Id |
Subject |
Object |
Predicate |
Lexical cue |
TextSentencer_T1 |
0-107 |
Sentence |
denotes |
Characterization of the LARGE family of putative glycosyltransferases associated with dystroglycanopathies. |
T1 |
0-107 |
Sentence |
denotes |
Characterization of the LARGE family of putative glycosyltransferases associated with dystroglycanopathies. |
T1 |
0-107 |
Sentence |
denotes |
Characterization of the LARGE family of putative glycosyltransferases associated with dystroglycanopathies. |
TextSentencer_T2 |
108-208 |
Sentence |
denotes |
The Large(myd) mouse has a loss-of-function mutation in the putative glycosyltransferase gene Large. |
T2 |
108-208 |
Sentence |
denotes |
The Large(myd) mouse has a loss-of-function mutation in the putative glycosyltransferase gene Large. |
T2 |
108-319 |
Sentence |
denotes |
The Large(myd) mouse has a loss-of-function mutation in the putative glycosyltransferase gene Large. Mutations in the human homolog (LARGE) have been described in a form of congenital muscular dystrophy (MDC1D). |
TextSentencer_T3 |
209-319 |
Sentence |
denotes |
Mutations in the human homolog (LARGE) have been described in a form of congenital muscular dystrophy (MDC1D). |
T3 |
209-319 |
Sentence |
denotes |
Mutations in the human homolog (LARGE) have been described in a form of congenital muscular dystrophy (MDC1D). |
TextSentencer_T4 |
320-492 |
Sentence |
denotes |
Other genes (POMT1, POMGnT1, fukutin, and FKRP) that encode known or putative glycosylation enzymes are also causally associated with human congenital muscular dystrophies. |
T3 |
320-492 |
Sentence |
denotes |
Other genes (POMT1, POMGnT1, fukutin, and FKRP) that encode known or putative glycosylation enzymes are also causally associated with human congenital muscular dystrophies. |
T4 |
320-492 |
Sentence |
denotes |
Other genes (POMT1, POMGnT1, fukutin, and FKRP) that encode known or putative glycosylation enzymes are also causally associated with human congenital muscular dystrophies. |
TextSentencer_T5 |
493-656 |
Sentence |
denotes |
All these diseases are associated with hypoglycosylation of the membrane protein alpha-dystroglycan (alpha-DG) and consequent loss of extracellular ligand binding. |
T4 |
493-656 |
Sentence |
denotes |
All these diseases are associated with hypoglycosylation of the membrane protein alpha-dystroglycan (alpha-DG) and consequent loss of extracellular ligand binding. |
T5 |
493-656 |
Sentence |
denotes |
All these diseases are associated with hypoglycosylation of the membrane protein alpha-dystroglycan (alpha-DG) and consequent loss of extracellular ligand binding. |
TextSentencer_T6 |
657-701 |
Sentence |
denotes |
Hence, they are termed dystroglycanopathies. |
T5 |
657-701 |
Sentence |
denotes |
Hence, they are termed dystroglycanopathies. |
T6 |
657-701 |
Sentence |
denotes |
Hence, they are termed dystroglycanopathies. |
TextSentencer_T7 |
702-791 |
Sentence |
denotes |
A paralogous gene for LARGE (LARGE2 or GYLTL1B) may also have a role in DG glycosylation. |
T6 |
702-791 |
Sentence |
denotes |
A paralogous gene for LARGE (LARGE2 or GYLTL1B) may also have a role in DG glycosylation. |
T7 |
702-791 |
Sentence |
denotes |
A paralogous gene for LARGE (LARGE2 or GYLTL1B) may also have a role in DG glycosylation. |
TextSentencer_T8 |
792-1032 |
Sentence |
denotes |
Using database interrogation and reverse-transcriptase polymerase chain reaction (RT-PCR), we identified vertebrate orthologs of each of these LARGE genes in many vertebrates, including human, mouse, dog, chicken, zebrafish, and pufferfish. |
T7 |
792-1032 |
Sentence |
denotes |
Using database interrogation and reverse-transcriptase polymerase chain reaction (RT-PCR), we identified vertebrate orthologs of each of these LARGE genes in many vertebrates, including human, mouse, dog, chicken, zebrafish, and pufferfish. |
T8 |
792-1032 |
Sentence |
