Homo sapiens	5-26
3116700-0	1987	Characterisation of a monoclonal antibody to von Willebrand factor as a potent inhibitor of ristocetin-mediated platelet interaction and platelet adhesion.	Ristocetin	92-102	von Willebrand factor	Homo sapiens	45-66
3101558-6	1987	Of the other 30 patients, a mild increase in ristocetin cofactor/vWF:Ag was seen in only 2 with secondary pulmonary hypertension and 1 with normal pulmonary artery pressure: these also had an abnormal vWF multimer pattern that was different from that observed in patients with primary pulmonary hypertension.	Ristocetin	45-55	von Willebrand factor	Homo sapiens	201-204
3111088-0	1987	Assessment of multimeric structure and ristocetin-induced binding to platelets of von Willebrand factor present in cryoprecipitate and different factor VIII concentrates.	Ristocetin	39-49	von Willebrand factor	Homo sapiens	82-103
3492062-7	1986	Antisera to human vWF that showed this paradoxical inhibitory/enhancing effect on botrocetin-induced agglutination also inhibited ristocetin-induced platelet agglutination at high concentrations, but failed to enhance agglutination at any concentration.	Ristocetin	130-140	von Willebrand factor	Homo sapiens	18-21
3551182-1	1986	Previously we have studied the binding domains on von Willebrand factor (vWF) involved in ristocetin-induced binding to platelets (ristocetin binding domain, RBD) and in the binding of vWF to collagen (collagen binding domain, CBD) using tryptic fragments of 125I-labelled vWF (21, 23).	Ristocetin	90-100	von Willebrand factor	Homo sapiens	50-71
3551182-1	1986	Previously we have studied the binding domains on von Willebrand factor (vWF) involved in ristocetin-induced binding to platelets (ristocetin binding domain, RBD) and in the binding of vWF to collagen (collagen binding domain, CBD) using tryptic fragments of 125I-labelled vWF (21, 23).	Ristocetin	90-100	von Willebrand factor	Homo sapiens	73-76
3551182-1	1986	Previously we have studied the binding domains on von Willebrand factor (vWF) involved in ristocetin-induced binding to platelets (ristocetin binding domain, RBD) and in the binding of vWF to collagen (collagen binding domain, CBD) using tryptic fragments of 125I-labelled vWF (21, 23).	Ristocetin	131-141	von Willebrand factor	Homo sapiens	50-71
3551182-1	1986	Previously we have studied the binding domains on von Willebrand factor (vWF) involved in ristocetin-induced binding to platelets (ristocetin binding domain, RBD) and in the binding of vWF to collagen (collagen binding domain, CBD) using tryptic fragments of 125I-labelled vWF (21, 23).	Ristocetin	131-141	von Willebrand factor	Homo sapiens	73-76
3101223-6	1986	The adhesion of FWP was inhibited by fibronectin (FN) and the binding of ristocetin cofactor (vWF:RCo) to collagen fiber was also inhibited by FN; bound vWF:RCo to 50 micrograms/ml collagen in the absence or presence of 125 micrograms/ml FN were 60% and 8% respectively.	Ristocetin	73-83	von Willebrand factor	Homo sapiens	94-97
3101223-6	1986	The adhesion of FWP was inhibited by fibronectin (FN) and the binding of ristocetin cofactor (vWF:RCo) to collagen fiber was also inhibited by FN; bound vWF:RCo to 50 micrograms/ml collagen in the absence or presence of 125 micrograms/ml FN were 60% and 8% respectively.	Ristocetin	73-83	fibronectin 1	Homo sapiens	143-145
3101223-6	1986	The adhesion of FWP was inhibited by fibronectin (FN) and the binding of ristocetin cofactor (vWF:RCo) to collagen fiber was also inhibited by FN; bound vWF:RCo to 50 micrograms/ml collagen in the absence or presence of 125 micrograms/ml FN were 60% and 8% respectively.	Ristocetin	73-83	von Willebrand factor	Homo sapiens	153-156
3101223-6	1986	The adhesion of FWP was inhibited by fibronectin (FN) and the binding of ristocetin cofactor (vWF:RCo) to collagen fiber was also inhibited by FN; bound vWF:RCo to 50 micrograms/ml collagen in the absence or presence of 125 micrograms/ml FN were 60% and 8% respectively.	Ristocetin	73-83	fibronectin 1	Homo sapiens	143-145
3097817-3	1986	Activities of vWf in plasmas of 51 patients were measured with either collagen (ColCof) or ristocetin (RCof).	Ristocetin	91-101	von Willebrand factor	Homo sapiens	14-17
3116700-5	1987	The 125I-FVIII/vWF binding to platelets in presence of ristocetin is totally inhibited by low 211 A6 concentrations.	Ristocetin	55-65	coagulation factor VIII	Homo sapiens	9-14
3116700-5	1987	The 125I-FVIII/vWF binding to platelets in presence of ristocetin is totally inhibited by low 211 A6 concentrations.	Ristocetin	55-65	von Willebrand factor	Homo sapiens	15-18
3116700-8	1987	The complete inhibition of platelet adhesion by 211 A6 questions the similarity or the interrelationship in vWF domains involved in ristocetin-induced platelet functions and platelet adhesion.	Ristocetin	132-142	von Willebrand factor	Homo sapiens	108-111
3492222-4	1987	A blood sample was taken from each subject for determination of the blood group and von Willebrand factor (vWf) level (measured as ristocetin cofactor and expressed in IU/dL after calibration of the internal pool against an international standard), and the parents were given a questionnaire concerning hemorrhagic symptoms in the members of the family in the last three generations.	Ristocetin	131-141	von Willebrand factor	Homo sapiens	74-105
3492222-4	1987	A blood sample was taken from each subject for determination of the blood group and von Willebrand factor (vWf) level (measured as ristocetin cofactor and expressed in IU/dL after calibration of the internal pool against an international standard), and the parents were given a questionnaire concerning hemorrhagic symptoms in the members of the family in the last three generations.	Ristocetin	131-141	von Willebrand factor	Homo sapiens	107-110
3123334-4	1987	We found that a commercially available factor VIII/vWf concentrate, Haemate P, contained the high-molecular-weight multimers of vWf and had a ratio of ristocetin cofactor (RCof) to vWf antigen (vWf:Ag) close to unity.	Ristocetin	151-161	von Willebrand factor	Homo sapiens	51-54
2946332-2	1986	The addition of 4.5 X 10(-7) mol/L plasmin to washed platelets caused a time-dependent decrease in ristocetin-induced, vWF-dependent platelet agglutination.	Ristocetin	99-109	plasminogen	Homo sapiens	35-42
2946332-2	1986	The addition of 4.5 X 10(-7) mol/L plasmin to washed platelets caused a time-dependent decrease in ristocetin-induced, vWF-dependent platelet agglutination.	Ristocetin	99-109	von Willebrand factor	Homo sapiens	119-122
3489493-2	1986	The binding of vWF to platelets was mediated and regulated by ristocetin.	Ristocetin	62-72	von Willebrand factor	Homo sapiens	15-18
3489493-9	1986	With addition of vWF to this PRP an enhanced response was observed at a ristocetin concentration inversely proportional to the vWF level.	Ristocetin	72-82	von Willebrand factor	Homo sapiens	17-20
3489493-9	1986	With addition of vWF to this PRP an enhanced response was observed at a ristocetin concentration inversely proportional to the vWF level.	Ristocetin	72-82	von Willebrand factor	Homo sapiens	127-130
3489493-14	1986	A dose-response 125I-vWF-platelet binding occurred with increasing ristocetin concentrations which was unchanged by the addition of collagen.	Ristocetin	67-77	von Willebrand factor	Homo sapiens	21-24
3489493-16	1986	The in vitro-enhanced CIPA represents a vWF-dependent aggregation of sufficient magnitude to overcome the inhibitory effect of ristocetin.	Ristocetin	127-137	von Willebrand factor	Homo sapiens	40-43
3016944-5	1986	Conversely, PG-1 selectively inhibited ristocetin-induced 125I-vWF binding, with the degree of inhibition inversely related to the ristocetin concentration.	Ristocetin	39-49	von Willebrand factor	Cavia porcellus	63-66
3016944-5	1986	Conversely, PG-1 selectively inhibited ristocetin-induced 125I-vWF binding, with the degree of inhibition inversely related to the ristocetin concentration.	Ristocetin	131-141	von Willebrand factor	Cavia porcellus	63-66
2941084-6	1986	Incubation of platelets suspended in autologous plasma with 400 ng/mL of TPA for one hour also inhibited ristocetin-induced agglutination.	Ristocetin	105-115	plasminogen activator, tissue type	Homo sapiens	73-76
2941084-14	1986	Plasmin generation leads to degradation of GPIb and decreased ristocetin-induced agglutination in normal and thrombasthenic platelets, as well as degradation of GPIIb/IIIa in normal washed platelets and inhibition of ADP and gamma thrombin-induced aggregation.	Ristocetin	62-72	plasminogen	Homo sapiens	0-7
3487353-4	1986	Addition of ristocetin to the patients" platelet-rich plasma resulted in the removal of vWF (and, more selectively, of the large multimers) at lower concentrations of ristocetin than normal, as in type IIB and pseudo-vWD.	Ristocetin	12-22	von Willebrand factor	Homo sapiens	88-91
3487353-5	1986	The defect in the patients was localized to their vWF, which had an enhanced capacity for aggregating washed normal platelets in the presence of low concentrations of ristocetin and for aggregating pseudo-vWD platelets (in the absence of ristocetin).	Ristocetin	167-177	von Willebrand factor	Homo sapiens	50-53
3487353-5	1986	The defect in the patients was localized to their vWF, which had an enhanced capacity for aggregating washed normal platelets in the presence of low concentrations of ristocetin and for aggregating pseudo-vWD platelets (in the absence of ristocetin).	Ristocetin	238-248	von Willebrand factor	Homo sapiens	50-53
3487353-7	1986	RIPA (at low ristocetin concentrations) in the patients" platelet-rich plasma was abolished by a monoclonal antibody (AP1) to GPIb and was markedly reduced by monoclonal antibodies (10E5 and LJP9) that block adenosine diphosphate and thrombin-induced binding of vWF and fibrinogen to GPIIb-IIIa but was unaffected by an antibody (LJP5) that only blocks vWF binding.	Ristocetin	13-23	JunB proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	118-121
3487357-9	1986	After infusion of 1-deamino-8-D-arginine vasopressin, the largest von Willebrand factor multimers, as well as new satellite bands with a mobility similar to those in normal plasma, appeared in the patient plasma, and the levels of von Willebrand factor antigen and ristocetin cofactor activity became normal.	Ristocetin	265-275	arginine vasopressin	Homo sapiens	41-52
3092393-3	1986	The level of ristocetin cofactor activity of vWF was between 70 and 144% in the control group.	Ristocetin	13-23	von Willebrand factor	Homo sapiens	45-48
3092393-5	1986	The vWF:Ag level closely paralleled the rise of ristocetin cofactor activity of vWF, with a peak of 336% on day 5.	Ristocetin	48-58	von Willebrand factor	Homo sapiens	4-7
3092393-5	1986	The vWF:Ag level closely paralleled the rise of ristocetin cofactor activity of vWF, with a peak of 336% on day 5.	Ristocetin	48-58	von Willebrand factor	Homo sapiens	80-83
3092393-8	1986	The ristocetin cofactor activity of vWF and vWF:Ag thus are sensitive biochemical indicators for recent AMI, and may serve as useful markers for up to 14 days following infarction, when the traditional enzymes have returned to normal levels.	Ristocetin	4-14	von Willebrand factor	Homo sapiens	36-39
3092393-8	1986	The ristocetin cofactor activity of vWF and vWF:Ag thus are sensitive biochemical indicators for recent AMI, and may serve as useful markers for up to 14 days following infarction, when the traditional enzymes have returned to normal levels.	Ristocetin	4-14	von Willebrand factor	Homo sapiens	44-47
3486014-0	1986	Identification of functional domains on von Willebrand factor by binding of tryptic fragments to collagen and to platelets in the presence of ristocetin.	Ristocetin	142-152	von Willebrand factor	Homo sapiens	40-61
3487975-6	1986	In four patients with abnormal ristocetin-induced aggregation, vWF:Ag, RCoF, and FVIII:C were all reduced.	Ristocetin	31-41	von Willebrand factor	Homo sapiens	63-66
3008890-2	1986	SpII (215 kd) and SpIII (320 kd), the S aureus V-8 protease homodimeric fragments representing the carboxy-terminal and amino-terminal segments of the vWF subunit, competitively inhibited the binding of multimeric vWF to thrombin-stimulated or ristocetin-stimulated platelets, respectively.	Ristocetin	244-254	von Willebrand factor	Homo sapiens	151-154
3486014-1	1986	With the use of monoclonal antibodies that inhibit the ristocetin-induced binding of von Willebrand factor (VWF) to platelets and the binding to collagen, we have previously identified two distinct tryptic fragments.	Ristocetin	55-65	von Willebrand factor	Homo sapiens	85-106
3008890-7	1986	In contrast, M Ab H9, which blocks ristocetin-induced binding of vWF to platelets, inhibited binding of SpIII to platelets and bound to SpIII as well as to monomeric 33-kd and 28-kd subtilisin fragments.	Ristocetin	35-45	von Willebrand factor	Homo sapiens	65-68
3486014-1	1986	With the use of monoclonal antibodies that inhibit the ristocetin-induced binding of von Willebrand factor (VWF) to platelets and the binding to collagen, we have previously identified two distinct tryptic fragments.	Ristocetin	55-65	von Willebrand factor	Homo sapiens	108-111
3484979-3	1986	Analysis of the factor VIII molecular complex revealed that six patients had reduced vWF measured both immunologically (vW:Ag) and by ristocetin cofactor assay (vW:rist).	Ristocetin	134-144	von Willebrand factor	Homo sapiens	85-88
3003157-7	1986	Complex formation was blocked by rabbit antiglycocalicin antiserum, but not by the monoclonal antibody 6D1, which is directed against the site on GPIb where von Willebrand factor (vWf) binds in the presence of ristocetin.	Ristocetin	210-220	von Willebrand factor	Homo sapiens	157-178
3003157-7	1986	Complex formation was blocked by rabbit antiglycocalicin antiserum, but not by the monoclonal antibody 6D1, which is directed against the site on GPIb where von Willebrand factor (vWf) binds in the presence of ristocetin.	Ristocetin	210-220	von Willebrand factor	Homo sapiens	180-183
3003157-10	1986	We conclude that the membrane site to which thrombin binds is the glycocalicin portion of platelet GPIb at a site remote from the point of ristocetin-dependent vWf binding.	Ristocetin	139-149	coagulation factor II, thrombin	Homo sapiens	44-52
2934387-3	1986	After extensive treatment with denaturants, the 52/48-kDa polypeptide retained its ability to inhibit ristocetin-induced platelet aggregation in the presence of native vWF, as well as aggregation induced by desialylated vWF alone.	Ristocetin	102-112	von Willebrand factor	Homo sapiens	168-171
2934387-3	1986	After extensive treatment with denaturants, the 52/48-kDa polypeptide retained its ability to inhibit ristocetin-induced platelet aggregation in the presence of native vWF, as well as aggregation induced by desialylated vWF alone.	Ristocetin	102-112	von Willebrand factor	Homo sapiens	220-223
3000477-3	1986	The binding to platelets of 6D1, a monoclonal antibody that recognizes an epitope on GpIb and blocks ristocetin-induced vWF binding to platelets, was inhibited by purified GC.	Ristocetin	101-111	von Willebrand factor	Homo sapiens	120-123
3000477-4	1986	In addition, purified GC inhibited ristocetin-dependent binding of 125I-labeled vWF to platelets.	Ristocetin	35-45	von Willebrand factor	Homo sapiens	80-83
2435633-2	1986	The von Willebrand molecule includes factor VIII related antigen (VIIIR: Ag) which represents the molecular substrate of the von Willebrand activity expressed as Ristocetin cofactor (VIIIR:RCoF) activity.	Ristocetin	162-172	cytochrome c oxidase subunit 8A	Homo sapiens	44-48
2435633-12	1986	Von Willebrand factor activity, expressed as its ability to induce platelet aggregation in the presence of the antibiotic Ristocetin, can be carried out using normal formalin fixed platelets, either with aggregometer or visual methods (glass slide test or tubes test and microtritation plate).	Ristocetin	122-132	von Willebrand factor	Homo sapiens	0-21
2436998-3	1986	F VIII preparations high in ristocetin cofactor activity (vWF:RICof) and low in the ratio of vWF:Ag to vWF:RiCof were found to be similar in the multimeric structure of vWF:Ag to normal plasma.	Ristocetin	28-38	cytochrome c oxidase subunit 8A	Homo sapiens	2-6
3155489-6	1985	Plasmin, 0.05 to 1.0 CU/mL, reduced ristocetin-mediated agglutination of washed platelets in the presence of von Willebrand factor (vWF) from 66% of control to 2% of control, following a one-hour incubation.	Ristocetin	36-46	plasminogen	Homo sapiens	0-7
3876857-6	1985	Therefore, it is concluded that vWF is unlikely to play a major role in platelet aggregation induced by majority of TTP plasmas and that the site of platelet GP Ib, to which vWF binds in the presence of ristocetin, is not involved in TTP plasma-induced aggregation.	Ristocetin	203-213	von Willebrand factor	Homo sapiens	174-177
2932740-3	1985	Ristocetin-induced platelet aggregation was enhanced by purified IIB vWF.	Ristocetin	0-10	von Willebrand factor	Homo sapiens	69-72
2932740-4	1985	The aggregation of washed normal platelets mixed with IIB vWF (0.4 microgram/ml) required lower amounts of ristocetin than the aggregation of normal platelets mixed with the same concentrations of normal vWF.	Ristocetin	107-117	von Willebrand factor	Homo sapiens	58-61
2934863-1	1985	The synergistic effects of platelet-activating factor (PAF) with ADP, collagen, thrombin, A23187, adrenaline, sodium arachidonate and ristocetin in human platelet aggregation and beta-thromboglobulin (beta-TG) release were investigated in citrated platelet-rich plasma (PRP).	Ristocetin	134-144	pro-platelet basic protein	Homo sapiens	179-199
2931492-2	1985	Isolated washed patient platelets bound more FVIII/vWF at high (1 and 0.75 mg/ml) and low (0.5 and 0.25 mg/ml) ristocetin concentrations than control platelets.	Ristocetin	111-121	coagulation factor VIII	Homo sapiens	45-50
2931492-2	1985	Isolated washed patient platelets bound more FVIII/vWF at high (1 and 0.75 mg/ml) and low (0.5 and 0.25 mg/ml) ristocetin concentrations than control platelets.	Ristocetin	111-121	von Willebrand factor	Homo sapiens	51-54
3927998-8	1985	The Ab was unable to bind isolated FVIII:C. The combined use of the new vWF-binding assay and a battery of tests for inhibition of vWF-dependent platelet aggregation with ristocetin (which detects high molecular weight vWF), with botrocetin (which detects high and low molecular weight vWF), and with platelet-aggregating factor (which detects high molecular weight vWF) provided a means of analysis of Ab effect on in vitro vWF function.	Ristocetin	171-181	von Willebrand factor	Homo sapiens	131-134
