PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 29618528-5 2018 By contrast, how effectively a pre-existing DPPC monolayer prevents fibrinogen adsorption depends upon its surface pressure. 1,2-Dipalmitoylphosphatidylcholine 44-48 fibrinogen beta chain Homo sapiens 68-78 31651923-5 2019 When injected into the subphase beneath a monolayer of the phospholipid dipalmitoylphosphatidylcholine (DPPC, the majority component of LS), fibrinogen preferentially penetrates disordered liquid expanded (LE) regions and accumulates on the boundaries between LE DPPC and liquid condensed (LC) DPPC domains. 1,2-Dipalmitoylphosphatidylcholine 72-102 fibrinogen beta chain Homo sapiens 141-151 31651923-5 2019 When injected into the subphase beneath a monolayer of the phospholipid dipalmitoylphosphatidylcholine (DPPC, the majority component of LS), fibrinogen preferentially penetrates disordered liquid expanded (LE) regions and accumulates on the boundaries between LE DPPC and liquid condensed (LC) DPPC domains. 1,2-Dipalmitoylphosphatidylcholine 104-108 fibrinogen beta chain Homo sapiens 141-151 31651923-5 2019 When injected into the subphase beneath a monolayer of the phospholipid dipalmitoylphosphatidylcholine (DPPC, the majority component of LS), fibrinogen preferentially penetrates disordered liquid expanded (LE) regions and accumulates on the boundaries between LE DPPC and liquid condensed (LC) DPPC domains. 1,2-Dipalmitoylphosphatidylcholine 263-267 fibrinogen beta chain Homo sapiens 141-151 31651923-5 2019 When injected into the subphase beneath a monolayer of the phospholipid dipalmitoylphosphatidylcholine (DPPC, the majority component of LS), fibrinogen preferentially penetrates disordered liquid expanded (LE) regions and accumulates on the boundaries between LE DPPC and liquid condensed (LC) DPPC domains. 1,2-Dipalmitoylphosphatidylcholine 263-267 fibrinogen beta chain Homo sapiens 141-151 29618528-6 2018 At low DPPC surface pressures, fibrinogen penetrates DPPC monolayers, imparting a mixed viscoelastic shear response. 1,2-Dipalmitoylphosphatidylcholine 7-11 fibrinogen beta chain Homo sapiens 31-41 29618528-6 2018 At low DPPC surface pressures, fibrinogen penetrates DPPC monolayers, imparting a mixed viscoelastic shear response. 1,2-Dipalmitoylphosphatidylcholine 53-57 fibrinogen beta chain Homo sapiens 31-41 20829000-1 2010 Adsorption of fibrinogen to the monolayers of mixed lipids, dipalmitoyl phosphatidyl choline (DPPC) and eicosylamine (EA) was measured at a surface pressure of 20 mN/m by an in situ surface plasmon resonance technique. 1,2-Dipalmitoylphosphatidylcholine 60-92 fibrinogen beta chain Homo sapiens 14-24 25112907-6 2014 This surfactant reduces the inhibitory effect of fibrinogen by selectively interacting with DPPC (dipalmitoylphosphatidylcholine) and mimicking some of the interfacial properties of the pulmonary surfactant protein B (SP-B). 1,2-Dipalmitoylphosphatidylcholine 92-96 fibrinogen beta chain Homo sapiens 49-59 25112907-6 2014 This surfactant reduces the inhibitory effect of fibrinogen by selectively interacting with DPPC (dipalmitoylphosphatidylcholine) and mimicking some of the interfacial properties of the pulmonary surfactant protein B (SP-B). 1,2-Dipalmitoylphosphatidylcholine 98-128 fibrinogen beta chain Homo sapiens 49-59 25112907-8 2014 Hysteresis behaviors of the monolayers, which are composed of mixtures of DPPC and IPL at different molar ratios, indicate that with increasing amounts of IPL, the lipid losses from the interface induced by the presence of fibrinogen significantly decrease. 1,2-Dipalmitoylphosphatidylcholine 74-78 fibrinogen beta chain Homo sapiens 223-233 20829000-1 2010 Adsorption of fibrinogen to the monolayers of mixed lipids, dipalmitoyl phosphatidyl choline (DPPC) and eicosylamine (EA) was measured at a surface pressure of 20 mN/m by an in situ surface plasmon resonance technique. 