PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 24790143-9 2014 Moreover, DNA-VWF interaction can be blocked using unfractionated and low-molecular-weight heparin, and DNA-VWF complexes attenuate platelet binding to VWF. Heparin 91-98 von Willebrand factor Homo sapiens 14-17 25969127-8 2015 Heparin reduced MSC-associated thrombosis incorporating platelets and VWF within the microvasculature. Heparin 0-7 von Willebrand factor Homo sapiens 70-73 23069711-8 2013 POC-Heparin supported EC and BOEC adhesion, viability, proliferation, NO production, and expression of endothelial cell-specific markers von Willebrand factor (vWF) and vascular endothelial-cadherin (VE-cadherin). Heparin 4-11 von Willebrand factor Homo sapiens 160-163 12022870-2 2002 To probe this molecular reaction as well as the role of electrostatic forces in VWF-heparin interaction, we performed mutagenesis and molecular modeling experiments. Heparin 84-91 von Willebrand factor Homo sapiens 80-83 16158039-0 2005 Elevation of plasma von Willebrand factor and tumor necrosis factor-a in obese subjects and their reduction by the low molecular weight heparin tinzaparin. Heparin 136-143 von Willebrand factor Homo sapiens 20-41 12801846-8 2003 With long periods of incubation (24-48h), both unfractionated heparin and enoxaparin significantly increased TFPI release (control vs. unfractionated heparin, p<0.05-0.001; control vs. enoxaparin, p<0.01-0.001) and also reduced the release of vWF in the culture medium, though no variations in endothelial cell procoagulant activity or TF content were observed. Heparin 62-69 von Willebrand factor Homo sapiens 249-252 12871332-5 2003 Recombinant VWF A1 domain (rVWF-A1) bound specifically and saturably to sulfatides (half-maximal concentration of approximately 12.5 microg mL(-1)), binding that was blocked by dextran sulfate (IC(50) approximately equal to 100 microg mL(-1)) but not by heparin at concentrations up to 100 U mL(-1). Heparin 254-261 von Willebrand factor Homo sapiens 12-15 23907946-10 2013 Of the tested heparin formulas UFH seems to be the most potent in altering the OPG, RANKL and vWF axis. Heparin 14-21 von Willebrand factor Homo sapiens 94-97 23907946-10 2013 Of the tested heparin formulas UFH seems to be the most potent in altering the OPG, RANKL and vWF axis. Heparin 31-34 von Willebrand factor Homo sapiens 94-97 20505748-7 2010 Furthermore, our data indicate a protective effect of heparins on EC activation as shown by reduced VWF release in response to MV3 supernatant. Heparin 54-62 von Willebrand factor Homo sapiens 100-103 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. Heparin 155-162 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. Heparin 155-162 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. Heparin 155-162 von Willebrand factor Homo sapiens 128-131 16338223-0 2006 Identification of amino acid residues essential for heparin binding by the A1 domain of human von Willebrand factor. Heparin 52-59 von Willebrand factor Homo sapiens 94-115 16338223-2 2006 Previous observations suggested that heparin competitively inhibits the binding of VWF to GPIb and may down-regulate platelet adhesion. Heparin 37-44 von Willebrand factor Homo sapiens 83-86 16338223-7 2006 Our findings suggest that heparin may inhibit the binding of VWF to GPIb by interacting with GPIb binding and interpret why some hemorrhagic complications of heparin therapy are not predictable based on techniques for monitoring the conventional anticoagulant effects of heparin. Heparin 26-33 von Willebrand factor Homo sapiens 61-64 16338223-7 2006 Our findings suggest that heparin may inhibit the binding of VWF to GPIb by interacting with GPIb binding and interpret why some hemorrhagic complications of heparin therapy are not predictable based on techniques for monitoring the conventional anticoagulant effects of heparin. Heparin 158-165 von Willebrand factor Homo sapiens 61-64 16338223-7 2006 Our findings suggest that heparin may inhibit the binding of VWF to GPIb by interacting with GPIb binding and interpret why some hemorrhagic complications of heparin therapy are not predictable based on techniques for monitoring the conventional anticoagulant effects of heparin. Heparin 158-165 von Willebrand factor Homo sapiens 61-64 15670034-6 2005 However, when patients were stratified by IL-1RN genotype, LMWH was superior to UFH in reducing Delta vWF only in allele *2 carriers (0.51 iU mL(-1) vs. 1.37, P < 0.01), but not in non-carriers (- 0.03 iU mL(-1) vs. 0.15, P = NS). Heparin 80-83 von Willebrand factor Homo sapiens 102-105 15358546-5 2004 Although soluble decorin prevented VWF binding to heparin, purified VWF-A1 domain failed to interact with the proteoglycan. Heparin 50-57 von Willebrand factor Homo sapiens 35-38 15249683-9 2004 Heparin also increased the digestion of purified plasma vWF. Heparin 0-7 von Willebrand factor Homo sapiens 56-59 12851529-7 2003 Our data suggest that a fragment of approximately 60 kDa that co-purified with FN, with affinity to heparin and gelatin, has the arFN that controls vWF multimer size. Heparin 100-107 von Willebrand factor Homo sapiens 148-151 12686329-11 2003 vWF is linked to inflammation and, like glycoprotein Ib/IX, is affected more favorably by the LWMHs than by UFH. Heparin 108-111 von Willebrand factor Homo sapiens 0-3 11992238-12 2002 The analysis of vWF multimers in the different fractions obtained by affinity chromatography on heparin Sepharose showed that the activity measured both with RCo assay and CBA correlated with the degree of multimerization. Heparin 96-103 von Willebrand factor Homo sapiens 16-19 11427638-5 2001 On bivariate regression analysis, vWF : Ag level was directly associated with the presence of CVD, age, fibrinogen and the use of enoxaparin (vs unfractionated heparin) during HD procedures, and inversely with albumin