3927998-8	1985	The Ab was unable to bind isolated FVIII:C. The combined use of the new vWF-binding assay and a battery of tests for inhibition of vWF-dependent platelet aggregation with ristocetin (which detects high molecular weight vWF), with botrocetin (which detects high and low molecular weight vWF), and with platelet-aggregating factor (which detects high molecular weight vWF) provided a means of analysis of Ab effect on in vitro vWF function.	Ristocetin	171-181	von Willebrand factor	Homo sapiens	131-134
3927998-8	1985	The Ab was unable to bind isolated FVIII:C. The combined use of the new vWF-binding assay and a battery of tests for inhibition of vWF-dependent platelet aggregation with ristocetin (which detects high molecular weight vWF), with botrocetin (which detects high and low molecular weight vWF), and with platelet-aggregating factor (which detects high molecular weight vWF) provided a means of analysis of Ab effect on in vitro vWF function.	Ristocetin	171-181	von Willebrand factor	Homo sapiens	131-134
3927998-8	1985	The Ab was unable to bind isolated FVIII:C. The combined use of the new vWF-binding assay and a battery of tests for inhibition of vWF-dependent platelet aggregation with ristocetin (which detects high molecular weight vWF), with botrocetin (which detects high and low molecular weight vWF), and with platelet-aggregating factor (which detects high molecular weight vWF) provided a means of analysis of Ab effect on in vitro vWF function.	Ristocetin	171-181	von Willebrand factor	Homo sapiens	131-134
3927998-8	1985	The Ab was unable to bind isolated FVIII:C. The combined use of the new vWF-binding assay and a battery of tests for inhibition of vWF-dependent platelet aggregation with ristocetin (which detects high molecular weight vWF), with botrocetin (which detects high and low molecular weight vWF), and with platelet-aggregating factor (which detects high molecular weight vWF) provided a means of analysis of Ab effect on in vitro vWF function.	Ristocetin	171-181	von Willebrand factor	Homo sapiens	131-134
3927998-12	1985	The findings indicate that the vWS Ab binds to an epitope on the molecular vWF in such a way that causes only limited inhibition of vWF/ristocetin function and no inhibition of vWF/botrocetin function, suggesting that these two functional domains are at separate sites.	Ristocetin	136-146	von Willebrand factor	Homo sapiens	75-78
4032439-1	1985	A series of ristocetin analogues with modifications (OH, C=O, C=NOH, NCOCH3) at the C-1" amino group was synthesized and found to possess antibacterial activity against gram-positive bacteria and to bind to Ac2-Lys-D-Ala-D-Ala, a model for the antibiotic"s site of action.	Ristocetin	12-22	adenylate cyclase 2	Homo sapiens	207-210
3936216-3	1985	Small molecular forms of FVIII/vWF from normal and variant type II plasma, and those derived by disulfide reduction of high-molecular weight FVIII/vWF, showed remarkably decreased reactivity in ristocetin-, botrocetin- and latex-assay.	Ristocetin	194-204	coagulation factor VIII	Homo sapiens	25-30
3936216-3	1985	Small molecular forms of FVIII/vWF from normal and variant type II plasma, and those derived by disulfide reduction of high-molecular weight FVIII/vWF, showed remarkably decreased reactivity in ristocetin-, botrocetin- and latex-assay.	Ristocetin	194-204	von Willebrand factor	Homo sapiens	31-34
3936216-3	1985	Small molecular forms of FVIII/vWF from normal and variant type II plasma, and those derived by disulfide reduction of high-molecular weight FVIII/vWF, showed remarkably decreased reactivity in ristocetin-, botrocetin- and latex-assay.	Ristocetin	194-204	coagulation factor VIII	Homo sapiens	141-146
3936216-3	1985	Small molecular forms of FVIII/vWF from normal and variant type II plasma, and those derived by disulfide reduction of high-molecular weight FVIII/vWF, showed remarkably decreased reactivity in ristocetin-, botrocetin- and latex-assay.	Ristocetin	194-204	von Willebrand factor	Homo sapiens	147-150
3918560-7	1985	The data derived from our study imply that perfusion experiments with reconstituted blood offer a new approach in characterization of these patients, which may be more relevant for the treatment of the patients than characterization by ristocetin induced adsorption of FVIII-VWF to platelets.	Ristocetin	236-246	coagulation factor VIII	Homo sapiens	269-274
3918560-7	1985	The data derived from our study imply that perfusion experiments with reconstituted blood offer a new approach in characterization of these patients, which may be more relevant for the treatment of the patients than characterization by ristocetin induced adsorption of FVIII-VWF to platelets.	Ristocetin	236-246	von Willebrand factor	Homo sapiens	275-278
3917314-1	1985	A monoclonal antibody directed against the von Willebrand factor moiety (vWF) of factor VIII-von Willebrand factor (FVIII-vWF), which blocks ristocetin-induced platelet aggregation as well as the binding of FVIII-vWF to platelets in the presence of ristocetin, inhibited platelet adherence to human artery subendothelium when present in normal flowing blood.	Ristocetin	141-151	von Willebrand factor	Homo sapiens	73-76
3917314-1	1985	A monoclonal antibody directed against the von Willebrand factor moiety (vWF) of factor VIII-von Willebrand factor (FVIII-vWF), which blocks ristocetin-induced platelet aggregation as well as the binding of FVIII-vWF to platelets in the presence of ristocetin, inhibited platelet adherence to human artery subendothelium when present in normal flowing blood.	Ristocetin	141-151	von Willebrand factor	Homo sapiens	43-64
3917314-1	1985	A monoclonal antibody directed against the von Willebrand factor moiety (vWF) of factor VIII-von Willebrand factor (FVIII-vWF), which blocks ristocetin-induced platelet aggregation as well as the binding of FVIII-vWF to platelets in the presence of ristocetin, inhibited platelet adherence to human artery subendothelium when present in normal flowing blood.	Ristocetin	141-151	coagulation factor VIII	Homo sapiens	116-121
3917314-1	1985	A monoclonal antibody directed against the von Willebrand factor moiety (vWF) of factor VIII-von Willebrand factor (FVIII-vWF), which blocks ristocetin-induced platelet aggregation as well as the binding of FVIII-vWF to platelets in the presence of ristocetin, inhibited platelet adherence to human artery subendothelium when present in normal flowing blood.	Ristocetin	141-151	von Willebrand factor	Homo sapiens	122-125
3917314-1	1985	A monoclonal antibody directed against the von Willebrand factor moiety (vWF) of factor VIII-von Willebrand factor (FVIII-vWF), which blocks ristocetin-induced platelet aggregation as well as the binding of FVIII-vWF to platelets in the presence of ristocetin, inhibited platelet adherence to human artery subendothelium when present in normal flowing blood.	Ristocetin	141-151	von Willebrand factor	Homo sapiens	122-125
3917314-1	1985	A monoclonal antibody directed against the von Willebrand factor moiety (vWF) of factor VIII-von Willebrand factor (FVIII-vWF), which blocks ristocetin-induced platelet aggregation as well as the binding of FVIII-vWF to platelets in the presence of ristocetin, inhibited platelet adherence to human artery subendothelium when present in normal flowing blood.	Ristocetin	249-259	von Willebrand factor	Homo sapiens	73-76
3917314-1	1985	A monoclonal antibody directed against the von Willebrand factor moiety (vWF) of factor VIII-von Willebrand factor (FVIII-vWF), which blocks ristocetin-induced platelet aggregation as well as the binding of FVIII-vWF to platelets in the presence of ristocetin, inhibited platelet adherence to human artery subendothelium when present in normal flowing blood.	Ristocetin	249-259	von Willebrand factor	Homo sapiens	43-64
3917314-1	1985	A monoclonal antibody directed against the von Willebrand factor moiety (vWF) of factor VIII-von Willebrand factor (FVIII-vWF), which blocks ristocetin-induced platelet aggregation as well as the binding of FVIII-vWF to platelets in the presence of ristocetin, inhibited platelet adherence to human artery subendothelium when present in normal flowing blood.	Ristocetin	249-259	coagulation factor VIII	Homo sapiens	116-121
3917314-1	1985	A monoclonal antibody directed against the von Willebrand factor moiety (vWF) of factor VIII-von Willebrand factor (FVIII-vWF), which blocks ristocetin-induced platelet aggregation as well as the binding of FVIII-vWF to platelets in the presence of ristocetin, inhibited platelet adherence to human artery subendothelium when present in normal flowing blood.	Ristocetin	249-259	von Willebrand factor	Homo sapiens	122-125
3917314-1	1985	A monoclonal antibody directed against the von Willebrand factor moiety (vWF) of factor VIII-von Willebrand factor (FVIII-vWF), which blocks ristocetin-induced platelet aggregation as well as the binding of FVIII-vWF to platelets in the presence of ristocetin, inhibited platelet adherence to human artery subendothelium when present in normal flowing blood.	Ristocetin	249-259	von Willebrand factor	Homo sapiens	122-125
3878608-4	1985	Binding of two distinct antibodies at one of these epitopes was associated with enhancement of the rate of vWf-dependent platelet agglutination in the presence of ristocetin.	Ristocetin	163-173	von Willebrand factor	Homo sapiens	107-110
3160414-4	1985	Treatment of washed platelets with plasmin resulted in progressive loss of GpIb as measured by fluorescence flow cytometry and by loss of agglutination response when combined with ristocetin in the presence of vWF.	Ristocetin	180-190	plasminogen	Homo sapiens	35-42
2414486-0	1985	[Studies on the effects of five monoclonal antibodies, polyclonal rabbit antibody and homologous antibody to human F VIII/vWF on ristocetin-induced platelet agglutination and platelet retention by glass bead column].	Ristocetin	129-139	cytochrome c oxidase subunit 8A	Homo sapiens	117-121
2414486-0	1985	[Studies on the effects of five monoclonal antibodies, polyclonal rabbit antibody and homologous antibody to human F VIII/vWF on ristocetin-induced platelet agglutination and platelet retention by glass bead column].	Ristocetin	129-139	von Willebrand factor	Homo sapiens	122-125
2864750-1	1985	This study compares the ability of unmodified and carbohydrate-modified forms of factor VIII/von Willebrand factor (FVIII/vWF) protein to bind to platelets in the presence of ristocetin or thrombin.	Ristocetin	175-185	coagulation factor VIII	Homo sapiens	116-121
2864750-1	1985	This study compares the ability of unmodified and carbohydrate-modified forms of factor VIII/von Willebrand factor (FVIII/vWF) protein to bind to platelets in the presence of ristocetin or thrombin.	Ristocetin	175-185	von Willebrand factor	Homo sapiens	122-125
3918558-3	1985	The purified IgA also interacted with normal platelets to inhibit ristocetin-induced platelet aggregation (RIPA).	Ristocetin	66-76	CD79a molecule	Homo sapiens	13-16
3155489-6	1985	Plasmin, 0.05 to 1.0 CU/mL, reduced ristocetin-mediated agglutination of washed platelets in the presence of von Willebrand factor (vWF) from 66% of control to 2% of control, following a one-hour incubation.	Ristocetin	36-46	von Willebrand factor	Homo sapiens	109-130
3155489-6	1985	Plasmin, 0.05 to 1.0 CU/mL, reduced ristocetin-mediated agglutination of washed platelets in the presence of von Willebrand factor (vWF) from 66% of control to 2% of control, following a one-hour incubation.	Ristocetin	36-46	von Willebrand factor	Homo sapiens	132-135
3155489-9	1985	By use of an enzyme-linked immunosorbent assay (ELISA) based immunoinhibition assay for glycocalicin, we were able to demonstrate that plasmin treatment of washed platelets released a glycocalicin-related antigen into the surrounding medium and that appearance of this material corresponding to loss of vWF-dependent, ristocetin-induced agglutination.	Ristocetin	318-328	plasminogen	Homo sapiens	135-142
6440307-1	1984	Ristocetin, protamine and Polybrene promote factor VIII:vWF binding and agglutination of formalinized platelets.	Ristocetin	0-10	cytochrome c oxidase subunit 8A	Homo sapiens	51-55
6241752-3	1984	In the presence of a small amount of normal vWF, ristocetin-induced agglutination of patient platelets was enhanced with low concentrations of ristocetin.	Ristocetin	49-59	von Willebrand factor	Homo sapiens	44-47
6241752-3	1984	In the presence of a small amount of normal vWF, ristocetin-induced agglutination of patient platelets was enhanced with low concentrations of ristocetin.	Ristocetin	143-153	von Willebrand factor	Homo sapiens	44-47
6239876-1	1984	To better define the role of carbohydrate in the structure and ristocetin cofactor activity of von Willebrand factor, we have removed up to 83% of total hexose by sequential treatment of the molecule with endo-beta-N-acetyl-glucosaminidase F (endo F), neuraminidase, and beta-galactosidase.	Ristocetin	63-73	von Willebrand factor	Homo sapiens	95-116
6239876-7	1984	Further treatment of von Willebrand factor with neuraminidase and beta-galactosidase reduced the D-galactose to 15% and ristocetin cofactor activity to 57%.	Ristocetin	120-130	von Willebrand factor	Homo sapiens	21-42
6239876-7	1984	Further treatment of von Willebrand factor with neuraminidase and beta-galactosidase reduced the D-galactose to 15% and ristocetin cofactor activity to 57%.	Ristocetin	120-130	neuraminidase 1	Homo sapiens	48-61
6239876-7	1984	Further treatment of von Willebrand factor with neuraminidase and beta-galactosidase reduced the D-galactose to 15% and ristocetin cofactor activity to 57%.	Ristocetin	120-130	galactosidase beta 1	Homo sapiens	66-84
6239876-8	1984	A similar decrease in ristocetin cofactor activity was seen if von Willebrand factor was treated only with neuraminidase and beta-galactosidase.	Ristocetin	22-32	von Willebrand factor	Homo sapiens	63-84
6239876-8	1984	A similar decrease in ristocetin cofactor activity was seen if von Willebrand factor was treated only with neuraminidase and beta-galactosidase.	Ristocetin	22-32	neuraminidase 1	Homo sapiens	107-120
6239876-8	1984	A similar decrease in ristocetin cofactor activity was seen if von Willebrand factor was treated only with neuraminidase and beta-galactosidase.	Ristocetin	22-32	galactosidase beta 1	Homo sapiens	125-143
2580547-2	1985	This antibody is a potent inhibitor of von Willebrand factor activity (VIII:vWF) in that it can totally neutralize ristocetin-induced aggregation of platelet rich plasma and inhibit platelet adhesion at high flow rates.	Ristocetin	115-125	cytochrome c oxidase subunit 8A	Homo sapiens	71-75
2580547-2	1985	This antibody is a potent inhibitor of von Willebrand factor activity (VIII:vWF) in that it can totally neutralize ristocetin-induced aggregation of platelet rich plasma and inhibit platelet adhesion at high flow rates.	Ristocetin	115-125	von Willebrand factor	Homo sapiens	76-79
2580547-5	1985	Results obtained in these patients showed a high degree of correlation between the monoclonally-defined epitope and VIII:vWF levels measured by ristocetin-induced aggregation of washed platelets.	Ristocetin	144-154	cytochrome c oxidase subunit 8A	Homo sapiens	116-120
2580547-5	1985	Results obtained in these patients showed a high degree of correlation between the monoclonally-defined epitope and VIII:vWF levels measured by ristocetin-induced aggregation of washed platelets.	Ristocetin	144-154	von Willebrand factor	Homo sapiens	121-124
6440307-1	1984	Ristocetin, protamine and Polybrene promote factor VIII:vWF binding and agglutination of formalinized platelets.	Ristocetin	0-10	von Willebrand factor	Homo sapiens	56-59
6438823-2	1984	Limited reduction of disulfide bonds in this complex by NADPH, thioredoxin reductase and thioredoxin leads to partial disaggregation of the multimeric VIII:vWF with concomitant loss of its platelet agglutinating activity in the presence of ristocetin, and with dissociation of factor VIII:C from the complex.	Ristocetin	240-250	peroxiredoxin 5	Homo sapiens	63-84
6438823-2	1984	Limited reduction of disulfide bonds in this complex by NADPH, thioredoxin reductase and thioredoxin leads to partial disaggregation of the multimeric VIII:vWF with concomitant loss of its platelet agglutinating activity in the presence of ristocetin, and with dissociation of factor VIII:C from the complex.	Ristocetin	240-250	thioredoxin	Homo sapiens	63-74
6438823-2	1984	Limited reduction of disulfide bonds in this complex by NADPH, thioredoxin reductase and thioredoxin leads to partial disaggregation of the multimeric VIII:vWF with concomitant loss of its platelet agglutinating activity in the presence of ristocetin, and with dissociation of factor VIII:C from the complex.	Ristocetin	240-250	cytochrome c oxidase subunit 8A	Homo sapiens	151-155
6438823-2	1984	Limited reduction of disulfide bonds in this complex by NADPH, thioredoxin reductase and thioredoxin leads to partial disaggregation of the multimeric VIII:vWF with concomitant loss of its platelet agglutinating activity in the presence of ristocetin, and with dissociation of factor VIII:C from the complex.	Ristocetin	240-250	von Willebrand factor	Homo sapiens	156-159
6332119-4	1984	CLB-RAg 35 also inhibited the ristocetin-induced platelet aggregation and the binding of FVIII-VWF to the platelet in the presence of ristocetin but did not affect the binding of FVIII-VWF to collagen.	Ristocetin	30-40	citramalyl-CoA lyase	Homo sapiens	0-3
6332119-4	1984	CLB-RAg 35 also inhibited the ristocetin-induced platelet aggregation and the binding of FVIII-VWF to the platelet in the presence of ristocetin but did not affect the binding of FVIII-VWF to collagen.	Ristocetin	134-144	citramalyl-CoA lyase	Homo sapiens	0-3
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.	Ristocetin	311-321	fibrinogen gamma chain	Homo sapiens	110-147
6332119-4	1984	CLB-RAg 35 also inhibited the ristocetin-induced platelet aggregation and the binding of FVIII-VWF to the platelet in the presence of ristocetin but did not affect the binding of FVIII-VWF to collagen.	Ristocetin	134-144	coagulation factor VIII	Homo sapiens	89-94
6332119-4	1984	CLB-RAg 35 also inhibited the ristocetin-induced platelet aggregation and the binding of FVIII-VWF to the platelet in the presence of ristocetin but did not affect the binding of FVIII-VWF to collagen.	Ristocetin	134-144	von Willebrand factor	Homo sapiens	95-98
6435280-6	1984	The combined results suggest that as well as the ristocetin-dependent, divalent cation-independent binding of FVIII/vWF to glycoprotein Ib, there is a divalent cation-dependent binding of FVIII/vWF to the activated platelet surface which is mediated via the glycoprotein IIb/IIIa complex.	Ristocetin	49-59	coagulation factor VIII	Homo sapiens	110-115
