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