PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 28834721-4 2017 Our results show that SP-C induces phase segregation at 37 C, resulting in an ordered phase with spectral features resembling an interdigitated state enriched in dipalmitoylphosphatidylcholine, a liquid-crystalline bilayer phase, and an extremely mobile phase consistent with small vesicles or micelles. 1,2-Dipalmitoylphosphatidylcholine 162-192 surfactant protein C Homo sapiens 22-26 21555131-4 2011 Due to the molecular level interaction, specifically at mole fraction 0.3, the isotherm obtained from that mixture resembled the isotherm obtained from the DPPC monolayer in the presence of SP-C. 1,2-Dipalmitoylphosphatidylcholine 156-160 surfactant protein C Homo sapiens 190-194 26632402-4 2016 The new synthetic SP-C PS (sSP-C PS) was synthesized from SPa-C, dipalmitoyl phosphatidylcholine, phosphatidyl glycerol, and palmitic acid. 1,2-Dipalmitoylphosphatidylcholine 65-96 surfactant protein C Homo sapiens 18-22 23805757-3 2013 The segregation of DPPC-enriched ordered phase has been related with the ability of surfactant films to produce very low tensions, while the presence in surfactant of two specific hydrophobic polypeptides, SP-B and SP-C, is absolutely required to facilitate surfactant dynamics, including film formation and re-spreading during expansion at inspiration. 1,2-Dipalmitoylphosphatidylcholine 19-23 surfactant protein C Homo sapiens 215-219 26397014-4 2015 In this work, the conformational behavior of both the acylated and deacylated SP-C isoforms was studied in a DPPC bilayer under different pH conditions using constant-pH molecular dynamics simulations. 1,2-Dipalmitoylphosphatidylcholine 109-113 surfactant protein C Homo sapiens 78-82 19917227-5 2009 SP-C modulates the effect of cholesterol to reduce the enthalpy associated with the gel-to-liquid-crystalline melting transition in dipalmitoylphosphatidylcholine (DPPC) bilayers, as analyzed by differential scanning calorimetry. 1,2-Dipalmitoylphosphatidylcholine 132-162 surfactant protein C Homo sapiens 0-4 20435014-8 2010 In contrast, the addition of PA has a charge-dependent condensing affect on DPPC monolayers containing SP-C. 1,2-Dipalmitoylphosphatidylcholine 76-80 surfactant protein C Homo sapiens 103-107 19917227-5 2009 SP-C modulates the effect of cholesterol to reduce the enthalpy associated with the gel-to-liquid-crystalline melting transition in dipalmitoylphosphatidylcholine (DPPC) bilayers, as analyzed by differential scanning calorimetry. 1,2-Dipalmitoylphosphatidylcholine 164-168 surfactant protein C Homo sapiens 0-4 19917227-7 2009 Incorporation of 1% or 2% SP-C (protein/phospholipid by weight) promotes almost instantaneous adsorption of suspensions of DPPC/palmitoyloleoylphospatidylcholine (POPC)/palmitoyloleoyl-phosphatidylglycerol (POPG) (50:25:15, w/w/w) into the air-liquid interface of a captive bubble, in both the absence and presence of cholesterol. 1,2-Dipalmitoylphosphatidylcholine 123-127 surfactant protein C Homo sapiens 26-30 17277191-5 2007 The free energy of association between dipalmitoylphosphatidylserines in the environment of dipalmitoylphosphatidylcholines has been calculated by using a novel approach to the dual topology technique of the PS-PC hybrid. 1,2-Dipalmitoylphosphatidylcholine 92-123 surfactant protein C Homo sapiens 208-213 18339301-10 2008 The effect of SP-C N-terminal peptides on the chain flexibility gradient of DPPC and DPPG bilayers is consistent with the existence of a peptide-promoted interdigitated phase at temperatures below the main gel-to-liquid-crystalline phase transition. 