6435280-6	1984	The combined results suggest that as well as the ristocetin-dependent, divalent cation-independent binding of FVIII/vWF to glycoprotein Ib, there is a divalent cation-dependent binding of FVIII/vWF to the activated platelet surface which is mediated via the glycoprotein IIb/IIIa complex.	Ristocetin	49-59	von Willebrand factor	Homo sapiens	116-119
6204681-10	1984	When these conclusions are considered within the context of a spatial map of the vWF protein surface developed by competitive displacement analysis, the epitopes related to platelet adhesion appear to be spaced and differ from those involved in ristocetin-induced platelet-platelet interaction.	Ristocetin	245-255	von Willebrand factor	Homo sapiens	81-84
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.	Ristocetin	311-321	von Willebrand factor	Homo sapiens	189-192
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.	Ristocetin	311-321	fibrinogen beta chain	Homo sapiens	110-120
6426553-1	1984	We have studied the role of factor VIII-von Willebrand factor (FVIII-vWF) in both platelet adherence to subendothelium and ristocetin-induced platelet aggregation using monoclonal antibodies to human FVIII-vWF.	Ristocetin	123-133	coagulation factor VIII	Homo sapiens	63-68
6426553-1	1984	We have studied the role of factor VIII-von Willebrand factor (FVIII-vWF) in both platelet adherence to subendothelium and ristocetin-induced platelet aggregation using monoclonal antibodies to human FVIII-vWF.	Ristocetin	123-133	von Willebrand factor	Homo sapiens	69-72
6426553-7	1984	These results demonstrate that a domain is present on the FVIII-vWF molecule that is associated both with ristocetin-induced aggregation and with the ability of FVIII-vWF to support platelet adherence to the subendothelium.	Ristocetin	106-116	coagulation factor VIII	Homo sapiens	58-63
6610952-1	1984	By the use of a series of monoclonal antibodies against platelet membrane glycoproteins (GP) and the von Willebrand factor (vWF), it is shown that thrombin-induced binding to GP IIb/IIIa involves a different site on vWF from ristocetin-induced binding to GP Ib.	Ristocetin	225-235	coagulation factor II, thrombin	Homo sapiens	147-155
6610952-1	1984	By the use of a series of monoclonal antibodies against platelet membrane glycoproteins (GP) and the von Willebrand factor (vWF), it is shown that thrombin-induced binding to GP IIb/IIIa involves a different site on vWF from ristocetin-induced binding to GP Ib.	Ristocetin	225-235	integrin subunit alpha 2b	Homo sapiens	175-181
6424741-5	1984	Pretreatment of FVIII-vWF with the calcium chelator EGTA (10 mM) resulted in loss of the ability to facilitate platelet adherence, while the ristocetin cofactor activity remained intact.	Ristocetin	141-151	coagulation factor VIII	Homo sapiens	16-21
6424741-5	1984	Pretreatment of FVIII-vWF with the calcium chelator EGTA (10 mM) resulted in loss of the ability to facilitate platelet adherence, while the ristocetin cofactor activity remained intact.	Ristocetin	141-151	von Willebrand factor	Homo sapiens	22-25
6426499-0	1984	The agglutination of human platelets by botrocetin: evidence that botrocetin and ristocetin act at different sites on the factor VIII molecule and platelet membrane.	Ristocetin	81-91	coagulation factor VIII	Homo sapiens	122-133
6426499-2	1984	The site of binding of FVIII to the platelet in response to ristocetin or botrocetin involves the glycoprotein I complex.	Ristocetin	60-70	coagulation factor VIII	Homo sapiens	23-28
6426499-9	1984	This suggested that the site of interaction on the FVIII molecule for botrocetin and ristocetin are different.	Ristocetin	85-95	coagulation factor VIII	Homo sapiens	51-56
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.	Ristocetin	140-150	von Willebrand factor	Homo sapiens	79-82
6231945-1	1984	Platelet glycoprotein I (GPI) is known to be required for the interaction of platelets with ristocetin and factor VIII:von Willebrand factor (VIII:vWf).	Ristocetin	92-102	glucose-6-phosphate isomerase	Homo sapiens	9-23
6231945-1	1984	Platelet glycoprotein I (GPI) is known to be required for the interaction of platelets with ristocetin and factor VIII:von Willebrand factor (VIII:vWf).	Ristocetin	92-102	glucose-6-phosphate isomerase	Homo sapiens	25-28
6421343-6	1984	Collagen fibrils not only bound FWP, but also adsorbed the FVIII complex with preferential adsorption of the forms of FVIIIR:Ag with the greatest ristocetin cofactor (FVIIIR:RCoF) activity.	Ristocetin	146-156	coagulation factor VIII	Homo sapiens	59-64
6607757-2	1984	The amount of functional vWF activity was assessed by ristocetin-induced platelet aggregation and by a radioreceptor platelet assay.	Ristocetin	54-64	von Willebrand factor	Homo sapiens	25-28
6232731-4	1984	However, in the presence of 0.75 mg/ml ristocetin, added vWF (2.9 micrograms/ml) caused a further 6.3 +/- 3.8% decrease in control platelet EPM, but caused no significant decrease in the enzyme-treated platelets (p less than 0.05).	Ristocetin	39-49	von Willebrand factor	Homo sapiens	57-60
6426553-7	1984	These results demonstrate that a domain is present on the FVIII-vWF molecule that is associated both with ristocetin-induced aggregation and with the ability of FVIII-vWF to support platelet adherence to the subendothelium.	Ristocetin	106-116	von Willebrand factor	Homo sapiens	64-67
6426553-7	1984	These results demonstrate that a domain is present on the FVIII-vWF molecule that is associated both with ristocetin-induced aggregation and with the ability of FVIII-vWF to support platelet adherence to the subendothelium.	Ristocetin	106-116	von Willebrand factor	Homo sapiens	167-170
6426553-8	1984	Based on these observations, it is concluded that ristocetin-induced binding of FVIII-vWF to platelets reflects, at least in part, a physiologic mechanism regulating the function of FVIII-vWF in primary hemostasis.	Ristocetin	50-60	coagulation factor VIII	Homo sapiens	80-85
6426553-8	1984	Based on these observations, it is concluded that ristocetin-induced binding of FVIII-vWF to platelets reflects, at least in part, a physiologic mechanism regulating the function of FVIII-vWF in primary hemostasis.	Ristocetin	50-60	von Willebrand factor	Homo sapiens	86-89
6426553-8	1984	Based on these observations, it is concluded that ristocetin-induced binding of FVIII-vWF to platelets reflects, at least in part, a physiologic mechanism regulating the function of FVIII-vWF in primary hemostasis.	Ristocetin	50-60	coagulation factor VIII	Homo sapiens	182-187
6426553-8	1984	Based on these observations, it is concluded that ristocetin-induced binding of FVIII-vWF to platelets reflects, at least in part, a physiologic mechanism regulating the function of FVIII-vWF in primary hemostasis.	Ristocetin	50-60	von Willebrand factor	Homo sapiens	188-191
6416054-2	1983	In this report the authors describe a 17-month-old male with Platelet-type von Willebrand"s disease, inherited from the paternal side of his family, who developed an inhibitor specific to Factor VIII:C. The patient"s plasma inhibited normal plasma VIII:C and partially purified VIII:C; it did not appear directed against normal VIIIR:Ag or ristocetin cofactor.	Ristocetin	340-350	cytochrome c oxidase subunit 8A	Homo sapiens	195-199
6084622-3	1984	Both monoclonal antibodies are capable of inhibiting strongly the FVIII.vWF associated ristocetin cofactor activity.	Ristocetin	87-97	coagulation factor VIII	Homo sapiens	66-71
6084622-3	1984	Both monoclonal antibodies are capable of inhibiting strongly the FVIII.vWF associated ristocetin cofactor activity.	Ristocetin	87-97	von Willebrand factor	Homo sapiens	72-75
6232731-5	1984	In the presence of 0.3 mg/ml ristocetin, added vWF (2.9-14.5 micrograms/ml) caused a small but significant decrease in control platelet EPM, but caused no significant decrease in the enzyme-treated platelets.	Ristocetin	29-39	von Willebrand factor	Homo sapiens	47-50
6605342-5	1983	In this study, the binding of bovine VWF and ristocetin to bovine platelets was investigated using fluorescence anisotropy of derivatized monomer protein and ristocetin and also by radioisotope methods using 125I-labeled monomer and native protein.	Ristocetin	158-168	von Willebrand factor	Bos taurus	37-40
6605342-7	1983	VWF binding to formaldehyde-fixed platelets was dependent on the presence of a promoter such as ristocetin.	Ristocetin	96-106	von Willebrand factor	Bos taurus	0-3
6605342-8	1983	The monomer and multimer VWF bound equally well in the presence of low ristocetin concentrations.	Ristocetin	71-81	von Willebrand factor	Bos taurus	25-28
6605342-11	1983	Ristocetin promoted the formation of small platelet aggregates, an effect that was amplified by the presence of VWF.	Ristocetin	0-10	von Willebrand factor	Bos taurus	112-115
6307433-1	1983	It is known that the antibiotic ristocetin exposes the platelet membrane receptor for factor VIII/von Willebrand glycoprotein (FVIII/vWF).	Ristocetin	32-42	coagulation factor VIII	Homo sapiens	127-132
6600621-8	1983	The data presented here give further support to the proposal that ristocetin-human VIIIR:WF and bovine VIIIR:WF share a common receptor on the platelet surface and indicate that this structure plays an important role in thrombin-induced platelet responses.	Ristocetin	66-76	coagulation factor II, thrombin	Bos taurus	220-228
6421207-2	1983	The assay of factor VIII, co-factor of Ristocetin (VIIIR:Co) is a relatively delicate procedure which is presently reserved to specialized laboratories.	Ristocetin	39-49	cytochrome c oxidase subunit 8A	Homo sapiens	20-24
6336654-0	1983	Studies with a murine monoclonal antibody that abolishes ristocetin-induced binding of von Willebrand factor to platelets: additional evidence in support of GPIb as a platelet receptor for von Willebrand factor.	Ristocetin	57-67	von Willebrand factor	Bos taurus	87-108
6336654-0	1983	Studies with a murine monoclonal antibody that abolishes ristocetin-induced binding of von Willebrand factor to platelets: additional evidence in support of GPIb as a platelet receptor for von Willebrand factor.	Ristocetin	57-67	von Willebrand factor	Bos taurus	189-210
6401215-0	1983	The relationship of the properties of antihemophilic factor (factor VIII) that support ristocetin-induced platelet agglutination (factor VIIIR:RC) and platelet retention by glass beads as demonstrated by a monoclonal antibody.	Ristocetin	87-97	coagulation factor VIII	Mus musculus	61-72
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.	Ristocetin	139-149	cytochrome c oxidase subunit 8A	Homo sapiens	13-17
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.	Ristocetin	139-149	cytochrome c oxidase subunit 8A	Homo sapiens	52-56
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.	Ristocetin	139-149	von Willebrand factor	Homo sapiens	57-60
6404328-4	1983	About 60% of this procoagulant mol wt approximately 2.6 X 10(5) VIII:C form in plasma is present in noncovalent complexes with larger VIII:vWF multimers, which attach reversibly to platelet surfaces in the presence of ristocetin.	Ristocetin	218-228	cytochrome c oxidase subunit 8A	Homo sapiens	64-70
6404328-4	1983	About 60% of this procoagulant mol wt approximately 2.6 X 10(5) VIII:C form in plasma is present in noncovalent complexes with larger VIII:vWF multimers, which attach reversibly to platelet surfaces in the presence of ristocetin.	Ristocetin	218-228	cytochrome c oxidase subunit 8A	Homo sapiens	64-68
6307433-1	1983	It is known that the antibiotic ristocetin exposes the platelet membrane receptor for factor VIII/von Willebrand glycoprotein (FVIII/vWF).	Ristocetin	32-42	von Willebrand factor	Homo sapiens	133-136
6307433-5	1983	With ristocetin present, the amount of 125I-FVIII/vWF that became platelet-bound correlated closely with the onset, rate, and extent of platelet aggregation.	Ristocetin	5-15	coagulation factor VIII	Homo sapiens	44-49
6307433-5	1983	With ristocetin present, the amount of 125I-FVIII/vWF that became platelet-bound correlated closely with the onset, rate, and extent of platelet aggregation.	Ristocetin	5-15	von Willebrand factor	Homo sapiens	50-53
6307433-6	1983	In contrast, at every thrombin concentration tested, the amount of 125I-FVIII/vWF that specifically bound to platelets was about 6% of that observed with ristocetin.	Ristocetin	154-164	von Willebrand factor	Homo sapiens	78-81
6815191-4	1982	The size of the functional unit of the ristocetin cofactor of the factor VIII complex was determined as being approximately 330,000 in both citrated and heparinized samples.	Ristocetin	39-49	cytochrome c oxidase subunit 8A	Homo sapiens	73-77
6814554-7	1982	These data strongly suggest that the sites on the FVIII molecule or the multimeric forms involved for ristocetin and botrocetin are different and that the ristocetin reaction is more closely aligned to the physiologic function of FVIII.	Ristocetin	155-165	coagulation factor VIII	Homo sapiens	230-235
6183384-7	1982	Ristocetin promoted the binding of bovine factor VIII: R to platelets but did not promote the agglutination of platelets by bovine factor VIII: R. Concentrations of dextran sulfate that strongly inhibited agglutination actually increased the binding of factor VIII: R to platelets.	Ristocetin	0-10	coagulation factor VIII	Bos taurus	42-53
6286015-3	1982	Binding of patient VIII/vWF to washed normal platelets was within normal limits, whereas binding of normal VIII/vWF to patient platelets was significantly increased (p less than 0.001 at 0.6 mg/ml ristocetin).	Ristocetin	197-207	cytochrome c oxidase subunit 8A	Homo sapiens	107-111
7164028-0	1982	Binding of porcine von Willebrand factor to human platelets in the presence of ristocetin.	Ristocetin	79-89	von Willebrand factor	Homo sapiens	19-40
7164028-1	1982	The interaction of porcine von Willebrand factor (vWF) with human platelets in the presence of ristocetin was examined.	Ristocetin	95-105	von Willebrand factor	Homo sapiens	27-48
7164028-1	1982	The interaction of porcine von Willebrand factor (vWF) with human platelets in the presence of ristocetin was examined.	Ristocetin	95-105	von Willebrand factor	Homo sapiens	50-53
7164028-3	1982	Assuming vWF to be a tetramer with a MW of 9.5 x 10(5), approximately 94,000 vWF binding sites per platelet were found with an average binding constant of 2.1 x 10(-8)M. Human vWF competed with the porcine protein for this site only in the presence of ristocetin.	Ristocetin	252-262	von Willebrand factor	Homo sapiens	9-12
6810495-5	1982	The functional studies reveal that after incubation with either of the Fab" fragments, platelets retain their reactivity in the ristocetin cofactor assay.	Ristocetin	128-138	FA complementation group B	Homo sapiens	71-74
6895702-3	1982	In general, thrombin-induced platelet aggregation was strongly affected by the amines while the effect was weak on cell aggregation by ristocetin.	Ristocetin	135-145	coagulation factor II, thrombin	Homo sapiens	12-20
6971912-1	1981	A patient with a reduced response to the platelet-aggregating agent ristocetin and a prolonged bleeding time was found to have an abnormally high level of vWf as measured by Laurell immunoelectrophoresis.	Ristocetin	68-78	von Willebrand factor	Homo sapiens	155-158
6752879-16	1982	The ristocetin-induced platelet membrane receptor for vWF seems to be glycoprotein Ib, platelet adhesion being also abnormal in Giant Platelet Syndrome.	Ristocetin	4-14	von Willebrand factor	Homo sapiens	54-57
6752879-17	1982	The in vivo counterpart for ristocetin is unknown, but it is possible that collagen, microfibrils, thrombin (which also induces the platelet receptor for vWF or sialidases (asialo-human vWF is able to directly bind to the platelet membrane) could replace ristocetin.	Ristocetin	255-265	coagulation factor II, thrombin	Homo sapiens	99-107
6752879-17	1982	The in vivo counterpart for ristocetin is unknown, but it is possible that collagen, microfibrils, thrombin (which also induces the platelet receptor for vWF or sialidases (asialo-human vWF is able to directly bind to the platelet membrane) could replace ristocetin.	Ristocetin	255-265	von Willebrand factor	Homo sapiens	186-189
6797459-8	1981	The binding of factor VIII/von Willebrand factor to platelet membrane in the presence of ristocetin was decreased in the binding site for factor VIII/von Willebrand factor to allow platelet adhesion to subendothelium.	Ristocetin	89-99	coagulation factor VIII	Bos taurus	15-26
6797459-8	1981	The binding of factor VIII/von Willebrand factor to platelet membrane in the presence of ristocetin was decreased in the binding site for factor VIII/von Willebrand factor to allow platelet adhesion to subendothelium.	Ristocetin	89-99	von Willebrand factor	Homo sapiens	27-48
6797459-8	1981	The binding of factor VIII/von Willebrand factor to platelet membrane in the presence of ristocetin was decreased in the binding site for factor VIII/von Willebrand factor to allow platelet adhesion to subendothelium.	Ristocetin	89-99	coagulation factor VIII	Bos taurus	138-149
6797459-8	1981	The binding of factor VIII/von Willebrand factor to platelet membrane in the presence of ristocetin was decreased in the binding site for factor VIII/von Willebrand factor to allow platelet adhesion to subendothelium.	Ristocetin	89-99	von Willebrand factor	Homo sapiens	150-171
6211398-4	1982	Fab fragments from the antiserum inhibited ristocetin-induced aggregation of platelets and partially inhibited collagen-induced aggregation but did not affect ADP aggregation.	Ristocetin	43-53	FA complementation group B	Homo sapiens	0-3
6797089-3	1981	We have studied the in vitro effects of ticlopidine on fibrinogen binding induced by ADP and adrenaline as well as factor VIII/vWF binding induced by ristocetin.	Ristocetin	150-160	von Willebrand factor	Homo sapiens	127-130
6797089-5	1981	The binding of 125I-factor VIII/vWF in the presence of 1 mg/ml ristocetin was measured in both washed and paraformaldehyde-fixed platelets.	Ristocetin	63-73	von Willebrand factor	Homo sapiens	32-35
6767976-2	1980	We have now identified 20 persons from five families whose qualitatively abnormal FVIII/vWF shows heightened responsiveness to ristocetin.	Ristocetin	127-137	coagulation factor VIII	Homo sapiens	82-87
6967100-1	1980	Ristocetin induces platelet agglutination in the presence of human factor VIII-associated ristocetin cofactor (vWF).	Ristocetin	0-10	von Willebrand factor	Homo sapiens	111-114
6967100-1	1980	Ristocetin induces platelet agglutination in the presence of human factor VIII-associated ristocetin cofactor (vWF).	Ristocetin	90-100	von Willebrand factor	Homo sapiens	111-114
6967100-4	1980	Radioiodinated vWF, a disulfide-linked polymer of 230,000 dalton subunits, attached to formalinized human platelets only in the presence of ristocetin.	Ristocetin	140-150	von Willebrand factor	Homo sapiens	15-18
