PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 8161212-11 1994 Accumulation of CDP-choline, decreased activity of PA phosphatase, and increased contribution of PI lipids to ER-transport vesicle membrane suggest that in ethanol-fed animals diglycerides are depleted and PA is utilized in a CDP-diacylglycerol pathway, thus leading to the generation of a different group of phospholipids and consequently modified ER-transport vesicle membrane. Diglycerides 230-244 cut-like homeobox 1 Rattus norvegicus 226-229 3947653-1 1986 When 600 X g supernatants of 10% (w/v) rat lung homogenates were incubated with CDP[Me-14C]choline both saturated and unsaturated species of phosphatidylcholine were formed from endogenous diacylglycerols. Diglycerides 189-204 cut-like homeobox 1 Rattus norvegicus 80-83 8418887-4 1993 A phosphocholine cytidylyltransferase-mediated rise in cellular CDP choline content may explain the gemfibrozil-dependent rise in phosphatidylcholine biosynthesis since homogenates of monolayers incubated with CDP choline preferentially incorporate labeled diacylglycerol into phosphatidylcholine rather than triacylglycerol. Diglycerides 257-271 cut-like homeobox 1 Rattus norvegicus 64-67 8418887-6 1993 These results suggest that CDP choline may be a key regulator of the diacylglycerol branchpoint, since diacylglycerol is primarily incorporated into phosphatidylcholine or triacylglycerol depending on whether CDP choline is or is not available. Diglycerides 69-83 cut-like homeobox 1 Rattus norvegicus 27-30 8418887-6 1993 These results suggest that CDP choline may be a key regulator of the diacylglycerol branchpoint, since diacylglycerol is primarily incorporated into phosphatidylcholine or triacylglycerol depending on whether CDP choline is or is not available. Diglycerides 69-83 cut-like homeobox 1 Rattus norvegicus 209-212 8418887-6 1993 These results suggest that CDP choline may be a key regulator of the diacylglycerol branchpoint, since diacylglycerol is primarily incorporated into phosphatidylcholine or triacylglycerol depending on whether CDP choline is or is not available. Diglycerides 103-117 cut-like homeobox 1 Rattus norvegicus 27-30 1590762-7 1992 This indicates that the same pool of diacylglycerol is shared by choline-phosphotransferase and diacylglycerol acyltransferase and that the relative activity of these enzymes depends on the CDP-choline supply. Diglycerides 37-51 cut-like homeobox 1 Rattus norvegicus 190-193 1309795-14 1992 Instead, phosphatidylcholine biosynthesis appears to be inhibited due to a decreased level of diacylglycerol, a substrate for CDP-choline: 1,2-diacylglycerol cholinephosphotransferase. Diglycerides 94-108 cut-like homeobox 1 Rattus norvegicus 126-129 2539092-3 1989 The observations suggested that the glucagon-induced inhibition of the biosynthesis of phosphatidylethanolamine is probably due to a decreased supply of diacylglycerols, resulting in a decreased formation of phosphatidylethanolamine from CDP-ethanolamine and diacylglycerols. Diglycerides 153-168 cut-like homeobox 1 Rattus norvegicus 238-241 2847386-0 1988 [An increase of CDP-choline: diglyceride phosphocholine transferase reaction in microsome fraction and its decrease in nuclear membranes of the rat liver after treatment with hydrocortisone]. Diglycerides 29-40 cut-like homeobox 1 Rattus norvegicus 16-19 7142817-2 1982 When labeled diacylglycerol was incubated in the presence of unlabeled CDP-choline, the rate of phospholipid labeling looked very different from that measured in incubations of unlabeled diacylglycerol with CDP-[methyl-14C]choline. Diglycerides 13-27 cut-like homeobox 1 Rattus norvegicus 71-74 2981098-5 1985 The final preparation contained levels of CDP-diacylglycerol hydrolase and CDP-diacylglycerol: sn-glycero-3-phosphate 3-phosphatidyltransferase activities that were less than 