1,2-Dipalmitoylphosphatidylcholine 76-80 surfactant protein C Homo sapiens 14-18 17051367-5 2007 Native SP-C added to DPPC/DPPG monolayers (molar ratio 80:20) induced the formation of the surface confined reservoir independent of its palmitoylation degree. 1,2-Dipalmitoylphosphatidylcholine 21-25 surfactant protein C Homo sapiens 7-11 10821681-4 2000 Surfactant proteins, SP-B or SP-C, when present in the films of DPPC:PG spread at pi(i) = 5 mN/m, enhanced the incorporation of SP-A in the monolayers to a similar extent; the Deltapi values being dependent on the levels of SP-B or SP-C, 3-17 wt %, in the lipid films. 1,2-Dipalmitoylphosphatidylcholine 64-68 surfactant protein C Homo sapiens 29-33 11520031-2 2001 The resulting derivative Dans-SP-C conserves the secondary structure of native SP-C as well as the ability to promote interfacial adsorption of DPPC suspensions and to affect the thermotropic behavior of DPPC bilayers. 1,2-Dipalmitoylphosphatidylcholine 144-148 surfactant protein C Homo sapiens 30-34 11520031-2 2001 The resulting derivative Dans-SP-C conserves the secondary structure of native SP-C as well as the ability to promote interfacial adsorption of DPPC suspensions and to affect the thermotropic behavior of DPPC bilayers. 1,2-Dipalmitoylphosphatidylcholine 204-208 surfactant protein C Homo sapiens 30-34 11245834-4 2001 Higher activity in DPPC refinement of the monolayer was observed for SP-B compared with SP-C. 1,2-Dipalmitoylphosphatidylcholine 19-23 surfactant protein C Homo sapiens 88-92 10866961-7 2000 The ternary mixture DPPC/DPPG/SP-C transferred from the collapse region exhibited SP-C-rich domains surrounding pure lipid areas. 1,2-Dipalmitoylphosphatidylcholine 20-24 surfactant protein C Homo sapiens 30-34 10866961-7 2000 The ternary mixture DPPC/DPPG/SP-C transferred from the collapse region exhibited SP-C-rich domains surrounding pure lipid areas. 1,2-Dipalmitoylphosphatidylcholine 20-24 surfactant protein C Homo sapiens 82-86 11001826-3 2000 SP-A and SP-D are large hydrophilic proteins, which play an important role in host defense, whereas the small hydrophobic peptides SP-B and SP-C interact with DPPC to generate and maintain a surface-active film. 1,2-Dipalmitoylphosphatidylcholine 159-163 surfactant protein C Homo sapiens 140-144 10821681-9 2000 Monolayers of DPPC:PG plus 17 wt % SP-B or SP-C, which had similar phase properties with LC phase occupying a maximum 25% of the total monolayer area, displayed different abilities to enhance the adsorption of SP-A to the surface. 1,2-Dipalmitoylphosphatidylcholine 14-18 surfactant protein C Homo sapiens 43-47 9858708-0 1998 Rotational dynamics of spin-labelled surfactant-associated proteins SP-B and SP-C in dipalmitoylphosphatidylcholine and dipalmitoylphosphatidylglycerol bilayers. 1,2-Dipalmitoylphosphatidylcholine 85-115 surfactant protein C Homo sapiens 77-81 9889301-2 1999 Surface thermodynamic properties, secondary structure, and orientation of native and deacylated SP-C in 1, 2-dipalmitoylphosphatidylcholine (DPPC) monolayers has been characterized by combined surface pressure-molecular area (pi-A) isotherms and infrared reflection-absorption spectroscopy (IRRAS) measurements. 1,2-Dipalmitoylphosphatidylcholine 104-139 surfactant protein C Homo sapiens 96-100 9889301-2 1999 Surface thermodynamic properties, secondary structure, and orientation of native and deacylated SP-C in 1, 2-dipalmitoylphosphatidylcholine (DPPC) monolayers has been characterized by combined surface pressure-molecular area (pi-A) isotherms and infrared reflection-absorption spectroscopy (IRRAS) measurements. 