PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
25282663-7	2015	Our data clearly demonstrate the preference of alpha-MSH to interact with anionic DMPG containing vesicles leading to significant permeabilization which is the molecular basis behind the selectivity of alpha-MSH for bacterial systems.	dimyristoylphosphatidylglycerol	82-86	proopiomelanocortin	Homo sapiens	47-56
25282663-7	2015	Our data clearly demonstrate the preference of alpha-MSH to interact with anionic DMPG containing vesicles leading to significant permeabilization which is the molecular basis behind the selectivity of alpha-MSH for bacterial systems.	dimyristoylphosphatidylglycerol	82-86	proopiomelanocortin	Homo sapiens	202-211
24299979-2	2014	In present work, we investigated the secondary structure and topology of the peptides associated to Slc11a1-TM2, TM3 and TM4 (wildtype peptides and function-relating mutants) in the phospholipid vesicles (DMPC, DMPG and their mixtures) using circular dichroism, fluorescence spectroscopy and differential scanning calorimetry.	dimyristoylphosphatidylglycerol	211-215	solute carrier family 11 member 1	Homo sapiens	100-107
24299979-6	2014	The E139A substitution of TM3 significantly impairs the pH dependence of the buried depth of TM3 and causes a pronounced increase in helicity in all DMPG-containing lipid vesicles at pH 5.5 and 7 and in DMPC at pH 4.	dimyristoylphosphatidylglycerol	149-153	tropomyosin 3	Homo sapiens	26-29
23033254-4	2012	DMPG-G-MP11-modified glassy carbon electrode (DMPG-G-MP11/GCE) exhibited a pair of well-defined quasi-reversible redox peaks of MP11 and showed high electrocatalytic activity towards hydrogen peroxide (H(2)O(2)).	dimyristoylphosphatidylglycerol	0-4	glycine decarboxylase	Homo sapiens	46-61
20961099-3	2010	Using solid-state nuclear magnetic resonance spectroscopy, we have now determined the conformation, dynamics, oligomeric state, and topology of a human alpha-defensin, HNP-1, in DMPC/DMPG bilayers.	dimyristoylphosphatidylglycerol	183-187	HNP1	Homo sapiens	168-173
21395305-3	2011	The fluorescence experiments reported that the Trp side chain of [Trp8]SP inserts into the hydrophobic core of the SDS micelles and DMPG liposomes but faces the DMPC hydrophilic region, indicating that electrostatic interactions between membrane and SP are essential for the alpha-helical fold.	dimyristoylphosphatidylglycerol	132-136	tachykinin precursor 1	Homo sapiens	71-73
21408153-7	2011	However, inclusion of DMPG instead of DMPC did not significantly alter the CLA of PDC-109, which could be due to the lower specificity of PDC-109 for DMPG as compared to DMPC.	dimyristoylphosphatidylglycerol	150-154	seminal plasma protein PDC-109	Bos taurus	138-145
21600190-1	2011	We studied the conformation of beta2-human glycoprotein (beta2GPI) in solution and bound to the anionic lipids palmitoyl oleoyl phosphatidylglycerol (POPG), dimiristoyl phosphatidylglycerol (DMPG) and dipalmitoyl phosphatidylglycerol (DPPG) as a function of the temperature.	dimyristoylphosphatidylglycerol	191-195	apolipoprotein H	Homo sapiens	31-55
20836507-1	2010	The present work demonstrates the modulation of excited state intramolecular proton transfer (ESIPT) emission of 1-hydroxy-2-naphthaldehyde (HN12) upon its interaction with the liposomal vesicles/bilayer of dimyristoyl-l-alpha-phosphatidylcholine (DMPC) and dimyristoyl-l-alpha-phosphatidylglycerol (DMPG) and its subsequent implementation as an efficient molecular reporter for probing of microheterogeneous environments of lipid-bilayer system.	dimyristoylphosphatidylglycerol	300-304	MT-RNR2 like 12 (pseudogene)	Homo sapiens	141-145
20836507-2	2010	Modifications on the emission profile of HN12 in terms of remarkable emission intensity enhancement coupled with a hypsochromic shift induced by the presence of DMPC and DMPG membranes have been interpreted to be vivid manifestations of the interactions between the two partners.	dimyristoylphosphatidylglycerol	170-174	MT-RNR2 like 12 (pseudogene)	Homo sapiens	41-45