6967100-6	1980	Ristocetin-induced binding was inhibited by vancomycin, unlabeled-purified vWF polymers, normal and hemophilia A plasma, and rabbit anti-human vWF.	Ristocetin	0-10	von Willebrand factor	Homo sapiens	75-78
6967100-6	1980	Ristocetin-induced binding was inhibited by vancomycin, unlabeled-purified vWF polymers, normal and hemophilia A plasma, and rabbit anti-human vWF.	Ristocetin	0-10	von Willebrand factor	Homo sapiens	143-146
6967100-11	1980	These results indicate that (1) the initial binding of human vWF polymers to platelets is a specific interaction which requires the presence of ristocetin; (2) ristocetin and human vWF do not form persistent complexes in solution; and (3) the association of ristocetin and platelets is of low affinity.	Ristocetin	144-154	von Willebrand factor	Homo sapiens	61-64
6967100-11	1980	These results indicate that (1) the initial binding of human vWF polymers to platelets is a specific interaction which requires the presence of ristocetin; (2) ristocetin and human vWF do not form persistent complexes in solution; and (3) the association of ristocetin and platelets is of low affinity.	Ristocetin	160-170	von Willebrand factor	Homo sapiens	61-64
6967100-11	1980	These results indicate that (1) the initial binding of human vWF polymers to platelets is a specific interaction which requires the presence of ristocetin; (2) ristocetin and human vWF do not form persistent complexes in solution; and (3) the association of ristocetin and platelets is of low affinity.	Ristocetin	160-170	von Willebrand factor	Homo sapiens	61-64
6779399-4	1980	When the same platelets were suspended in human plasma and ristocetin or collagen was added, more clumps were formed and more vWF (human) was associated with these clumps.	Ristocetin	59-69	von Willebrand factor	Homo sapiens	126-129
6773982-11	1980	In subtype IIB, binding of factor VIII/von Willebrand factor to platelets occurred at lower concentrations of ristocetin than required for normal and multimers of smaller size than in normal bound.	Ristocetin	110-120	von Willebrand factor	Homo sapiens	39-60
6767976-2	1980	We have now identified 20 persons from five families whose qualitatively abnormal FVIII/vWF shows heightened responsiveness to ristocetin.	Ristocetin	127-137	von Willebrand factor	Homo sapiens	88-91
6767976-3	1980	We have classified this form of the disease as Type IIB and reclassified as Type IIA the form previously described as Type II, in which the interaction of the abnormal FVIII/vWF with platelets is decreased or absent in the presence of ristocetin.	Ristocetin	235-245	von Willebrand factor	Homo sapiens	174-177
6767976-4	1980	The enhanced reactivity of FVIII/vWF in Type IIB was evident in studies of ristocetin-induced platelet agglutination and of binding of FVIII/vWF to platelets in the presence of ristocetin.	Ristocetin	75-85	coagulation factor VIII	Homo sapiens	27-32
6767976-4	1980	The enhanced reactivity of FVIII/vWF in Type IIB was evident in studies of ristocetin-induced platelet agglutination and of binding of FVIII/vWF to platelets in the presence of ristocetin.	Ristocetin	75-85	von Willebrand factor	Homo sapiens	33-36
6767976-4	1980	The enhanced reactivity of FVIII/vWF in Type IIB was evident in studies of ristocetin-induced platelet agglutination and of binding of FVIII/vWF to platelets in the presence of ristocetin.	Ristocetin	177-187	coagulation factor VIII	Homo sapiens	27-32
6767976-4	1980	The enhanced reactivity of FVIII/vWF in Type IIB was evident in studies of ristocetin-induced platelet agglutination and of binding of FVIII/vWF to platelets in the presence of ristocetin.	Ristocetin	177-187	von Willebrand factor	Homo sapiens	33-36
317771-0	1979	von Willebrand factor: characterization of interaction among von Willebrand factor, ristocetin and platelet.	Ristocetin	84-94	von Willebrand factor	Homo sapiens	0-21
6773172-1	1980	When compared to the values obtained in healthy normal-weight, normolipemic controls, the plasma level of ristocetin-cofactor (VIII:R-cof.)	Ristocetin	106-116	cytochrome c oxidase subunit 8A	Homo sapiens	127-131
6965350-4	1980	However, binding was highly dependent on ristocetin concentration, as the number of human factor VIII/von Willebrand factor molecules bound per platelet was a function of the ristocetin concentration.	Ristocetin	41-51	cytochrome c oxidase subunit 8A	Homo sapiens	97-101
6965350-4	1980	However, binding was highly dependent on ristocetin concentration, as the number of human factor VIII/von Willebrand factor molecules bound per platelet was a function of the ristocetin concentration.	Ristocetin	41-51	von Willebrand factor	Homo sapiens	102-123
6965350-4	1980	However, binding was highly dependent on ristocetin concentration, as the number of human factor VIII/von Willebrand factor molecules bound per platelet was a function of the ristocetin concentration.	Ristocetin	175-185	cytochrome c oxidase subunit 8A	Homo sapiens	97-101
6965350-4	1980	However, binding was highly dependent on ristocetin concentration, as the number of human factor VIII/von Willebrand factor molecules bound per platelet was a function of the ristocetin concentration.	Ristocetin	175-185	von Willebrand factor	Homo sapiens	102-123
6965350-5	1980	At a ristocetin concentration of 0.55 mg/ml, each platelet binds approximately 11,000 factor VIII/von Willebrand factor molecules per platelet.	Ristocetin	5-15	cytochrome c oxidase subunit 8A	Homo sapiens	93-97
6965350-5	1980	At a ristocetin concentration of 0.55 mg/ml, each platelet binds approximately 11,000 factor VIII/von Willebrand factor molecules per platelet.	Ristocetin	5-15	von Willebrand factor	Homo sapiens	98-119
6965350-8	1980	As with ristocetin-induced platelet agglutination, the carbohydrate content plays a significant role in the binding of the factor VIII/von Willebrand factor protein to the platelet.	Ristocetin	8-18	cytochrome c oxidase subunit 8A	Homo sapiens	130-134
6965350-8	1980	As with ristocetin-induced platelet agglutination, the carbohydrate content plays a significant role in the binding of the factor VIII/von Willebrand factor protein to the platelet.	Ristocetin	8-18	von Willebrand factor	Homo sapiens	135-156
888824-5	1977	The results obtained support the hypothesis that the binding of the carbohydrate groups of factor VIII plays an important role in the induction of platelet aggregation and in the maintenance of aggregates formed in response to the treatment of platelet-rich plasma with bovine factor VIII or ristocetin.	Ristocetin	292-302	coagulation factor VIII	Bos taurus	277-288
316281-1	1979	An inexpensive assay for von Willebrand factor using microtitration plates, formalin-fixed platelets, and ristocetin is described.	Ristocetin	106-116	von Willebrand factor	Homo sapiens	25-46
315561-4	1979	Our results demonstrate a highly significant linear correlation between the degree of FVIII/vWF receptor binding and the extent of ristocetin-induced platelet aggregation.	Ristocetin	131-141	coagulation factor VIII	Homo sapiens	86-91
315561-4	1979	Our results demonstrate a highly significant linear correlation between the degree of FVIII/vWF receptor binding and the extent of ristocetin-induced platelet aggregation.	Ristocetin	131-141	von Willebrand factor	Homo sapiens	92-95
508625-0	1979	Studies on the mechanism of ristocetin-induced platelet aggregation: binding of factor VIII to platelets.	Ristocetin	28-38	cytochrome c oxidase subunit 8A	Homo sapiens	87-91
508625-1	1979	The effect of ristocetin on the binding of [125I]factor VIII to platelets was studied.	Ristocetin	14-24	cytochrome c oxidase subunit 8A	Homo sapiens	56-60
508625-4	1979	Ristocetin increased the binding of F.VIII to both types of binding sites by increasing the affinity of F.VIII for the platelet and increasing the total number of platelet binding sites.	Ristocetin	0-10	cytochrome c oxidase subunit 8A	Homo sapiens	38-42
508625-4	1979	Ristocetin increased the binding of F.VIII to both types of binding sites by increasing the affinity of F.VIII for the platelet and increasing the total number of platelet binding sites.	Ristocetin	0-10	coagulation factor VIII	Homo sapiens	36-42
486540-1	1979	Both ristocetin-induced aggregation in the presence of human factor VIII and bovine factor VIII-induced aggregation of washed normal human platelets were inhibited or reversed by the addition of heparin or dextran sulfate.	Ristocetin	5-15	coagulation factor VIII	Bos taurus	61-72
486540-1	1979	Both ristocetin-induced aggregation in the presence of human factor VIII and bovine factor VIII-induced aggregation of washed normal human platelets were inhibited or reversed by the addition of heparin or dextran sulfate.	Ristocetin	5-15	coagulation factor VIII	Bos taurus	84-95
30781922-5	1979	The bovine factor VIII related protein as such directly binds to the platelet membrane (Kirby and Sha May Tang 1977) and thus represents a simpler system than ristocetin plus the human cofactor which may have to interact with each other before excerting their effect on the platelet membrane.	Ristocetin	159-169	coagulation factor VIII	Bos taurus	11-22
495016-0	1979	[Inhibitory effect of kallikrein on ristocetin-induced platelet aggregation (author"s transl)].	Ristocetin	36-46	kallikrein related peptidase 4	Homo sapiens	22-32
524146-4	1979	Recently, a third function of the F VIII "complex" was discovered with the help of ristocetin (von Willebrand"s Factor, VIIIR: RCo).	Ristocetin	83-93	coagulation factor VIII	Homo sapiens	34-40
307560-2	1978	The normal Factor VIII/von Willebrand factor protein has the ability to agglutinate or aggregate normal platelets in the presence of ristocetin (von Willebrand factor activity).	Ristocetin	133-143	von Willebrand factor	Homo sapiens	23-44
307560-2	1978	The normal Factor VIII/von Willebrand factor protein has the ability to agglutinate or aggregate normal platelets in the presence of ristocetin (von Willebrand factor activity).	Ristocetin	133-143	von Willebrand factor	Homo sapiens	145-166
309191-1	1978	The aggregation of platelets by the antibiotic, ristocetin, requires a plasma cofactor (VIII:vWF) and one or more specific binding sites on the platelet membrane.	Ristocetin	48-58	cytochrome c oxidase subunit 8A	Homo sapiens	88-92
309191-1	1978	The aggregation of platelets by the antibiotic, ristocetin, requires a plasma cofactor (VIII:vWF) and one or more specific binding sites on the platelet membrane.	Ristocetin	48-58	von Willebrand factor	Homo sapiens	93-96
309191-3	1978	In the presence of ristocetin (1.5 mg/ml), from 70 to 90% of the 125I-VIII:vWF became platelet-bound.	Ristocetin	19-29	cytochrome c oxidase subunit 8A	Homo sapiens	70-74
309191-3	1978	In the presence of ristocetin (1.5 mg/ml), from 70 to 90% of the 125I-VIII:vWF became platelet-bound.	Ristocetin	19-29	von Willebrand factor	Homo sapiens	75-78
309191-7	1978	It is concluded that VIII:vWF binds to the platelet membrane in the presence of ristocetin.	Ristocetin	80-90	cytochrome c oxidase subunit 8A	Homo sapiens	21-25
309191-7	1978	It is concluded that VIII:vWF binds to the platelet membrane in the presence of ristocetin.	Ristocetin	80-90	von Willebrand factor	Homo sapiens	26-29
307006-1	1978	Ristocetin will induce the agglutination of platelets in the presence of von Willebrand factor.	Ristocetin	0-10	von Willebrand factor	Homo sapiens	73-94
307006-2	1978	In previous studies, an electrostatic mechanism was proposed for this phenomenon wherein first the platelet"s surface charge is reduced by the binding of ristocetin and then the von Willebrand factor acts as a bridge between platelets.	Ristocetin	154-164	von Willebrand factor	Homo sapiens	178-199
653643-0	1978	Lithium inhibition of ristocetin-induced fibrinogen precipitation.	Ristocetin	22-32	fibrinogen beta chain	Homo sapiens	41-51
739056-3	1978	The most striking difference was a reduced or absent ristocetin-induced platelet aggregation in Nigerian platelet-rich plasma, probably due to a plasma component interacting with the von Willebrand activity (VWF), since factor VIII coagulant activity, factor VIII related antigen, and isolated VWF were normal or high by European standards.	Ristocetin	53-63	von Willebrand factor	Homo sapiens	208-211
739056-3	1978	The most striking difference was a reduced or absent ristocetin-induced platelet aggregation in Nigerian platelet-rich plasma, probably due to a plasma component interacting with the von Willebrand activity (VWF), since factor VIII coagulant activity, factor VIII related antigen, and isolated VWF were normal or high by European standards.	Ristocetin	53-63	von Willebrand factor	Homo sapiens	294-297
739058-1	1978	The addition of the antibiotic ristocetin to plasma accelerated the thrombin clotting time (TCT) in 20 out of 22 subjects.	Ristocetin	31-41	coagulation factor II, thrombin	Homo sapiens	68-76
739058-2	1978	Prior incubation of ristocetin with thrombin or plasma did not alter its effect on the TCT.	Ristocetin	20-30	coagulation factor II, thrombin	Homo sapiens	36-44
707435-1	1978	The ristocetin precipitation test was designed as a simplified test to detect fibrin monomers and fibrinogen/fibrin degradation products (FPD/fdp).	Ristocetin	4-14	fibrinogen beta chain	Homo sapiens	98-108
707435-4	1978	The ristocetin precipitation test is positive in plasmas collected from rabbits after the infusion of thrombin (2.7 u/kg) or thrombin and streptokinase (10,000 u/kg); the test is negative in plasmas from animals treated with streptokinase or saline solution alone.	Ristocetin	4-14	prothrombin	Oryctolagus cuniculus	102-110
707435-4	1978	The ristocetin precipitation test is positive in plasmas collected from rabbits after the infusion of thrombin (2.7 u/kg) or thrombin and streptokinase (10,000 u/kg); the test is negative in plasmas from animals treated with streptokinase or saline solution alone.	Ristocetin	4-14	prothrombin	Oryctolagus cuniculus	125-133
670391-9	1978	The fraction of 125I-VIII binding to platelets in the presence of ristocetin (containing the highest molecular weight forms of Factor VIII including the ristocetin cofactor) represented about 50% of the radioactivity present in plasma after infusion and showed a t 1/2 of 11.7 +/- 0.9 h (SEM) for the second phase.	Ristocetin	66-76	cytochrome c oxidase subunit 8A	Homo sapiens	21-25
670391-9	1978	The fraction of 125I-VIII binding to platelets in the presence of ristocetin (containing the highest molecular weight forms of Factor VIII including the ristocetin cofactor) represented about 50% of the radioactivity present in plasma after infusion and showed a t 1/2 of 11.7 +/- 0.9 h (SEM) for the second phase.	Ristocetin	66-76	cytochrome c oxidase subunit 8A	Homo sapiens	134-138
670391-9	1978	The fraction of 125I-VIII binding to platelets in the presence of ristocetin (containing the highest molecular weight forms of Factor VIII including the ristocetin cofactor) represented about 50% of the radioactivity present in plasma after infusion and showed a t 1/2 of 11.7 +/- 0.9 h (SEM) for the second phase.	Ristocetin	153-163	cytochrome c oxidase subunit 8A	Homo sapiens	21-25
343683-4	1978	In this disorder, the platelets are poorly aggregated by ristocetin, a defect ascribed to deficiency of antihemophilic factor.	Ristocetin	57-67	coagulation factor VIII	Homo sapiens	104-125
343683-5	1978	Structural studies of antihemophilic factor suggest that it is composed of two dissociable subcomponents, one of high molecular weight that contains the bulk of protein and sustains ristocetin-induced platelet aggregation, and another of lower molecular weight with procoagulant activity.	Ristocetin	182-192	coagulation factor VIII	Homo sapiens	22-43
888824-5	1977	The results obtained support the hypothesis that the binding of the carbohydrate groups of factor VIII plays an important role in the induction of platelet aggregation and in the maintenance of aggregates formed in response to the treatment of platelet-rich plasma with bovine factor VIII or ristocetin.	Ristocetin	292-302	coagulation factor VIII	Bos taurus	91-102
974043-6	1976	Desialylated factor VIII retains its antigenic reactivity, its procoagulant or ristocetin cofactor properties and the capacity of its subunits to dissociate and recombine.	Ristocetin	79-89	cytochrome c oxidase subunit 8A	Homo sapiens	20-24
863293-4	1977	However, neonatal PRP was approximately 20% more sensitive to ristocetin than adult PRP.	Ristocetin	62-72	prion protein	Homo sapiens	18-21
885379-2	1977	This was noted in two different systems, namely, platelet aggregation induced by neuraminidase-treated human cryoprecipitate and platelet aggregation induced by ristocetin-human factor VIII complex.	Ristocetin	161-171	coagulation factor VIII	Bos taurus	178-189
1086910-6	1976	The bleeding-time corrective factor and the ristocetin-related vWF or platelet-aggregating factor are dissociable, distinct activites.	Ristocetin	44-54	von Willebrand factor	Homo sapiens	63-66
825957-6	1976	The reduced platelet retention of these animals was not significantly altered following infusion, whereas ristocetin-induced platelet aggregation was corrected in one of the dogs given human factor VIII.	Ristocetin	106-116	coagulation factor VIII	Canis lupus familiaris	191-202
947407-1	1976	Partially purified human antihemophilic factor (AHF, factor VIII), when treated with high concentrations of salt, has been shown to dissociate into two components: one, of relatively low molecular weight, possesses procoagulant activity, and the other, of higher molecular weight, forms precipitates with heterologous antiserum against AHF and supports ristocetin-induced platelet aggregation.	Ristocetin	353-363	coagulation factor VIII	Homo sapiens	25-46
947407-1	1976	Partially purified human antihemophilic factor (AHF, factor VIII), when treated with high concentrations of salt, has been shown to dissociate into two components: one, of relatively low molecular weight, possesses procoagulant activity, and the other, of higher molecular weight, forms precipitates with heterologous antiserum against AHF and supports ristocetin-induced platelet aggregation.	Ristocetin	353-363	coagulation factor VIII	Homo sapiens	48-51
4176-1	1976	Quantitative ristocetin-induced platelet aggregation of normal platelet-rich plasma (PRP) decreased with time after PRP preparation.	Ristocetin	13-23	complement component 4 binding protein alpha	Homo sapiens	85-88
4176-1	1976	Quantitative ristocetin-induced platelet aggregation of normal platelet-rich plasma (PRP) decreased with time after PRP preparation.	Ristocetin	13-23	complement component 4 binding protein alpha	Homo sapiens	116-119
4176-7	1976	A simple device for maintaining PRP pH constant by control of the ambient pCO2 was designed and found effective in keeping both pH and quantitative ristocetin aggregation constant over a prolonged period of time.	Ristocetin	148-158	complement component 4 binding protein alpha	Homo sapiens	32-35
