| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-133 |
Sentence |
denotes |
Type IIB mutation His-505-->Asp implicates a new segment in the control of von Willebrand factor binding to platelet glycoprotein Ib. |
| TextSentencer_T2 |
134-272 |
Sentence |
denotes |
Type IIB von Willebrand disease is characterized by increased affinity of mutant von Willebrand factor (vWF) for platelet glycoprotein Ib. |
| TextSentencer_T3 |
273-523 |
Sentence |
denotes |
Eight different missense mutations that cause this phenotype have been reported within the disulfide loop defined by Cys-509 and Cys-695 of the mature vWF subunit; this disulfide loop is required for normal binding of vWF to platelet glycoprotein Ib. |
| TextSentencer_T4 |
524-848 |
Sentence |
denotes |
A new mutation was identified in a patient with type IIB von Willebrand disease (vWD) characterized by a lifelong bleeding disorder, mild thrombocytopenia, normal levels of factor VIII, vWF antigen, and ristocetin cofactor activity but increased ristocetin-induced platelet agglutination at low concentrations of ristocetin. |
| TextSentencer_T5 |
849-920 |
Sentence |
denotes |
Exon 28 of the patient's vWF gene was amplified, cloned, and sequenced. |
| TextSentencer_T6 |
921-1094 |
Sentence |
denotes |
At nucleotide 3802 (numbering the cDNA from translation initiation), a C to G transversion was identified, which changes the encoded amino acid sequence from His-505 to Asp. |
| TextSentencer_T7 |
1095-1187 |
Sentence |
denotes |
The corresponding mutant recombinant vWF was expressed in transiently transfected COS cells. |
| TextSentencer_T8 |
1188-1414 |
Sentence |
denotes |
Relative to wild type vWF, the mutant vWF exhibited markedly increased binding to platelets at low concentrations of ristocetin, confirming the association between the His-505-->Asp substitution and the type IIB vWD phenotype. |
| TextSentencer_T9 |
1415-1605 |
Sentence |
denotes |
The His-505-->Asp mutation lies outside the disulfide loop affected by other type IIB vWD mutations and implicates a new segment of vWF in the regulation of platelet glycoprotein Ib binding. |
| T1 |
0-133 |
Sentence |
denotes |
Type IIB mutation His-505-->Asp implicates a new segment in the control of von Willebrand factor binding to platelet glycoprotein Ib. |
| T2 |
134-272 |
Sentence |
denotes |
Type IIB von Willebrand disease is characterized by increased affinity of mutant von Willebrand factor (vWF) for platelet glycoprotein Ib. |
| T3 |
273-523 |
Sentence |
denotes |
Eight different missense mutations that cause this phenotype have been reported within the disulfide loop defined by Cys-509 and Cys-695 of the mature vWF subunit; this disulfide loop is required for normal binding of vWF to platelet glycoprotein Ib. |
| T4 |
524-848 |
Sentence |
denotes |
A new mutation was identified in a patient with type IIB von Willebrand disease (vWD) characterized by a lifelong bleeding disorder, mild thrombocytopenia, normal levels of factor VIII, vWF antigen, and ristocetin cofactor activity but increased ristocetin-induced platelet agglutination at low concentrations of ristocetin. |
| T5 |
849-920 |
Sentence |
denotes |
Exon 28 of the patient's vWF gene was amplified, cloned, and sequenced. |
| T6 |
921-1094 |
Sentence |
denotes |
At nucleotide 3802 (numbering the cDNA from translation initiation), a C to G transversion was identified, which changes the encoded amino acid sequence from His-505 to Asp. |
| T7 |
1095-1187 |
Sentence |
denotes |
The corresponding mutant recombinant vWF was expressed in transiently transfected COS cells. |
| T8 |
1188-1414 |
Sentence |
denotes |
Relative to wild type vWF, the mutant vWF exhibited markedly increased binding to platelets at low concentrations of ristocetin, confirming the association between the His-505-->Asp substitution and the type IIB vWD phenotype. |
| T9 |
1415-1605 |
Sentence |
denotes |
The His-505-->Asp mutation lies outside the disulfide loop affected by other type IIB vWD mutations and implicates a new segment of vWF in the regulation of platelet glycoprotein Ib binding. |