16877761-5	2006	Here, we have demonstrated that PGLa is able to assume such an I-state in a 1:1 mixture with magainin 2 at a peptide-to-lipid ratio as low as 1:100 in dimyristoylphosphatidylcholine/dimyristoylphosphatidylglycerol model membranes.	dimyristoylphosphatidylglycerol	182-213	prepro-PGLa S homeolog	Xenopus laevis	32-36
18068665-5	2008	Using lipid vesicles made of DMPG/DMPC at a molar ratio of 1:1 at 10mg/ml in the presence of different non-muscle myosin II concentrations showed a variation of the main phase transition of the lipid vesicle at around 23 degrees C. With increasing concentrations of non-muscle myosin II the thermotropic properties of the lipid vesicle changed, which is indicative of protein-lipid interaction/insertion.	dimyristoylphosphatidylglycerol	29-33	myosin heavy chain 14	Homo sapiens	114-120
18068665-5	2008	Using lipid vesicles made of DMPG/DMPC at a molar ratio of 1:1 at 10mg/ml in the presence of different non-muscle myosin II concentrations showed a variation of the main phase transition of the lipid vesicle at around 23 degrees C. With increasing concentrations of non-muscle myosin II the thermotropic properties of the lipid vesicle changed, which is indicative of protein-lipid interaction/insertion.	dimyristoylphosphatidylglycerol	29-33	myosin heavy chain 14	Homo sapiens	277-283
20532386-3	2010	Here we present the results of molecular dynamics simulations of PR3 anchored at three different phospholipid bilayers: DMPC, DMPG and an equimolar mixture of DMPC/DMPG.	dimyristoylphosphatidylglycerol	126-130	proteinase 3	Homo sapiens	65-68
20532386-3	2010	Here we present the results of molecular dynamics simulations of PR3 anchored at three different phospholipid bilayers: DMPC, DMPG and an equimolar mixture of DMPC/DMPG.	dimyristoylphosphatidylglycerol	164-168	proteinase 3	Homo sapiens	65-68
16819842-6	2006	Fluorescence quenching together with a Trp emission blue shift showed that the Trp residues remain largely shielded from the solvent when interacting with DMPG, which would be consistent with at least some portions of betaLG having been inserted into the lipid membrane.	dimyristoylphosphatidylglycerol	155-159	beta-lactoglobulin	Bos taurus	218-224
16945585-7	2006	In phospholipid vesicle solubilization assays, LA apoE3-NT was more effective than WT apoE3-NT at inducing a time-dependent decrease in dimyristoylphosphatidylglycerol vesicle light scattering intensity.	dimyristoylphosphatidylglycerol	136-167	apolipoprotein E	Homo sapiens	50-55
16945585-7	2006	In phospholipid vesicle solubilization assays, LA apoE3-NT was more effective than WT apoE3-NT at inducing a time-dependent decrease in dimyristoylphosphatidylglycerol vesicle light scattering intensity.	dimyristoylphosphatidylglycerol	136-167	apolipoprotein E	Homo sapiens	86-91
16420479-8	2006	In phospholipid vesicle solubilization assays, HT apoE3-NT was more effective than wild-type apoE3-NT at inducing a time dependent decrease in dimyristoylphosphatidylglycerol vesicle light scattering intensity.	dimyristoylphosphatidylglycerol	143-174	apolipoprotein E	Homo sapiens	50-55
16420479-8	2006	In phospholipid vesicle solubilization assays, HT apoE3-NT was more effective than wild-type apoE3-NT at inducing a time dependent decrease in dimyristoylphosphatidylglycerol vesicle light scattering intensity.	dimyristoylphosphatidylglycerol	143-174	apolipoprotein E	Homo sapiens	93-98
11470084-0	2001	Spin-label electron paramagnetic resonance studies on the interaction of avidin with dimyristoyl-phosphatidylglycerol membranes.	dimyristoylphosphatidylglycerol	85-117	spindlin 1	Homo sapiens	0-4
12646385-8	2003	The results revealed that apoE2-NT was the most stable, followed by apoE3-NT and apoE4-NT, establishing an inverse correlation between helix bundle stability and DMPG vesicle transformation rate at pH 7.	dimyristoylphosphatidylglycerol	162-166	apolipoprotein E	Homo sapiens	26-31