and pre-dialysis BP. Heparin 160-167 von Willebrand factor Homo sapiens 34-37 11853892-1 2002 The ability of a soluble heparin-binding oligopeptide sequence derived from the von Willebrand factor (vWF) to modulate the adhesion and chemokinetic migration behavior of arterial smooth muscle cells was assessed using a novel glass microsphere centrifugation assay and automated time-lapse fluorescence videomicroscopy, respectively. Heparin 25-32 von Willebrand factor Homo sapiens 80-101 11853892-1 2002 The ability of a soluble heparin-binding oligopeptide sequence derived from the von Willebrand factor (vWF) to modulate the adhesion and chemokinetic migration behavior of arterial smooth muscle cells was assessed using a novel glass microsphere centrifugation assay and automated time-lapse fluorescence videomicroscopy, respectively. Heparin 25-32 von Willebrand factor Homo sapiens 103-106 11853892-4 2002 The specificity of this response to the vWF-derived heparin-binding peptide was supported by the absence of an observed effect in the presence of either a scrambled peptide or a consensus heparin-binding peptide sequence of similar heparin affinity. Heparin 52-59 von Willebrand factor Homo sapiens 40-43 11776314-1 2001 The aim of our study was to characterise heparin-binding properties of mutated von Willebrand factor (VWF) in 24 patients plasmas with type 2 von Willebrand disease (VWD). Heparin 41-48 von Willebrand factor Homo sapiens 79-100 11776314-1 2001 The aim of our study was to characterise heparin-binding properties of mutated von Willebrand factor (VWF) in 24 patients plasmas with type 2 von Willebrand disease (VWD). Heparin 41-48 von Willebrand factor Homo sapiens 102-105 11535495-6 2001 In this study, the purification of human vWF-cleaving protease from a commercial preparation of factor VIII/vWF concentrate by means of several column chromatographic steps, including 2 steps of heparin-Sepharose column, is reported. Heparin 195-202 von Willebrand factor Homo sapiens 41-44 10590063-0 1999 Modulation by heparin of the interaction of the A1 domain of Von Willebrand factor with glycoprotein Ib. Heparin 14-21 von Willebrand factor Homo sapiens 61-82 11254909-1 2001 As thrombin stimulates P-selectin expression on platelets and its release into plasma, we hypothesized that enhancing antithrombin activity by unfractionated heparin (UFH) could decrease plasma levels of circulating (c)P-selectin, (c)E-selectin, and von Willebrand Factor (vWF). Heparin 167-170 von Willebrand factor Homo sapiens 250-271 11254909-1 2001 As thrombin stimulates P-selectin expression on platelets and its release into plasma, we hypothesized that enhancing antithrombin activity by unfractionated heparin (UFH) could decrease plasma levels of circulating (c)P-selectin, (c)E-selectin, and von Willebrand Factor (vWF). Heparin 167-170 von Willebrand factor Homo sapiens 273-276 10739395-7 2000 When protamine sulphate was added to PRP containing heparin, even at clinically relevant neutralizing doses the GPIb-vWF activity was reduced by 20-30% (p < 0.001). Heparin 52-59 von Willebrand factor Homo sapiens 117-120 11920189-0 2000 von Willebrand factor binding to heparin in various types of von Willebrand disease. Heparin 33-40 von Willebrand factor Homo sapiens 0-21 11920189-1 2000 INTRODUCTION: The purpose was to study von Willebrand factor (vWF) binding to heparin in different types of von Willebrand disease (vWD). Heparin 78-85 von Willebrand factor Homo sapiens 39-60 11920189-1 2000 INTRODUCTION: The purpose was to study von Willebrand factor (vWF) binding to heparin in different types of von Willebrand disease (vWD). Heparin 78-85 von Willebrand factor Homo sapiens 62-65 11920189-4 2000 We determined the range of vWF concentrations in plasma where the percentage of (125)I-MAb/vWF complexes bound to heparin-agarose beads was constant. Heparin 114-121 von Willebrand factor Homo sapiens 27-30 11920189-4 2000 We determined the range of vWF concentrations in plasma where the percentage of (125)I-MAb/vWF complexes bound to heparin-agarose beads was constant. Heparin 114-121 von Willebrand factor Homo sapiens 91-94 11920189-6 2000 RESULTS: The multimeric composition of vWF had hardly any influence on the ability of vWF to bind to heparin. Heparin 101-108 von Willebrand factor Homo sapiens 86-89 11920189-10 2000 Furthermore, when comparing the mean values of plasma vWF-heparin binding ratios by ANOVA F-test in the six groups (one normal and five vWD), we found significant differences between them (P<0.0001). Heparin 58-65 von Willebrand factor Homo sapiens 54-57 11920189-12 2000 CONCLUSION: Our data suggest a relationship between the ability of vWF to bind to heparin and to the platelet GPIb receptor, since type 2B and 2N patients have an increased or normal ability to bind to GPIb whereas type 2A and 2M patients have an impaired interaction with that receptor. Heparin 82-89 von Willebrand factor Homo sapiens 67-70 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. Heparin 233-240 von Willebrand factor Homo sapiens 37-40 10590063-8 1999 These results indicated that heparin was able to induce vWF-dependent CHO-GPIbalphabeta/IX cell aggregation. Heparin 29-36 von Willebrand factor Homo sapiens 56-59 10590063-9 1999 In conclusion, we demonstrated that heparin is capable of positively modulating the vWF interaction with the GPIb/V/IX complex. Heparin 36-43 von Willebrand factor Homo sapiens 84-87 10089894-0 1999 Selectivity of von Willebrand factor triplet bands towards heparin binding supports structural model. Heparin 59-66 von Willebrand factor Homo sapiens 15-36 10089894-2 1999 Because heparin binding sites are contained in each vWF subunit, high molecular weight multimers of r-vWF and hp-vWF, respectively, were eluted with higher salt concentration, in comparison to r-vWF and hp-vWF molecules with a low