denotes |
Using database interrogation and reverse-transcriptase polymerase chain reaction (RT-PCR), we identified vertebrate orthologs of each of these LARGE genes in many vertebrates, including human, mouse, dog, chicken, zebrafish, and pufferfish. |
TextSentencer_T9 |
1033-1117 |
Sentence |
denotes |
However, within invertebrate genomes, we were able to identify only single homologs. |
T8 |
1033-1117 |
Sentence |
denotes |
However, within invertebrate genomes, we were able to identify only single homologs. |
T9 |
1033-1117 |
Sentence |
denotes |
However, within invertebrate genomes, we were able to identify only single homologs. |
TextSentencer_T10 |
1118-1186 |
Sentence |
denotes |
We suggest that vertebrate LARGE orthologs be referred to as LARGE1. |
T9 |
1118-1186 |
Sentence |
denotes |
We suggest that vertebrate LARGE orthologs be referred to as LARGE1. |
T10 |
1118-1186 |
Sentence |
denotes |
We suggest that vertebrate LARGE orthologs be referred to as LARGE1. |
TextSentencer_T11 |
1187-1309 |
Sentence |
denotes |
RT-PCR, dot-blot, and northern analysis indicated that LARGE2 has a more restricted tissue-expression profile than LARGE1. |
T10 |
1187-1309 |
Sentence |
denotes |
RT-PCR, dot-blot, and northern analysis indicated that LARGE2 has a more restricted tissue-expression profile than LARGE1. |
T11 |
1187-1309 |
Sentence |
denotes |
RT-PCR, dot-blot, and northern analysis indicated that LARGE2 has a more restricted tissue-expression profile than LARGE1. |
TextSentencer_T12 |
1310-1409 |
Sentence |
denotes |
Using epitope-tagged proteins, we show that both LARGE1 and LARGE2 localize to the Golgi apparatus. |
T11 |
1310-1409 |
Sentence |
denotes |
Using epitope-tagged proteins, we show that both LARGE1 and LARGE2 localize to the Golgi apparatus. |
T12 |
1310-1409 |
Sentence |
denotes |
Using epitope-tagged proteins, we show that both LARGE1 and LARGE2 localize to the Golgi apparatus. |
TextSentencer_T13 |
1410-1497 |
Sentence |
denotes |
The high similarity between the LARGE paralogs suggests that LARGE2 may also act on DG. |
T12 |
1410-1497 |
Sentence |
denotes |
The high similarity between the LARGE paralogs suggests that LARGE2 may also act on DG. |
T13 |
1410-1497 |
Sentence |
denotes |
The high similarity between the LARGE paralogs suggests that LARGE2 may also act on DG. |
TextSentencer_T14 |
1498-1641 |
Sentence |
denotes |
Overexpression of LARGE2 in mouse C2C12 myoblasts results in increased glycosylation of alpha-DG accompanied by an increase in laminin binding. |
T13 |
1498-1641 |
Sentence |
denotes |
Overexpression of LARGE2 in mouse C2C12 myoblasts results in increased glycosylation of alpha-DG accompanied by an increase in laminin binding. |
T14 |
1498-1641 |
Sentence |
denotes |
Overexpression of LARGE2 in mouse C2C12 myoblasts results in increased glycosylation of alpha-DG accompanied by an increase in laminin binding. |
TextSentencer_T15 |
1642-1709 |
Sentence |
denotes |
Thus, there may be functional redundancy between LARGE1 and LARGE2. |
T14 |
1642-1709 |
Sentence |
denotes |
Thus, there may be functional redundancy between LARGE1 and LARGE2. |
T15 |
1642-1709 |
Sentence |
denotes |
Thus, there may be functional redundancy between LARGE1 and LARGE2. |
TextSentencer_T16 |
1710-1877 |
Sentence |
denotes |
Consistent with this idea, we show that alpha-DG is still fully glycosylated in kidney (a tissue that expresses a high level of LARGE2 mRNA) of Large(myd) mutant mice. |
T15 |
1710-1877 |
Sentence |
denotes |
Consistent with this idea, we show that alpha-DG is still fully glycosylated in kidney (a tissue that expresses a high level of LARGE2 mRNA) of Large(myd) mutant mice. |
T16 |
1710-1877 |
Sentence |
denotes |
Consistent with this idea, we show that alpha-DG is still fully glycosylated in kidney (a tissue that expresses a high level of LARGE2 mRNA) of Large(myd) mutant mice. |