PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
2295617-3	1990	The phospholipid-induced inactivation of PKC was concentration and time dependent and only affected the kinase activity without influencing phorbol ester binding.	Phospholipids	4-16	protein kinase C iota	Homo sapiens	41-44	
2295617-1	1990	Interactions of types I, II, and III protein kinase C (PKC) with phospholipids were investigated by following the changes in protein kinase activity and phorbol ester binding.	Phospholipids	65-78	protein kinase C iota	Homo sapiens	55-58	
2295617-2	1990	The acidic phospholipids such as phosphatidylserine (PS), phosphatidic acid, phosphatidyl-glycerol, and cardiolipin, which are activators of PKC in the assay of protein phosphorylation, could differentially inactivate PKC I, II, and III during preincubation in the absence of divalent cation.	Phospholipids	11-24	protein kinase C iota	Homo sapiens	141-144	
2295617-2	1990	The acidic phospholipids such as phosphatidylserine (PS), phosphatidic acid, phosphatidyl-glycerol, and cardiolipin, which are activators of PKC in the assay of protein phosphorylation, could differentially inactivate PKC I, II, and III during preincubation in the absence of divalent cation.	Phospholipids	11-24	protein kinase C iota	Homo sapiens	218-236	
2295617-4	1990	PKC I was the most susceptible to the phospholipid-induced inactivation, and PKC III was the least.	Phospholipids	38-50	protein kinase C iota	Homo sapiens	0-5	
2295617-6	1990	Addition of divalent cation such as Ca2+ or Mg2+ suppressed the phospholipid-induced inactivation of PKC.	Phospholipids	64-76	protein kinase C iota	Homo sapiens	101-104	
2295617-11	1990	The phospholipid-induced inactivation of PKC apparently results from a direct interaction of phospholipid with the catalytic domain of PKC; this interaction can be suppressed by divalent cations.	Phospholipids	4-16	protein kinase C iota	Homo sapiens	41-44	
2295617-11	1990	The phospholipid-induced inactivation of PKC apparently results from a direct interaction of phospholipid with the catalytic domain of PKC; this interaction can be suppressed by divalent cations.	Phospholipids	4-16	protein kinase C iota	Homo sapiens	135-138	
2295617-11	1990	The phospholipid-induced inactivation of PKC apparently results from a direct interaction of phospholipid with the catalytic domain of PKC; this interaction can be suppressed by divalent cations.	Phospholipids	93-105	protein kinase C iota	Homo sapiens	41-44	
2295617-11	1990	The phospholipid-induced inactivation of PKC apparently results from a direct interaction of phospholipid with the catalytic domain of PKC; this interaction can be suppressed by divalent cations.	Phospholipids	93-105	protein kinase C iota	Homo sapiens	135-138