1,2-Dipalmitoylphosphatidylcholine 141-145 surfactant protein C Homo sapiens 96-100 9858708-5 1998 Both proteins, TEMPO-SP-B and TEMPO-SP-C, showed considerable increases in mobility at temperatures above the pretransition of pure DPPC. 1,2-Dipalmitoylphosphatidylcholine 132-136 surfactant protein C Homo sapiens 36-40 9858708-6 1998 Finally, the mobility of the spin probes attached to both SP-B and SP-C was more restricted in DPPG than in DPPC bilayers, demonstrating that electrostatic interactions of the positively charged residues at the protein surface influence the rotational dynamics of the proteins in anionic lipid bilayers. 1,2-Dipalmitoylphosphatidylcholine 108-112 surfactant protein C Homo sapiens 67-71 9370454-3 1997 In gel phase DPPC/DPPG (7:3) bilayers with one or the other lipid component chain-perdeuterated, SP-C was found to affect first spectral moment more strongly for DPPG-d62 than for DPPC-d62. 1,2-Dipalmitoylphosphatidylcholine 13-17 surfactant protein C Homo sapiens 97-101 9518582-9 1998 The study suggests that the method of purification of SP-B and SP-C may modify their ability to enhance the adsorption rates of DPPC/protein mixtures, and this may be relevant to the formulation of protein-supplemented lipids for exogenous treatment of pulmonary surfactant insufficiency. 1,2-Dipalmitoylphosphatidylcholine 128-132 surfactant protein C Homo sapiens 63-67 9020791-6 1997 It is estimated that about 10 wt % SP-C might remain in the SP-C/(DPPC/CH) monolayers compressed to high surface pressures of about 72 mN/m, whereas SP-C at concentrations of > or = 5 wt % was squeezed out at pi approximately 50 mN/m from SP-C/DPPC films without cholesterol. 1,2-Dipalmitoylphosphatidylcholine 66-70 surfactant protein C Homo sapiens 60-64 9108235-10 1997 SP-C is a lipopeptide containing covalently linked palmitoyl chains and is folded into a 3.7-nm alpha-helix with a central 2.3-nm all-aliphatic part, making it perfectly suited to interact in a transmembranous way with a fluid bilayer composed of dipalmitoylglycerophosphocholine, the main component of surfactant. 1,2-Dipalmitoylphosphatidylcholine 247-279 surfactant protein C Homo sapiens 0-4 9020791-5 1997 In contrast, CH appeared to enhance the mixing of SP-C with DPPC/CH in ternary SP-C/(DPPC/CH) films compared to the miscibility of SP-C with DPPC in the SP-C/DPPC films. 1,2-Dipalmitoylphosphatidylcholine 60-64 surfactant protein C Homo sapiens 79-83 9020791-5 1997 In contrast, CH appeared to enhance the mixing of SP-C with DPPC/CH in ternary SP-C/(DPPC/CH) films compared to the miscibility of SP-C with DPPC in the SP-C/DPPC films. 1,2-Dipalmitoylphosphatidylcholine 60-64 surfactant protein C Homo sapiens 79-83 9020791-5 1997 In contrast, CH appeared to enhance the mixing of SP-C with DPPC/CH in ternary SP-C/(DPPC/CH) films compared to the miscibility of SP-C with DPPC in the SP-C/DPPC films. 1,2-Dipalmitoylphosphatidylcholine 60-64 surfactant protein C Homo sapiens 79-83 9020791-5 1997 In contrast, CH appeared to enhance the mixing of SP-C with DPPC/CH in ternary SP-C/(DPPC/CH) films compared to the miscibility of SP-C with DPPC in the SP-C/DPPC films. 1,2-Dipalmitoylphosphatidylcholine 85-89 surfactant protein C Homo sapiens 50-54 9020791-5 1997 In contrast, CH appeared to enhance the mixing of SP-C with DPPC/CH in ternary SP-C/(DPPC/CH) films compared to the miscibility of SP-C with DPPC in the SP-C/DPPC films. 