PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 6587389-1 1984 Spin-labeled analogs of phosphatidylcholine, phosphatidylserine, and phosphatidylethanolamine have been used to study phospholipid transverse diffusion and asymmetry in the human erythrocyte membrane. Phosphatidylcholines 24-43 spindlin 1 Homo sapiens 0-4 2554971-6 1989 Spin-labeled phosphatidylglycerol shows a preferential interaction over the corresponding monogalactosyldiacylglycerol and phosphatidylcholine analogues, in contrast to the common behavior of this lipid in mammalian systems. Phosphatidylcholines 123-142 spindlin 1 Homo sapiens 0-4 2820490-5 1987 (2) Spin-labeled lipophilic cations were synthesized and the binding to liposomes of egg phosphatidylcholine was examined. Phosphatidylcholines 89-108 spindlin 1 Homo sapiens 4-8 2554971-5 1989 Spin-labeled monogalactosyldiacylglycerol exhibits very little preferential interaction over phosphatidylchline, which suggests that part of the role of monogalactosyldiacylglycerol in thylakoid membranes is structural, as is the case for phosphatidylcholine in mammalian membranes. Phosphatidylcholines 239-258 spindlin 1 Homo sapiens 0-4 3137572-1 1988 Spin-labeled phospholipids have been used to study the outside----inside and inside----outside transport of phospholipids across the human erythrocyte membrane at 37 degrees C. As already shown, inward transport is much faster for aminophospholipids than for phosphatidylcholine. Phosphatidylcholines 259-278 spindlin 1 Homo sapiens 0-4 2835102-1 1988 The intramembrane locations of several spin labeled probes in small egg phosphatidylcholine (egg PC) vesicles were determined from the enhancement of the 13C nuclear spin lattice relaxation of the membrane phospholipid. Phosphatidylcholines 72-91 spindlin 1 Homo sapiens 39-43 2835102-1 1988 The intramembrane locations of several spin labeled probes in small egg phosphatidylcholine (egg PC) vesicles were determined from the enhancement of the 13C nuclear spin lattice relaxation of the membrane phospholipid. Phosphatidylcholines 72-91 spindlin 1 Homo sapiens 166-170 3028505-1 1987 Temperature relationship was measured of ESR spectra of spin probes--derivatives of fatty acids whose nitroxyl fragments are incorporated into surface and inner layers of phosphatidylcholine liposomes (T = 180-260 K), as well as of the probe in model ethanol solution (T = 110-220 K). Phosphatidylcholines 171-190 spindlin 1 Homo sapiens 56-60 3002470-0 1986 Spin-label studies on phosphatidylcholine-cholesterol membranes: effects of alkyl chain length and unsaturation in the fluid phase. Phosphatidylcholines 22-41 spindlin 1 Homo sapiens 0-4 2990533-4 1985 Spin-labeling and radiolabeling data show that the incorporation of (4 +/- 1) X 10(6) molecules of exogenous phosphatidylcholine per cell converts discocytes to stage 3 echinocytes with about 35 conical spicules. Phosphatidylcholines 109-128 spindlin 1 Homo sapiens 0-4 178361-3 1976 Spin labeled analogs of phosphatidylcholine were used to study the transverse diffusion (flip-flop) of phospholipids in the erythrocyte membrane. Phosphatidylcholines 24-43 spindlin 1 Homo sapiens 0-4 6243999-3 1980 Spin labels derived from five carboxylic acids of different lengths were synthesized and incorporated in varying amounts into multilamellar and unilamellar vesicles made up of four different phosphatidylcholines. Phosphatidylcholines 191-211 spindlin 1 Homo sapiens 0-4 6260171-1 1981 ESR spectrometry has been used to study fatty acid spin-labeled phosphatidylcholine exchange from single bilayer donor vesicles to various acceptor systems, such as intact or differently treated mitochondria, phospholipid multilamellar vesicles or single bilayer vesicles. Phosphatidylcholines 64-83 spindlin 1 Homo sapiens 51-55 178361-5 1976 These labeled phosphatidylcholine molecules were incorporated into the membrane by incubation of the red cells at 22 degrees C with sonicated spin-labed phosphatidylcholine vesicles from which all traces of free fatty acids and lyso derivatives were carefully removed by bovine serum albumin treatment. Phosphatidylcholines 153-172 spindlin 1 Homo sapiens 142-146 178361-7 1976 When spin-labeled phosphatidylcholine, having a nitroxide on the beta chain but near the polar head-group, was incorporated into the erythrocyte membrane, ascorbate treatment at 0 degrees C allows selective reduction of the signal coming from the