degree of multimerization. Heparin 8-15 von Willebrand factor Homo sapiens 52-55 10089894-2 1999 Because heparin binding sites are contained in each vWF subunit, high molecular weight multimers of r-vWF and hp-vWF, respectively, were eluted with higher salt concentration, in comparison to r-vWF and hp-vWF molecules with a low degree of multimerization. Heparin 8-15 von Willebrand factor Homo sapiens 102-105 10089894-2 1999 Because heparin binding sites are contained in each vWF subunit, high molecular weight multimers of r-vWF and hp-vWF, respectively, were eluted with higher salt concentration, in comparison to r-vWF and hp-vWF molecules with a low degree of multimerization. Heparin 8-15 von Willebrand factor Homo sapiens 102-105 10089894-2 1999 Because heparin binding sites are contained in each vWF subunit, high molecular weight multimers of r-vWF and hp-vWF, respectively, were eluted with higher salt concentration, in comparison to r-vWF and hp-vWF molecules with a low degree of multimerization. Heparin 8-15 von Willebrand factor Homo sapiens 102-105 10089894-2 1999 Because heparin binding sites are contained in each vWF subunit, high molecular weight multimers of r-vWF and hp-vWF, respectively, were eluted with higher salt concentration, in comparison to r-vWF and hp-vWF molecules with a low degree of multimerization. Heparin 8-15 von Willebrand factor Homo sapiens 102-105 10089894-4 1999 By contrast, faster migrating satellite bands and slower migrating satellite bands of hp-vWF exhibited reduced and increased heparin affinity, respectively, compared to the intermediate band of the same triplet. Heparin 125-132 von Willebrand factor Homo sapiens 89-92 10089894-5 1999 Because heparin binding sites are localised in the N-terminal domain of the hp-vWF subunit, this result confirms a structural model of hp-vWF (Fischer et al., Biochem. Heparin 8-15 von Willebrand factor Homo sapiens 79-82 21340993-8 1999 The A1 domain is involved in binding of vWF to platelet glycoprotein 1b (GpIb), binding to fibrillar collagen, sulfatides, and heparin. Heparin 127-134 von Willebrand factor Homo sapiens 40-43 10743240-5 1998 In 16 patients with stable COPD and F1 + 2 greater than 1.65 nmol/L (mean +2s of control), intra-venose heparin therapy (100 mg qd for 10 days) significantly reduced F1 + 2(P < 0.005), vWF (P < 0.05), GMP-140 (P < 0.05), and PaCO2 (P < 0.05). Heparin 104-111 von Willebrand factor Homo sapiens 188-191 9711933-9 1998 Moreover the early increase of von Willebrand factor was more frequent and more severe with unfractionated heparin than with enoxaparin (mean change was +8.7+/-8.8% with enoxaparin versus +93.9+/-11.7% with unfractionated heparin, P<0.0001). Heparin 107-114 von Willebrand factor Homo sapiens 31-52 9711933-9 1998 Moreover the early increase of von Willebrand factor was more frequent and more severe with unfractionated heparin than with enoxaparin (mean change was +8.7+/-8.8% with enoxaparin versus +93.9+/-11.7% with unfractionated heparin, P<0.0001). Heparin 222-229 von Willebrand factor Homo sapiens 31-52 9447247-2 1997 Heparin affinity chromatography yielded r-vWF polymers of different degrees of multimerization. Heparin 0-7 von Willebrand factor Homo sapiens 42-45 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. Heparin 121-128 von Willebrand factor Homo sapiens 30-33 9490688-12 1998 Because heparin binding inhibits the interaction with GpIb, this provides an explanation of vWF upregulation. Heparin 8-15 von Willebrand factor Homo sapiens 92-95 8873615-10 1996 The interaction of vWF with heparin was significantly reduced by substitution of Lys residues 642-645, indicating that these residues may form part of a heparin-binding domain in the carboxy-terminal half of the Cys509-Cys695 loop. Heparin 28-35 von Willebrand factor Homo sapiens 19-22 8873615-10 1996 The interaction of vWF with heparin was significantly reduced by substitution of Lys residues 642-645, indicating that these residues may form part of a heparin-binding domain in the carboxy-terminal half of the Cys509-Cys695 loop. Heparin 153-160 von Willebrand factor Homo sapiens 19-22 8598091-4 1996 METHODS AND RESULTS: Immobilized synthetic peptides based on a known heparin-binding domain of vWF were used to yield novel fractions of standard heparin that demonstrated a sevenfold increase in their ability to inhibit vWF-dependent platelet agglutination and vWF/platelet binding. Heparin 69-76 von Willebrand factor Homo sapiens 95-98 8885147-1 1996 The smallest circulating von Willebrand factor (vWF) molecule is a dimer composed of two identical subunits containing binding sites for heparin, collagen, platelet glycoproteins and coagulation factor VIII (FVIII). Heparin 137-144 von Willebrand factor Homo sapiens 25-46 8885147-1 1996 The smallest circulating von Willebrand factor (vWF) molecule is a dimer composed of two identical subunits containing binding sites for heparin, collagen, platelet glycoproteins and coagulation factor VIII (FVIII). Heparin 137-144 von Willebrand factor Homo sapiens 48-51 8885147-5 1996 Heparin affinity chromatography was used to isolate vWF polymers of different degree of multimerization. Heparin 0-7 von Willebrand factor Homo sapiens 52-55 8598091-4 1996 METHODS AND RESULTS: Immobilized synthetic peptides based on a known heparin-binding domain of vWF were used to yield novel fractions of standard heparin that demonstrated a sevenfold increase in their ability to inhibit vWF-dependent platelet agglutination and vWF/platelet binding. Heparin 146-153 von Willebrand factor Homo sapiens 95-98 8598091-4 1996 METHODS AND RESULTS: Immobilized synthetic peptides based on a known heparin-binding domain of vWF were used to yield novel fractions of standard heparin that demonstrated a sevenfold increase in their ability to inhibit vWF-dependent platelet agglutination