55785-1	1976	Samples of apparently normal skin from one patient with von Willebrand"s disease (vWD) and five patients without vWD were examined with fluorescein-tagged antiserum to the component of factor VIII required for aggregation of platelets by ristocetin (VIII-R.A.F.).	Ristocetin	238-248	cytochrome c oxidase subunit 8A	Homo sapiens	192-196
1083144-4	1976	In contrast, the cryoprecipitate did increase plasma RAF to the expected level, and this RAF bound readily to the patient"s platelets in the presence of ristocetin.	Ristocetin	153-163	zinc fingers and homeoboxes 2	Homo sapiens	89-92
1087117-3	1976	Ristocetin-induced platelet aggregation causes a consumption of vWF, Factor VIII procoagulant activity, and Factor VIII antigen from the supernatant plasma which is proportional to the number of platelets aggregated.	Ristocetin	0-10	von Willebrand factor	Homo sapiens	64-67
950175-0	1976	Further studies of the interaction between ristocetin and fibrinogen.	Ristocetin	43-53	fibrinogen beta chain	Homo sapiens	58-68
950175-1	1976	Fibrinogen (FG) precipitation by ristocetin is enhanced by lowering the temperature to 4 degrees C. The  precipitate has similar properties to an acquired cryofibrinogen being resolubilised on rewarming to 37 degrees C, and the process of precipitation and resolubilsation can be repeated indefinitely by lowering and raising the temperature.	Ristocetin	33-43	fibrinogen beta chain	Homo sapiens	0-10
950175-1	1976	Fibrinogen (FG) precipitation by ristocetin is enhanced by lowering the temperature to 4 degrees C. The  precipitate has similar properties to an acquired cryofibrinogen being resolubilised on rewarming to 37 degrees C, and the process of precipitation and resolubilsation can be repeated indefinitely by lowering and raising the temperature.	Ristocetin	33-43	fibrinogen beta chain	Homo sapiens	12-14
1198487-0	1975	Proceedings: Inhibition of ristocetin-induced platelet aggregation (RIPA) by Haemaccel and fibrinogen.	Ristocetin	27-37	fibrinogen beta chain	Homo sapiens	91-101
1080491-6	1975	However, the partially purified Factor VIII/von Willebrand factor protein had markedly reduced von Willebrand factor activity in a ristocetin assay.	Ristocetin	131-141	von Willebrand factor	Homo sapiens	44-65
1080491-6	1975	However, the partially purified Factor VIII/von Willebrand factor protein had markedly reduced von Willebrand factor activity in a ristocetin assay.	Ristocetin	131-141	von Willebrand factor	Homo sapiens	95-116
1078779-2	1975	Ristocetin-induced platelet aggregation (RIPA) was decreased in 13 of 18 patients with von Willebrand"s disease (VWD) who had decreased plasma levels of VIII-VWF.	Ristocetin	0-10	cytochrome c oxidase subunit 8A	Homo sapiens	153-161
1120188-0	1975	Some factors affecting fibrinogen precipitation by ristocetin: ultrastructure of precipitates.	Ristocetin	51-61	fibrinogen beta chain	Homo sapiens	23-33
1120188-1	1975	Fibrinogen in aqueous solution is precipitated by the antibiotic ristocetin.	Ristocetin	65-75	fibrinogen beta chain	Homo sapiens	0-10
1120188-4	1975	Ristocetin-precipitated fibrinogen takes the form of fibrils or clumps, composed of irregularly spaced, structure-less particles.	Ristocetin	0-10	fibrinogen beta chain	Homo sapiens	24-34
1120188-5	1975	The addition of ristocetin to washed platelets suspended in fibrinogen-containing media produces fibrinogen clumps in both the media and in the surface cannalicular system of the platelets.	Ristocetin	16-26	fibrinogen beta chain	Homo sapiens	60-70
1120188-5	1975	The addition of ristocetin to washed platelets suspended in fibrinogen-containing media produces fibrinogen clumps in both the media and in the surface cannalicular system of the platelets.	Ristocetin	16-26	fibrinogen beta chain	Homo sapiens	97-107
1120188-7	1975	The role of the latter is confirmed by the observation that the addition of ristocetin to inert latex particles suspended in fibrinogen solution produces typical aggregation curves.	Ristocetin	76-86	fibrinogen beta chain	Homo sapiens	125-135
1168691-3	1975	The antibiotic ristocetin, which aggregates human platelets in the presence of von Willebrand factor, nonspecifically precipitates platelet membrane factor VIII antigen.	Ristocetin	15-25	von Willebrand factor	Homo sapiens	79-100
122889-6	1975	Both normal and hemophilic factor VIII as well as thrombin-inactivated factor VIII support ristocetin-induced platelet aggregation.	Ristocetin	91-101	coagulation factor II, thrombin	Homo sapiens	50-58
4201262-0	1973	Defective ristocetin-induced platelet aggregation in von Willebrand"s disease and its correction by factor VIII.	Ristocetin	10-20	cytochrome c oxidase subunit 8A	Homo sapiens	107-111
4201262-4	1973	The magnitude of the defect in ristocetin-induced platelet aggregation correlated well with the degree of abnormality of the bleeding time and the levels of antihemophilic factor (AHF, VIII(AHF)) procoagulant activity.	Ristocetin	31-41	coagulation factor VIII	Homo sapiens	157-178
4201262-4	1973	The magnitude of the defect in ristocetin-induced platelet aggregation correlated well with the degree of abnormality of the bleeding time and the levels of antihemophilic factor (AHF, VIII(AHF)) procoagulant activity.	Ristocetin	31-41	cytochrome c oxidase subunit 8A	Homo sapiens	185-189
4542944-2	1973	In a previous paper, we showed that the abnormality of ristocetin-induced platelet aggregation in platelet-rich plasma in 10 patients with von Willebrand"s disease could be corrected by a factor in normal plasma that was present in the same fractions as factor VIII procoagulant activity (antihemophilic factor, AHF, VIII(AHF)) when prepared by chromatography on Bio-Gel 5 M (Bio-Rad Laboratories, Richmond, Calif.).	Ristocetin	55-65	cytochrome c oxidase subunit 8A	Homo sapiens	261-265
4542944-2	1973	In a previous paper, we showed that the abnormality of ristocetin-induced platelet aggregation in platelet-rich plasma in 10 patients with von Willebrand"s disease could be corrected by a factor in normal plasma that was present in the same fractions as factor VIII procoagulant activity (antihemophilic factor, AHF, VIII(AHF)) when prepared by chromatography on Bio-Gel 5 M (Bio-Rad Laboratories, Richmond, Calif.).	Ristocetin	55-65	cytochrome c oxidase subunit 8A	Homo sapiens	317-321
4542944-4	1973	In the present paper, we describe, an assay for this factor, the von Willebrand factor (VIII(VWF)), based on the observation that a log-log relationship exists between the amount of ristocetin-induced aggregation of washed, normal platelets and the concentration of normal plasma present in the test system.	Ristocetin	182-192	von Willebrand factor	Homo sapiens	65-86
4542944-4	1973	In the present paper, we describe, an assay for this factor, the von Willebrand factor (VIII(VWF)), based on the observation that a log-log relationship exists between the amount of ristocetin-induced aggregation of washed, normal platelets and the concentration of normal plasma present in the test system.	Ristocetin	182-192	von Willebrand factor	Homo sapiens	88-97
30849118-10	2019	In contrast, induction of binding of VWF to glycoprotein 1b on platelets using the VWF-activating protein ristocetin resulted in the removal of platelet sialic acid by translocation of platelet neuraminidase to the platelet surface.	Ristocetin	106-116	von Willebrand factor	Homo sapiens	37-40
33387210-6	2021	These results were associated with higher agglutination rates induced by ristocetin, thereby indirectly indicating an increased capability of vWF to bind to platelets.	Ristocetin	73-83	von Willebrand factor	Homo sapiens	142-145
33550910-3	2021	Hemostasis results and gene analysis revealed von Willebrand disease (VWD) type 2B with normal multimers and a novel mutation c.4136 G>T (R1379L), which appears to be a novel mutation of VWD type 2B that is mainly diagnosed with hypersensitivity to ristocetin and an hyperfixation of platelet Willebrand to a recombinant Gp1b.	Ristocetin	249-259	glycoprotein Ib platelet subunit alpha	Homo sapiens	321-325
32607039-7	2020	PK parameters for VWF markers were generally comparable to adults but showed lower VWF:ristocetin cofactor (RCo) exposure.	Ristocetin	87-97	von Willebrand factor	Homo sapiens	18-21
32607039-7	2020	PK parameters for VWF markers were generally comparable to adults but showed lower VWF:ristocetin cofactor (RCo) exposure.	Ristocetin	87-97	von Willebrand factor	Homo sapiens	83-86
30592326-1	2019	von Willebrand factor (VWF) ristocetin cofactor activity (VWF:RCo) by platelet aggregometry has been considered the gold standard for evaluating the ability of VWF to bind platelets for over 40 years.	Ristocetin	28-38	von Willebrand factor	Homo sapiens	0-21
30592326-1	2019	von Willebrand factor (VWF) ristocetin cofactor activity (VWF:RCo) by platelet aggregometry has been considered the gold standard for evaluating the ability of VWF to bind platelets for over 40 years.	Ristocetin	28-38	von Willebrand factor	Homo sapiens	23-26
30592326-1	2019	von Willebrand factor (VWF) ristocetin cofactor activity (VWF:RCo) by platelet aggregometry has been considered the gold standard for evaluating the ability of VWF to bind platelets for over 40 years.	Ristocetin	28-38	von Willebrand factor	Homo sapiens	58-61
30592326-1	2019	von Willebrand factor (VWF) ristocetin cofactor activity (VWF:RCo) by platelet aggregometry has been considered the gold standard for evaluating the ability of VWF to bind platelets for over 40 years.	Ristocetin	28-38	von Willebrand factor	Homo sapiens	58-61
33132157-12	2020	TLR4-mediated signalling induced platelet adhesion and facilitated ristocetin-induced platelet agglutination.	Ristocetin	67-77	toll like receptor 4	Homo sapiens	0-4
32971099-5	2020	The in vitro assay showed that atrase B remarkably inhibited ristocetin- and thrombin-induced platelet aggregation by cleavage of the platelet membrane glycoprotein Ib, and the coagulation of normal human plasma, which may be caused by inhibiting coagulation factor VIII predominantly.	Ristocetin	61-71	coagulation factor VIII	Homo sapiens	247-270
32774267-6	2020	The VWF ristocetin cofactor assay (VWF: RCo) was low, but VWF antigen level (VWF: Ag) was normal.	Ristocetin	8-18	von Willebrand factor	Homo sapiens	4-7
32774267-6	2020	The VWF ristocetin cofactor assay (VWF: RCo) was low, but VWF antigen level (VWF: Ag) was normal.	Ristocetin	8-18	von Willebrand factor	Homo sapiens	35-38
32774267-6	2020	The VWF ristocetin cofactor assay (VWF: RCo) was low, but VWF antigen level (VWF: Ag) was normal.	Ristocetin	8-18	von Willebrand factor	Homo sapiens	35-38
31229334-5	2019	More recently, the treatment of VWD has undergone a slow yet significant change from plasma-derived VWF/FVIII concentrates with VWF:ristocetin cofactor (RCo)/FVIII ratios <=1, to those with VWF:RCo/FVIII ratios >10, to a recombinant VWF.	Ristocetin	132-142	von Willebrand factor	Homo sapiens	100-103
31229334-5	2019	More recently, the treatment of VWD has undergone a slow yet significant change from plasma-derived VWF/FVIII concentrates with VWF:ristocetin cofactor (RCo)/FVIII ratios <=1, to those with VWF:RCo/FVIII ratios >10, to a recombinant VWF.	Ristocetin	132-142	coagulation factor VIII	Homo sapiens	104-109
31229334-5	2019	More recently, the treatment of VWD has undergone a slow yet significant change from plasma-derived VWF/FVIII concentrates with VWF:ristocetin cofactor (RCo)/FVIII ratios <=1, to those with VWF:RCo/FVIII ratios >10, to a recombinant VWF.	Ristocetin	132-142	von Willebrand factor	Homo sapiens	128-131
31229334-5	2019	More recently, the treatment of VWD has undergone a slow yet significant change from plasma-derived VWF/FVIII concentrates with VWF:ristocetin cofactor (RCo)/FVIII ratios <=1, to those with VWF:RCo/FVIII ratios >10, to a recombinant VWF.	Ristocetin	132-142	von Willebrand factor	Homo sapiens	128-131
31229334-5	2019	More recently, the treatment of VWD has undergone a slow yet significant change from plasma-derived VWF/FVIII concentrates with VWF:ristocetin cofactor (RCo)/FVIII ratios <=1, to those with VWF:RCo/FVIII ratios >10, to a recombinant VWF.	Ristocetin	132-142	von Willebrand factor	Homo sapiens	128-131
30849118-10	2019	In contrast, induction of binding of VWF to glycoprotein 1b on platelets using the VWF-activating protein ristocetin resulted in the removal of platelet sialic acid by translocation of platelet neuraminidase to the platelet surface.	Ristocetin	106-116	von Willebrand factor	Homo sapiens	83-86
30849118-10	2019	In contrast, induction of binding of VWF to glycoprotein 1b on platelets using the VWF-activating protein ristocetin resulted in the removal of platelet sialic acid by translocation of platelet neuraminidase to the platelet surface.	Ristocetin	106-116	neuraminidase 1	Homo sapiens	194-207
30842734-7	2019	Surprisingly, HD1 and HD22 aptamers (3 muM) potentiated ristocetin-induced platelet aggregation in WP.	Ristocetin	56-66	histone deacetylase 1	Homo sapiens	14-17
30842734-7	2019	Surprisingly, HD1 and HD22 aptamers (3 muM) potentiated ristocetin-induced platelet aggregation in WP.	Ristocetin	56-66	latexin	Homo sapiens	39-42
30337247-8	2018	FINDINGS: Both rLep-vWA-I and rLep-vWA-II were able to bind to Hu-platelets and inhibit rHu-vWF/ristocetin-induced Hu-platelet aggregation, but Hu-GPIbalpha-IgG, rLep-vWA-I-IgG and rLep-vWA-II-IgG blocked this binding or inhibition.	Ristocetin	96-106	von Willebrand factor	Homo sapiens	92-95
30450617-7	2019	RESULTS: While vWF-ristocetin cofactor activity is significantly decreased (-41.13%; p < .0001) in SpDP, a model of vWF-mediated platelet adhesion to collagen under flow showed enhanced function (+13%; p < .01).	Ristocetin	19-29	von Willebrand factor	Homo sapiens	15-18
30450617-11	2019	The apparent paradox between vWF-ristocetin cofactor assay and vWF-mediated platelet adhesion may be explained by the increase in smaller multimers of vWF in SpDP, producing different outcomes in these assays.	Ristocetin	33-43	von Willebrand factor	Homo sapiens	29-32
31359769-8	2019	However, VWF ristocetin cofactor activity or gain-of-function mutant glycoprotein Ib binding activity <36.5 IU/dL and VWF collagen binding activity <34.5 IU/dL could predict increased bleeding risk (BS >=3) by 92.3% specificity and 70.0% sensitivity (P < .0001).	Ristocetin	13-23	von Willebrand factor	Homo sapiens	9-12
29985231-0	2018	Perhaps it"s not the platelet: Ristocetin uncovers the potential role of von Willebrand factor in impaired platelet aggregation following traumatic brain injury.	Ristocetin	31-41	von Willebrand factor	Homo sapiens	73-94
30152919-8	2018	Methods The ability of GoF ADAMTS-13 to dissolve VWF-platelet agglutinates was examined with an assay of ristocetin-induced platelet agglutination and in parallel-flow models of arterial thrombosis.	Ristocetin	105-115	a disintegrin-like and metallopeptidase (reprolysin type) with thrombospondin type 1 motif, 13	Mus musculus	27-36
29985231-2	2018	Ristocetin is an antimicrobial substance that induces vWF-mediated aggregation of platelets.	Ristocetin	0-10	von Willebrand factor	Homo sapiens	54-57
29985231-15	2018	The impaired platelet aggregation response to ristocetin stimulation and corresponding increase in factor VIII activity in TBI patients may be secondary to a TBI-induced effect on vWF quantity (due to injury-driven consumption of vWF) or vWF function with resultant increase in circulating factor VIII activity (due to impaired carrying capacity of vWF).	Ristocetin	46-56	von Willebrand factor	Homo sapiens	180-183
29985231-15	2018	The impaired platelet aggregation response to ristocetin stimulation and corresponding increase in factor VIII activity in TBI patients may be secondary to a TBI-induced effect on vWF quantity (due to injury-driven consumption of vWF) or vWF function with resultant increase in circulating factor VIII activity (due to impaired carrying capacity of vWF).	Ristocetin	46-56	von Willebrand factor	Homo sapiens	230-233
29985231-15	2018	The impaired platelet aggregation response to ristocetin stimulation and corresponding increase in factor VIII activity in TBI patients may be secondary to a TBI-induced effect on vWF quantity (due to injury-driven consumption of vWF) or vWF function with resultant increase in circulating factor VIII activity (due to impaired carrying capacity of vWF).	Ristocetin	46-56	von Willebrand factor	Homo sapiens	230-233
29985231-15	2018	The impaired platelet aggregation response to ristocetin stimulation and corresponding increase in factor VIII activity in TBI patients may be secondary to a TBI-induced effect on vWF quantity (due to injury-driven consumption of vWF) or vWF function with resultant increase in circulating factor VIII activity (due to impaired carrying capacity of vWF).	Ristocetin	46-56	von Willebrand factor	Homo sapiens	230-233
30287479-8	2018	Ristocetin-induced platelet aggregation was similar in H1HA mouse and human platelet-rich plasma, and it was comparably inhibited by monoclonal antibody NMC-4, which is known to block human GPIbalpha-VWFA1 binding, which also inhibited FeCl3-induced mouse carotid artery thrombosis.	Ristocetin	0-10	glycoprotein Ib platelet subunit alpha	Homo sapiens	190-199
29897666-6	2018	The new assays appear to have improved performance characteristics compared with the old reference standard, ristocetin cofactor activity (VWF:RCo), but information is limited about how they compare with VWF:RCo and each other.	Ristocetin	109-119	von Willebrand factor	Homo sapiens	139-142
30084138-4	2018	RESULTS: PFA-100 was always significantly prolonged, and ristocetin-induced platelet aggregation (RIPA) and VWF ristocetin cofactor (VWF:RCo) greatly reduced or absent.	Ristocetin	112-122	von Willebrand factor	Homo sapiens	108-111
29541457-10	2018	These results strongly suggest that anti-platelet agents inhibit the HSP27 release from platelets stimulated by ristocetin but not the aggregation in type 2 DM patients.	Ristocetin	112-122	heat shock protein family B (small) member 1	Homo sapiens	69-74
29541457-0	2018	Ristocetin induces phosphorylated-HSP27 (HSPB1) release from the platelets of type 2 DM patients: Anti-platelet agent-effect on the release.	Ristocetin	0-10	heat shock protein family B (small) member 1	Homo sapiens	34-39
29541457-0	2018	Ristocetin induces phosphorylated-HSP27 (HSPB1) release from the platelets of type 2 DM patients: Anti-platelet agent-effect on the release.	Ristocetin	0-10	heat shock protein family B (small) member 1	Homo sapiens	41-46
29541457-2	2018	In the present study, we investigated the effect of ristocetin, a glycoprotein (GP)Ib/IX/V activator, on the release of HSP27 and the effect of anti-platelet agents, such as acetylsalicylic acid (ASA), on this release.	Ristocetin	52-62	heat shock protein family B (small) member 1	Homo sapiens	120-125
