PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 7493000-3 1995 Free myristic acid, released from DMPC upon PLA2 treatment, was anthrylmethylated with 9-anthryldiazomethane (ADAM) and determined by reversed-phase HPLC. Dimyristoylphosphatidylcholine 34-38 phospholipase A2 group IB Homo sapiens 44-48 17603006-8 2007 The rate increase is modeled with the assumption that the binding of PLA2 to DMPC interface is cooperatively promoted by bile salt followed by allosteric k(cat)(*)-activation of the bound enzyme by the anionic interface. Dimyristoylphosphatidylcholine 77-81 phospholipase A2 group IB Homo sapiens 69-73 17442288-2 2007 The disruption of DMPC multilamellar vesicles (MLV"s) with monomyristoylphosphatidylcholine (lysoPC), a product of hydrolysis of phospholipase A(2) (PLA(2)), is more efficient at 18 degrees C, where DMPC MLV"s are known to be in the ripple P(beta") phase, than at 10 degrees C (L(beta") flat gel phase). Dimyristoylphosphatidylcholine 18-22 phospholipase A2 group IB Homo sapiens 129-147 17442288-2 2007 The disruption of DMPC multilamellar vesicles (MLV"s) with monomyristoylphosphatidylcholine (lysoPC), a product of hydrolysis of phospholipase A(2) (PLA(2)), is more efficient at 18 degrees C, where DMPC MLV"s are known to be in the ripple P(beta") phase, than at 10 degrees C (L(beta") flat gel phase). Dimyristoylphosphatidylcholine 18-22 phospholipase A2 group IB Homo sapiens 149-155 17442288-2 2007 The disruption of DMPC multilamellar vesicles (MLV"s) with monomyristoylphosphatidylcholine (lysoPC), a product of hydrolysis of phospholipase A(2) (PLA(2)), is more efficient at 18 degrees C, where DMPC MLV"s are known to be in the ripple P(beta") phase, than at 10 degrees C (L(beta") flat gel phase). Dimyristoylphosphatidylcholine 199-203 phospholipase A2 group IB Homo sapiens 129-147 17603006-4 2007 The PLA2-catalyzed rate of hydrolysis of zwitterionic dimyristoylphosphatidylcholine (DMPC) vesicles depends on the concentration and structure of the bile salt. Dimyristoylphosphatidylcholine 86-90 phospholipase A2 group IB Homo sapiens 4-8 15240475-3 2004 PLA(2) is shown to have higher activity toward the ripple phase compared to the gel phase in 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) membranes, indicating its preference for this highly curved membrane morphology. Dimyristoylphosphatidylcholine 93-136 phospholipase A2 group IB Homo sapiens 0-6 15240475-3 2004 PLA(2) is shown to have higher activity toward the ripple phase compared to the gel phase in 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) membranes, indicating its preference for this highly curved membrane morphology. Dimyristoylphosphatidylcholine 138-142 phospholipase A2 group IB Homo sapiens 0-6 15240475-8 2004 Bulk high-performance liquid chromatography measurements indicate that PLA(2) preferentially hydrolyzes DMPC in the DMPC/DSPC ripples. Dimyristoylphosphatidylcholine 104-108 phospholipase A2 group IB Homo sapiens 71-77 15240475-8 2004 Bulk high-performance liquid chromatography measurements indicate that PLA(2) preferentially hydrolyzes DMPC in the DMPC/DSPC ripples. Dimyristoylphosphatidylcholine 116-120 phospholipase A2 group IB Homo sapiens 71-77 11718669-2 2001 In this study the activity of PLA(2) towards large unilamellar vesicles composed of DPPC:SMPC and DMPC:DSPC:SMPC is investigated using fluorescence and HPLC techniques. Dimyristoylphosphatidylcholine 98-102 phospholipase A2 group IB Homo sapiens 30-36 8563913-1 1995 Phospholipase A2 hydrolysis of dioleoylphosphatidylcholine, dimyristoylphosphatidylcholine or their equimolar mixture with sphingomyelin in liposomes exposed to gamma-radiation has been investigated. Dimyristoylphosphatidylcholine 60-90 phospholipase A2 group IB Homo sapiens 0-16 7811738-0 1995 Hydrolysis of DMPC or DPPC by pancreatic phospholipase A2 is slowed down when (perfluoroalkyl) alkanes are