| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-105 |
Sentence |
denotes |
Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy. |
| T1 |
0-105 |
Sentence |
denotes |
Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy. |
| T1 |
0-105 |
Sentence |
denotes |
Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy. |
| TextSentencer_T2 |
106-222 |
Sentence |
denotes |
Cardiac-type sarco(endo)plasmic reticulum Ca(2)-ATPase (SERCA2a) plays a major role in cardiac muscle contractility. |
| T2 |
106-222 |
Sentence |
denotes |
Cardiac-type sarco(endo)plasmic reticulum Ca(2)-ATPase (SERCA2a) plays a major role in cardiac muscle contractility. |
| T2 |
106-222 |
Sentence |
denotes |
Cardiac-type sarco(endo)plasmic reticulum Ca(2)-ATPase (SERCA2a) plays a major role in cardiac muscle contractility. |
| TextSentencer_T3 |
223-309 |
Sentence |
denotes |
Phospholamban (PLN) regulates the function of SERCA2a via its Ser(16)-phosphorylation. |
| T3 |
223-309 |
Sentence |
denotes |
Phospholamban (PLN) regulates the function of SERCA2a via its Ser(16)-phosphorylation. |
| T3 |
223-309 |
Sentence |
denotes |
Phospholamban (PLN) regulates the function of SERCA2a via its Ser(16)-phosphorylation. |
| TextSentencer_T4 |
310-542 |
Sentence |
denotes |
Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes. |
| T4 |
310-542 |
Sentence |
denotes |
Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes. |
| T4 |
310-542 |
Sentence |
denotes |
Since it has been proposed that the Ser/Thr residues on cytoplasmic and nuclear proteins are modified by O-linked N-acetylglucosamine (O-GlcNAc), we examined the effect of O-GlcNAcylation on PLN function in rat adult cardiomyocytes. |
| TextSentencer_T5 |
543-739 |
Sentence |
denotes |
Studies using enzymatic labeling and co-immunoprecipitation of wild type and a series of mutants of PLN showed that PLN was O-GlcNAcylated and Ser(16) of PLN might be the site for O-GlcNAcylation. |
| T5 |
543-739 |
Sentence |
denotes |
Studies using enzymatic labeling and co-immunoprecipitation of wild type and a series of mutants of PLN showed that PLN was O-GlcNAcylated and Ser(16) of PLN might be the site for O-GlcNAcylation. |
| T5 |
543-739 |
Sentence |
denotes |
Studies using enzymatic labeling and co-immunoprecipitation of wild type and a series of mutants of PLN showed that PLN was O-GlcNAcylated and Ser(16) of PLN might be the site for O-GlcNAcylation. |
| TextSentencer_T6 |
740-928 |
Sentence |
denotes |
In cardiomyocytes treated with O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), the O-GlcNAcylation was significantly increased compared to non-treated cells. |
| T6 |
740-928 |
Sentence |
denotes |
In cardiomyocytes treated with O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), the O-GlcNAcylation was significantly increased compared to non-treated cells. |
| T6 |
740-928 |
Sentence |
denotes |
In cardiomyocytes treated with O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), the O-GlcNAcylation was significantly increased compared to non-treated cells. |
| TextSentencer_T7 |
929-988 |
Sentence |
denotes |
Simultaneously, Ser(16)-phosphorylation of PLN was reduced. |
| T7 |
929-988 |
Sentence |
denotes |
Simultaneously, Ser(16)-phosphorylation of PLN was reduced. |
| T7 |
929-988 |
Sentence |
denotes |
Simultaneously, Ser(16)-phosphorylation of PLN was reduced. |
| TextSentencer_T8 |
989-1171 |
Sentence |
denotes |
In Chinese hamster ovary cells where PLN cDNA and O-GlcNAc transferase siRNA were co-transfected, the Ser(16)-phosphorylation of PLN was significantly increased compared to controls. |
| T8 |
989-1171 |
Sentence |
denotes |
In Chinese hamster ovary cells where PLN cDNA and O-GlcNAc transferase siRNA were co-transfected, the Ser(16)-phosphorylation of PLN was significantly increased compared to controls. |
| T8 |
989-1171 |
Sentence |
denotes |
In Chinese hamster ovary cells where PLN cDNA and O-GlcNAc transferase siRNA were co-transfected, the Ser(16)-phosphorylation of PLN was significantly increased compared to controls. |
| TextSentencer_T9 |
1172-1243 |
Sentence |
denotes |
The same results were observed in heart homogenates from diabetic rats. |
| T9 |
1172-1243 |
Sentence |
denotes |
The same results were observed in heart homogenates from diabetic rats. |
| T9 |
1172-1243 |
Sentence |
denotes |
The same results were observed in heart homogenates from diabetic rats. |
| TextSentencer_T10 |
1244-1390 |
Sentence |
denotes |
In a co-immunoprecipitation of PLN with SERCA2a, the physical interaction between the two proteins was increased in PUGNAc-treated cardiomyocytes. |
| T10 |
1244-1390 |
Sentence |
denotes |
In a co-immunoprecipitation of PLN with SERCA2a, the physical interaction between the two proteins was increased in PUGNAc-treated cardiomyocytes. |
| T10 |
1244-1390 |
Sentence |
denotes |
In a co-immunoprecipitation of PLN with SERCA2a, the physical interaction between the two proteins was increased in PUGNAc-treated cardiomyocytes. |
| TextSentencer_T11 |
1391-1584 |
Sentence |
denotes |
Unlike non-treated cells, the activity of SERCA2a and the profiles of calcium transients in PUGNAc-treated cardiomyocytes were not significantly changed even after treatment with catecholamine. |
| T11 |
1391-1584 |
Sentence |
denotes |
Unlike non-treated cells, the activity of SERCA2a and the profiles of calcium transients in PUGNAc-treated cardiomyocytes were not significantly changed even after treatment with catecholamine. |
| T11 |
1391-1584 |
Sentence |
denotes |
Unlike non-treated cells, the activity of SERCA2a and the profiles of calcium transients in PUGNAc-treated cardiomyocytes were not significantly changed even after treatment with catecholamine. |
| TextSentencer_T12 |
1585-1738 |
Sentence |
denotes |
These data suggest that PLN is O-GlcNAcylated to induce the inhibition of its phosphorylation, which correlates to the deterioration of cardiac function. |
| T12 |
1585-1738 |
Sentence |
denotes |
These data suggest that PLN is O-GlcNAcylated to induce the inhibition of its phosphorylation, which correlates to the deterioration of cardiac function. |
| T12 |
1585-1738 |
Sentence |
denotes |
These data suggest that PLN is O-GlcNAcylated to induce the inhibition of its phosphorylation, which correlates to the deterioration of cardiac function. |
| TextSentencer_T13 |
1739-1910 |
Sentence |
denotes |
This might define a novel mechanism by which PLN regulation of SERCA2a is altered under conditions where O-GlcNAcylation is increased, such as those occurring in diabetes. |
| T13 |
1739-1910 |
Sentence |
denotes |
This might define a novel mechanism by which PLN regulation of SERCA2a is altered under conditions where O-GlcNAcylation is increased, such as those occurring in diabetes. |
| T13 |
1739-1910 |
Sentence |
denotes |
This might define a novel mechanism by which PLN regulation of SERCA2a is altered under conditions where O-GlcNAcylation is increased, such as those occurring in diabetes. |