and vWF/platelet binding. Heparin 146-153 von Willebrand factor Homo sapiens 221-224 8598091-4 1996 METHODS AND RESULTS: Immobilized synthetic peptides based on a known heparin-binding domain of vWF were used to yield novel fractions of standard heparin that demonstrated a sevenfold increase in their ability to inhibit vWF-dependent platelet agglutination and vWF/platelet binding. Heparin 146-153 von Willebrand factor Homo sapiens 221-224 8598091-5 1996 The high vWF affinity heparin showed enhanced anti-factor Xa activity but comparable activated partial thromboplastin time activity. Heparin 22-29 von Willebrand factor Homo sapiens 9-12 8598091-6 1996 Chemical modification of a standard heparin by periodate oxidation and borohydride reduction enhanced its ability to inhibit platelet/vWF interactions by threefold, while eliminating more than 90% of its activated partial thromboplastin time and anti-factor Xa activity. Heparin 36-43 von Willebrand factor Homo sapiens 134-137 8598091-8 1996 CONCLUSIONS: Subspecies of heparin can be developed with significantly enhanced potency to inhibit vWF/platelet interactions. Heparin 27-34 von Willebrand factor Homo sapiens 99-102 8598091-9 1996 The vWF-inhibiting property of heparin can be dissociated from its antithrombin-binding activity. Heparin 31-38 von Willebrand factor Homo sapiens 4-7 8598091-10 1996 Based on a growing understanding of heparin/vWF interactions, combinations of affinity separations and chemical modifications could be designed to yield heparins uniquely suitable for prevention of arterial thrombosis. Heparin 153-161 von Willebrand factor Homo sapiens 44-47 7495084-7 1995 Addition of heparin or ECGS (endothelial cell growth supplement) decreased the von Willebrand factor content in the matrix. Heparin 12-19 von Willebrand factor Homo sapiens 79-100 8747526-3 1996 VCL inhibited 50% of vWf binding to heparin, but it did not inhibit vWf binding to type I collagen. Heparin 36-43 von Willebrand factor Homo sapiens 21-24 7540413-1 1995 Monoclonal antibody (MoAb) B724 to von Willebrand factor (vWF) completely inhibits its interaction with heparin, sulphatides and botrocetin and consequently botrocetin-induced binding of vWF to platelets. Heparin 104-111 von Willebrand factor Homo sapiens 35-56 7540413-1 1995 Monoclonal antibody (MoAb) B724 to von Willebrand factor (vWF) completely inhibits its interaction with heparin, sulphatides and botrocetin and consequently botrocetin-induced binding of vWF to platelets. Heparin 104-111 von Willebrand factor Homo sapiens 58-61 8598091-0 1996 Heparins designed to specifically inhibit platelet interactions with von Willebrand factor. Heparin 0-8 von Willebrand factor Homo sapiens 69-90 8598091-2 1996 Previously, we demonstrated that heparin interfered with platelet/vWF hemostatic mechanisms by binding to vWF within the proteins"s domain responsible for binding the platelet vWF receptor, glycoprotein Ib. Heparin 33-40 von Willebrand factor Homo sapiens 66-69 8598091-2 1996 Previously, we demonstrated that heparin interfered with platelet/vWF hemostatic mechanisms by binding to vWF within the proteins"s domain responsible for binding the platelet vWF receptor, glycoprotein Ib. Heparin 33-40 von Willebrand factor Homo sapiens 106-109 8598091-2 1996 Previously, we demonstrated that heparin interfered with platelet/vWF hemostatic mechanisms by binding to vWF within the proteins"s domain responsible for binding the platelet vWF receptor, glycoprotein Ib. Heparin 33-40 von Willebrand factor Homo sapiens 106-109 8598091-3 1996 The purpose of the present study was to develop and refine heparins with greater potency to inhibit platelet/vWF interactions. Heparin 59-67 von Willebrand factor Homo sapiens 109-112 21043709-0 1995 Inhibition of Binding of von Willebrand Factor to the Platelet Glycoprotein Ib-IX Complex, Heparin and Sulfatides by Polyanionic Compounds. Heparin 91-98 von Willebrand factor Homo sapiens 25-46 21043709-8 1995 In addition, aurintricarboxylic acid, Evans blue and fucoidan all inhibited binding of vWF to both heparin and sulfatides with similar ICso values. Heparin 99-106 von Willebrand factor Homo sapiens 87-90 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. Heparin 71-78 von Willebrand factor Homo sapiens 64-67 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. Heparin 71-78 von Willebrand factor Homo sapiens 159-162 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. Heparin 71-78 von Willebrand factor Homo sapiens 159-162 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. Heparin 293-300 von Willebrand factor Homo sapiens 64-67 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. Heparin 293-300 von Willebrand factor Homo sapiens 159-162 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. Heparin 293-300 von Willebrand factor Homo sapiens 159-162 21043709-11 1995 These combined experiments provide evidence for an electrostatic model of vWF modulation, and suggest that the heparin-binding domain of vWF may be an important regulatory site involved in the adhesion of vWF to the platelet GP Ib-IX complex. Heparin 111-118 von Willebrand factor Homo sapiens 74-77 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. Heparin 142-149 von Willebrand factor Homo sapiens 11-14 21043709-11 1995 These combined experiments provide evidence for an electrostatic model of vWF modulation, and suggest that the heparin-binding domain of vWF may be an important regulatory site involved in the adhesion of vWF to the platelet GP Ib-IX complex. Heparin 111-118 von Willebrand factor Homo sapiens 137-140 21043709-11 1995 These combined experiments provide evidence for an electrostatic model of vWF modulation, and suggest that the heparin-binding domain of vWF may be an important regulatory site involved in the adhesion of vWF to the platelet GP Ib-IX complex. Heparin 