Pub. Date : 2005 Oct 1
PMID : 16179605
8 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
1 | Phosphatidylinositol (3,4,5)-trisphosphate specifically interacts with the phox homology domain of phospholipase D1 and stimulates its activity. | phosphatidylinositol 3,4,5-triphosphate | phospholipase D1 | Homo sapiens |
2 | Interestingly, the PX domain of PLD1, but not that of PLD2, was found to specifically interact with phosphatidylinositol (3,4,5)-trisphosphate (PtdIns(3,4,5)P3). | phosphatidylinositol 3,4,5-triphosphate | phospholipase D1 | Homo sapiens |
3 | Interestingly, the PX domain of PLD1, but not that of PLD2, was found to specifically interact with phosphatidylinositol (3,4,5)-trisphosphate (PtdIns(3,4,5)P3). | phosphatidylinositol 3,4,5-triphosphate | phospholipase D1 | Homo sapiens |
4 | We found that mutation of the conserved arginine at position 179 of the PLD1 PX domain to lysine or to alanine (R179A or R179K, respectively) disrupts PtdIns(3,4,5)P3 binding. | phosphatidylinositol 3,4,5-triphosphate | phospholipase D1 | Homo sapiens |
5 | The enzymatic activity of PLD1 was stimulated by adding PtdIns(3,4,5)P3 in vitro. | phosphatidylinositol 3,4,5-triphosphate | phospholipase D1 | Homo sapiens |
6 | Our results suggest that the PLD1 PX domain enables PLD1 to mediate signal transduction via ERK1/2 by providing a direct binding site for PtdIns(3,4,5)P3 and by activating PLD1. | phosphatidylinositol 3,4,5-triphosphate | phospholipase D1 | Homo sapiens |
7 | Our results suggest that the PLD1 PX domain enables PLD1 to mediate signal transduction via ERK1/2 by providing a direct binding site for PtdIns(3,4,5)P3 and by activating PLD1. | phosphatidylinositol 3,4,5-triphosphate | phospholipase D1 | Homo sapiens |
8 | Our results suggest that the PLD1 PX domain enables PLD1 to mediate signal transduction via ERK1/2 by providing a direct binding site for PtdIns(3,4,5)P3 and by activating PLD1. | phosphatidylinositol 3,4,5-triphosphate | phospholipase D1 | Homo sapiens |