1,2-Dipalmitoylphosphatidylcholine 85-89 surfactant protein C Homo sapiens 50-54 9020791-5 1997 In contrast, CH appeared to enhance the mixing of SP-C with DPPC/CH in ternary SP-C/(DPPC/CH) films compared to the miscibility of SP-C with DPPC in the SP-C/DPPC films. 1,2-Dipalmitoylphosphatidylcholine 85-89 surfactant protein C Homo sapiens 50-54 9020791-6 1997 It is estimated that about 10 wt % SP-C might remain in the SP-C/(DPPC/CH) monolayers compressed to high surface pressures of about 72 mN/m, whereas SP-C at concentrations of > or = 5 wt % was squeezed out at pi approximately 50 mN/m from SP-C/DPPC films without cholesterol. 1,2-Dipalmitoylphosphatidylcholine 66-70 surfactant protein C Homo sapiens 35-39 9020791-6 1997 It is estimated that about 10 wt % SP-C might remain in the SP-C/(DPPC/CH) monolayers compressed to high surface pressures of about 72 mN/m, whereas SP-C at concentrations of > or = 5 wt % was squeezed out at pi approximately 50 mN/m from SP-C/DPPC films without cholesterol. 1,2-Dipalmitoylphosphatidylcholine 66-70 surfactant protein C Homo sapiens 60-64 9020791-6 1997 It is estimated that about 10 wt % SP-C might remain in the SP-C/(DPPC/CH) monolayers compressed to high surface pressures of about 72 mN/m, whereas SP-C at concentrations of > or = 5 wt % was squeezed out at pi approximately 50 mN/m from SP-C/DPPC films without cholesterol. 1,2-Dipalmitoylphosphatidylcholine 66-70 surfactant protein C Homo sapiens 60-64 9020791-6 1997 It is estimated that about 10 wt % SP-C might remain in the SP-C/(DPPC/CH) monolayers compressed to high surface pressures of about 72 mN/m, whereas SP-C at concentrations of > or = 5 wt % was squeezed out at pi approximately 50 mN/m from SP-C/DPPC films without cholesterol. 1,2-Dipalmitoylphosphatidylcholine 247-251 surfactant protein C Homo sapiens 35-39 8038387-9 1994 This led to a conclusion that there was independent behavior of SP-B and SP-C in (SP-B:SP-C)/DPPC monolayers. 1,2-Dipalmitoylphosphatidylcholine 93-97 surfactant protein C Homo sapiens 73-77 8599660-1 1995 The interactions of the hydrophobic pulmonary surfactant proteins SP-B and SP-C with 1,2-dipalmitoylphosphatidylcholine in mixed, spread monolayer films have been studied in situ at the air/water interface with the technique of external reflection absorption infrared spectroscopy (IRRAS). 1,2-Dipalmitoylphosphatidylcholine 85-119 surfactant protein C Homo sapiens 75-79 7696261-0 1995 Interactions of hydrophobic lung surfactant proteins SP-B and SP-C with dipalmitoylphosphatidylcholine and dipalmitoylphosphatidylglycerol bilayers studied by electron spin resonance spectroscopy. 1,2-Dipalmitoylphosphatidylcholine 72-102 surfactant protein C Homo sapiens 62-66 7696261-1 1995 Hydrophobic surfactant-associated proteins SP-B and SP-C have been isolated from porcine lungs and reconstituted in multilamellar vesicles of dipalmitoylphosphatidylcholine (DPPC) or dipalmitoylphosphatidylglycerol (DPPG) containing different phospholipid spin probes, in order to characterize the lipid--protein interactions by electron spin resonance (ESR) spectroscopy. 1,2-Dipalmitoylphosphatidylcholine 174-178 surfactant protein C Homo sapiens 52-56 7696261-4 1995 The effect was saturated at protein/lipid ratios of 20% and 30% (w/w) for SP-B and SP-C, respectively, in bilayers of DPPC. 1,2-Dipalmitoylphosphatidylcholine 118-122 surfactant protein C Homo sapiens 83-87 7696261-5 1995 SP-B and SP-C increased the ordering and decreased the mobility of the lipid acyl chains in both DPPC and DPPG bilayers in the fluid phase, without affecting the gel phase on the convention ESR time scale. 