| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-88 |
Sentence |
denotes |
Binding of the CC-chemokine RANTES to syndecan-1 and syndecan-4 expressed on HeLa cells. |
| T1 |
0-88 |
Sentence |
denotes |
Binding of the CC-chemokine RANTES to syndecan-1 and syndecan-4 expressed on HeLa cells. |
| T1 |
0-88 |
Sentence |
denotes |
Binding of the CC-chemokine RANTES to syndecan-1 and syndecan-4 expressed on HeLa cells. |
| TextSentencer_T2 |
89-169 |
Sentence |
denotes |
It is believed that proteoglycans influence biological properties of chemokines. |
| T2 |
89-169 |
Sentence |
denotes |
It is believed that proteoglycans influence biological properties of chemokines. |
| T2 |
89-169 |
Sentence |
denotes |
It is believed that proteoglycans influence biological properties of chemokines. |
| TextSentencer_T3 |
170-391 |
Sentence |
denotes |
We show that the CC chemokine RANTES binds not only to high-affinity binding sites on CCR5-positive HeLa cells but also to low-affinity binding sites on HeLa cells expressing or lacking RANTES G protein-coupled receptors. |
| T3 |
170-391 |
Sentence |
denotes |
We show that the CC chemokine RANTES binds not only to high-affinity binding sites on CCR5-positive HeLa cells but also to low-affinity binding sites on HeLa cells expressing or lacking RANTES G protein-coupled receptors. |
| T3 |
170-391 |
Sentence |
denotes |
We show that the CC chemokine RANTES binds not only to high-affinity binding sites on CCR5-positive HeLa cells but also to low-affinity binding sites on HeLa cells expressing or lacking RANTES G protein-coupled receptors. |
| TextSentencer_T4 |
392-554 |
Sentence |
denotes |
Coimmunoprecipitation studies demonstrate that RANTES forms complexes with glycanated syndecan (SD)-1 and -4, in addition to CCR5 on the CCR5-positive HeLa cells. |
| T4 |
392-554 |
Sentence |
denotes |
Coimmunoprecipitation studies demonstrate that RANTES forms complexes with glycanated syndecan (SD)-1 and -4, in addition to CCR5 on the CCR5-positive HeLa cells. |
| T4 |
392-554 |
Sentence |
denotes |
Coimmunoprecipitation studies demonstrate that RANTES forms complexes with glycanated syndecan (SD)-1 and -4, in addition to CCR5 on the CCR5-positive HeLa cells. |
| TextSentencer_T5 |
555-646 |
Sentence |
denotes |
Moreover, confocal microscopy analysis shows the colocalization of RANTES with SD-1 and -4. |
| T5 |
555-646 |
Sentence |
denotes |
Moreover, confocal microscopy analysis shows the colocalization of RANTES with SD-1 and -4. |
| T5 |
555-646 |
Sentence |
denotes |
Moreover, confocal microscopy analysis shows the colocalization of RANTES with SD-1 and -4. |
| TextSentencer_T6 |
647-828 |
Sentence |
denotes |
Glycosaminoglycans removal from the cells by glycosaminidases treatment prevented RANTES binding to SD-1 and -4 and decreased RANTES binding to CCR5 on the CCR5-positive HeLa cells. |
| T6 |
647-828 |
Sentence |
denotes |
Glycosaminoglycans removal from the cells by glycosaminidases treatment prevented RANTES binding to SD-1 and -4 and decreased RANTES binding to CCR5 on the CCR5-positive HeLa cells. |
| T6 |
647-828 |
Sentence |
denotes |
Glycosaminoglycans removal from the cells by glycosaminidases treatment prevented RANTES binding to SD-1 and -4 and decreased RANTES binding to CCR5 on the CCR5-positive HeLa cells. |
| TextSentencer_T7 |
829-985 |
Sentence |
denotes |
Removal of glycosaminoglycans by glycosaminidases treatment of the complexes, RANTES/SD-1/SD-4/+/-CCR5, immobilized on beads, reversed SD-1 and -4 bindings. |
| T7 |
829-985 |
Sentence |
denotes |
Removal of glycosaminoglycans by glycosaminidases treatment of the complexes, RANTES/SD-1/SD-4/+/-CCR5, immobilized on beads, reversed SD-1 and -4 bindings. |
| T7 |
829-985 |
Sentence |
denotes |
Removal of glycosaminoglycans by glycosaminidases treatment of the complexes, RANTES/SD-1/SD-4/+/-CCR5, immobilized on beads, reversed SD-1 and -4 bindings. |
| TextSentencer_T8 |
986-1101 |
Sentence |
denotes |
Therefore, RANTES bindings to SD-1 and -4 depend on glycosaminoglycans and facilitate RANTES interaction with CCR5. |
| T8 |
986-1101 |
Sentence |
denotes |
Therefore, RANTES bindings to SD-1 and -4 depend on glycosaminoglycans and facilitate RANTES interaction with CCR5. |
| T8 |
986-1101 |
Sentence |
denotes |
Therefore, RANTES bindings to SD-1 and -4 depend on glycosaminoglycans and facilitate RANTES interaction with CCR5. |
| TextSentencer_T9 |
1102-1263 |
Sentence |
denotes |
Extracting plasma membrane cholesterol abolished the coimmunoprecipitation of SD-1 with RANTES, suggesting that rafts are involved in RANTES association to SD-1. |
| T9 |
1102-1263 |
Sentence |
denotes |
Extracting plasma membrane cholesterol abolished the coimmunoprecipitation of SD-1 with RANTES, suggesting that rafts are involved in RANTES association to SD-1. |
| T9 |
1102-1263 |
Sentence |
denotes |
Extracting plasma membrane cholesterol abolished the coimmunoprecipitation of SD-1 with RANTES, suggesting that rafts are involved in RANTES association to SD-1. |
| TextSentencer_T10 |
1264-1438 |
Sentence |
denotes |
Confocal microscopy analysis as well as coimmunoprecipitation experiments show a RANTES-independent heteromeric complex on the CCR5-positive HeLa cells, SD-1, SD-4, and CCR5. |
| T10 |
1264-1438 |
Sentence |
denotes |
Confocal microscopy analysis as well as coimmunoprecipitation experiments show a RANTES-independent heteromeric complex on the CCR5-positive HeLa cells, SD-1, SD-4, and CCR5. |
| T10 |
1264-1438 |
Sentence |
denotes |
Confocal microscopy analysis as well as coimmunoprecipitation experiments show a RANTES-independent heteromeric complex on the CCR5-positive HeLa cells, SD-1, SD-4, and CCR5. |
| TextSentencer_T11 |
1439-1539 |
Sentence |
denotes |
This complex is likely a functional unit in which proteoglycans may modulate RANTES binding to CCR5. |
| T11 |
1439-1539 |
Sentence |
denotes |
This complex is likely a functional unit in which proteoglycans may modulate RANTES binding to CCR5. |
| T11 |
1439-1539 |
Sentence |
denotes |
This complex is likely a functional unit in which proteoglycans may modulate RANTES binding to CCR5. |