outer layer of the membrane. Phosphatidylcholines 18-37 spindlin 1 Homo sapiens 5-9 178361-9 1976 The anisotropic distribution of spin-labeled phosphatidylcholine in the erythrocyte membrane was found to be stable at 22 and 37 degrees C for more than 4 h. It is therefore concluded that the rate of outside-inside and inside-outside transition is so slow that the anisotropic distribution of the phospholipids in the erythrocyte membrane can be maintained during cell life. Phosphatidylcholines 45-64 spindlin 1 Homo sapiens 32-36 178361-5 1976 These labeled phosphatidylcholine molecules were incorporated into the membrane by incubation of the red cells at 22 degrees C with sonicated spin-labed phosphatidylcholine vesicles from which all traces of free fatty acids and lyso derivatives were carefully removed by bovine serum albumin treatment. Phosphatidylcholines 14-33 spindlin 1 Homo sapiens 142-146 17729124-1 2007 A new potentially antioxidant compound, spin-labelled lutein (SL-lut), was synthesized and incorporated into egg yolk phosphatidylcholine (EYPC) liposome membrane. Phosphatidylcholines 118-137 spindlin 1 Homo sapiens 40-44 11470084-4 2001 In the fluid phase region, the outer hyperfine splitting increases for all phosphatidylcholine spin-label positional isomers, indicating that the chain mobility is decreased by binding avidin. Phosphatidylcholines 75-94 spindlin 1 Homo sapiens 95-99 8938187-2 1996 After incorporation into the outer membrane leaflet spin-labeled aminophospholipids phosphatidylserine (PS) and phosphatidylethanolamine (PE) moved rapidly to the inner monolayer, whereas the analog of phosphatidylcholine (PC) disappeared more slowly from the outer leaflet. Phosphatidylcholines 202-221 spindlin 1 Homo sapiens 52-56 9826612-4 1998 For phosphatidylcholine also spin-labeled at the 8 position of the sn-2 chain, this ratio was reversed: the relaxation enhancement by Ni2+ ions was half that induced by molecular oxygen. Phosphatidylcholines 4-23 spindlin 1 Homo sapiens 29-33 9826612-6 1998 For a double-labeled system, in which both N-biotinyl phosphatidylethanolamine and phosphatidylcholine were spin-labeled on the 12 C atom of the sn-2 chain, the relaxation rate in the absence of avidin was greater than that predicted from linear additivity of the corresponding singly labeled systems, because of mutual spin-spin interactions between the two labeled lipid species. Phosphatidylcholines 83-102 spindlin 1 Homo sapiens 108-112 11015229-2 2000 Comparison of the positional dependences of the spectral data for the two series of spin-labeled lipids suggests that the N-acyl chain is positioned at approximately the same level as the sn-2 chain of the phosphatidylcholine spin-label. Phosphatidylcholines 206-225 spindlin 1 Homo sapiens 84-88 11015229-2 2000 Comparison of the positional dependences of the spectral data for the two series of spin-labeled lipids suggests that the N-acyl chain is positioned at approximately the same level as the sn-2 chain of the phosphatidylcholine spin-label. Phosphatidylcholines 206-225 spindlin 1 Homo sapiens 226-230 11015229-3 2000 Further, similar conclusions are reached when the ESR spectra of the N-acyl PE spin-labels in dimyristoylphosphatidylcholine (DMPC) or dimyristoylphosphatidylethanolamine (DMPE) host matrixes are compared with those of phosphatidylcholine spin-labels in these two lipids. Phosphatidylcholines 105-124 spindlin 1 Homo sapiens 79-83 9200687-1 1997 The specific binding of hen egg white avidin to phosphatidylcholine lipid membranes containing spin-labeled N-biotinylphosphatidylethanolamines (biotin-PESLs) was investigated by using ESR spectroscopy. Phosphatidylcholines 48-67 spindlin 1 Homo sapiens 95-99 8938187-2 1996 After incorporation into the outer membrane leaflet spin-labeled aminophospholipids phosphatidylserine (PS) and phosphatidylethanolamine (PE) moved rapidly to the inner monolayer, whereas the analog of phosphatidylcholine (PC) disappeared more slowly from the outer leaflet. Phosphatidylcholines 223-225 spindlin 1 Homo sapiens 52-56 8026481-3 1994 Asymmetrical distributions and translocation kinetics were very different for spin-labeled phosphatidylserine and spin-labeled phosphatidylcholine in fresh platelet plasma membranes. Phosphatidylcholines 127-146 spindlin 1 Homo sapiens 114-118 8026481-5 1994 However, spin-labeled phosphatidylcholine was mainly retained on the external leaflet. Phosphatidylcholines 