111-118 von Willebrand factor Homo sapiens 137-140 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. Heparin 142-149 von Willebrand factor Homo sapiens 52-55 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. Heparin 142-149 von Willebrand factor Homo sapiens 52-55 21043709-6 1995 Firstly, it was confirmed using a solid-phase binding assay that, like sulfatides, heparin specifically bound to a purified 39/WkiloDalton fragment of vWF (Leu-480 to Gly-718) that encompasses the A1 domain. Heparin 83-90 von Willebrand factor Homo sapiens 151-154 21043709-7 1995 Secondly, the ability of a number of polyanionic compounds to inhibit binding of vWF to heparin, but not to immobilized sulfatides, supported previous data suggesting that heparin and sulfatides bind to distinct sites on vWF. Heparin 88-95 von Willebrand factor Homo sapiens 81-84 21043709-7 1995 Secondly, the ability of a number of polyanionic compounds to inhibit binding of vWF to heparin, but not to immobilized sulfatides, supported previous data suggesting that heparin and sulfatides bind to distinct sites on vWF. Heparin 172-179 von Willebrand factor Homo sapiens 81-84 21043709-7 1995 Secondly, the ability of a number of polyanionic compounds to inhibit binding of vWF to heparin, but not to immobilized sulfatides, supported previous data suggesting that heparin and sulfatides bind to distinct sites on vWF. Heparin 172-179 von Willebrand factor Homo sapiens 221-224 8276857-5 1994 We propose that, in addition to catalyzing the inhibition of thrombin and other intrinsic pathway coagulation proteases by antithrombin, heparin functions as an anticoagulant by direct inhibition of the activation of the fVIII-vWf complex by thrombin. Heparin 137-144 von Willebrand factor Homo sapiens 227-230 7819071-7 1994 Platelet and plasma vWf bound to collagen with similar affinities; however, platelet vWf bound to thrombin-stimulated platelets and to heparin with a higher affinity than plasma vWf. Heparin 135-142 von Willebrand factor Homo sapiens 85-88 7819071-7 1994 Platelet and plasma vWf bound to collagen with similar affinities; however, platelet vWf bound to thrombin-stimulated platelets and to heparin with a higher affinity than plasma vWf. Heparin 135-142 von Willebrand factor Homo sapiens 85-88 7900084-0 1994 Heparin enhances endothelial cell von Willebrand factor content by growth factor dependent mechanisms. Heparin 0-7 von Willebrand factor Homo sapiens 34-55 7900084-3 1994 We studied the effect of pharmacologic doses of heparin on the vWf content of endothelial cells. Heparin 48-55 von Willebrand factor Homo sapiens 63-66 7900084-4 1994 After a lag of 8 h and in the presence of crude or purified growth factor, heparin at doses between 0.25 and 2 U (1.4-11 micrograms)/ml, increased the content of high molecular weight vWf. Heparin 75-82 von Willebrand factor Homo sapiens 184-187 7900084-6 1994 Lower molecular weight highly sulfated heparin or heparin-like compounds were most active in growth factor dependent endothelial cell vWf expression. Heparin 39-46 von Willebrand factor Homo sapiens 134-137 7900084-6 1994 Lower molecular weight highly sulfated heparin or heparin-like compounds were most active in growth factor dependent endothelial cell vWf expression. Heparin 50-57 von Willebrand factor Homo sapiens 134-137 7974349-4 1994 The epitope of MAb 710, which inhibits the binding of vWF to glycoprotein Ib (GPIb), was identified between Ser 593 and Ser 678 on the tryptic 52/48 kDa fragment (aa 449-728) which contains binding domains for GPIb, collagen, heparin, sulfatides and subendothelium extracellular matrices. Heparin 226-233 von Willebrand factor Homo sapiens 54-57 8276857-0 1994 Inhibition by heparin of thrombin-catalyzed activation of the factor VIII-von Willebrand factor complex. Heparin 14-21 von Willebrand factor Homo sapiens 74-95 8276857-2 1994 In a defined, plasma-free assay of fVIII activation and at physiological ionic strength and pH, heparin inhibited the rate of activation of either human or porcine fVIII by thrombin in either the presence or absence of von Willebrand factor (vWf). Heparin 96-103 von Willebrand factor Homo sapiens 242-245 8276857-4 1994 At plasma concentrations of fVIII (approximately 1 nM) and vWf (approximately 35 nM), the rate of fVIII activation was inhibited by 50% at approximately 0.1 unit/ml heparin, which is below the normal range of heparin concentrations in plasma during therapeutic anticoagulation (0.2-0.7 unit/ml). Heparin 165-172 von Willebrand factor Homo sapiens 59-62 8276857-4 1994 At plasma concentrations of fVIII (approximately 1 nM) and vWf (approximately 35 nM), the rate of fVIII activation was inhibited by 50% at approximately 0.1 unit/ml heparin, which is below the normal range of heparin concentrations in plasma during therapeutic anticoagulation (0.2-0.7 unit/ml). Heparin 209-216 von Willebrand factor Homo sapiens 59-62 8165633-1 1994 To investigate the influence of the structure of heparin on its binding to vWF, we compared heparin fractions of different molecular weight (MW) or affinity for antithrombin III (ATIII). Heparin 49-56 von Willebrand factor Homo sapiens 75-78 8215459-0 1993 Heparin-von Willebrand factor binding as assessed by isothermal titration calorimetry and by affinity fractionation of heparins using synthetic peptides. Heparin 119-127 von Willebrand factor Homo sapiens 8-29 8215459-2 1993 Based on the motif of a consensus heparin-binding synthetic peptide, a 23-residue sequence (Y565-A587) of human von Willebrand factor (vWF) was previously identified which binds heparin with affinity comparable to that of the native protein (Sobel, M., Soler, D. F., Kermode, J. C., and Harris, R. B. Heparin 34-41 von Willebrand factor Homo sapiens 112-133 8215459-2 1993 Based on the motif of a consensus heparin-binding synthetic peptide, a 23-residue