1,2-Dipalmitoylphosphatidylcholine 94-98 fibrinogen beta chain Homo sapiens 14-24 20829000-5 2010 At a higher protein concentration (0.06 mg/ml) both the fibrinogen adsorbed amount and its maximum adsorption rate showed excess values relative to the pure EA for 1:1, 2:1 and 3:1 DPPC+EA monolayers. 1,2-Dipalmitoylphosphatidylcholine 181-185 fibrinogen beta chain Homo sapiens 56-66 7923477-1 1994 An abnormal fibrinogen that caused aggregation of red blood cells (RBC) in a patient with gangrene was examined by real-time X-ray diffraction to determine its effects on dipalmitoylphosphatidylcholine (DPPC) and 1-palmitoyl-2-oleoylphosphatidylethanolamine (POPE) phase transitions. 1,2-Dipalmitoylphosphatidylcholine 171-201 fibrinogen beta chain Homo sapiens 12-22 16831006-4 2006 For a mixed DPPC/fibrinogen layer at the interface, the amide I RA intensity-area hysteresis curves suggest that the fibrinogen molecules were expelled from the interface upon compression, apparently because of the presence of insoluble DPPC molecules. 1,2-Dipalmitoylphosphatidylcholine 12-16 fibrinogen beta chain Homo sapiens 117-127 16831006-4 2006 For a mixed DPPC/fibrinogen layer at the interface, the amide I RA intensity-area hysteresis curves suggest that the fibrinogen molecules were expelled from the interface upon compression, apparently because of the presence of insoluble DPPC molecules. 1,2-Dipalmitoylphosphatidylcholine 237-241 fibrinogen beta chain Homo sapiens 17-27 16831006-4 2006 For a mixed DPPC/fibrinogen layer at the interface, the amide I RA intensity-area hysteresis curves suggest that the fibrinogen molecules were expelled from the interface upon compression, apparently because of the presence of insoluble DPPC molecules. 1,2-Dipalmitoylphosphatidylcholine 237-241 fibrinogen beta chain Homo sapiens 117-127 16831006-5 2006 The squeeze-out of fibrinogen evidently removed a pronounced amount of DPPC from the interface, as judged from the corresponding nu(a)-CH2 intensity and wavenumber data. 1,2-Dipalmitoylphosphatidylcholine 71-75 fibrinogen beta chain Homo sapiens 19-29 16831006-7 2006 With the in situ IRRAS analysis of the mixed layer behavior at the interface, the induced loss of DPPC by fibrinogen expulsion from the compressed interface and the dominant adsorption of fibrinogen to the expanded interface were clearly demonstrated. 1,2-Dipalmitoylphosphatidylcholine 98-102 fibrinogen beta chain Homo sapiens 106-116 16115641-2 2006 For FB/DPPC mixtures with 750 ppm (0.075 wt%) FB and 1000 ppm (0.10 wt%) DPPC, the tension behavior was found to be similar to that of FB when alone, even with DPPC and FB being at the interface. 1,2-Dipalmitoylphosphatidylcholine 7-11 fibrinogen beta chain Homo sapiens 46-48 16115641-2 2006 For FB/DPPC mixtures with 750 ppm (0.075 wt%) FB and 1000 ppm (0.10 wt%) DPPC, the tension behavior was found to be similar to that of FB when alone, even with DPPC and FB being at the interface. 1,2-Dipalmitoylphosphatidylcholine 7-11 fibrinogen beta chain Homo sapiens 46-48 16115641-2 2006 For FB/DPPC mixtures with 750 ppm (0.075 wt%) FB and 1000 ppm (0.10 wt%) DPPC, the tension behavior was found to be similar to that of FB when alone, even with DPPC and FB being at the interface. 1,2-Dipalmitoylphosphatidylcholine 7-11 fibrinogen beta chain Homo sapiens 46-48 16115641-2 2006 For FB/DPPC mixtures with 750 ppm (0.075 wt%) FB and 1000 ppm (0.10 wt%) DPPC, the tension behavior was found to be similar to that of FB when alone, even with DPPC and FB being at the interface. 1,2-Dipalmitoylphosphatidylcholine 73-77 fibrinogen beta chain Homo sapiens 4-6 16115641-2 2006 For FB/DPPC mixtures with 750 ppm (0.075 wt%) FB and 1000 ppm (0.10 wt%) DPPC, the tension behavior was found to be similar to that of FB when alone, even with DPPC and FB being at the interface. 