12646385-8	2003	The results revealed that apoE2-NT was the most stable, followed by apoE3-NT and apoE4-NT, establishing an inverse correlation between helix bundle stability and DMPG vesicle transformation rate at pH 7.	dimyristoylphosphatidylglycerol	162-166	apolipoprotein E	Homo sapiens	81-86
12368478-3	2002	In anionic membranes of dimyristoylphosphatidylglycerol and dimyristoylphosphatidylserine, both HSP17 and alpha-crystallin strongly stabilize the liquid-crystalline state.	dimyristoylphosphatidylglycerol	24-55	heat shock protein family B (small) member 3	Homo sapiens	96-101
15747405-0	2004	Cytochrome c-dimyristoylphosphatidylglycerol interactions studied by asymmetrical flow field-flow fractionation.	dimyristoylphosphatidylglycerol	13-44	cytochrome c, somatic	Homo sapiens	0-12
15747405-3	2004	In this study, asymmetrical flow field-flow fractionation (AsFlFFF) was used to compare the interactions of cyt c with the acidic phospholipid 1,2-dimyristoyl-sn-glycero-3-phospho-rac-glycerol (DMPG), oleic acid (OA), and sodium dodecyl sulfate (SDS).	dimyristoylphosphatidylglycerol	194-198	cytochrome c, somatic	Homo sapiens	108-113
15747405-7	2004	AsFlFFF revealed the binding of cyt c to DMPG and to OA to be mainly electrostatic.	dimyristoylphosphatidylglycerol	41-45	cytochrome c, somatic	Homo sapiens	32-37
15041697-4	2004	However, doping the dimyristoyl/dihexanoyl system with both Ca2+ and DMPG resulted in ULVs whose <Ro> was found to be Clp dependent.	dimyristoylphosphatidylglycerol	69-73	calmodulin like 3	Homo sapiens	124-127
12719234-6	2003	The dissociation rate constant (k(-1)) for the DMPC/PDC-109 system was found to be 2.7 x 10(-2) s(-1) whereas the k(-1) values obtained with DMPG and DMPA was about three to four times higher.	dimyristoylphosphatidylglycerol	141-145	seminal plasma protein PDC-109	Bos taurus	52-59
12719234-11	2003	Analysis of the activation parameters indicates that the interaction of PDC-109 with DMPC membranes is favored by a strong entropic contribution, whereas negative entropic contribution is primarily responsible for the rather weak interaction of this protein with DMPA and DMPG.	dimyristoylphosphatidylglycerol	272-276	seminal plasma protein PDC-109	Bos taurus	72-79
12646385-5	2003	By contrast, differences were noted in apoE-NT isoform-specific transformation of bilayer vesicles of dimyristoylphosphatidylglycerol (DMPG) into discoidal complexes.	dimyristoylphosphatidylglycerol	102-133	apolipoprotein E	Homo sapiens	39-43
12646385-5	2003	By contrast, differences were noted in apoE-NT isoform-specific transformation of bilayer vesicles of dimyristoylphosphatidylglycerol (DMPG) into discoidal complexes.	dimyristoylphosphatidylglycerol	135-139	apolipoprotein E	Homo sapiens	39-43
12646385-7	2003	To determine if differences in the rate of apoE-NT induced DMPG vesicle transformation is due to isoform-specific differences in helix bundle stability, guanidine HCl denaturation studies were conducted.	dimyristoylphosphatidylglycerol	59-63	apolipoprotein E	Homo sapiens	43-47
15080496-5	2002	INF-alpha was encapsulated in different liposomal formulations, Dimyristoylphosphatidylcholine (DMPC), Dioleyl-phosphatidyl-ethanolamine/Dimyristoylphosphatidylcholine (DOPE/DMPC) and DOPE/Dimyristoylphosphatidylglycerol (DOPE/DMPG).	dimyristoylphosphatidylglycerol	227-231	interferon alpha 17	Homo sapiens	0-9
11470084-1	2001	The interaction of avidin--a basic protein from hen egg-white--with dimyristoyl-phosphatidylglycerol membranes was investigated by spin-label electron paramagnetic resonance spectroscopy.	dimyristoylphosphatidylglycerol	68-100	spindlin 1	Homo sapiens	131-135
11423415-0	2001	Two-dimensional infrared correlation spectroscopy study of the aggregation of cytochrome c in the presence of dimyristoylphosphatidylglycerol.	dimyristoylphosphatidylglycerol	110-141	cytochrome c, somatic	Homo sapiens	78-90
11423415-1	2001	Two-dimensional infrared correlation spectroscopy (2D-IR) was used in this study to investigate the aggregation of cytochrome c in the presence of dimyristoylphosphatidylglycerol.	dimyristoylphosphatidylglycerol	147-178	cytochrome c, somatic	Homo sapiens	115-127