sequence (Y565-A587) of human von Willebrand factor (vWF) was previously identified which binds heparin with affinity comparable to that of the native protein (Sobel, M., Soler, D. F., Kermode, J. C., and Harris, R. B. Heparin 34-41 von Willebrand factor Homo sapiens 135-138 8215459-2 1993 Based on the motif of a consensus heparin-binding synthetic peptide, a 23-residue sequence (Y565-A587) of human von Willebrand factor (vWF) was previously identified which binds heparin with affinity comparable to that of the native protein (Sobel, M., Soler, D. F., Kermode, J. C., and Harris, R. B. Heparin 178-185 von Willebrand factor Homo sapiens 112-133 8215459-2 1993 Based on the motif of a consensus heparin-binding synthetic peptide, a 23-residue sequence (Y565-A587) of human von Willebrand factor (vWF) was previously identified which binds heparin with affinity comparable to that of the native protein (Sobel, M., Soler, D. F., Kermode, J. C., and Harris, R. B. Heparin 178-185 von Willebrand factor Homo sapiens 135-138 8215459-11 1993 They bind a species of heparin which possesses significantly enhanced affinity for native vWF. Heparin 23-30 von Willebrand factor Homo sapiens 90-93 8215459-13 1993 Thus, the vWF peptides are a useful model for studying the physiological role of heparin binding to the native protein. Heparin 81-88 von Willebrand factor Homo sapiens 10-13 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. Heparin 69-76 von Willebrand factor Homo sapiens 5-8 8322266-1 1993 We developed a simple and fast method for studying the heparin binding of von Willebrand factor (vWF) in the plasma milieu. Heparin 55-62 von Willebrand factor Homo sapiens 74-95 8322266-1 1993 We developed a simple and fast method for studying the heparin binding of von Willebrand factor (vWF) in the plasma milieu. Heparin 55-62 von Willebrand factor Homo sapiens 97-100 8322266-3 1993 Further experiments performed with purified vWF of various multimeric composition, obtained either by gradual reduction or gel filtration, confirmed that heparin binding is dependent on the multimerization of vWF and that high molecular weight (HMW) multimers of vWF are required for normal heparin binding. Heparin 154-161 von Willebrand factor Homo sapiens 44-47 8322266-3 1993 Further experiments performed with purified vWF of various multimeric composition, obtained either by gradual reduction or gel filtration, confirmed that heparin binding is dependent on the multimerization of vWF and that high molecular weight (HMW) multimers of vWF are required for normal heparin binding. Heparin 154-161 von Willebrand factor Homo sapiens 209-212 8322266-3 1993 Further experiments performed with purified vWF of various multimeric composition, obtained either by gradual reduction or gel filtration, confirmed that heparin binding is dependent on the multimerization of vWF and that high molecular weight (HMW) multimers of vWF are required for normal heparin binding. Heparin 154-161 von Willebrand factor Homo sapiens 209-212 8322266-4 1993 After reduction of plasma vWF by 1.5 mM DTT, the vWF monomer still binds to heparin but to a lower extent. Heparin 76-83 von Willebrand factor Homo sapiens 49-52 8322266-5 1993 Under these conditions, no significant differences were obtained between control and patients showing that the heparin binding domain located on the vWF subunit is not altered in the subtypes IIA, IIB and IIC studied. Heparin 111-118 von Willebrand factor Homo sapiens 149-152 8165633-5 1994 Using heparin-derived oligosaccharides, we also demonstrated that a minimal chain length of 18 monosaccharides was required for heparin binding to vWF. Heparin 6-13 von Willebrand factor Homo sapiens 147-150 8165633-6 1994 In addition, different fractions with low affinity for ATIII were compared as competitors of 125I-vWF binding to heparin-agarose. Heparin 113-120 von Willebrand factor Homo sapiens 98-101 8165633-8 1994 Thus, heparin interaction with vWF is independent of the presence of the ATIII binding site and is mostly dependent on the length of the heparin chain. Heparin 6-13 von Willebrand factor Homo sapiens 31-34 8165633-8 1994 Thus, heparin interaction with vWF is independent of the presence of the ATIII binding site and is mostly dependent on the length of the heparin chain. Heparin 137-144 von Willebrand factor Homo sapiens 31-34 8165633-9 1994 These data suggest that unfractionated heparin is a more potent inhibitor of vWF-dependent functions than low MW heparin fractions. Heparin 39-46 von Willebrand factor Homo sapiens 77-80 8320843-4 1993 Each vWf subunit has binding sites for collagen, heparin, GP Ib, GPIIb/IIIa and factor VIII. Heparin 49-56 von Willebrand factor Homo sapiens 5-8 8443144-10 1993 Heparin is known to be a vWF ligand, but did not appear as a competitor of vWF binding to the ECM, nor did heparan sulfate. Heparin 0-7 von Willebrand factor Homo sapiens 25-28 8443388-8 1993 Unfractionated heparin, but not low molecular weight heparin, apparently binds to rvWF445-733 and counteracts the inhibitory effects of the vWF fragment in vitro on shear-aggregation and platelet-collagen adhesion. Heparin 15-22 von Willebrand factor Homo sapiens 83-86 1333636-1 1992 In plasma from healthy subjects a coupling was identified between von Willebrand factor (vWf), fibrinogen (fg), and fibronectin (fn) that was dependent of anticoagulants heparin, EDTA, and citrate. Heparin 170-177 von Willebrand factor Homo sapiens 66-87 1333636-1 1992 In plasma from healthy subjects a coupling was identified between von Willebrand factor (vWf), fibrinogen (fg), and fibronectin (fn) that was dependent of anticoagulants heparin, EDTA, and citrate. Heparin 170-177 von Willebrand factor Homo sapiens 89-92 1333636-4 1992 The largest degree of coupling was found in heat-treated lyophilized heparin plasma, where C[fg/vWf] and C[fn/vWf] were 