1,2-Dipalmitoylphosphatidylcholine 73-77 fibrinogen beta chain Homo sapiens 4-6 16115641-3 2006 Thus, FB interferes with adsorption of DPPC and inhibits its surface tension lowering ability. 1,2-Dipalmitoylphosphatidylcholine 39-43 fibrinogen beta chain Homo sapiens 6-8 16115641-4 2006 When FB protein is introduced in the solution after a DPPC monolayer has formed, the adsorption of FB is inhibited by the DPPC monolayer. 1,2-Dipalmitoylphosphatidylcholine 54-58 fibrinogen beta chain Homo sapiens 5-7 16115641-4 2006 When FB protein is introduced in the solution after a DPPC monolayer has formed, the adsorption of FB is inhibited by the DPPC monolayer. 1,2-Dipalmitoylphosphatidylcholine 54-58 fibrinogen beta chain Homo sapiens 99-101 16115641-4 2006 When FB protein is introduced in the solution after a DPPC monolayer has formed, the adsorption of FB is inhibited by the DPPC monolayer. 1,2-Dipalmitoylphosphatidylcholine 122-126 fibrinogen beta chain Homo sapiens 5-7 16115641-4 2006 When FB protein is introduced in the solution after a DPPC monolayer has formed, the adsorption of FB is inhibited by the DPPC monolayer. 1,2-Dipalmitoylphosphatidylcholine 122-126 fibrinogen beta chain Homo sapiens 99-101 16115641-5 2006 When a DPPC monolayer is spread onto a solution with a preadsorbed FB layer, the DPPC monolayer excludes FB from the surface and controls the tension behavior with little inhibition by FB. 1,2-Dipalmitoylphosphatidylcholine 7-11 fibrinogen beta chain Homo sapiens 67-69 16115641-5 2006 When a DPPC monolayer is spread onto a solution with a preadsorbed FB layer, the DPPC monolayer excludes FB from the surface and controls the tension behavior with little inhibition by FB. 1,2-Dipalmitoylphosphatidylcholine 7-11 fibrinogen beta chain Homo sapiens 105-107 16115641-5 2006 When a DPPC monolayer is spread onto a solution with a preadsorbed FB layer, the DPPC monolayer excludes FB from the surface and controls the tension behavior with little inhibition by FB. 1,2-Dipalmitoylphosphatidylcholine 7-11 fibrinogen beta chain Homo sapiens 105-107 16115641-5 2006 When a DPPC monolayer is spread onto a solution with a preadsorbed FB layer, the DPPC monolayer excludes FB from the surface and controls the tension behavior with little inhibition by FB. 1,2-Dipalmitoylphosphatidylcholine 81-85 fibrinogen beta chain Homo sapiens 67-69 16115641-5 2006 When a DPPC monolayer is spread onto a solution with a preadsorbed FB layer, the DPPC monolayer excludes FB from the surface and controls the tension behavior with little inhibition by FB. 1,2-Dipalmitoylphosphatidylcholine 81-85 fibrinogen beta chain Homo sapiens 105-107 16115641-5 2006 When a DPPC monolayer is spread onto a solution with a preadsorbed FB layer, the DPPC monolayer excludes FB from the surface and controls the tension behavior with little inhibition by FB. 1,2-Dipalmitoylphosphatidylcholine 81-85 fibrinogen beta chain Homo sapiens 105-107 16115641-6 2006 When a DPPC dispersion is introduced with the Trurnit method, or sprayed dropwise, onto an aqueous FB/DPPC surfaces, the DPPC layer formed on the surface prevents the adsorption of FB and dominates the surface tension behavior. 1,2-Dipalmitoylphosphatidylcholine 7-11 fibrinogen beta chain Homo sapiens 99-101 16115641-6 2006 When a DPPC dispersion is introduced with the Trurnit method, or sprayed dropwise, onto an aqueous FB/DPPC surfaces, the DPPC layer formed on the surface prevents the adsorption of FB and dominates the surface tension behavior. 1,2-Dipalmitoylphosphatidylcholine 7-11 fibrinogen beta chain Homo sapiens 181-183 16115641-6 2006 When a DPPC dispersion is introduced with the Trurnit method, or sprayed dropwise, onto an aqueous FB/DPPC surfaces, the DPPC layer formed on the surface prevents the adsorption of FB and dominates the surface tension behavior. 