1,2-Dipalmitoylphosphatidylcholine 97-101 surfactant protein C Homo sapiens 9-13 7696261-7 1995 The selectivity of the interaction of SP-B and SP-C with different phospholipid species was determined from the ESR spectra of spin-labeled phospholipids with different headgroups in host bilayers of either DPPC or DPPG. 1,2-Dipalmitoylphosphatidylcholine 207-211 surfactant protein C Homo sapiens 47-51 7993894-0 1994 Dynamic surface properties of pulmonary surfactant proteins SP-B and SP-C and their mixtures with dipalmitoylphosphatidylcholine. 1,2-Dipalmitoylphosphatidylcholine 98-128 surfactant protein C Homo sapiens 69-73 7993894-5 1994 Likewise, SP-C-DPPC complexes were reversibly excluded at pi approximately 55 mN m-1 from the SP-C/DPPC films that contained > or = 5 weight % protein. 1,2-Dipalmitoylphosphatidylcholine 15-19 surfactant protein C Homo sapiens 10-14 7993894-5 1994 Likewise, SP-C-DPPC complexes were reversibly excluded at pi approximately 55 mN m-1 from the SP-C/DPPC films that contained > or = 5 weight % protein. 1,2-Dipalmitoylphosphatidylcholine 15-19 surfactant protein C Homo sapiens 94-98 7993894-6 1994 Dynamic compression of the mixed protein-lipid films beyond the collapse pressure of DPPC showed that SP-B and SP-C improved the respreading of DPPC in a concentration dependent manner. 1,2-Dipalmitoylphosphatidylcholine 85-89 surfactant protein C Homo sapiens 111-115 7993894-6 1994 Dynamic compression of the mixed protein-lipid films beyond the collapse pressure of DPPC showed that SP-B and SP-C improved the respreading of DPPC in a concentration dependent manner. 1,2-Dipalmitoylphosphatidylcholine 144-148 surfactant protein C Homo sapiens 111-115 7993894-8 1994 The results from this study suggest a possible interfacial role for SP-B and SP-C in lipid replenishment at the alveolar-air interface, through enhancement of the respreading of DPPC collapse phases (SP-B and SP-C) or through reversible removal of phospholipid (SP-C) during dynamic cyclic compression-expansion of the alveolar surface. 1,2-Dipalmitoylphosphatidylcholine 178-182 surfactant protein C Homo sapiens 77-81 8874011-2 1996 Epifluorescence microscopy of monolayers spontaneously adsorbed from vesicles of dipalmitoylphosphatidylcholine or dipalmitoylphosphatidylcholine plus surfactant protein C (SP-C) showed gas, liquid expanded, and liquid condensed (LC) domains. 1,2-Dipalmitoylphosphatidylcholine 115-145 surfactant protein C Homo sapiens 173-177 7788796-4 1995 In lipid mixtures including DPPC and DPPG, SP-C was associated with shorter chain and unsaturated lipids below the bulk lipid phase transition. 1,2-Dipalmitoylphosphatidylcholine 28-32 surfactant protein C Homo sapiens 43-47 8038386-2 1994 The interaction of the hydrophobic pulmonary surfactant protein SP-C with dipalmitoylphosphatidylcholine (DPPC), dipalmitoylphosphatidylglycerol (DPPG) and DPPC:DPPG (7:3, mol:mol) in spread monolayers at the air-water interface has been studied. 1,2-Dipalmitoylphosphatidylcholine 74-104 surfactant protein C Homo sapiens 64-68 8038386-2 1994 The interaction of the hydrophobic pulmonary surfactant protein SP-C with dipalmitoylphosphatidylcholine (DPPC), dipalmitoylphosphatidylglycerol (DPPG) and DPPC:DPPG (7:3, mol:mol) in spread monolayers at the air-water interface has been studied. 1,2-Dipalmitoylphosphatidylcholine 106-110 surfactant protein C Homo sapiens 64-68 8038386-2 1994 The interaction of the hydrophobic pulmonary surfactant protein SP-C with dipalmitoylphosphatidylcholine (DPPC), dipalmitoylphosphatidylglycerol (DPPG) and DPPC:DPPG (7:3, mol:mol) in spread monolayers at the air-water interface has been studied. 