PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
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	
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	
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	
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	
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	
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	
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	
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