incorporated into the liposomal membrane. Dimyristoylphosphatidylcholine 14-18 phospholipase A2 group IB Homo sapiens 41-57 1799438-0 1991 Dependence on neutral salt concentration of the latency phase in the time course of hydrolysis of dimyristoylphosphatidylcholine liposomes by phospholipase A2. Dimyristoylphosphatidylcholine 98-128 phospholipase A2 group IB Homo sapiens 142-158 1799438-1 1991 The time course of the hydrolytic action of porcine pancreatic phospholipase A2 on sonicated dimyristoylphosphatidylcholine liposomes in the presence of variable NaCl concentrations has been studied at temperatures between 17 and 36 degrees C; at these temperatures liposomes are in the gel phase. Dimyristoylphosphatidylcholine 93-123 phospholipase A2 group IB Homo sapiens 63-79 1799439-0 1991 The interfacial calcium ion concentration as modulator of the latency phase in the hydrolysis of dimyristoylphosphatidylcholine liposomes by phospholipase A2. Dimyristoylphosphatidylcholine 97-127 phospholipase A2 group IB Homo sapiens 141-157 3167047-1 1988 Porcine pancreatic phospholipase A2 (PL A2) was used as a probe to study the structure of phospholipid domains of dimyristoylphosphatidylcholine (DMPC) vesicles +/- 2% cholesteryl oleate (CO), of discoidal structures formed by the interaction of apolipoprotein E (apoE) with these vesicles, and of large CO/DMPC microemulsion particles +/- apoE. Dimyristoylphosphatidylcholine 114-144 phospholipase A2 group IB Homo sapiens 37-42 2054375-3 1991 DMPC liposomes released entrapped solute on exposure to phospholipase A2, whereas mixed vesicles were resistant. Dimyristoylphosphatidylcholine 0-4 phospholipase A2 group IB Homo sapiens 56-72 3167047-1 1988 Porcine pancreatic phospholipase A2 (PL A2) was used as a probe to study the structure of phospholipid domains of dimyristoylphosphatidylcholine (DMPC) vesicles +/- 2% cholesteryl oleate (CO), of discoidal structures formed by the interaction of apolipoprotein E (apoE) with these vesicles, and of large CO/DMPC microemulsion particles +/- apoE. Dimyristoylphosphatidylcholine 114-144 phospholipase A2 group IB Homo sapiens 19-35 3167047-1 1988 Porcine pancreatic phospholipase A2 (PL A2) was used as a probe to study the structure of phospholipid domains of dimyristoylphosphatidylcholine (DMPC) vesicles +/- 2% cholesteryl oleate (CO), of discoidal structures formed by the interaction of apolipoprotein E (apoE) with these vesicles, and of large CO/DMPC microemulsion particles +/- apoE. Dimyristoylphosphatidylcholine 146-150 phospholipase A2 group IB Homo sapiens 37-42 3167047-1 1988 Porcine pancreatic phospholipase A2 (PL A2) was used as a probe to study the structure of phospholipid domains of dimyristoylphosphatidylcholine (DMPC) vesicles +/- 2% cholesteryl oleate (CO), of discoidal structures formed by the interaction of apolipoprotein E (apoE) with these vesicles, and of large CO/DMPC microemulsion particles +/- apoE. Dimyristoylphosphatidylcholine 307-311 phospholipase A2 group IB Homo sapiens 37-42 3676290-2 1987 The action of residual phospholipase A2 in melittin samples resulted in mixtures of DMPC and its hydrolytic products that underwent reversible transitions at temperatures between 30 and 35 degrees C from extended bilayers to micellar particles which gave narrow single-line deuterium and phosphorus-31 NMR spectra. Dimyristoylphosphatidylcholine 84-88 phospholipase A2 group IB Homo sapiens 23-39 3389515-9 1988 The hydrolysis of DMPC-PPHTE vesicles was measured by following the increase in pyrene monomer fluorescence emission due to phospholipase A2 action on PPHTE. Dimyristoylphosphatidylcholine 18-22 phospholipase A2 group IB Homo sapiens 124-140 7084452-0 1982 Human C-apolipoproteins promote hydrolysis of dimyristoyl phosphatidylcholine by snake venom phospholipase A2. Dimyristoylphosphatidylcholine 46-77 phospholipase A2 group IB Homo sapiens 93-109