PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 8949361-5 1996 Both ET-1 and vWF were higher in salt sensitive than salt resistant patients (ET-1 p < 0.01; vWF p < 0.03). Salts 33-37 von Willebrand factor Homo sapiens 14-17 8949361-5 1996 Both ET-1 and vWF were higher in salt sensitive than salt resistant patients (ET-1 p < 0.01; vWF p < 0.03). Salts 33-37 von Willebrand factor Homo sapiens 96-99 8949361-5 1996 Both ET-1 and vWF were higher in salt sensitive than salt resistant patients (ET-1 p < 0.01; vWF p < 0.03). Salts 53-57 von Willebrand factor Homo sapiens 14-17 8767102-14 1996 vWF was quite resistant against the protease in a physiologic buffer but was degraded at low salt concentration or in the presence of 1 M urea. Salts 93-97 von Willebrand factor Homo sapiens 0-3 8639781-7 1996 vWF was resistant against the protease in a neutral buffer at physiological ionic strength but became degraded at low salt concentration or in the presence of 1 mol/L urea. Salts 118-122 von Willebrand factor Homo sapiens 0-3 30797858-5 2019 Under supraphysiologic salt concentrations, strong electrostatic screening dramatically decreases platelet binding to VWF in flow, revealing the critical role of electrostatic attraction in VWF-platelet binding during bleeding. Salts 23-27 von Willebrand factor Homo sapiens 118-121 30797858-5 2019 Under supraphysiologic salt concentrations, strong electrostatic screening dramatically decreases platelet binding to VWF in flow, revealing the critical role of electrostatic attraction in VWF-platelet binding during bleeding. Salts 23-27 von Willebrand factor Homo sapiens 190-193 16805860-6 2006 Furthermore, A1-mediated binding to type III collagen of DeltaA3-VWF binding was strongly salt-sensitive. Salts 90-94 von Willebrand factor Homo sapiens 65-68 9822445-5 1998 Salt-sensitive hypertensives showed higher plasma ET-1 (P<0.05), vWf (P<0.005), and S-E-selectin levels (P<0.04) and increased UAE (P<0.05) than salt-resistant hypertensives. Salts 0-4 von Willebrand factor Homo sapiens 68-71 9822445-11 1998 This study shows increased plasma levels of the endothelium-derived substances E-selectin, vWf, and ET-1 in salt-sensitive hypertensives. Salts 108-112 von Willebrand factor Homo sapiens 91-94 2455942-3 1988 With application of combined salt/pH gradients good resolution of VIII/vWf from most of the applied proteins can be achieved. Salts 29-33 von Willebrand factor Homo sapiens 71-74 24363113-8 2014 The specificity of the approach could be demonstrated by incubating VWF with FVIII in the presence of a high salt buffer which inhibits the interaction between these two proteins. Salts 109-113 von Willebrand factor Homo sapiens 68-71 23443727-7 2013 Conversely, the VWF rs2239153 C variant was associated with increased salt sensitivity, conferring larger DBP and MAP reductions during low-sodium intervention (P = 1.22x10(-4) and 4.44x10(-5), respectively). Salts 70-74 von Willebrand factor Homo sapiens 16-19 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. Salts 156-160 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. Salts 156-160 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. Salts 156-160 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. Salts 156-160 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. Salts 156-160 von Willebrand factor Homo sapiens 102-105