1,2-Dipalmitoylphosphatidylcholine 102-106 fibrinogen beta chain Homo sapiens 181-183 16115641-6 2006 When a DPPC dispersion is introduced with the Trurnit method, or sprayed dropwise, onto an aqueous FB/DPPC surfaces, the DPPC layer formed on the surface prevents the adsorption of FB and dominates the surface tension behavior. 1,2-Dipalmitoylphosphatidylcholine 102-106 fibrinogen beta chain Homo sapiens 181-183 17408294-5 2007 The addition of DPPC vesicles into these unstable FB dispersions reversed FB aggregation and precipitation and produced stable translucent microdispersions. 1,2-Dipalmitoylphosphatidylcholine 16-20 fibrinogen beta chain Homo sapiens 50-52 16256461-0 2003 Induced removal of dipalmitoyl phosphatidylcholine by the exclusion of fibrinogen from compressed monolayers at air/liquid interfaces. 1,2-Dipalmitoylphosphatidylcholine 19-50 fibrinogen beta chain Homo sapiens 71-81 16256461-1 2003 The induced removal of dipalmitoyl phosphatidylcholine (DPPC) by the exclusion of fibrinogen from mixed DPPC/fibrinogen monolayers at compressed air/liquid interfaces was analyzed. 1,2-Dipalmitoylphosphatidylcholine 23-54 fibrinogen beta chain Homo sapiens 82-92 16256461-1 2003 The induced removal of dipalmitoyl phosphatidylcholine (DPPC) by the exclusion of fibrinogen from mixed DPPC/fibrinogen monolayers at compressed air/liquid interfaces was analyzed. 1,2-Dipalmitoylphosphatidylcholine 56-60 fibrinogen beta chain Homo sapiens 82-92 16256461-1 2003 The induced removal of dipalmitoyl phosphatidylcholine (DPPC) by the exclusion of fibrinogen from mixed DPPC/fibrinogen monolayers at compressed air/liquid interfaces was analyzed. 1,2-Dipalmitoylphosphatidylcholine 56-60 fibrinogen beta chain Homo sapiens 109-119 16256461-4 2003 For mixed monolayers of DPPC with fibrinogen, the fibrinogen molecules were expelled from the interface upon compression due to the presence of insoluble DPPC molecules. 1,2-Dipalmitoylphosphatidylcholine 24-28 fibrinogen beta chain Homo sapiens 34-44 16256461-4 2003 For mixed monolayers of DPPC with fibrinogen, the fibrinogen molecules were expelled from the interface upon compression due to the presence of insoluble DPPC molecules. 1,2-Dipalmitoylphosphatidylcholine 24-28 fibrinogen beta chain Homo sapiens 50-60 16256461-4 2003 For mixed monolayers of DPPC with fibrinogen, the fibrinogen molecules were expelled from the interface upon compression due to the presence of insoluble DPPC molecules. 1,2-Dipalmitoylphosphatidylcholine 154-158 fibrinogen beta chain Homo sapiens 34-44 16256461-4 2003 For mixed monolayers of DPPC with fibrinogen, the fibrinogen molecules were expelled from the interface upon compression due to the presence of insoluble DPPC molecules. 1,2-Dipalmitoylphosphatidylcholine 154-158 fibrinogen beta chain Homo sapiens 50-60 16256461-5 2003 The squeeze-out of fibrinogen molecules evidently removed a significant number of DPPC molecules from the interface, with the extent depending on fibrinogen surface concentration. 1,2-Dipalmitoylphosphatidylcholine 82-86 fibrinogen beta chain Homo sapiens 19-29 16256461-5 2003 The squeeze-out of fibrinogen molecules evidently removed a significant number of DPPC molecules from the interface, with the extent depending on fibrinogen surface concentration. 1,2-Dipalmitoylphosphatidylcholine 82-86 fibrinogen beta chain Homo sapiens 146-156 16256461-7 2003 The induced loss of free DPPC molecules at the interface by the expelled fibrinogen molecules during the area compression stage was then evaluated from the hysteresis curves. 1,2-Dipalmitoylphosphatidylcholine 25-29 fibrinogen beta chain Homo sapiens 73-83 7923477-1 1994 An abnormal fibrinogen that caused aggregation of red blood cells (RBC) in a patient with gangrene was examined by real-time X-ray diffraction to determine its effects on dipalmitoylphosphatidylcholine (DPPC) and 1-palmitoyl-2-oleoylphosphatidylethanolamine (POPE) phase transitions. 1,2-Dipalmitoylphosphatidylcholine 203-207 fibrinogen beta chain Homo sapiens 12-22