10103046-6	1999	In calorimetric assays, using lipid vesicles of mixed DMPC/DMPG, increasing PR3 concentrations (protein/lipid molar ratio from 0 to 1 : 110) induced a significant decrease of the main chain transition enthalpy and a shift in chain melting temperatures which is indicative of partial insertion of PR3 into the hydrophobic region of the lipid membranes.	dimyristoylphosphatidylglycerol	59-63	proteinase 3	Homo sapiens	76-79
10986285-6	2000	ApoE3-(126-183) efficiently transforms dimyristoylphosphatidylglycerol (DMPG) vesicles into peptide-lipid complexes.	dimyristoylphosphatidylglycerol	39-70	apolipoprotein E	Homo sapiens	0-5
10986285-6	2000	ApoE3-(126-183) efficiently transforms dimyristoylphosphatidylglycerol (DMPG) vesicles into peptide-lipid complexes.	dimyristoylphosphatidylglycerol	72-76	apolipoprotein E	Homo sapiens	0-5
10986285-10	2000	Far UV CD analysis of apoE3-(126-183).DMPG discs provided evidence that the peptide adopts a helical conformation.	dimyristoylphosphatidylglycerol	38-42	apolipoprotein E	Homo sapiens	22-27
10986285-11	2000	Competition binding experiments with (125)I-labeled low density lipoprotein (LDL) were conducted to assess the ability of apoE3-(126-183).DMPG complexes to bind to the LDL receptor.	dimyristoylphosphatidylglycerol	138-142	apolipoprotein E	Homo sapiens	122-127
10986285-11	2000	Competition binding experiments with (125)I-labeled low density lipoprotein (LDL) were conducted to assess the ability of apoE3-(126-183).DMPG complexes to bind to the LDL receptor.	dimyristoylphosphatidylglycerol	138-142	low density lipoprotein receptor	Homo sapiens	168-180
10986285-12	2000	Both N-terminal apoE and the peptide, when complexed with DMPG, competed with (125)I-LDL for binding sites on the surface of cultured human skin fibroblasts.	dimyristoylphosphatidylglycerol	58-62	apolipoprotein E	Homo sapiens	16-20
11099172-1	2000	The cationic tridecapeptide alpha-melanocyte stimulating hormone (alpha-MSH) is known to interact with anionic vesicles of 1,2-dimyristoyl-sn-glycero-3-phosphoglycerol (DMPG), partially penetrating the lipid membrane.	dimyristoylphosphatidylglycerol	169-173	proopiomelanocortin	Homo sapiens	28-64
11099172-1	2000	The cationic tridecapeptide alpha-melanocyte stimulating hormone (alpha-MSH) is known to interact with anionic vesicles of 1,2-dimyristoyl-sn-glycero-3-phosphoglycerol (DMPG), partially penetrating the lipid membrane.	dimyristoylphosphatidylglycerol	169-173	proopiomelanocortin	Homo sapiens	66-75
10794719-3	2000	Here we study the membrane-induced conformational change of Apo H by CD spectroscopy with two different model systems: anionic-phospholipid-containing liposomes [such as 1, 2-dimyristoyl-sn-glycero-3-phosphoglycerol (DMPG) and cardiolipin], and the water/methanol mixtures at moderately low pH, which mimic the micro-physicochemical environment near the membrane surface.	dimyristoylphosphatidylglycerol	217-221	apolipoprotein H	Homo sapiens	60-65
10413525-3	1999	The observed blue shift upon addition of DMPG vesicles indicated that the tryptophan residues of ApoH moved from a polar to a nonpolar environment.	dimyristoylphosphatidylglycerol	41-45	apolipoprotein H	Homo sapiens	97-101
10413525-4	1999	The insertion ability of ApoH into PG-containing vesicles did not depend on the PG content in a stoichiometric way as did the blue shift, indicating that the negatively charged DMPG does not serve as a specific binding site but rather provides a suitable microenvironment for ApoH interaction.	dimyristoylphosphatidylglycerol	177-181	apolipoprotein H	Homo sapiens	25-29
10413525-4	1999	The insertion ability of ApoH into PG-containing vesicles did not depend on the PG content in a stoichiometric way as did the blue shift, indicating that the negatively charged DMPG does not serve as a specific binding site but rather provides a suitable microenvironment for ApoH interaction.	dimyristoylphosphatidylglycerol	177-181	apolipoprotein H	Homo sapiens	276-280