1% of PI synthetase activity. Diglycerides 46-60 cut-like homeobox 1 Rattus norvegicus 42-45 7142817-2 1982 When labeled diacylglycerol was incubated in the presence of unlabeled CDP-choline, the rate of phospholipid labeling looked very different from that measured in incubations of unlabeled diacylglycerol with CDP-[methyl-14C]choline. Diglycerides 13-27 cut-like homeobox 1 Rattus norvegicus 207-210 7142817-2 1982 When labeled diacylglycerol was incubated in the presence of unlabeled CDP-choline, the rate of phospholipid labeling looked very different from that measured in incubations of unlabeled diacylglycerol with CDP-[methyl-14C]choline. Diglycerides 187-201 cut-like homeobox 1 Rattus norvegicus 71-74 7142817-2 1982 When labeled diacylglycerol was incubated in the presence of unlabeled CDP-choline, the rate of phospholipid labeling looked very different from that measured in incubations of unlabeled diacylglycerol with CDP-[methyl-14C]choline. Diglycerides 187-201 cut-like homeobox 1 Rattus norvegicus 207-210 6247410-1 1980 Selectivity of CDP-choline:diacylglycerol choline phosphotransferase and CDP-ethanolamine:diacylglycerol ethanolamine phosphotransferase for molecular species of diglyceride has been studied in rat brain microsomes in vitro. Diglycerides 162-173 cut-like homeobox 1 Rattus norvegicus 15-18 6247410-1 1980 Selectivity of CDP-choline:diacylglycerol choline phosphotransferase and CDP-ethanolamine:diacylglycerol ethanolamine phosphotransferase for molecular species of diglyceride has been studied in rat brain microsomes in vitro. Diglycerides 162-173 cut-like homeobox 1 Rattus norvegicus 73-76 6247410-2 1980 Diglyceride-labeled microsomes were prepared by incubation with labeled sn-glycerol-3-phosphate; the microsomes were then incubated with CDP-choline or CDP-ethanolamine for different time intervals. Diglycerides 0-11 cut-like homeobox 1 Rattus norvegicus 137-140 6247410-2 1980 Diglyceride-labeled microsomes were prepared by incubation with labeled sn-glycerol-3-phosphate; the microsomes were then incubated with CDP-choline or CDP-ethanolamine for different time intervals. Diglycerides 0-11 cut-like homeobox 1 Rattus norvegicus 152-155 5726197-3 1968 The results indicated that initial phosphorylation of the free choline followed by the formation of CDP-choline and the subsequent transfer of the phosphorylcholine to a diglyceride is one of the principal routes by which choline lipids in brain are formed. Diglycerides 170-181 cut-like homeobox 1 Rattus norvegicus 100-103 167919-2 1975 Incorporation of CDP[14C]choline into lecithin in rat liver or BHK-21 mitochondria could be attributed to residual contamination from elements of the endoplasmic reticulum, with added diglycerides or with endogenous diglycerides produced by the phospholipase C treatment. Diglycerides 184-196 cut-like homeobox 1 Rattus norvegicus 17-20 167919-2 1975 Incorporation of CDP[14C]choline into lecithin in rat liver or BHK-21 mitochondria could be attributed to residual contamination from elements of the endoplasmic reticulum, with added diglycerides or with endogenous diglycerides produced by the phospholipase C treatment. Diglycerides 216-228 cut-like homeobox 1 Rattus norvegicus 17-20 10082883-2 1999 Administration of CDP-choline to rats increases blood and brain cytidine and choline levels; this enhances the production of endogenous CDP-choline which then combines with fatty acids (as diacylglycerol), to yield phosphatidylcholine. Diglycerides 189-203 cut-like homeobox 1 Rattus norvegicus 18-21 10082883-2 1999 Administration of CDP-choline to rats increases blood and brain cytidine and choline levels; this enhances the production of endogenous CDP-choline which then combines with fatty acids (as diacylglycerol), to yield phosphatidylcholine. Diglycerides 189-203 cut-like homeobox 1 Rattus norvegicus 136-139