29541457-6	2018	On the other hand, the levels of phosphorylated-HSP27 induced by ristocetin in the platelets from a patient of the anti-platelet group taking ASA were significantly lower than those from a patient of the control group.	Ristocetin	65-75	heat shock protein family B (small) member 1	Homo sapiens	48-53
29541457-7	2018	The levels of HSP27 release from the ristocetin-stimulated platelets were significantly correlated with the levels of phosphorylated-HSP27 in the platelets from patients in the two groups.	Ristocetin	37-47	heat shock protein family B (small) member 1	Homo sapiens	14-19
29541457-7	2018	The levels of HSP27 release from the ristocetin-stimulated platelets were significantly correlated with the levels of phosphorylated-HSP27 in the platelets from patients in the two groups.	Ristocetin	37-47	heat shock protein family B (small) member 1	Homo sapiens	133-138
29140542-4	2018	Accordingly, we observed that vWF-Ag and its activity-estimated by ristocetin cofactor measurement-increased immediately after induction of liver regeneration and was associated with platelet accumulation within the liver.	Ristocetin	67-77	von Willebrand factor	Homo sapiens	30-33
29168270-2	2018	Current VWF activity tests include ristocetin cofactor and collagen binding (VWF:CB) assays.	Ristocetin	35-45	von Willebrand factor	Homo sapiens	8-11
29355554-6	2018	Furthermore, a solid phase binding assay revealed that HY023016 inhibited ristocetin-induced washed platelets bind to von Willebrand factor (vWF).	Ristocetin	74-84	von Willebrand factor	Homo sapiens	118-139
29355554-6	2018	Furthermore, a solid phase binding assay revealed that HY023016 inhibited ristocetin-induced washed platelets bind to von Willebrand factor (vWF).	Ristocetin	74-84	von Willebrand factor	Homo sapiens	141-144
29251812-16	2018	An anti-D"D3 mAb DD3.3 that displays enhanced binding to VWF containing the N-terminal mucin insert also exhibited increased binding to wild-type VWF under shear and upon ristocetin addition.	Ristocetin	171-181	Von Willebrand factor	Mus musculus	57-60
29651351-5	2018	Ristocetin cofactor activity (VWF:RCo) was 0.09 IU/ml, and collagen binding activity (VWF:CB) was 0.10 IU/ml.	Ristocetin	0-10	von Willebrand factor	Homo sapiens	30-33
30046704-5	2018	Historically, VWF binding to platelet GPIbalpha was measured by the ristocetin cofactor assay (VWF:RCo); a new assay using platelet GPIbalpha in the absence of ristocetin (VWF:GPIbM) is gradually replacing the VWF:RCo due to improved accuracy in diagnosis.	Ristocetin	68-78	von Willebrand factor	Homo sapiens	14-17
30046704-5	2018	Historically, VWF binding to platelet GPIbalpha was measured by the ristocetin cofactor assay (VWF:RCo); a new assay using platelet GPIbalpha in the absence of ristocetin (VWF:GPIbM) is gradually replacing the VWF:RCo due to improved accuracy in diagnosis.	Ristocetin	68-78	glycoprotein Ib platelet subunit alpha	Homo sapiens	38-47
28637952-6	2017	Our results showed that addition of HSP72 increased platelet aggregation in the presence of low concentrations of ADP, collagen, TRAP-6, ristocetin, and arachidonic acid.	Ristocetin	137-147	heat shock protein family A (Hsp70) member 1A	Rattus norvegicus	36-41
28957942-5	2018	The process resulted in a very highly purified vWF, with a mean specific activity of 95.3 IU of vWF:ristocetin cofactor assay/mg of total proteins.	Ristocetin	100-110	von Willebrand factor	Homo sapiens	47-50
28957942-5	2018	The process resulted in a very highly purified vWF, with a mean specific activity of 95.3 IU of vWF:ristocetin cofactor assay/mg of total proteins.	Ristocetin	100-110	von Willebrand factor	Homo sapiens	96-99
29126301-20	2017	Testing the functional activity of VWF, utilizes the drug ristocetin.The state of multimerization of VWF is important and is assessed by electrophoresis on agarose gels.	Ristocetin	58-68	von Willebrand factor	Homo sapiens	35-38
29126301-20	2017	Testing the functional activity of VWF, utilizes the drug ristocetin.The state of multimerization of VWF is important and is assessed by electrophoresis on agarose gels.	Ristocetin	58-68	von Willebrand factor	Homo sapiens	101-104
28603902-12	2017	Results The phosphorylation levels of ERK5 were significantly enhanced in human platelets stimulated with botrocetin/VWF or ristocetin/VWF.	Ristocetin	124-134	mitogen-activated protein kinase 7	Homo sapiens	38-42
28603902-12	2017	Results The phosphorylation levels of ERK5 were significantly enhanced in human platelets stimulated with botrocetin/VWF or ristocetin/VWF.	Ristocetin	124-134	von Willebrand factor	Homo sapiens	135-138
28603902-13	2017	The ERK5 inhibitor XMD8-92 suppressed the second wave of human platelet aggregation induced by botrocetin/VWF or ristocetin/VWF and inhibited human platelet adhesion on immobilized VWF under shear stress.	Ristocetin	113-123	mitogen-activated protein kinase 7	Homo sapiens	4-8
28120508-2	2017	Diagnosis requires measurement of VWF-platelet binding function, for which VWF ristocetin cofactor activity (VWF:RCo) is the reference method.	Ristocetin	79-89	von Willebrand factor	Homo sapiens	75-78
28120508-2	2017	Diagnosis requires measurement of VWF-platelet binding function, for which VWF ristocetin cofactor activity (VWF:RCo) is the reference method.	Ristocetin	79-89	von Willebrand factor	Homo sapiens	75-78
28142075-6	2017	METHODS: Platelet TF-PCA was induced by GPIbalpha activation with VWF-ristocetin.	Ristocetin	70-80	glycoprotein Ib platelet subunit alpha	Homo sapiens	40-49
28142075-6	2017	METHODS: Platelet TF-PCA was induced by GPIbalpha activation with VWF-ristocetin.	Ristocetin	70-80	von Willebrand factor	Homo sapiens	66-69
28817667-4	2017	We found that thrombin, Trap-6, arachidonic acid, collagen, A23187, epinephrine and ADP significantly increased glycolytic flux (3-38 times vs. non-activated platelets) whereas ristocetin was ineffective.	Ristocetin	177-187	coagulation factor II, thrombin	Homo sapiens	14-22
28640903-3	2017	The minimum aggregating dose of ristocetin was similarly reduced in both patient groups, and modulated by their underlying VWF mutations.	Ristocetin	32-42	von Willebrand factor	Homo sapiens	123-126
28279966-9	2017	Rather under shear stress conditions, or in the presence of denaturants, such as urea or ristocetin, plasmin cleaves the K1491-R1492 peptide bond within the VWF A1-A2 linker region.	Ristocetin	89-99	plasminogen	Homo sapiens	101-108
28279966-9	2017	Rather under shear stress conditions, or in the presence of denaturants, such as urea or ristocetin, plasmin cleaves the K1491-R1492 peptide bond within the VWF A1-A2 linker region.	Ristocetin	89-99	von Willebrand factor	Homo sapiens	157-160
28804843-5	2017	Classically, the most often used assay for measuring GPIb binding activity was the ristocetin cofactor assay (VWF:RCo), which historically measured agglutination of fixed human platelets by VWF in the presence of ristocetin.	Ristocetin	83-93	von Willebrand factor	Homo sapiens	110-113
28804843-5	2017	Classically, the most often used assay for measuring GPIb binding activity was the ristocetin cofactor assay (VWF:RCo), which historically measured agglutination of fixed human platelets by VWF in the presence of ristocetin.	Ristocetin	83-93	von Willebrand factor	Homo sapiens	190-193
28804843-5	2017	Classically, the most often used assay for measuring GPIb binding activity was the ristocetin cofactor assay (VWF:RCo), which historically measured agglutination of fixed human platelets by VWF in the presence of ristocetin.	Ristocetin	213-223	von Willebrand factor	Homo sapiens	110-113
28804846-4	2017	The current paper describes several protocols for assessment of VWF activity by means of VWF ristocetin cofactor (VWF:RCo).	Ristocetin	93-103	von Willebrand factor	Homo sapiens	64-67
28804846-4	2017	The current paper describes several protocols for assessment of VWF activity by means of VWF ristocetin cofactor (VWF:RCo).	Ristocetin	93-103	von Willebrand factor	Homo sapiens	89-92
28804846-4	2017	The current paper describes several protocols for assessment of VWF activity by means of VWF ristocetin cofactor (VWF:RCo).	Ristocetin	93-103	von Willebrand factor	Homo sapiens	89-92
28804846-5	2017	These assays identify VWF activity by quantitative assessment of VWF protein adhesion to platelets or other particles and subsequent detection of the adhered VWF as facilitated by inclusion of ristocetin.	Ristocetin	193-203	von Willebrand factor	Homo sapiens	22-25
28804847-3	2017	For many years, the most frequently used assay for measuring GPIb binding activity was the ristocetin cofactor assay (VWF:RCo), which measures the agglutination of fixed human platelets by VWF in the presence of ristocetin.	Ristocetin	91-101	von Willebrand factor	Homo sapiens	118-121
28804847-3	2017	For many years, the most frequently used assay for measuring GPIb binding activity was the ristocetin cofactor assay (VWF:RCo), which measures the agglutination of fixed human platelets by VWF in the presence of ristocetin.	Ristocetin	91-101	von Willebrand factor	Homo sapiens	189-192
28804847-3	2017	For many years, the most frequently used assay for measuring GPIb binding activity was the ristocetin cofactor assay (VWF:RCo), which measures the agglutination of fixed human platelets by VWF in the presence of ristocetin.	Ristocetin	212-222	von Willebrand factor	Homo sapiens	118-121
28804847-5	2017	One published method (now abbreviated VWF:GPIbR) uses wild-type GPIb for triggering the binding reaction in the presence of ristocetin.	Ristocetin	124-134	von Willebrand factor	Homo sapiens	38-41
28804847-6	2017	Another more widely used method (now abbreviated VWF:GPIbM) uses gain-of-function GPIb without ristocetin; this permits spontaneous binding of VWF to GPIb and avoids problems associated with the nonphysiological substance ristocetin.	Ristocetin	95-105	von Willebrand factor	Homo sapiens	49-52
28804847-6	2017	Another more widely used method (now abbreviated VWF:GPIbM) uses gain-of-function GPIb without ristocetin; this permits spontaneous binding of VWF to GPIb and avoids problems associated with the nonphysiological substance ristocetin.	Ristocetin	222-232	von Willebrand factor	Homo sapiens	49-52
28804849-1	2017	Ristocetin-induced platelet aggregation (RIPA) is used as an in vitro test to determine the presence and integrity of the platelet glycoprotein (GP) Ibalpha-V-IX complex and von Willebrand factor (VWF) interaction and is usually performed using platelet-rich plasma (PRP).	Ristocetin	0-10	von Willebrand factor	Homo sapiens	174-195
28804849-1	2017	Ristocetin-induced platelet aggregation (RIPA) is used as an in vitro test to determine the presence and integrity of the platelet glycoprotein (GP) Ibalpha-V-IX complex and von Willebrand factor (VWF) interaction and is usually performed using platelet-rich plasma (PRP).	Ristocetin	0-10	von Willebrand factor	Homo sapiens	197-200
28804849-2	2017	Impairment in the response of VWF/GPIbalpha-V-IX is measured with reference to several established concentrations of ristocetin and may indicate defects in VWF or in GPIbalpha-V-IX function.	Ristocetin	117-127	von Willebrand factor	Homo sapiens	30-33
28804849-4	2017	For example, the correction of an abnormal RIPA trace after mixing PRP with normal plasma and rechallenging with ristocetin at 1.0 mg/mL suggests VWF function/quantity defect.	Ristocetin	113-123	von Willebrand factor	Homo sapiens	146-149
27554083-5	2016	In A1-A2-A3 and full-length VWF, this macrophage-binding site is cryptic but becomes exposed following exposure to shear or ristocetin.	Ristocetin	124-134	von Willebrand factor	Homo sapiens	28-31
27978591-1	2017	von Willebrand disease type 2B (VWD2B) expresses gain-of-function mutations that enhance binding of an individual"s von Willebrand factor (VWF) to its platelet ligand, glycoprotein Ib (GPIb), and which are usually identified by increased ristocetin-induced platelet aggregation (RIPA).	Ristocetin	238-248	von Willebrand factor	Homo sapiens	116-137
27978591-1	2017	von Willebrand disease type 2B (VWD2B) expresses gain-of-function mutations that enhance binding of an individual"s von Willebrand factor (VWF) to its platelet ligand, glycoprotein Ib (GPIb), and which are usually identified by increased ristocetin-induced platelet aggregation (RIPA).	Ristocetin	238-248	von Willebrand factor	Homo sapiens	139-142
27913545-3	2016	While VWF protein measurements by immunoassay are reasonably comparable between institutions, the measurement of VWF ristocetin cofactor activity (VWF:RCo) has significant variability.	Ristocetin	117-127	von Willebrand factor	Homo sapiens	113-116
27913545-3	2016	While VWF protein measurements by immunoassay are reasonably comparable between institutions, the measurement of VWF ristocetin cofactor activity (VWF:RCo) has significant variability.	Ristocetin	117-127	von Willebrand factor	Homo sapiens	113-116
27716777-8	2016	In agreement with the proteomics data, small molecule inhibitors of thioredoxin selectively inhibited GPVI-mediated platelet activation, and attenuated ristocetin-induced GPIb-vWF-mediated platelet agglutination, thus validating the findings of the proteomics study.	Ristocetin	152-162	thioredoxin	Homo sapiens	68-79
27716777-8	2016	In agreement with the proteomics data, small molecule inhibitors of thioredoxin selectively inhibited GPVI-mediated platelet activation, and attenuated ristocetin-induced GPIb-vWF-mediated platelet agglutination, thus validating the findings of the proteomics study.	Ristocetin	152-162	von Willebrand factor	Homo sapiens	176-179
27184018-5	2016	The functionality of stored platelets was determined employing aggregometry and ristocetin-induced VWF binding.	Ristocetin	80-90	von Willebrand factor	Homo sapiens	99-102
27749315-5	2016	The clinical profile of this young girl and the findings of less than 5% for von Willebrand factor (VWF):Ag and 10% for VWF Ristocetin cofactor suggests a type 3 VWD.	Ristocetin	124-134	von Willebrand factor	Homo sapiens	120-123
27184018-8	2016	Also, ristocetin-induced VWF binding was impaired in a small population of platelets.	Ristocetin	6-16	von Willebrand factor	Homo sapiens	25-28
27052467-6	2016	VWF binding to MMRN1 was enhanced by shear exposure and ristocetin, and required VWF A1A2A3 region, specifically the A1 and A3 domains.	Ristocetin	56-66	von Willebrand factor	Homo sapiens	0-3
27651919-5	2016	VWF function was determined by ristocetin-induced platelet aggregation (VWF ristocetin cofactor, VWF:RCo) and VWF levels by turbidimetric assay (VWF antigen, VWF:Ag).	Ristocetin	31-41	von Willebrand factor	Homo sapiens	0-3
27651919-5	2016	VWF function was determined by ristocetin-induced platelet aggregation (VWF ristocetin cofactor, VWF:RCo) and VWF levels by turbidimetric assay (VWF antigen, VWF:Ag).	Ristocetin	76-86	von Willebrand factor	Homo sapiens	0-3
27052467-6	2016	VWF binding to MMRN1 was enhanced by shear exposure and ristocetin, and required VWF A1A2A3 region, specifically the A1 and A3 domains.	Ristocetin	56-66	multimerin 1	Homo sapiens	15-20
27148840-1	2016	Type 2B von Willebrand disease (VWD2B) is a rare, autosomal-dominant inherited bleeding disorder, characterized by an enhanced ristocetin-induced platelet aggregation in platelet-rich plasma and often with variable degree of thrombocytopenia and loss of high-molecular-weight multimers von Willebrand factor (VWF).	Ristocetin	127-137	von Willebrand factor	Homo sapiens	286-307
27148840-1	2016	Type 2B von Willebrand disease (VWD2B) is a rare, autosomal-dominant inherited bleeding disorder, characterized by an enhanced ristocetin-induced platelet aggregation in platelet-rich plasma and often with variable degree of thrombocytopenia and loss of high-molecular-weight multimers von Willebrand factor (VWF).	Ristocetin	127-137	von Willebrand factor	Homo sapiens	309-312
27237807-4	2016	We compared the new assay with the reference assay: ristocetin cofactor activity (VWF:RCo) performed on the BCS-XP analyser by testing retrospectively samples from 82 healthy normal subjects and 61 patients with von Willebrand disease (VWD).	Ristocetin	52-62	von Willebrand factor	Homo sapiens	82-85
27040683-8	2016	Finally, in a patient with IgG MM, maximally prolonged PFA-100  closure times and a specific defect in ristocetin-induced platelet agglutination, both of which resolved after remission induction, indicated interference of the paraprotein with VWF binding to platelet GPIb.	Ristocetin	103-113	von Willebrand factor	Homo sapiens	243-246
26858830-7	2015	Patients who were homozygous for the mutant PlA2 allele had an increased aggregatory response to adenosine diphosphate, collagen, adrenaline, ristocetin, thrombin receptor-activating peptide 6 and U46619, when assessed using agonist-concentration response curves.	Ristocetin	142-152	phospholipase A2 group IB	Homo sapiens	44-48
26172561-1	2015	BACKGROUND: The ability of von Willebrand factor (VWF) to bind platelet GP Ib and promote platelet plug formation is measured in vitro using the ristocetin cofactor (VWF:RCo) assay.	Ristocetin	145-155	von Willebrand factor	Homo sapiens	27-48
26172561-1	2015	BACKGROUND: The ability of von Willebrand factor (VWF) to bind platelet GP Ib and promote platelet plug formation is measured in vitro using the ristocetin cofactor (VWF:RCo) assay.	Ristocetin	145-155	von Willebrand factor	Homo sapiens	50-53
26172561-1	2015	BACKGROUND: The ability of von Willebrand factor (VWF) to bind platelet GP Ib and promote platelet plug formation is measured in vitro using the ristocetin cofactor (VWF:RCo) assay.	Ristocetin	145-155	von Willebrand factor	Homo sapiens	166-169
26172561-14	2015	This study indicates that the specific modifications - namely the combination of increased ristocetin concentration, reduced platelet content, VWF-depleted plasma as on-board diluent and a two-curve calculation mode - reduces the issues seen with current VWF:RCo activity assays.	Ristocetin	91-101	von Willebrand factor	Homo sapiens	255-258
26206100-1	2015	BACKGROUND: Diagnosis of von Willebrand disease (VWD) type 2 usually relies on the discrepancy between the von Willebrand factor (VWF) ristocetin cofactor activity (VWF:RCo) and VWF antigen (VWF:Ag).	Ristocetin	135-145	von Willebrand factor	Homo sapiens	130-133
26206100-1	2015	BACKGROUND: Diagnosis of von Willebrand disease (VWD) type 2 usually relies on the discrepancy between the von Willebrand factor (VWF) ristocetin cofactor activity (VWF:RCo) and VWF antigen (VWF:Ag).	Ristocetin	135-145	von Willebrand factor	Homo sapiens	165-168
