| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-150 |
Sentence |
denotes |
von Willebrand disease type B: a missense mutation selectively abolishes ristocetin-induced von Willebrand factor binding to platelet glycoprotein Ib. |
| T1 |
0-150 |
Sentence |
denotes |
von Willebrand disease type B: a missense mutation selectively abolishes ristocetin-induced von Willebrand factor binding to platelet glycoprotein Ib. |
| TextSentencer_T2 |
151-309 |
Sentence |
denotes |
von Willebrand factor (vWF) is a multimeric glycoprotein that mediates the adhesion of platelets to the subendothelium by binding to platelet glycoprotein Ib. |
| T2 |
151-309 |
Sentence |
denotes |
von Willebrand factor (vWF) is a multimeric glycoprotein that mediates the adhesion of platelets to the subendothelium by binding to platelet glycoprotein Ib. |
| TextSentencer_T3 |
310-433 |
Sentence |
denotes |
For human vWF, this interaction can be induced in vitro by the antibiotic ristocetin or the snake venom protein botrocetin. |
| T3 |
310-433 |
Sentence |
denotes |
For human vWF, this interaction can be induced in vitro by the antibiotic ristocetin or the snake venom protein botrocetin. |
| TextSentencer_T4 |
434-709 |
Sentence |
denotes |
A missense mutation, Gly-561-->Ser, was identified within the proposed glycoprotein Ib binding domain of vWF in the proband with von Willebrand disease type B, a unique variant characterized by no ristocetin-induced, but normal botrocetin-induced, binding to glycoprotein Ib. |
| T4 |
434-709 |
Sentence |
denotes |
A missense mutation, Gly-561-->Ser, was identified within the proposed glycoprotein Ib binding domain of vWF in the proband with von Willebrand disease type B, a unique variant characterized by no ristocetin-induced, but normal botrocetin-induced, binding to glycoprotein Ib. |
| TextSentencer_T5 |
710-930 |
Sentence |
denotes |
The corresponding mutant recombinant protein, rvWF(G561S), formed normal multimers and exhibited the same functional defect as the patient's plasma vWF, confirming that this mutation causes von Willebrand disease type B. |
| T5 |
710-930 |
Sentence |
denotes |
The corresponding mutant recombinant protein, rvWF(G561S), formed normal multimers and exhibited the same functional defect as the patient's plasma vWF, confirming that this mutation causes von Willebrand disease type B. |
| TextSentencer_T6 |
931-1134 |
Sentence |
denotes |
These data show that botrocetin and ristocetin cofactor activities of vWF can be dissociated by a point mutation and confirm that these mediators promote vWF binding to platelets by different mechanisms. |
| T6 |
931-1134 |
Sentence |
denotes |
These data show that botrocetin and ristocetin cofactor activities of vWF can be dissociated by a point mutation and confirm that these mediators promote vWF binding to platelets by different mechanisms. |
| TextSentencer_T7 |
1135-1394 |
Sentence |
denotes |
The normal botrocetin-induced binding and the defective ristocetin-induced binding of rvWF(G561S) suggest that the primary defect in von Willebrand disease type B may be a failure of normal allosteric regulation of the glycoprotein Ib binding function of vWF. |
| T7 |
1135-1394 |
Sentence |
denotes |
The normal botrocetin-induced binding and the defective ristocetin-induced binding of rvWF(G561S) suggest that the primary defect in von Willebrand disease type B may be a failure of normal allosteric regulation of the glycoprotein Ib binding function of vWF. |