| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-179 |
Sentence |
denotes |
L1503R is a member of group I mutation and has dominant-negative effect on secretion of full-length VWF multimers: an analysis of two patients with type 2A von Willebrand disease. |
| TextSentencer_T2 |
180-385 |
Sentence |
denotes |
Type 2A von Willebrand disease (VWD) is characterized by decreased platelet-dependent function of von Willebrand factor (VWF); this in turn is associated with an absence of high-molecular-weight multimers. |
| TextSentencer_T3 |
386-601 |
Sentence |
denotes |
Sequence analysis of the VWF gene from two unrelated type 2A VWD patients showed an identical, novel, heterozygous T-->G transversion at nucleotide 4508, resulting in the substitution of L1503R in the VWF A2 domain. |
| TextSentencer_T4 |
602-761 |
Sentence |
denotes |
This substitution, which was not found in 60 unrelated normal individuals, was introduced into a full-length VWF cDNA and subsequently expressed in 293T cells. |
| TextSentencer_T5 |
762-867 |
Sentence |
denotes |
Only trace amount of the mutant VWF protein was secreted but most of the same was retained in 293T cells. |
| TextSentencer_T6 |
868-1130 |
Sentence |
denotes |
Co-transfection experiment of both wild-type and mutant plasmids indicated the dominant-negative mechanism of disease development; as more of mutant DNA was transfected, VWF secretion was impaired in the media, whereas more of VWF was stored in the cell lysates. |
| TextSentencer_T7 |
1131-1431 |
Sentence |
denotes |
Molecular dynamic simulations of structural changes induced by L1503R indicated that the mean value of all-atom root-mean-squared-deviation was shifted from those with wild type or another mutation L1503Q that has been reported to be a group II mutation, which is susceptible to ADAMTS13 proteolysis. |
| TextSentencer_T8 |
1432-1648 |
Sentence |
denotes |
Protein instability of L1503R may be responsible for its intracellular retention and perhaps the larger VWF multimers, containing more mutant VWF subunits, are likely to be mal-processed and retained within the cell. |
| T1 |
0-179 |
Sentence |
denotes |
L1503R is a member of group I mutation and has dominant-negative effect on secretion of full-length VWF multimers: an analysis of two patients with type 2A von Willebrand disease. |
| T2 |
180-385 |
Sentence |
denotes |
Type 2A von Willebrand disease (VWD) is characterized by decreased platelet-dependent function of von Willebrand factor (VWF); this in turn is associated with an absence of high-molecular-weight multimers. |
| T3 |
386-601 |
Sentence |
denotes |
Sequence analysis of the VWF gene from two unrelated type 2A VWD patients showed an identical, novel, heterozygous T-->G transversion at nucleotide 4508, resulting in the substitution of L1503R in the VWF A2 domain. |
| T4 |
602-761 |
Sentence |
denotes |
This substitution, which was not found in 60 unrelated normal individuals, was introduced into a full-length VWF cDNA and subsequently expressed in 293T cells. |
| T5 |
762-867 |
Sentence |
denotes |
Only trace amount of the mutant VWF protein was secreted but most of the same was retained in 293T cells. |
| T6 |
868-1130 |
Sentence |
denotes |
Co-transfection experiment of both wild-type and mutant plasmids indicated the dominant-negative mechanism of disease development; as more of mutant DNA was transfected, VWF secretion was impaired in the media, whereas more of VWF was stored in the cell lysates. |
| T7 |
1131-1431 |
Sentence |
denotes |
Molecular dynamic simulations of structural changes induced by L1503R indicated that the mean value of all-atom root-mean-squared-deviation was shifted from those with wild type or another mutation L1503Q that has been reported to be a group II mutation, which is susceptible to ADAMTS13 proteolysis. |
| T8 |
1432-1648 |
Sentence |
denotes |
Protein instability of L1503R may be responsible for its intracellular retention and perhaps the larger VWF multimers, containing more mutant VWF subunits, are likely to be mal-processed and retained within the cell. |