22-41 spindlin 1 Homo sapiens 9-13 8347671-0 1993 Spin-label studies on phosphatidylcholine-polar carotenoid membranes: effects of alkyl-chain length and unsaturation. Phosphatidylcholines 22-41 spindlin 1 Homo sapiens 0-4 8347671-1 1993 Spin-labeling methods were used to study the structure and dynamic properties of phosphatidylcholine (PC)-dihydroxycarotenoid membranes as a function of phospholipid alkyl chain length, alkyl chain saturation, temperature and mol fraction of carotenoids. Phosphatidylcholines 81-100 spindlin 1 Homo sapiens 0-4 8347671-1 1993 Spin-labeling methods were used to study the structure and dynamic properties of phosphatidylcholine (PC)-dihydroxycarotenoid membranes as a function of phospholipid alkyl chain length, alkyl chain saturation, temperature and mol fraction of carotenoids. Phosphatidylcholines 102-104 spindlin 1 Homo sapiens 0-4 8347671-4 1993 (2) The abrupt changes of spin-label motion observed at the main-phase transition of the saturated PC membranes are broadened and shifted to lower temperatures. Phosphatidylcholines 99-101 spindlin 1 Homo sapiens 26-30 8347671-6 1993 (3) In fluid-phase PC membranes possessing short alkyl chains (12-14 carbons), the activation energy of the rotational diffusion of 16-doxylstearic acid spin label (16-SASL) is significantly lower at a carotenoid concentration of 10 mol%. Phosphatidylcholines 19-21 spindlin 1 Homo sapiens 153-157 8386549-2 1993 The integrated intensities of the saturation transfer EPR spectra from spin-labelled phosphatidylcholine are linearly dependent on the protein/lipid ratio, and correspond to a fixed stoichiometry of approximately 11 lipids per monomer associated with the protein in the gel phase. Phosphatidylcholines 85-104 spindlin 1 Homo sapiens 71-75 8386549-3 1993 The normalized saturation transfer intensities of spin-labelled phosphatidic acid, on the other hand, display a non-linear dependence on the protein/lipid ratio that can be described well by a selectivity for interaction with the protein in the gel phase with an average association constant relative to phosphatidylcholine of approx. Phosphatidylcholines 304-323 spindlin 1 Homo sapiens 50-54 8457575-5 1993 The maximum fraction of spin-labeled phospholipids translocated to the inner membrane layer was 84% for phosphatidylserine, 65% for phosphatidylethanolamine, 20-40% for phosphatidylcholine, and below 20% for sphingomyelin. Phosphatidylcholines 169-188 spindlin 1 Homo sapiens 24-28 2159807-7 1990 A comparison of the apparent order parameters and polarity profiles of the phosphatidylcholine and fatty acid spin labels indicates that the fatty acid spin labels are intercalated approximately one CH2 unit more deeply in the hydrocarbon region than are the positionally isomeric phosphatidylcholine spin labels. Phosphatidylcholines 75-94 spindlin 1 Homo sapiens 152-156 2159807-7 1990 A comparison of the apparent order parameters and polarity profiles of the phosphatidylcholine and fatty acid spin labels indicates that the fatty acid spin labels are intercalated approximately one CH2 unit more deeply in the hydrocarbon region than are the positionally isomeric phosphatidylcholine spin labels. Phosphatidylcholines 75-94 spindlin 1 Homo sapiens 152-156 2159807-7 1990 A comparison of the apparent order parameters and polarity profiles of the phosphatidylcholine and fatty acid spin labels indicates that the fatty acid spin labels are intercalated approximately one CH2 unit more deeply in the hydrocarbon region than are the positionally isomeric phosphatidylcholine spin labels. Phosphatidylcholines 281-300 spindlin 1 Homo sapiens 110-114 2159807-7 1990 A comparison of the apparent order parameters and polarity profiles of the phosphatidylcholine and fatty acid spin labels indicates that the fatty acid spin labels are intercalated approximately one CH2 unit more deeply in the hydrocarbon region than are the positionally isomeric phosphatidylcholine spin labels. Phosphatidylcholines 281-300 spindlin 1 Homo sapiens 152-156 2159807-7 1990 A comparison of the apparent order parameters and polarity profiles of the phosphatidylcholine and fatty acid spin labels indicates that the fatty acid spin labels are intercalated approximately one CH2 unit more deeply in the hydrocarbon region than are the positionally isomeric phosphatidylcholine spin labels. Phosphatidylcholines 281-300 spindlin 1 Homo sapiens 152-156