PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 12773039-4 2003 Common chemical features in the steroid and nonsteroid human CYP17 enzyme inhibitors, as deduced by the Catalyst/HipHop program, are one to two hydrogen bond acceptors (HBAs) and three hydrophobic groups. Hydrogen 144-152 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 61-66 12773039-6 2003 A model that permits hydrogen bond interaction between the azole functionality on ring D and the enzyme is consistent with experimental deductions for type II CYP17 inhibitors where a sixth ligating atom interacts with Fe(II) of heme. Hydrogen 21-29 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 159-164 1314112-14 1992 In this model of PLD activation, alpha-thrombin receptor occupancy leads to the breakdown of phosphatidylinositol 4,5-bisphosphate catalyzed by phospholipase C producing the Ca2+ secretagogue IP3 and DAG. Phosphatidylinositol 4,5-Diphosphate 93-130 coagulation factor II, thrombin Homo sapiens 39-47 1537886-0 1992 Endothelin stimulates phosphatidic acid formation in cultured rat mesangial cells: role of a protein kinase C-regulated phospholipase D. We have previously reported that endothelin-1 stimulates phospholipase C-induced hydrolysis of phosphatidylinositol-4,5-bisphosphate. Phosphatidylinositol 4,5-Diphosphate 232-269 endothelin 1 Rattus norvegicus 170-182 1313794-4 1992 Biochemical analyses of these mutant proteins have clearly shown that Lys112 and Lys114 of cofilin are crucially but differently involved in its interaction with actin and phosphatidylinositol 4,5-bisphosphate. Phosphatidylinositol 4,5-Diphosphate 172-209 cofilin 1 Homo sapiens 91-98 1313007-1 1992 The effective resolution of human platelet cytosolic phosphoinositide-phospholipase C (PLC) revealed five distinct activity peaks by Q-Sepharose and heparin-Sepharose column chromatographies when assayed using phosphatidylinositol (PI) and phosphatidylinositol 4,5-bisphosphate (PIP2). Phosphatidylinositol 4,5-Diphosphate 240-277 phospholipase C gamma 1 Homo sapiens 53-85 1313007-1 1992 The effective resolution of human platelet cytosolic phosphoinositide-phospholipase C (PLC) revealed five distinct activity peaks by Q-Sepharose and heparin-Sepharose column chromatographies when assayed using phosphatidylinositol (PI) and phosphatidylinositol 4,5-bisphosphate (PIP2). Phosphatidylinositol 4,5-Diphosphate 240-277 phospholipase C gamma 1 Homo sapiens 87-90 1313007-1 1992 The effective resolution of human platelet cytosolic phosphoinositide-phospholipase C (PLC) revealed five distinct activity peaks by Q-Sepharose and heparin-Sepharose column chromatographies when assayed using phosphatidylinositol (PI) and phosphatidylinositol 4,5-bisphosphate (PIP2). Phosphatidylinositol 4,5-Diphosphate 279-283 phospholipase C gamma 1 Homo sapiens 53-85 1313007-1 1992 The effective resolution of human platelet cytosolic phosphoinositide-phospholipase C (PLC) revealed five distinct activity peaks by Q-Sepharose and heparin-Sepharose column chromatographies when assayed using phosphatidylinositol (PI) and phosphatidylinositol 4,5-bisphosphate (PIP2). Phosphatidylinositol 4,5-Diphosphate 279-283 phospholipase C gamma 1 Homo sapiens 87-90 1313007-11 1992 The inhibitory effect of gelsolin on PIP2-hydrolysis by PLC-gamma 1 was diminished by a large amount of PIP2 substrate. Phosphatidylinositol 4,5-Diphosphate 37-41 gelsolin Homo sapiens 25-33 1313007-11 1992 The inhibitory effect of gelsolin on PIP2-hydrolysis by PLC-gamma 1 was diminished by a large amount of PIP2 substrate. Phosphatidylinositol 4,5-Diphosphate 37-41 phospholipase C gamma 1 Homo sapiens 56-67 1313007-12 1992 These results suggested that the inhibition of PLC by gelsolin is due to sequestration of substrate PIP2 by its competitive binding. Phosphatidylinositol 4,5-Diphosphate 100-104 phospholipase C gamma 1 Homo sapiens 47-50 1313007-12 1992 These results suggested that the inhibition of PLC by gelsolin is due to sequestration of substrate PIP2 by its competitive binding. Phosphatidylinositol 4,5-Diphosphate 100-104 gelsolin Homo sapiens 54-62 1316594-0 1992 Immunocytochemical studies on light-induced changes in phosphatidylinositol 4,5-bisphosphate immunoreactivity in the visual system of normal and norpA mutant of Drosophila. Phosphatidylinositol 4,5-Diphosphate 55-92 no receptor potential A Drosophila melanogaster 145-150 1316594-5 1992 These results suggest that the PIP2 in the photoreceptor cells is hydrolyzed by phospholipase C coded by the norpA gene upon light stimulation. Phosphatidylinositol 4,5-Diphosphate 31-35 no