12.9 +/- 1.4 (mol/mol)% and 2.4 +/- 0.1 (mol/mol)% (mean +/- SD). Heparin 69-76 von Willebrand factor Homo sapiens 96-99 1333636-4 1992 The largest degree of coupling was found in heat-treated lyophilized heparin plasma, where C[fg/vWf] and C[fn/vWf] were 12.9 +/- 1.4 (mol/mol)% and 2.4 +/- 0.1 (mol/mol)% (mean +/- SD). Heparin 69-76 von Willebrand factor Homo sapiens 110-113 2022745-1 1991 The intravenous administration of heparin to patients before open heart surgery reduced ristocetin cofactor activity by 58% (P less than 0.01, t test), and this impairment of von Willebrand factor-dependent platelet function was closely related to plasma heparin levels (r2 = 0.9), but not to plasma von Willebrand factor (vWF) levels. Heparin 34-41 von Willebrand factor Homo sapiens 175-196 1400429-4 1992 In type IIB vWD, plasma vWF exhibits increased affinity for platelet GPIb, but decreased binding to collagen and heparin. Heparin 113-120 von Willebrand factor Homo sapiens 24-27 1400429-13 1992 In type IIB vWD, the defective binding of plasma vWF to collagen and heparin may be secondary to post-synthetic modifications that occur in vivo, such as the loss of high molecular weight vWF multimers. Heparin 69-76 von Willebrand factor Homo sapiens 49-52 1834252-10 1991 Further mapping of this new functional domain of vWF, based on experiments of competitive inhibition of binding by either heparin or monoclonal antibodies directed toward vWF, showed that the site interacting with sulfatides is distinct from those involved in binding to platelet glycoprotein Ib, collagen, or heparin. Heparin 122-129 von Willebrand factor Homo sapiens 49-52 1834252-10 1991 Further mapping of this new functional domain of vWF, based on experiments of competitive inhibition of binding by either heparin or monoclonal antibodies directed toward vWF, showed that the site interacting with sulfatides is distinct from those involved in binding to platelet glycoprotein Ib, collagen, or heparin. Heparin 310-317 von Willebrand factor Homo sapiens 49-52 1577724-1 1992 Human von Willebrand factor, a plasma glycoprotein which plays a critical role in regulating hemostasis, binds heparin, but the physiological importance and mode of this interaction is poorly understood. Heparin 111-118 von Willebrand factor Homo sapiens 6-27 1577724-2 1992 Using the motif of an amino acid sequence of a consensus heparin binding synthetic peptide, a 23-residue sequence (Tyr565-Ala587) of human von Willebrand factor was identified that retains the consensus motif and binds heparin with affinity comparable with native von Willebrand factor and the consensus peptide. Heparin 57-64 von Willebrand factor Homo sapiens 139-160 1577724-2 1992 Using the motif of an amino acid sequence of a consensus heparin binding synthetic peptide, a 23-residue sequence (Tyr565-Ala587) of human von Willebrand factor was identified that retains the consensus motif and binds heparin with affinity comparable with native von Willebrand factor and the consensus peptide. Heparin 57-64 von Willebrand factor Homo sapiens 264-285 1577724-2 1992 Using the motif of an amino acid sequence of a consensus heparin binding synthetic peptide, a 23-residue sequence (Tyr565-Ala587) of human von Willebrand factor was identified that retains the consensus motif and binds heparin with affinity comparable with native von Willebrand factor and the consensus peptide. Heparin 219-226 von Willebrand factor Homo sapiens 139-160 1577724-2 1992 Using the motif of an amino acid sequence of a consensus heparin binding synthetic peptide, a 23-residue sequence (Tyr565-Ala587) of human von Willebrand factor was identified that retains the consensus motif and binds heparin with affinity comparable with native von Willebrand factor and the consensus peptide. Heparin 219-226 von Willebrand factor Homo sapiens 264-285 1577724-3 1992 In a fluid phase binding assay, the Tyr565-Ala587 peptide competed effectively with von Willebrand factor for binding heparin. Heparin 118-125 von Willebrand factor Homo sapiens 84-105 2022745-1 1991 The intravenous administration of heparin to patients before open heart surgery reduced ristocetin cofactor activity by 58% (P less than 0.01, t test), and this impairment of von Willebrand factor-dependent platelet function was closely related to plasma heparin levels (r2 = 0.9), but not to plasma von Willebrand factor (vWF) levels. Heparin 34-41 von Willebrand factor Homo sapiens 300-321 2022745-1 1991 The intravenous administration of heparin to patients before open heart surgery reduced ristocetin cofactor activity by 58% (P less than 0.01, t test), and this impairment of von Willebrand factor-dependent platelet function was closely related to plasma heparin levels (r2 = 0.9), but not to plasma von Willebrand factor (vWF) levels. Heparin 34-41 von Willebrand factor Homo sapiens 323-326 2022745-1 1991 The intravenous administration of heparin to patients before open heart surgery reduced ristocetin cofactor activity by 58% (P less than 0.01, t test), and this impairment of von Willebrand factor-dependent platelet function was closely related to plasma heparin levels (r2 = 0.9), but not to plasma von Willebrand factor (vWF) levels. Heparin 255-262 von Willebrand factor Homo sapiens 175-196 2022745-2 1991 We hypothesized that heparin may inhibit vWF-dependent platelet hemostatic functions by directly binding vWF in solution and interfering with vWF-GpIb binding. Heparin 21-28 von Willebrand factor Homo sapiens 41-44 2022745-2 1991 We hypothesized that heparin may inhibit vWF-dependent platelet hemostatic functions by directly binding vWF in solution and interfering with vWF-GpIb binding. Heparin 21-28 von Willebrand factor Homo sapiens 105-108 2022745-2 1991 We hypothesized that heparin may inhibit vWF-dependent platelet hemostatic functions by directly binding vWF in solution