PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 1871720-8 1991 Both vWf binding and platelet adhesion to sulfatides can be inhibited by the sulfated polysaccharide dextran sulfate at low concentration, fucoidan at high concentrations, but not by heparin, fibrinogen, fibronectin, or the synthetic peptides Gly-Arg-Gly-Asp-Ser-Pro or Gly-Arg-Gly-Glu-Ser-Pro. Polysaccharides 86-100 von Willebrand factor Homo sapiens 5-8 20418283-2 2010 Blocking the addition of N-linked glycans (NLGs) or inhibiting initial glycan processing prevented secretion of VWF. Polysaccharides 34-40 von Willebrand factor Homo sapiens 112-115 19965639-3 2010 In this study, the role of terminal sialic acid residues on VWF glycans in mediating proteolysis by ADAMTS13 was investigated. Polysaccharides 64-71 von Willebrand factor Homo sapiens 60-63 27717713-7 2017 Advanced mass spectrometry led to detailed identification of the glycan structures carried by VWF. Polysaccharides 65-71 von Willebrand factor Homo sapiens 94-97 3485094-4 1986 vWF binding is inhibited at high ionic strength or low pH, by some sulfated polysaccharides and by antibodies to vWF. Polysaccharides 76-91 von Willebrand factor Homo sapiens 0-3 6801813-10 1982 Thus, the high degree of heterogeneity of the FVIII/vWf carbohydrate moiety requires further structural studies in order to precise which class of glycans is involved in the biological activity of FVIII/vWf. Polysaccharides 147-154 von Willebrand factor Homo sapiens 52-55 6801813-10 1982 Thus, the high degree of heterogeneity of the FVIII/vWf carbohydrate moiety requires further structural studies in order to precise which class of glycans is involved in the biological activity of FVIII/vWf. Polysaccharides 147-154 von Willebrand factor Homo sapiens 203-206 33110150-3 2020 In addition, ABO(H) structures are also present on VWF glycans. Polysaccharides 55-62 von Willebrand factor Homo sapiens 51-54 28279966-0 2017 Plasmin Cleaves Von Willebrand Factor at K1491-R1492 in the A1-A2 Linker Region in a Shear- and Glycan-Dependent Manner In Vitro. Polysaccharides 96-102 von Willebrand factor Homo sapiens 16-37 6792684-4 1981 Furthermore, chemical analysis of glycans released from F VIII/vWf by alkaline-borohydride treatment or hydrazinolysis shows the absence of N-acetylgalactosamine residues in non-reducing terminal positions. Polysaccharides 34-41 von Willebrand factor Homo sapiens 63-66 30770394-1 2019 Glycan determinants on von Willebrand factor (VWF) play critical roles in regulating its susceptibility to proteolysis and clearance. Polysaccharides 0-6 von Willebrand factor Homo sapiens 23-44 30770394-1 2019 Glycan determinants on von Willebrand factor (VWF) play critical roles in regulating its susceptibility to proteolysis and clearance. Polysaccharides 0-6 von Willebrand factor Homo sapiens 46-49 30770394-4 2019 To address this, we developed a novel lectin-binding panel to enable human VWF glycan characterization. Polysaccharides 79-85 von Willebrand factor Homo sapiens 75-78 30770394-5 2019 This methodology was then used to study glycan expression in a cohort of 110 patients with low VWF compared with O blood group-matched healthy controls. Polysaccharides 40-46 von Willebrand factor Homo sapiens 95-98 30770394-6 2019 Interestingly, significant interindividual heterogeneity in VWF glycan expression was seen in the healthy control population. Polysaccharides 64-70 von Willebrand factor Homo sapiens 60-63 27554083-7 2016 We further demonstrate that these glycans presented at N1515 and N1574 also play a critical role in protecting VWF against macrophage binding and clearance. Polysaccharides 34-41 von Willebrand factor Homo sapiens 111-114 26773038-9 2016 Glycan stabilization of the VWF A2 domain acts together with the Ca(2+)binding site and vicinal cysteine disulfide bond to control unfolding and ADAMTS13 proteolysis. Polysaccharides 0-6 von Willebrand factor Homo sapiens 28-31 27584569-1 2016 VWF is extensively glycosylated with biantennary core fucosylated glycans. Polysaccharides 66-73 von Willebrand factor Homo sapiens 0-3 22849435-2 2012 There is ample evidence that vWF glycan moieties are crucial determinants of its expression and function. Polysaccharides 33-39 von Willebrand factor Homo sapiens 29-32 24404057-3 2013 However, the fact that 20% of VWF molecular weight originates from glycan moieties has so far been neglected in these calculations. Polysaccharides 67-73 von Willebrand factor Homo sapiens 30-33 25564400-5 2015 However, a glycan attached at position 476 appreciably reduced both VWF binding and proteolysis. Polysaccharides 11-17 von Willebrand factor Homo sapiens 68-71 24106205-4 2013 We have characterized terminal glycan expression on platelet-VWF. Polysaccharides 31-37 von Willebrand factor Homo sapiens 61-64 24335029-1 2013 In this issue of Blood, McGrath et al show that the terminal glycan structures of platelet von Willebrand factor (VWF) are markedly different compared with such structures present on plasma VWF.1 Unexpectedly, these differences endow platelet VWF with a specific resistance against proteolysis by the VWF-cleaving protease ADAMTS13, thereby potentially increasing the hemostatic potential of platelet VWF during the formation of platelet-rich thrombi. Polysaccharides 61-67 von Willebrand factor Homo sapiens 91-112 24335029-1 2013 In this issue of Blood, McGrath et al show that the terminal glycan structures of platelet von Willebrand factor (VWF) are markedly different compared with such structures present on plasma VWF.1 Unexpectedly, these differences endow platelet VWF with a specific resistance against proteolysis by the VWF-cleaving protease ADAMTS13, thereby potentially increasing the hemostatic potential of platelet VWF during the formation of platelet-rich thrombi. Polysaccharides 61-67 von Willebrand factor Homo sapiens 114-117