26206100-1	2015	BACKGROUND: Diagnosis of von Willebrand disease (VWD) type 2 usually relies on the discrepancy between the von Willebrand factor (VWF) ristocetin cofactor activity (VWF:RCo) and VWF antigen (VWF:Ag).	Ristocetin	135-145	von Willebrand factor	Homo sapiens	107-128
26206100-1	2015	BACKGROUND: Diagnosis of von Willebrand disease (VWD) type 2 usually relies on the discrepancy between the von Willebrand factor (VWF) ristocetin cofactor activity (VWF:RCo) and VWF antigen (VWF:Ag).	Ristocetin	135-145	von Willebrand factor	Homo sapiens	165-168
26206100-1	2015	BACKGROUND: Diagnosis of von Willebrand disease (VWD) type 2 usually relies on the discrepancy between the von Willebrand factor (VWF) ristocetin cofactor activity (VWF:RCo) and VWF antigen (VWF:Ag).	Ristocetin	135-145	von Willebrand factor	Homo sapiens	165-168
25935884-6	2015	RESULTS: At baseline, a significant link between vWF abnormalities and the severity of AVS was evidenced: mean aortic transvalvular gradient was negatively correlated with the levels of vWF antigen (vWF:Ag) (r = -0.29; P &lt; 0.05), vWF ristocetin cofactor activity (r = -0.402; P = 0.006), and vWF collagen-binding activity (vWF:CB; r = -0.441; P = 0.005).	Ristocetin	237-247	von Willebrand factor	Homo sapiens	49-52
25753785-4	2015	We have chosen to study the reliability of PFA-100 for screening VWF ristocetin cofactor (VWF:RCo) deficiency.	Ristocetin	69-79	von Willebrand factor	Homo sapiens	65-68
25753785-4	2015	We have chosen to study the reliability of PFA-100 for screening VWF ristocetin cofactor (VWF:RCo) deficiency.	Ristocetin	69-79	von Willebrand factor	Homo sapiens	90-93
25760062-0	2015	alphaB-crystallin reduces ristocetin-induced soluble CD40 ligand release in human platelets: suppression of thromboxane A2 generation.	Ristocetin	26-36	CD40 molecule	Homo sapiens	53-57
25935884-6	2015	RESULTS: At baseline, a significant link between vWF abnormalities and the severity of AVS was evidenced: mean aortic transvalvular gradient was negatively correlated with the levels of vWF antigen (vWF:Ag) (r = -0.29; P &lt; 0.05), vWF ristocetin cofactor activity (r = -0.402; P = 0.006), and vWF collagen-binding activity (vWF:CB; r = -0.441; P = 0.005).	Ristocetin	237-247	von Willebrand factor	Homo sapiens	186-189
25935884-6	2015	RESULTS: At baseline, a significant link between vWF abnormalities and the severity of AVS was evidenced: mean aortic transvalvular gradient was negatively correlated with the levels of vWF antigen (vWF:Ag) (r = -0.29; P &lt; 0.05), vWF ristocetin cofactor activity (r = -0.402; P = 0.006), and vWF collagen-binding activity (vWF:CB; r = -0.441; P = 0.005).	Ristocetin	237-247	von Willebrand factor	Homo sapiens	186-189
25661290-2	2015	Measurement of von Willebrand factor (VWF) activity in plasma is often based on platelet agglutination stimulated by the ristocetin cofactor activity.	Ristocetin	121-131	von Willebrand factor	Homo sapiens	15-36
25935884-6	2015	RESULTS: At baseline, a significant link between vWF abnormalities and the severity of AVS was evidenced: mean aortic transvalvular gradient was negatively correlated with the levels of vWF antigen (vWF:Ag) (r = -0.29; P &lt; 0.05), vWF ristocetin cofactor activity (r = -0.402; P = 0.006), and vWF collagen-binding activity (vWF:CB; r = -0.441; P = 0.005).	Ristocetin	237-247	von Willebrand factor	Homo sapiens	186-189
25935884-6	2015	RESULTS: At baseline, a significant link between vWF abnormalities and the severity of AVS was evidenced: mean aortic transvalvular gradient was negatively correlated with the levels of vWF antigen (vWF:Ag) (r = -0.29; P &lt; 0.05), vWF ristocetin cofactor activity (r = -0.402; P = 0.006), and vWF collagen-binding activity (vWF:CB; r = -0.441; P = 0.005).	Ristocetin	237-247	von Willebrand factor	Homo sapiens	186-189
25728415-8	2015	As expected, full-length wt-VWF was unable to bind LRP1 under static conditions unless ristocetin was added.	Ristocetin	87-97	von Willebrand factor	Homo sapiens	28-31
25728415-9	2015	In contrast, the presence of the p.V1316M or p.R1306Q mutation induced spontaneous binding to LRP1 without the need for ristocetin or shear stress.	Ristocetin	120-130	low density lipoprotein receptor-related protein 1	Mus musculus	94-98
25661290-2	2015	Measurement of von Willebrand factor (VWF) activity in plasma is often based on platelet agglutination stimulated by the ristocetin cofactor activity.	Ristocetin	121-131	von Willebrand factor	Homo sapiens	38-41
25677981-5	2015	The ability of platelet aggregation induced by ristocetin and collagen related to GPIbalpha and GPVI in the sheared blood samples, respectively, was evaluated by aggregometry.	Ristocetin	47-57	glycoprotein Ib platelet subunit alpha	Homo sapiens	82-91
25677981-5	2015	The ability of platelet aggregation induced by ristocetin and collagen related to GPIbalpha and GPVI in the sheared blood samples, respectively, was evaluated by aggregometry.	Ristocetin	47-57	glycoprotein VI platelet	Homo sapiens	96-100
27526539-9	2014	It was also observed that patients with high TM levels have significantly higher levels of von Willebrand factor antigen (vWFAg) and ristocetin cofactor activity (vWFRCo) which are associated with marked endothelial dysfunction.	Ristocetin	133-143	thrombomodulin	Homo sapiens	45-47
25103956-1	2014	The ristocetin cofactor activity assay (VWF:RCo) is the reference method for assessing von Willebrand factor (VWF) activity but remains difficult to perform, and the coefficient of variation of the method is high (about 20-30%).	Ristocetin	4-14	von Willebrand factor	Homo sapiens	40-43
24786773-4	2014	BS &gt;10 and VWF:ristocetin cofactor activity &lt;10 U/dL were associated with the risk of bleeding, but only a BS &gt;10 remained highly associated in a multivariable Cox proportional hazard model (adjusted hazard ratio: 7.27 [95% confidence interval, 3.83-13.83]).	Ristocetin	18-28	von Willebrand factor	Homo sapiens	14-17
24891215-1	2014	INTRODUCTION: Ristocetin cofactor activity of Von Willebrand factor (VWF:RCo) and the ratio VWF:RCo to its antigen VWF:Ag are used as routine screening to estimate VWF function and to detect types of Von Willebrand disease (VWD) caused by loss of high molecular weight multimers.	Ristocetin	14-24	von Willebrand factor	Homo sapiens	46-67
24891215-1	2014	INTRODUCTION: Ristocetin cofactor activity of Von Willebrand factor (VWF:RCo) and the ratio VWF:RCo to its antigen VWF:Ag are used as routine screening to estimate VWF function and to detect types of Von Willebrand disease (VWD) caused by loss of high molecular weight multimers.	Ristocetin	14-24	von Willebrand factor	Homo sapiens	69-72
25192242-0	2014	Performance evaluation and multicentre study of a von Willebrand factor activity assay based on GPIb binding in the absence of ristocetin.	Ristocetin	127-137	von Willebrand factor	Homo sapiens	50-71
25192242-1	2014	The functional activity of von Willebrand factor (VWF) is most frequently measured by using the ristocetin cofactor assay (VWF:RCo).	Ristocetin	96-106	von Willebrand factor	Homo sapiens	27-48
25192242-1	2014	The functional activity of von Willebrand factor (VWF) is most frequently measured by using the ristocetin cofactor assay (VWF:RCo).	Ristocetin	96-106	von Willebrand factor	Homo sapiens	50-53
25192242-1	2014	The functional activity of von Willebrand factor (VWF) is most frequently measured by using the ristocetin cofactor assay (VWF:RCo).	Ristocetin	96-106	von Willebrand factor	Homo sapiens	123-126
24978322-6	2014	The early 1970s saw a revolution in diagnostics when ristocetin was identified to induce platelet aggregation, and this formed the basis of the first consistent and reliable VWF "activity" test, permitting quantification of the platelet adhesive function missing in VWD.	Ristocetin	53-63	von Willebrand factor	Homo sapiens	174-177
24750681-1	2014	INTRODUCTION: The development of an automated, von Willebrand factor (VWF) activity assay, Innovance( ) VWF Ac (VWF:Ac), which measures VWF binding to the platelet receptor glycoprotein Ibalpha without ristocetin, led us to evaluate the assay for diagnosing von Willebrand disease (VWD) and monitoring therapy.	Ristocetin	202-212	von Willebrand factor	Homo sapiens	104-107
24658160-9	2014	Decoration with VBP resulted in substantial construct adhesion to ristocetin-treated VWF even if the A1-domain was blocked by glycocalicin.	Ristocetin	66-76	von Willebrand factor	Homo sapiens	85-88
24750680-2	2014	Technical innovations have been applied to improve the precision and lower limit of detection of von Willebrand factor (VWF) assays, including the ristocetin cofactor activity assay (VWF:RCo) that uses the antibiotic ristocetin to induce plasma VWF binding to glycoprotein (GP) IbIXV on target platelets.	Ristocetin	147-157	von Willebrand factor	Homo sapiens	183-186
24750680-2	2014	Technical innovations have been applied to improve the precision and lower limit of detection of von Willebrand factor (VWF) assays, including the ristocetin cofactor activity assay (VWF:RCo) that uses the antibiotic ristocetin to induce plasma VWF binding to glycoprotein (GP) IbIXV on target platelets.	Ristocetin	147-157	von Willebrand factor	Homo sapiens	183-186
24750680-2	2014	Technical innovations have been applied to improve the precision and lower limit of detection of von Willebrand factor (VWF) assays, including the ristocetin cofactor activity assay (VWF:RCo) that uses the antibiotic ristocetin to induce plasma VWF binding to glycoprotein (GP) IbIXV on target platelets.	Ristocetin	217-227	von Willebrand factor	Homo sapiens	183-186
24750680-2	2014	Technical innovations have been applied to improve the precision and lower limit of detection of von Willebrand factor (VWF) assays, including the ristocetin cofactor activity assay (VWF:RCo) that uses the antibiotic ristocetin to induce plasma VWF binding to glycoprotein (GP) IbIXV on target platelets.	Ristocetin	217-227	von Willebrand factor	Homo sapiens	183-186
24750680-5	2014	Some common polymorphisms in the VWF gene that do not cause bleeding are associated with falsely low VWF activity by ristocetin-dependent methods.	Ristocetin	117-127	von Willebrand factor	Homo sapiens	33-36
24750680-6	2014	To overcome the need for ristocetin, some new VWF activity assays use gain-of-function GPIbalpha mutants that bind VWF without the need for ristocetin, with an improved precision and lower limit of detection than measuring VWF:RCo by aggregometry.	Ristocetin	25-35	von Willebrand factor	Homo sapiens	46-49
24750680-6	2014	To overcome the need for ristocetin, some new VWF activity assays use gain-of-function GPIbalpha mutants that bind VWF without the need for ristocetin, with an improved precision and lower limit of detection than measuring VWF:RCo by aggregometry.	Ristocetin	140-150	von Willebrand factor	Homo sapiens	46-49
24750681-1	2014	INTRODUCTION: The development of an automated, von Willebrand factor (VWF) activity assay, Innovance( ) VWF Ac (VWF:Ac), which measures VWF binding to the platelet receptor glycoprotein Ibalpha without ristocetin, led us to evaluate the assay for diagnosing von Willebrand disease (VWD) and monitoring therapy.	Ristocetin	202-212	von Willebrand factor	Homo sapiens	47-68
24750681-1	2014	INTRODUCTION: The development of an automated, von Willebrand factor (VWF) activity assay, Innovance( ) VWF Ac (VWF:Ac), which measures VWF binding to the platelet receptor glycoprotein Ibalpha without ristocetin, led us to evaluate the assay for diagnosing von Willebrand disease (VWD) and monitoring therapy.	Ristocetin	202-212	von Willebrand factor	Homo sapiens	70-73
24750681-1	2014	INTRODUCTION: The development of an automated, von Willebrand factor (VWF) activity assay, Innovance( ) VWF Ac (VWF:Ac), which measures VWF binding to the platelet receptor glycoprotein Ibalpha without ristocetin, led us to evaluate the assay for diagnosing von Willebrand disease (VWD) and monitoring therapy.	Ristocetin	202-212	von Willebrand factor	Homo sapiens	104-107
24750681-1	2014	INTRODUCTION: The development of an automated, von Willebrand factor (VWF) activity assay, Innovance( ) VWF Ac (VWF:Ac), which measures VWF binding to the platelet receptor glycoprotein Ibalpha without ristocetin, led us to evaluate the assay for diagnosing von Willebrand disease (VWD) and monitoring therapy.	Ristocetin	202-212	von Willebrand factor	Homo sapiens	104-107
24139617-13	2014	The highest molecular weight vWF multimers were absent, and the vWF-ristocetin platelet aggregation pathway was significantly impaired.	Ristocetin	68-78	von Willebrand factor	Bos taurus	64-67
24705415-1	2014	von Willebrand factor/ristocetin (vWF/R) induces GPIb-dependent platelet agglutination and activation of alphaIIbbeta3 integrin, which also binds vWF.	Ristocetin	22-32	von Willebrand factor	Homo sapiens	34-37
24705415-1	2014	von Willebrand factor/ristocetin (vWF/R) induces GPIb-dependent platelet agglutination and activation of alphaIIbbeta3 integrin, which also binds vWF.	Ristocetin	22-32	von Willebrand factor	Homo sapiens	146-149
24296552-6	2014	VWF multimer analysis showed a loss of high-molecular-weight multimers and his plasma aggregated normal platelets under low ristocetin concentration, consistent with type 2B von Willebrand disease (VWD).	Ristocetin	124-134	von Willebrand factor	Homo sapiens	0-3
23789907-4	2014	vWF was determined by measuring vWF antigen (vWF:Ag) and vWF ristocetin cofactor (vWF:RCo) and by multimer analysis.	Ristocetin	61-71	von Willebrand factor	Homo sapiens	0-3
23730809-2	2013	The VWF activity is usually assessed based on measurement of the ristocetin cofactor (VWF:RCo).	Ristocetin	65-75	von Willebrand factor	Homo sapiens	4-7
23730809-2	2013	The VWF activity is usually assessed based on measurement of the ristocetin cofactor (VWF:RCo).	Ristocetin	65-75	von Willebrand factor	Homo sapiens	86-89
23570742-8	2013	From the immediate post-operative phase throughout the entire observation, the VWF ristocetin cofactor activity (Rco)/antigen (Ag) ratio of patients with HeartMate II and CircuLite devices was consistently lower compared with HTx patients.	Ristocetin	83-93	von Willebrand factor	Homo sapiens	79-82
23233321-4	2013	vWF inhibition was assessed by vWF antigen level (vWF:Ag) and activity by ristocetin test (vWF:RiCo).	Ristocetin	74-84	von Willebrand factor	Homo sapiens	0-3
23520336-1	2013	The diagnosis of von Willebrand disease (VWD) is complicated by issues with current laboratory testing, particularly the ristocetin cofactor activity assay (VWF:RCo).	Ristocetin	121-131	von Willebrand factor	Homo sapiens	157-160
23777763-3	2013	The PK of rVWF ristocetin cofactor activity, VWF antigen, and collagen-binding activity were similar to those of the comparator plasma-derived (pd) VWF-pdFVIII.	Ristocetin	15-25	von Willebrand factor	Rattus norvegicus	10-14
23295157-10	2013	In vitro experiments revealed that SZ-123 not only blocks the collagen-VWF A3 interaction but also indirectly inhibits VWF A1 binding to GPIbalpha induced by ristocetin.	Ristocetin	158-168	von Willebrand factor	Macaca mulatta	119-122
23295157-10	2013	In vitro experiments revealed that SZ-123 not only blocks the collagen-VWF A3 interaction but also indirectly inhibits VWF A1 binding to GPIbalpha induced by ristocetin.	Ristocetin	158-168	glycoprotein Ib platelet subunit alpha	Macaca mulatta	137-146
23107512-2	2013	Current VWF activity tests include the ristocetin cofactor assay and the collagen-binding assay (VWF:CB).	Ristocetin	39-49	von Willebrand factor	Homo sapiens	8-11
23205618-1	2013	The ristocetin cofactor assay (VWF:RCo) is the reference method for assessing von Willebrand factor (VWF) activity in the diagnosis of von Willebrand"s Disease (VWD).	Ristocetin	4-14	von Willebrand factor	Homo sapiens	31-34
23205618-1	2013	The ristocetin cofactor assay (VWF:RCo) is the reference method for assessing von Willebrand factor (VWF) activity in the diagnosis of von Willebrand"s Disease (VWD).	Ristocetin	4-14	von Willebrand factor	Homo sapiens	78-99
23205618-1	2013	The ristocetin cofactor assay (VWF:RCo) is the reference method for assessing von Willebrand factor (VWF) activity in the diagnosis of von Willebrand"s Disease (VWD).	Ristocetin	4-14	von Willebrand factor	Homo sapiens	101-104
22537243-9	2012	Impairment of GPIbalpha binding was more marked for I1416N rVWF than I1416T under both static and flow conditions: this was in spite of similar VWF:Ristocetin cofactor (RCo) activities in patient plasma and is consistent with a respective clinical phenotype.	Ristocetin	148-158	glycoprotein Ib platelet subunit alpha	Homo sapiens	14-23
22896002-2	2012	Assessment of ristocetin cofactor activity (VWF:RCo) and von Willebrand factor (VWF) antigen (VWF:Ag) in 72 consecutive patients with WM showed a negative relation between VWF levels &lt; 130 U/dL and both monoclonal immunoglobulin M concentration (mIgMC) and viscosity.	Ristocetin	14-24	von Willebrand factor	Homo sapiens	44-47
23143686-6	2012	Expression of GPIbalpha/beta on GPIXW127X platelets was sufficient to support adhesion to immobilized von Willebrand factor and type III collagen and ristocetin-induced platelet agglutination.	Ristocetin	150-160	glycoprotein Ib platelet subunit alpha	Homo sapiens	14-23
22922961-0	2012	Simultaneous exposure of sites in von Willebrand factor for glycoprotein Ib binding and ADAMTS13 cleavage: studies with ristocetin.	Ristocetin	120-130	von Willebrand factor	Homo sapiens	34-55
22922961-2	2012	Because ristocetin induces VWF to bind glycoprotein Ibalpha in the absence of shear stress, we evaluated whether it could also enhance ADAMTS13 proteolysis of VWF.	Ristocetin	8-18	von Willebrand factor	Homo sapiens	27-30
22922961-2	2012	Because ristocetin induces VWF to bind glycoprotein Ibalpha in the absence of shear stress, we evaluated whether it could also enhance ADAMTS13 proteolysis of VWF.	Ristocetin	8-18	glycoprotein Ib platelet subunit alpha	Homo sapiens	39-59
22922961-4	2012	Ristocetin accelerated ADAMTS13 cleavage of multimeric VWF and of each of the recombinant VWF fragments except for the A2 domain lacking the ristocetin-binding site.	Ristocetin	0-10	ADAM metallopeptidase with thrombospondin type 1 motif 13	Homo sapiens	23-31
22922961-4	2012	Ristocetin accelerated ADAMTS13 cleavage of multimeric VWF and of each of the recombinant VWF fragments except for the A2 domain lacking the ristocetin-binding site.	Ristocetin	0-10	von Willebrand factor	Homo sapiens	55-58
22922961-4	2012	Ristocetin accelerated ADAMTS13 cleavage of multimeric VWF and of each of the recombinant VWF fragments except for the A2 domain lacking the ristocetin-binding site.	Ristocetin	0-10	von Willebrand factor	Homo sapiens	90-93
23043782-10	2012	According to the sequence analysis and platelet aggregation tests, we propose that the function of GPIbalpha, especially regarding the ristocetin-vWF-GPIbalpha  interaction, differs between pigs and humans.	Ristocetin	135-145	glycoprotein Ib platelet subunit alpha	Sus scrofa	99-108