and interfering with vWF-GpIb binding. Heparin 21-28 von Willebrand factor Homo sapiens 105-108 2022745-3 1991 Using the in vitro techniques of ristocetin-induced platelet agglutination, fluorescent flow cytometric measurement of vWF-platelet binding, and conventional radioligand binding assays we observed that heparin inhibited both vWF-dependent platelet function and vWF-platelet binding in a parallel and dose-dependent manner. Heparin 202-209 von Willebrand factor Homo sapiens 119-122 2022745-3 1991 Using the in vitro techniques of ristocetin-induced platelet agglutination, fluorescent flow cytometric measurement of vWF-platelet binding, and conventional radioligand binding assays we observed that heparin inhibited both vWF-dependent platelet function and vWF-platelet binding in a parallel and dose-dependent manner. Heparin 202-209 von Willebrand factor Homo sapiens 225-228 2022745-3 1991 Using the in vitro techniques of ristocetin-induced platelet agglutination, fluorescent flow cytometric measurement of vWF-platelet binding, and conventional radioligand binding assays we observed that heparin inhibited both vWF-dependent platelet function and vWF-platelet binding in a parallel and dose-dependent manner. Heparin 202-209 von Willebrand factor Homo sapiens 225-228 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. Heparin 0-7 von Willebrand factor Homo sapiens 110-113 2022745-6 1991 Heparin impairment of vWF function may explain why some hemorrhagic complications of heparin therapy are not predictable based on techniques for monitoring the conventional anticoagulant effects of heparin. Heparin 85-92 von Willebrand factor Homo sapiens 22-25 2022745-6 1991 Heparin impairment of vWF function may explain why some hemorrhagic complications of heparin therapy are not predictable based on techniques for monitoring the conventional anticoagulant effects of heparin. Heparin 198-205 von Willebrand factor Homo sapiens 22-25 2686638-2 1989 This fragment, which corresponds to Val 449-Asn 730 of vWF and includes the GPIb-binding domain and binding sites for collagen and heparin, was subcloned into an expression vector containing an inducible lambda PL promoter. Heparin 131-138 von Willebrand factor Homo sapiens 55-58 2205950-4 1990 Protease I destroyed the heparin binding domain in human vWF. Heparin 25-32 von Willebrand factor Homo sapiens 57-60 2690940-1 1989 A 39/34-kilodalton (kDa) monomeric dispase fragment of von Willebrand factor (vWF) has been purified by heparin affinity chromatography. Heparin 104-111 von Willebrand factor Homo sapiens 55-76 2690940-1 1989 A 39/34-kilodalton (kDa) monomeric dispase fragment of von Willebrand factor (vWF) has been purified by heparin affinity chromatography. Heparin 104-111 von Willebrand factor Homo sapiens 78-81 3100536-3 1987 We have now established that the fragment extends to residue Lys-728 and demonstrate here that a high affinity heparin-binding domain of vWF also lies within this region and in close proximity to that for GPIb. Heparin 111-118 von Willebrand factor Homo sapiens 137-140 2673431-11 1989 The domains on the vWF molecule involved in the interactions of vWF with GP Ib, GP IIb-IIIa, collagen, F. VIII and heparin have been localized to varying extents. Heparin 115-122 von Willebrand factor Homo sapiens 19-22 2673431-11 1989 The domains on the vWF molecule involved in the interactions of vWF with GP Ib, GP IIb-IIIa, collagen, F. VIII and heparin have been localized to varying extents. Heparin 115-122 von Willebrand factor Homo sapiens 64-67 2477370-6 1989 Both 116-kDa and 52/48-kDa fragments inhibited vWF binding to heparin with similar potency, while fragment III-T2 had no effect in this regard. Heparin 62-69 von Willebrand factor Homo sapiens 47-50 3100536-4 1987 We have used an assay employing heparin coupled to Sepharose CL-6B to show that 125I-vWF binds to heparin in a time-dependent, saturable, and reversible manner. Heparin 32-39 von Willebrand factor Homo sapiens 85-88 3100536-4 1987 We have used an assay employing heparin coupled to Sepharose CL-6B to show that 125I-vWF binds to heparin in a time-dependent, saturable, and reversible manner. Heparin 98-105 von Willebrand factor Homo sapiens 85-88 3100536-9 1987 Twelve monoclonal antibodies to the 52/48-kDa fragment were evaluated for their ability to block binding of 125I-vWF to heparin. Heparin 120-127 von Willebrand factor Homo sapiens 113-116 3486185-3 1986 Heparin strongly inhibits binding of thrombospondin but only weakly inhibits binding of laminin and von Willebrand factor. Heparin 0-7 von Willebrand factor Homo sapiens 100-121 2936763-9 1986 A 285,000-D fragment of vWF multimer was separated from heterogeneous 210,000-225,000-D fragments by its ability to bind to heparin. Heparin 124-131 von Willebrand factor Homo sapiens 24-27 33278841-7 2021 We detected a non-significant trend to loss of VWF:RCo after heparinisation and a significant recovery after protamine reversal which could reflect a direct heparin effect. Heparin 61-68 von Willebrand factor Homo sapiens 47-50 28279966-10 2017 Finally, we demonstrate that VWF susceptibility to plasmin proteolysis at K1491-R1492 is modulated by local N-linked glycan expression within A1A2A3, and specifically inhibited by heparin binding to the A1 domain. Heparin 180-187 von Willebrand factor Homo sapiens 29-32 32496552-7 2020 Our simulations attribute the previously-observed platelet-recruitment reduction and heparin-size modulation, upon establishment of DNA-vWF interactions, to indirect steric hindrance and partial overlap of the binding sites, respectively. Heparin 85-92 von Willebrand factor Homo sapiens 136-139 28898897-7 2018 Several studies report unselective antagonism of VWF for drugs used in daily clinical practice, including heparin and statins. Heparin 106-113 von Willebrand factor Homo sapiens 49-52