1,2-Dipalmitoylphosphatidylcholine 156-160 surfactant protein C Homo sapiens 64-68 8323965-12 1993 The alpha-helical content of SP-C in micelles of LPC and vesicles of DPPC, 60 and 70%, respectively, was calculated to be higher than the alpha-helical content of the protein dissolved in any aqueous organic solvent. 1,2-Dipalmitoylphosphatidylcholine 69-73 surfactant protein C Homo sapiens 29-33 8422370-2 1993 The presence of either SP-B or SP-C in dipalmitoylphosphatidylcholine (DPPC) or dipalmitoylphosphatidylglycerol (DPPG) multilamellar vesicles broadened the DSC thermogram and reduced the enthalpy of transition in a concentration-dependent manner. 1,2-Dipalmitoylphosphatidylcholine 39-69 surfactant protein C Homo sapiens 31-35 8422370-2 1993 The presence of either SP-B or SP-C in dipalmitoylphosphatidylcholine (DPPC) or dipalmitoylphosphatidylglycerol (DPPG) multilamellar vesicles broadened the DSC thermogram and reduced the enthalpy of transition in a concentration-dependent manner. 1,2-Dipalmitoylphosphatidylcholine 71-75 surfactant protein C Homo sapiens 31-35 1420867-0 1992 Pulmonary surfactant protein SP-C causes packing rearrangements of dipalmitoylphosphatidylcholine in spread monolayers. 1,2-Dipalmitoylphosphatidylcholine 67-97 surfactant protein C Homo sapiens 29-33 1420867-1 1992 The hydrophobic pulmonary surfactant protein SP-C has been isolated from porcine lung surfactant, and it has been incorporated into monolayers of dipalmitoylphosphatidylcholine (DPPC). 1,2-Dipalmitoylphosphatidylcholine 146-176 surfactant protein C Homo sapiens 45-49 1420867-1 1992 The hydrophobic pulmonary surfactant protein SP-C has been isolated from porcine lung surfactant, and it has been incorporated into monolayers of dipalmitoylphosphatidylcholine (DPPC). 1,2-Dipalmitoylphosphatidylcholine 178-182 surfactant protein C Homo sapiens 45-49 1420867-3 1992 SP-C altered the packing arrangements of DPPC in the monolayer, causing the production of many more, smaller condensed lipid domains in its presence than in its absence. 1,2-Dipalmitoylphosphatidylcholine 41-45 surfactant protein C Homo sapiens 0-4 1616924-1 1992 Lipid-protein interactions of pulmonary surfactant-associated protein SP-C in model DPPC/DPPG and DPPC/DPPG/eggPC vesicles were studied using steady-state and time-resolved fluorescence measurements of two fluorescent phospholipid probes, NBD-PC and NBD-PG. 1,2-Dipalmitoylphosphatidylcholine 84-88 surfactant protein C Homo sapiens 70-74 1616924-1 1992 Lipid-protein interactions of pulmonary surfactant-associated protein SP-C in model DPPC/DPPG and DPPC/DPPG/eggPC vesicles were studied using steady-state and time-resolved fluorescence measurements of two fluorescent phospholipid probes, NBD-PC and NBD-PG. 1,2-Dipalmitoylphosphatidylcholine 98-102 surfactant protein C Homo sapiens 70-74 1616924-4 1992 Time-resolved measurements, as well as steady-state intensity measurements indicate that incorporation of SP-C into DPPC/DPPG or DPPC/DPPG/eggPC vesicles results in a increase in the fraction of the long-lifetime species of NBD-PC. 1,2-Dipalmitoylphosphatidylcholine 116-120 surfactant protein C Homo sapiens 106-110 1616057-2 1992 To determine possible mechanisms of tubular myelin formation, we studied the effects of purified surfactant proteins (SP-A, SP-B, and SP-C) on large unilamellar dipalmitoylphosphatidylcholine-egg phosphatidylglycerol (7/3; wt/wt) liposomes. 1,2-Dipalmitoylphosphatidylcholine 161-191 surfactant protein C Homo sapiens 134-138