receptor potential A Drosophila melanogaster 80-95 1316594-5 1992 These results suggest that the PIP2 in the photoreceptor cells is hydrolyzed by phospholipase C coded by the norpA gene upon light stimulation. Phosphatidylinositol 4,5-Diphosphate 31-35 no receptor potential A Drosophila melanogaster 109-114 1312950-1 1992 The effect on the structure of profilin of phosphatidylinositol 4,5-bisphosphate (PIP2) binding was probed by fluorescence and circular dichroism (CD) spectroscopy. Phosphatidylinositol 4,5-Diphosphate 43-80 profilin Gossypium hirsutum 31-39 1312950-1 1992 The effect on the structure of profilin of phosphatidylinositol 4,5-bisphosphate (PIP2) binding was probed by fluorescence and circular dichroism (CD) spectroscopy. Phosphatidylinositol 4,5-Diphosphate 82-86 profilin Gossypium hirsutum 31-39 1312950-2 1992 Fluorescence of Trp3 and Trp31 of profilin at 292 nm showed a linear decrease in solution emission at 340 nm as PIP2/profilin was increased from 0 to 80:1, apparently due to a static quenching mechanism involving formation of a nonfluorescent PIP2/profilin complex. Phosphatidylinositol 4,5-Diphosphate 112-116 profilin Gossypium hirsutum 34-42 1312950-2 1992 Fluorescence of Trp3 and Trp31 of profilin at 292 nm showed a linear decrease in solution emission at 340 nm as PIP2/profilin was increased from 0 to 80:1, apparently due to a static quenching mechanism involving formation of a nonfluorescent PIP2/profilin complex. Phosphatidylinositol 4,5-Diphosphate 112-116 profilin Gossypium hirsutum 117-125 1312950-2 1992 Fluorescence of Trp3 and Trp31 of profilin at 292 nm showed a linear decrease in solution emission at 340 nm as PIP2/profilin was increased from 0 to 80:1, apparently due to a static quenching mechanism involving formation of a nonfluorescent PIP2/profilin complex. Phosphatidylinositol 4,5-Diphosphate 112-116 profilin Gossypium hirsutum 117-125 1312950-3 1992 CD spectra revealed an increase of up to 3.3-fold in the molar ellpticity at 222 nm for profilin as it binds PIP2, as well as changes in the Cotton effect between 250 and 310 nm. Phosphatidylinositol 4,5-Diphosphate 109-113 profilin Gossypium hirsutum 88-96 1312950-4 1992 These results are consistent with a possible increase in the alpha-helix content of profilin triggered by the binding of PIP2. Phosphatidylinositol 4,5-Diphosphate 121-125 profilin Gossypium hirsutum 84-92 1370476-5 1992 These results suggest that the inhibition of PtdIns 4,5-P2 hydrolysis by PMA and cAMP is attributable to reduced tyrosine phosphorylation of PLC-gamma 1. Phosphatidylinositol 4,5-Diphosphate 45-58 phospholipase C gamma 1 Homo sapiens 141-152 1346114-1 1992 An immediate consequence of T cell activation via the T cell receptor (TcR)/CD3 complex and CD2 antigen is the hydrolysis of phosphatidylinositol-(4,5)-bisphosphate and the generation of inositol-(1,4,5)-trisphosphate and diacylglycerol which then regulate intracellular calcium and protein kinase C. Changes in cellular levels of phosphoinositides phosphorylated on the D-4 and D-5 position during T cell activation have been well documented. Phosphatidylinositol 4,5-Diphosphate 125-164 CD2 molecule Homo sapiens 92-95 1309423-4 1992 EC significantly blocked the thrombin stimulated breakdown of phosphatidylinositol-4,5-bisphosphate (PIP2) and the production of phosphatidic acid in [32P]orthophosphate-labeled platelets and of inositol trisphosphate in [3H]myoinositol-labeled platelets. Phosphatidylinositol 4,5-Diphosphate 62-99 coagulation factor II, thrombin Homo sapiens 29-37 1309423-4 1992 EC significantly blocked the thrombin stimulated breakdown of phosphatidylinositol-4,5-bisphosphate (PIP2) and the production of phosphatidic acid in [32P]orthophosphate-labeled platelets and of inositol trisphosphate in [3H]myoinositol-labeled platelets. Phosphatidylinositol 4,5-Diphosphate 101-105 coagulation factor II, thrombin Homo sapiens 29-37 1309423-7 1992 These data indicate that EDRF blocks thrombin-induced platelet aggregation by inhibiting the activation of PIP2-specific phospholipase C and thereby suppressing the consequent activation of PKC and the mobilization of [Ca2+]i. Phosphatidylinositol 4,5-Diphosphate 107-111 alpha hemoglobin stabilizing protein Homo sapiens 25-29 1309423-7 1992 These data indicate that EDRF blocks thrombin-induced platelet aggregation by inhibiting the activation of PIP2-specific phospholipase C and thereby suppressing the consequent activation of PKC and the mobilization of [Ca2+]i. Phosphatidylinositol 4,5-Diphosphate 107-111 coagulation factor II, thrombin Homo sapiens 37-45