| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-94 |
Sentence |
denotes |
Human glucocerebrosidase: heterologous expression of active site mutants in murine null cells. |
| T1 |
0-94 |
Sentence |
denotes |
Human glucocerebrosidase: heterologous expression of active site mutants in murine null cells. |
| T1 |
0-94 |
Sentence |
denotes |
Human glucocerebrosidase: heterologous expression of active site mutants in murine null cells. |
| TextSentencer_T2 |
95-286 |
Sentence |
denotes |
Using bioinformatics methods, we have previously identified Glu235 and Glu340 as the putative acid/base catalyst and nucleophile, respectively, in the active site of human glucocerebrosidase. |
| T2 |
95-286 |
Sentence |
denotes |
Using bioinformatics methods, we have previously identified Glu235 and Glu340 as the putative acid/base catalyst and nucleophile, respectively, in the active site of human glucocerebrosidase. |
| T2 |
95-286 |
Sentence |
denotes |
Using bioinformatics methods, we have previously identified Glu235 and Glu340 as the putative acid/base catalyst and nucleophile, respectively, in the active site of human glucocerebrosidase. |
| TextSentencer_T3 |
287-401 |
Sentence |
denotes |
Thus, we undertook site-directed mutagenesis studies to obtain experimental evidence supporting these predictions. |
| T3 |
287-401 |
Sentence |
denotes |
Thus, we undertook site-directed mutagenesis studies to obtain experimental evidence supporting these predictions. |
| T3 |
287-401 |
Sentence |
denotes |
Thus, we undertook site-directed mutagenesis studies to obtain experimental evidence supporting these predictions. |
| TextSentencer_T4 |
402-539 |
Sentence |
denotes |
Recombinant retroviruses were used to express wild-type and E235A and E340A mutant proteins in glucocerebrosidase-deficient murine cells. |
| T4 |
402-539 |
Sentence |
denotes |
Recombinant retroviruses were used to express wild-type and E235A and E340A mutant proteins in glucocerebrosidase-deficient murine cells. |
| T4 |
402-539 |
Sentence |
denotes |
Recombinant retroviruses were used to express wild-type and E235A and E340A mutant proteins in glucocerebrosidase-deficient murine cells. |
| TextSentencer_T5 |
540-625 |
Sentence |
denotes |
In contrast to wild-type enzyme, the mutants were found to be catalytically inactive. |
| T5 |
540-625 |
Sentence |
denotes |
In contrast to wild-type enzyme, the mutants were found to be catalytically inactive. |
| T5 |
540-625 |
Sentence |
denotes |
In contrast to wild-type enzyme, the mutants were found to be catalytically inactive. |
| TextSentencer_T6 |
626-870 |
Sentence |
denotes |
We also report the results of various studies (Western blotting, glycosylation analysis, subcellular fractionation, and confocal microscopy) indicating that the wild-type and mutant enzymes are identically processed and sorted to the lysosomes. |
| T6 |
626-870 |
Sentence |
denotes |
We also report the results of various studies (Western blotting, glycosylation analysis, subcellular fractionation, and confocal microscopy) indicating that the wild-type and mutant enzymes are identically processed and sorted to the lysosomes. |
| T6 |
626-870 |
Sentence |
denotes |
We also report the results of various studies (Western blotting, glycosylation analysis, subcellular fractionation, and confocal microscopy) indicating that the wild-type and mutant enzymes are identically processed and sorted to the lysosomes. |
| TextSentencer_T7 |
871-971 |
Sentence |
denotes |
Thus, enzymatic inactivity of the mutant proteins is not the result of incorrect folding/processing. |
| T7 |
871-971 |
Sentence |
denotes |
Thus, enzymatic inactivity of the mutant proteins is not the result of incorrect folding/processing. |
| T7 |
871-971 |
Sentence |
denotes |
Thus, enzymatic inactivity of the mutant proteins is not the result of incorrect folding/processing. |
| TextSentencer_T8 |
972-1121 |
Sentence |
denotes |
These findings indicate that Glu235 plays a key role in the catalytic machinery of human glucocerebrosidase and may indeed be the acid/base catalyst. |
| T8 |
972-1121 |
Sentence |
denotes |
These findings indicate that Glu235 plays a key role in the catalytic machinery of human glucocerebrosidase and may indeed be the acid/base catalyst. |
| T8 |
972-1121 |
Sentence |
denotes |
These findings indicate that Glu235 plays a key role in the catalytic machinery of human glucocerebrosidase and may indeed be the acid/base catalyst. |
| TextSentencer_T9 |
1122-1331 |
Sentence |
denotes |
As concerns Glu340, the results both support our computer-based predictions and confirm, at the biological level, previous identification of Glu340 as the nucleophile by use of active site labeling techniques. |
| T9 |
1122-1331 |
Sentence |
denotes |
As concerns Glu340, the results both support our computer-based predictions and confirm, at the biological level, previous identification of Glu340 as the nucleophile by use of active site labeling techniques. |
| T9 |
1122-1331 |
Sentence |
denotes |
As concerns Glu340, the results both support our computer-based predictions and confirm, at the biological level, previous identification of Glu340 as the nucleophile by use of active site labeling techniques. |
| TextSentencer_T10 |
1332-1500 |
Sentence |
denotes |
Finally, our findings may help to better understand the molecular basis of Gaucher disease, the human lysosomal disease resulting from deficiency in glucocerebrosidase. |
| T10 |
1332-1500 |
Sentence |
denotes |
Finally, our findings may help to better understand the molecular basis of Gaucher disease, the human lysosomal disease resulting from deficiency in glucocerebrosidase. |
| T10 |
1332-1500 |
Sentence |
denotes |
Finally, our findings may help to better understand the molecular basis of Gaucher disease, the human lysosomal disease resulting from deficiency in glucocerebrosidase. |