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1 lack of interaction between huVWF and murine glycoprotein Ib.
2 as integrins or the von Willebrand receptor glycoprotein Ib.
3 platelet binding, which depended on platelet glycoprotein Ib.
4 tease-activated receptor 1 (PAR1), PAR4, and glycoprotein Ib.
5 y of a noncatalytic interaction site such as glycoprotein Ib.
6 that mediates vWF interaction with platelet glycoprotein Ib.
7 the two other thrombin receptors, PAR-3 and glycoprotein Ib.
8 raction with a peptide derived from platelet glycoprotein Ib.
9 sible for binding the platelet vWF receptor, glycoprotein Ib.
10 (RGD) sequence in the C-terminus of vWF, and glycoprotein Ib alpha (GP Ib alpha), which interacts wit
17 that the loop to beta-hairpin transition in glycoprotein Ib alpha is induced by flow before binding
20 t neither von Willebrand factor nor platelet glycoprotein Ib-alpha receptor (GPIb-alpha) is required
21 ligands, including FVIII, platelet-receptor glycoprotein Ib-alpha, VWF-cleaving protease ADAMTS13, s
23 es and platelets, where, in association with glycoprotein Ib beta, glycoprotein V, and glycoprotein I
24 lytically inactive FPR-thrombin, which binds glycoprotein Ib but does not inhibit rPAR1(T) cleavage,
26 tegrin alpha2beta1, glycoprotein VI, and the glycoprotein Ib complex, represent unexploited targets o
28 actor (pvWF) has been shown to bind to human glycoprotein Ib (GPIb) and cause activation of human (or
30 esence of ITP plasma containing antiplatelet glycoprotein Ib (GPIb) autoantibodies (P <.001) as compa
31 sites that are involved in downregulation of glycoprotein Ib (GpIb) binding to vWF shows that these a
35 ultrastructural studies have suggested that Glycoprotein Ib (GPIb) has a different distribution on e
36 munosorbent assay (ELISA)-based assay of VWF-glycoprotein Ib (GPIb) interactions using a gain-of-func
37 of vascular damage through interaction with glycoprotein Ib (GPIb) of the platelet GPIb/IX complex.
40 s is mediated by interaction of the platelet glycoprotein Ib (GPIb) surface receptor and its arterial
42 elets contain 2 receptors that bind VWF: the glycoprotein Ib (GPIb)-IX-V complex and the integrin alp
46 orption with mouse antihuman CD42b [platelet glycoprotein Ib (GPIb)] mAb, had sizes and cargo protein
48 hat inhibits binding of thrombin to platelet glycoprotein Ib inhibits secretory responses to thrombin
49 ezers to study the unbinding forces from the glycoprotein Ib-IX (GP Ib-IX) complex of plasma VWF, ULV
50 ebrand factor (VWF) to the platelet membrane glycoprotein Ib-IX (GPIb-IX) results in platelet activat
51 by VWF binding to its receptor, the platelet glycoprotein Ib-IX (GPIb-IX), and p38 inhibitors diminis
52 et receptor for von Willebrand factor (vWF), glycoprotein Ib-IX (GPIb-IX), mediates initial platelet
53 atelet von Willebrand factor (vWF) receptor, glycoprotein Ib-IX (GPIb-IX), mediates platelet adhesion
54 ctor (vWF) binding to its platelet receptor, glycoprotein Ib-IX (GPIb-IX), via the protein kinase G (
55 A limited number of mutations within the glycoprotein Ib-IX complex have been described that perm
57 ly dependent on integrin alpha6beta1 and the glycoprotein Ib-IX complex, which binds to plasmatic von
60 (vWF)-dependent recruitment of the platelet glycoprotein Ib-IX receptor complex and collagen interac
61 factor (VWF) axis caused by mutations in the glycoprotein Ib-IX receptor that lead to an increased af
63 topes for drug-dependent antibody binding on glycoprotein Ib-IX, glycoprotein IIb-IIIa, and platelet-
64 et receptor for von Willebrand factor (vWF), glycoprotein Ib-IX, integrin alphaIIb, and mutants of be
67 due to absent or decreased expression of the glycoprotein Ib-IX-V (GpIb-IX-V) receptor complex on the
69 he von Willebrand Factor (VWF) receptor, the glycoprotein Ib-IX-V complex (GPIb-IX), but not by GPIb-
74 , the ligand binding subunit of the platelet glycoprotein Ib-IX-V complex, is sulfated on three tyros
76 thin the glycoprotein Ibalpha subunit of the glycoprotein Ib-IX-V complex, we utilized mocarhagin, a
78 intracellular signal-mediated regulation of glycoprotein Ib-IX-V receptor function that requires the
79 telet activation occurs after binding of the glycoprotein Ib-IX-V receptor to von Willebrand factor i
80 in understanding the mechanism(s) regulating glycoprotein Ib-IX-V should help develop inhibitors and
81 n of intracellular molecules and pathways in glycoprotein Ib-IX-V signaling has implications in the d
84 his process requires the binding of platelet glycoprotein Ib-IX-V to the A1 domain of VWF monomeric s
85 platelet rolling via interaction of platelet glycoprotein Ib-IX-V with endothelial-released von Wille
87 -VWD) is a bleeding disorder of the platelet glycoprotein Ib-IX/von Willebrand factor (VWF) axis caus
90 to thrombin but not to TRAP, so occupancy of glycoprotein Ib per se accounts for only part of the att
91 A2, and A3 domains in vWF mediate binding to glycoprotein Ib, ristocetin, botrocetin, collagen, sulph