23043782-10	2012	According to the sequence analysis and platelet aggregation tests, we propose that the function of GPIbalpha, especially regarding the ristocetin-vWF-GPIbalpha  interaction, differs between pigs and humans.	Ristocetin	135-145	von Willebrand factor	Homo sapiens	146-149
23043782-10	2012	According to the sequence analysis and platelet aggregation tests, we propose that the function of GPIbalpha, especially regarding the ristocetin-vWF-GPIbalpha  interaction, differs between pigs and humans.	Ristocetin	135-145	glycoprotein Ib platelet subunit alpha	Homo sapiens	150-159
22819492-1	2012	We have previously shown that ristocetin, an activator of glycoprotein Ib/IX/V, induces release of soluble CD40 (sCD40) ligand via thromboxane (TX) A(2) production from human platelets.	Ristocetin	30-40	CD40 molecule	Homo sapiens	107-111
22819492-2	2012	In the present study, we investigated the effect of antithrombin-III (AT-III), an anticoagulant, on the ristocetin-induced glycoprotein Ib/IX/V activation in human platelets.	Ristocetin	104-114	serpin family C member 1	Homo sapiens	52-68
22819492-2	2012	In the present study, we investigated the effect of antithrombin-III (AT-III), an anticoagulant, on the ristocetin-induced glycoprotein Ib/IX/V activation in human platelets.	Ristocetin	104-114	serpin family C member 1	Homo sapiens	70-76
22819492-3	2012	AT-III inhibited ristocetin-stimulated platelet aggregation.	Ristocetin	17-27	serpin family C member 1	Homo sapiens	0-6
22819492-4	2012	The ristocetin-induced production of 11-dehydro-TXB(2), a stable metabolite of TXA(2), and the release of sCD40 ligand were suppressed by AT-III.	Ristocetin	4-14	serpin family C member 1	Homo sapiens	138-144
22819492-5	2012	AT-III also reduced the ristocetin-stimulated secretion of platelet-derived growth factor (PDGF)-AB.	Ristocetin	24-34	serpin family C member 1	Homo sapiens	0-6
22819492-7	2012	AT-III reduced the binding of SZ2, a monoclonal antibody to the sulfated sequence in the alpha-chain of glycoprotein Ib, to the ristocetin-stimulated platelets.	Ristocetin	128-138	serpin family C member 1	Homo sapiens	0-6
22819492-8	2012	These results strongly suggest that AT-III reduced ristocetin-stimulated release of sCD40 ligand due to inhibiting TXA(2) production in human platelets.	Ristocetin	51-61	serpin family C member 1	Homo sapiens	36-42
22740102-7	2012	VWF ristocetin cofactor activity (VWF:RCo) showed a median 10-fold increase 8 hours after end of infusion, while the median VWF-antigen and FVIII increase was less (5-fold and 4-fold, respectively).	Ristocetin	4-14	von Willebrand factor	Homo sapiens	0-3
22740102-7	2012	VWF ristocetin cofactor activity (VWF:RCo) showed a median 10-fold increase 8 hours after end of infusion, while the median VWF-antigen and FVIII increase was less (5-fold and 4-fold, respectively).	Ristocetin	4-14	von Willebrand factor	Homo sapiens	34-37
22740102-7	2012	VWF ristocetin cofactor activity (VWF:RCo) showed a median 10-fold increase 8 hours after end of infusion, while the median VWF-antigen and FVIII increase was less (5-fold and 4-fold, respectively).	Ristocetin	4-14	von Willebrand factor	Homo sapiens	34-37
22517896-4	2012	The T1255A, Clus1, and DC variants caused increased ristocetin-mediated GPIbalpha binding to VWF.	Ristocetin	52-62	glycoprotein Ib platelet subunit alpha	Homo sapiens	72-81
22517896-4	2012	The T1255A, Clus1, and DC variants caused increased ristocetin-mediated GPIbalpha binding to VWF.	Ristocetin	52-62	von Willebrand factor	Homo sapiens	93-96
22487084-3	2012	VWF activity is classically assessed by using VWF ristocetin cofactor activity (VWF:RCo), although VWF collagen-binding (VWF:CB) and VWF mAb-based (VWF activity [VWF:Act]) assays are used by some laboratories.	Ristocetin	50-60	von Willebrand factor	Homo sapiens	0-3
22975950-0	2012	Effect of cytochrome P450-dependent epoxyeicosanoids on Ristocetin-induced thrombocyte aggregation.	Ristocetin	56-66	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	10-25
21951857-2	2012	The VWF activity is usually assessed based on measurement of the ristocetin cofactor (VWF:RCo).	Ristocetin	65-75	von Willebrand factor	Homo sapiens	4-7
21951857-2	2012	The VWF activity is usually assessed based on measurement of the ristocetin cofactor (VWF:RCo).	Ristocetin	65-75	von Willebrand factor	Homo sapiens	86-89
22268616-0	2012	Development of an ELISA method for testing VWF ristocetin cofactor activity with improved sensitivity and reliability in the diagnosis of von Willebrand disease.	Ristocetin	47-57	von Willebrand factor	Homo sapiens	43-46
22268616-4	2012	VWF was captured by rfGPIbalpha in the presence of ristocetin, and then detected by HRP-conjugated rabbit anti-human VWF IgG.	Ristocetin	51-61	von Willebrand factor	Homo sapiens	0-3
22232560-6	2012	A selection of compounds showing good in silico docking scores into the predicted pockets was retained for testing their in vitro effect on VWF-GPIbalpha complex formation, by which we identified a compound that surprisingly stimulated the VWF-GPIbalpha binding in a ristocetin cofactor ELISA and increased platelet adhesion in whole blood to collagen under arterial shear rate but in contrast inhibited ristocetin-induced platelet aggregation.	Ristocetin	267-277	von Willebrand factor	Homo sapiens	140-143
22232560-6	2012	A selection of compounds showing good in silico docking scores into the predicted pockets was retained for testing their in vitro effect on VWF-GPIbalpha complex formation, by which we identified a compound that surprisingly stimulated the VWF-GPIbalpha binding in a ristocetin cofactor ELISA and increased platelet adhesion in whole blood to collagen under arterial shear rate but in contrast inhibited ristocetin-induced platelet aggregation.	Ristocetin	267-277	glycoprotein Ib platelet subunit alpha	Homo sapiens	144-153
22232560-6	2012	A selection of compounds showing good in silico docking scores into the predicted pockets was retained for testing their in vitro effect on VWF-GPIbalpha complex formation, by which we identified a compound that surprisingly stimulated the VWF-GPIbalpha binding in a ristocetin cofactor ELISA and increased platelet adhesion in whole blood to collagen under arterial shear rate but in contrast inhibited ristocetin-induced platelet aggregation.	Ristocetin	267-277	von Willebrand factor	Homo sapiens	240-243
22232560-6	2012	A selection of compounds showing good in silico docking scores into the predicted pockets was retained for testing their in vitro effect on VWF-GPIbalpha complex formation, by which we identified a compound that surprisingly stimulated the VWF-GPIbalpha binding in a ristocetin cofactor ELISA and increased platelet adhesion in whole blood to collagen under arterial shear rate but in contrast inhibited ristocetin-induced platelet aggregation.	Ristocetin	267-277	glycoprotein Ib platelet subunit alpha	Homo sapiens	244-253
22232560-6	2012	A selection of compounds showing good in silico docking scores into the predicted pockets was retained for testing their in vitro effect on VWF-GPIbalpha complex formation, by which we identified a compound that surprisingly stimulated the VWF-GPIbalpha binding in a ristocetin cofactor ELISA and increased platelet adhesion in whole blood to collagen under arterial shear rate but in contrast inhibited ristocetin-induced platelet aggregation.	Ristocetin	404-414	von Willebrand factor	Homo sapiens	140-143
22232560-6	2012	A selection of compounds showing good in silico docking scores into the predicted pockets was retained for testing their in vitro effect on VWF-GPIbalpha complex formation, by which we identified a compound that surprisingly stimulated the VWF-GPIbalpha binding in a ristocetin cofactor ELISA and increased platelet adhesion in whole blood to collagen under arterial shear rate but in contrast inhibited ristocetin-induced platelet aggregation.	Ristocetin	404-414	glycoprotein Ib platelet subunit alpha	Homo sapiens	144-153
22232560-6	2012	A selection of compounds showing good in silico docking scores into the predicted pockets was retained for testing their in vitro effect on VWF-GPIbalpha complex formation, by which we identified a compound that surprisingly stimulated the VWF-GPIbalpha binding in a ristocetin cofactor ELISA and increased platelet adhesion in whole blood to collagen under arterial shear rate but in contrast inhibited ristocetin-induced platelet aggregation.	Ristocetin	404-414	von Willebrand factor	Homo sapiens	240-243
22232560-6	2012	A selection of compounds showing good in silico docking scores into the predicted pockets was retained for testing their in vitro effect on VWF-GPIbalpha complex formation, by which we identified a compound that surprisingly stimulated the VWF-GPIbalpha binding in a ristocetin cofactor ELISA and increased platelet adhesion in whole blood to collagen under arterial shear rate but in contrast inhibited ristocetin-induced platelet aggregation.	Ristocetin	404-414	glycoprotein Ib platelet subunit alpha	Homo sapiens	244-253
22654514-9	2012	MLV-FBN inhibited aggregation induced by arachidonic acid (52.1% +- 8.1% versus 88.0% +- 2.1% in control; P &lt; 0.01) and ristocetin (40.3% +- 8.8% versus 94.3% +- 1.1%; P &lt; 0.005), but it did not modify closure times in PFA-100( ) studies.	Ristocetin	123-133	fibrinogen beta chain	Homo sapiens	4-7
21917758-9	2011	HOCl-oxidized VWF was hyperfunctional, agglutinating platelets at ristocetin concentrations that induced minimal agglutination using unoxidized VWF and binding more of the nanobody AU/VWFa-11, which detects a gain-of-function conformation of the A1 domain.	Ristocetin	66-76	von Willebrand factor	Homo sapiens	14-17
22155434-4	2012	Supportive of our hypothesis, we found remarkably high levels of factor VIII activity, Von Willebrand factor (vWF) antigen and vWF ristocetin cofactor activity (268%, 740%, 590% respectively).	Ristocetin	131-141	von Willebrand factor	Homo sapiens	127-130
20724302-4	2011	In the first prospective study, we demonstrate that in most cases of VWD, VWF ristocetin cofactor activity (VWF:RCo) and VWF:Act are highly correlated but that they both cannot be considered a good screening assay when used alone, since they could miss about 25% of VWF abnormalities.	Ristocetin	78-88	von Willebrand factor	Homo sapiens	74-77
20724302-4	2011	In the first prospective study, we demonstrate that in most cases of VWD, VWF ristocetin cofactor activity (VWF:RCo) and VWF:Act are highly correlated but that they both cannot be considered a good screening assay when used alone, since they could miss about 25% of VWF abnormalities.	Ristocetin	78-88	von Willebrand factor	Homo sapiens	108-111
20724302-4	2011	In the first prospective study, we demonstrate that in most cases of VWD, VWF ristocetin cofactor activity (VWF:RCo) and VWF:Act are highly correlated but that they both cannot be considered a good screening assay when used alone, since they could miss about 25% of VWF abnormalities.	Ristocetin	78-88	von Willebrand factor	Homo sapiens	108-111
22338157-2	2011	METHODS: The VWF binding to GP I b alpha induced by ristocetin was analyzed by flow cytometry, in three GP I b-IX-expressing Chinese hamster ovary (CHO) cell lines 1b9, delta 565 and delta 551, adhesion of above cells on VWF by flow chamber analysis at shear rate of 200 s(-1).	Ristocetin	52-62	von Willebrand factor	Cricetulus griseus	13-16
21822587-2	2011	We have previously reported two monoclonal antibodies (mAbs), SZ-123 and SZ-125, which specifically bind the VWF A3 domain and block the interaction of VWF with collagen type III and ristocetin- or botrocetin-induced platelet aggregation.	Ristocetin	183-193	von Willebrand factor	Homo sapiens	109-112
21822587-2	2011	We have previously reported two monoclonal antibodies (mAbs), SZ-123 and SZ-125, which specifically bind the VWF A3 domain and block the interaction of VWF with collagen type III and ristocetin- or botrocetin-induced platelet aggregation.	Ristocetin	183-193	von Willebrand factor	Homo sapiens	152-155
21643680-6	2011	VWD was diagnosed by comprehensive laboratory tests including factor VIII clotting activity, von Willebrand factor antigen assay, VWF:ristocetin cofactor activity (VWF:RCo) and platelet function analyzer (PFA)-100 closure times.	Ristocetin	134-144	von Willebrand factor	Homo sapiens	0-3
22338157-2	2011	METHODS: The VWF binding to GP I b alpha induced by ristocetin was analyzed by flow cytometry, in three GP I b-IX-expressing Chinese hamster ovary (CHO) cell lines 1b9, delta 565 and delta 551, adhesion of above cells on VWF by flow chamber analysis at shear rate of 200 s(-1).	Ristocetin	52-62	glycoprotein 1b, alpha polypeptide	Mus musculus	28-40
22338157-4	2011	RESULTS: The VWF binding to GP I b alpha was higher in delta 565 cells stimulated by ristocetin than in delta 551 or 1b9 cells.	Ristocetin	85-95	Von Willebrand factor	Mus musculus	13-16
21186048-0	2011	A rapid, automated VWF ristocetin cofactor activity assay improves reliability in the diagnosis of Von Willebrand disease.	Ristocetin	23-33	von Willebrand factor	Homo sapiens	19-22
22338157-4	2011	RESULTS: The VWF binding to GP I b alpha was higher in delta 565 cells stimulated by ristocetin than in delta 551 or 1b9 cells.	Ristocetin	85-95	glycoprotein 1b, alpha polypeptide	Mus musculus	28-40
22102188-5	2011	Laboratory testing shows low VWF:ristocetin cofactor and low or normal VWF:antigen and characteristically an enhanced ristocetin-induced platelet agglutination (RIPA).	Ristocetin	33-43	von Willebrand factor	Homo sapiens	29-32
22102197-4	2011	There are 103 patients with VWF ristocetin (RCo) &lt;=50 IU/dL: 38 (37%) severe (VWF:RCo &lt;10 IU/dL), 28 (27%) moderate (VWF:RCo 10 to 29 IU/dL), and 37 (36%) mild (VWF:RCo 30 to 50 IU/dL).	Ristocetin	32-42	von Willebrand factor	Homo sapiens	28-31
22102202-9	2011	Haemosolvate FVIII contains a VWF antigen concentration of 167 +- 27 IU/mL, a ristocetin cofactor activity of 100 +- 29 IU/mL, a collagen binding activity of 99 +- 29 IU/mL, normal VWF multimers, and a FVIII concentration of 50 IU/mL.	Ristocetin	78-88	coagulation factor VIII	Homo sapiens	13-18
21655675-7	2011	The efficacy of ALX-0081 was assessed by in vitro experiments: flow chamber experiments, ristocetin-induced platelet aggregation (RIPA), and the platelet function analyser (PFA-100 ).	Ristocetin	89-99	hematopoietic SH2 domain containing	Homo sapiens	16-19
21301783-10	2011	In addition, G-CSF enhanced ristocetin-induced platelet aggregation (+18%) whereas TRAP-induced platelet aggregation decreased slightly (-14%) in response to filgrastim.	Ristocetin	28-38	colony stimulating factor 3	Homo sapiens	13-18
21070498-1	2011	von Willebrand"s disease (VWD) is regarded as the most common congenital bleeding disorder, and although not available in all laboratories von Willebrand factor (VWF) activity is most frequently assessed as ristocetin cofactor (VWF:RCo).	Ristocetin	207-217	von Willebrand factor	Homo sapiens	139-160
21070498-1	2011	von Willebrand"s disease (VWD) is regarded as the most common congenital bleeding disorder, and although not available in all laboratories von Willebrand factor (VWF) activity is most frequently assessed as ristocetin cofactor (VWF:RCo).	Ristocetin	207-217	von Willebrand factor	Homo sapiens	162-165
21148813-7	2011	As previously reported, VWF:RCo/VWF:Ag ratio was decreased with a common A1 domain polymorphism, D1472H, as was direct binding to ristocetin for a 1472H A1 loop construct.	Ristocetin	130-140	von Willebrand factor	Homo sapiens	24-27
21193108-3	2011	The classification is based on phenotypic assays including FVIII, VWF:Ag and VWF activity, typically by ristocetin cofactor (VWF:RCo), but also increasingly by collagen binding (VWF:CB).	Ristocetin	104-114	von Willebrand factor	Homo sapiens	77-80
21193108-3	2011	The classification is based on phenotypic assays including FVIII, VWF:Ag and VWF activity, typically by ristocetin cofactor (VWF:RCo), but also increasingly by collagen binding (VWF:CB).	Ristocetin	104-114	von Willebrand factor	Homo sapiens	77-80
21193108-3	2011	The classification is based on phenotypic assays including FVIII, VWF:Ag and VWF activity, typically by ristocetin cofactor (VWF:RCo), but also increasingly by collagen binding (VWF:CB).	Ristocetin	104-114	von Willebrand factor	Homo sapiens	77-80
21035359-11	2010	The reduced ristocetin-mediated agglutination of thrombocytes in a plate tilting assay, using blood from adult zebrafish injected with VMO, provided evidence that vWF is involved in the hemostatic process.	Ristocetin	12-22	von Willebrand factor	Danio rerio	163-166
20979592-6	2010	Platelet adhesion to ristocetin-activated VWF was studied in the presence of reduced beta(2) GPI.	Ristocetin	21-31	von Willebrand factor	Homo sapiens	42-45
20738304-4	2010	In a multiple stepwise regression model, age- and sex-adjusted PFA-100 ADP and VWF ristocetin cofactor activity (VWF:RCo) were independently associated with BS.	Ristocetin	83-93	von Willebrand factor	Homo sapiens	79-82
20738304-4	2010	In a multiple stepwise regression model, age- and sex-adjusted PFA-100 ADP and VWF ristocetin cofactor activity (VWF:RCo) were independently associated with BS.	Ristocetin	83-93	von Willebrand factor	Homo sapiens	113-116
20589372-0	2010	Ristocetin-induced self-aggregation of von Willebrand factor.	Ristocetin	0-10	von Willebrand factor	Homo sapiens	39-60
20589372-3	2010	Ristocetin also promotes the interaction of VWF with GpIb and is able to induce platelet aggregation, and thus is largely used to mimic this effect in vitro.	Ristocetin	0-10	von Willebrand factor	Homo sapiens	44-47
20589372-4	2010	In this research paper, we followed the time course of VWF self-association in solution induced by ristocetin binding by light scattering and at the same time we collected atomic force microscopy images to clarify the nature of the assembly that is formed.	Ristocetin	99-109	von Willebrand factor	Homo sapiens	55-58
20727070-3	2010	RESULTS:  Addition of extra ristocetin resulted in improved measurement of VWF recoveries from various VWF-containing concentrates that were underestimated using the standard automated protocol.	Ristocetin	28-38	von Willebrand factor	Homo sapiens	75-78
20727070-3	2010	RESULTS:  Addition of extra ristocetin resulted in improved measurement of VWF recoveries from various VWF-containing concentrates that were underestimated using the standard automated protocol.	Ristocetin	28-38	von Willebrand factor	Homo sapiens	103-106
20979592-6	2010	Platelet adhesion to ristocetin-activated VWF was studied in the presence of reduced beta(2) GPI.	Ristocetin	21-31	apolipoprotein H	Homo sapiens	85-96