PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
32826291-4	2020	Phosphatidylinositol (4,5)-bisphosphate [PI(4,5)P2] becomes enriched at WPB-plasma membrane contact sites at the time of fusion, most likely downstream of phospholipase D1-mediated production of phosphatidic acid (PA) that activates phosphatidylinositol 4-phosphate (PI4P) 5-kinase gamma.	pi(4,5)p2	41-50	phospholipase D1	Homo sapiens	155-171	
32198492-0	2020	Crystal structure of human PLD1 provides insight into activation by PI(4,5)P2 and RhoA.	pi(4,5)p2	68-77	phospholipase D1	Homo sapiens	27-31	
10660303-5	2000	Furthermore, PLD1 bound specifically and with high affinity to lipid surfaces containing PI(4,5)P2 independently of the substrate phosphatidylcholine, suggesting a key role for the PH domain in PLD function.	pi(4,5)p2	89-98	phospholipase D1	Homo sapiens	13-17	
10660303-6	2000	Importantly, a glutathione-S-transferase (GST) fusion protein comprising GST and the PH domain of PLD1 (GST-PLD1-PH) also bound specifically to supported lipid monolayers containing PI(4,5)P2.	pi(4,5)p2	182-191	phospholipase D1	Homo sapiens	98-102	
10660303-6	2000	Importantly, a glutathione-S-transferase (GST) fusion protein comprising GST and the PH domain of PLD1 (GST-PLD1-PH) also bound specifically to supported lipid monolayers containing PI(4,5)P2.	pi(4,5)p2	182-191	phospholipase D1	Homo sapiens	104-115