10103046-8	1999	The molar affinity of PR3, HNE, and MPO to lipid vesicles of different DMPC/DMPG ratios was then determined by spectrophotometry.	dimyristoylphosphatidylglycerol	76-80	proteinase 3	Homo sapiens	22-25
10103046-9	1999	At a DMPC/DMPG ratio of 1 : 1, molar affinities of PR3, Kd = 4.5 +/- 0.3 microm; HNE, 14.5 +/- 1.2 microm; and MPO, 50 +/- 5 microm (n = 3) were estimated.	dimyristoylphosphatidylglycerol	10-14	proteinase 3	Homo sapiens	51-54
10103046-9	1999	At a DMPC/DMPG ratio of 1 : 1, molar affinities of PR3, Kd = 4.5 +/- 0.3 microm; HNE, 14.5 +/- 1.2 microm; and MPO, 50 +/- 5 microm (n = 3) were estimated.	dimyristoylphosphatidylglycerol	10-14	elastase, neutrophil expressed	Homo sapiens	81-84
9708994-1	1998	Cytochrome c oxidase isolated from beef heart mitochondria was reconstituted in bilayer membranes of the anionic lipid dimyristoylphosphatidylglycerol (DMPG) with varying enzyme/DMPG ratio.	dimyristoylphosphatidylglycerol	119-150	cytochrome c, somatic	Homo sapiens	0-12
9708994-1	1998	Cytochrome c oxidase isolated from beef heart mitochondria was reconstituted in bilayer membranes of the anionic lipid dimyristoylphosphatidylglycerol (DMPG) with varying enzyme/DMPG ratio.	dimyristoylphosphatidylglycerol	152-156	cytochrome c, somatic	Homo sapiens	0-12
9708994-1	1998	Cytochrome c oxidase isolated from beef heart mitochondria was reconstituted in bilayer membranes of the anionic lipid dimyristoylphosphatidylglycerol (DMPG) with varying enzyme/DMPG ratio.	dimyristoylphosphatidylglycerol	178-182	cytochrome c, somatic	Homo sapiens	0-12
9733956-9	1998	Involvement of electrostatic attraction between the acidic phosphate of DMPG and cationic residues in apoB is suggested by the finding that increasing the content of dimyristoylphosphatidylcholine (DMPC) in DMPG liposomes reduced their aggregation and at XDMPC=0.50 no response was evident.	dimyristoylphosphatidylglycerol	72-76	apolipoprotein B	Homo sapiens	102-106
9733956-9	1998	Involvement of electrostatic attraction between the acidic phosphate of DMPG and cationic residues in apoB is suggested by the finding that increasing the content of dimyristoylphosphatidylcholine (DMPC) in DMPG liposomes reduced their aggregation and at XDMPC=0.50 no response was evident.	dimyristoylphosphatidylglycerol	207-211	apolipoprotein B	Homo sapiens	102-106
9548943-5	1998	However, upon the insertion of the negatively charged lipid DMPG at 1:1 molar ratio into the DMPC bilayers, myosin was found to interact electrostatically with the liposomes, thereby affecting significantly both the quadrupole splittings and spin-lattice relaxation rates of the alpha-, beta-, and gamma-deuterons in labeled DMPC.	dimyristoylphosphatidylglycerol	60-64	myosin heavy chain 14	Homo sapiens	108-114
9708994-6	1998	However, the motionally restricted lipid population associated with reconstituted cytochrome c oxidase/DMPG membranes increased on binding cytochrome c, indicating structural/dynamic changes taking place in the membrane.	dimyristoylphosphatidylglycerol	103-107	cytochrome c, somatic	Homo sapiens	82-94
9708994-6	1998	However, the motionally restricted lipid population associated with reconstituted cytochrome c oxidase/DMPG membranes increased on binding cytochrome c, indicating structural/dynamic changes taking place in the membrane.	dimyristoylphosphatidylglycerol	103-107	cytochrome c, somatic	Homo sapiens	139-151
9708994-7	1998	Depending on the DMPG/cytochrome c oxidase ratio, apparent stoichiometries of up to 115 motionally restricted lipid molecules/cytochrome c oxidase monomer were found, when saturating amounts of cytochrome c were bound.	dimyristoylphosphatidylglycerol	17-21	cytochrome c, somatic	Homo sapiens	126-138
9708994-7	1998	Depending on the DMPG/cytochrome c oxidase ratio, apparent stoichiometries of up to 115 motionally restricted lipid molecules/cytochrome c oxidase monomer were found, when saturating amounts of cytochrome c were bound.	dimyristoylphosphatidylglycerol	17-21	cytochrome c, somatic	Homo sapiens	126-138
9708994-8	1998	Under these conditions, cytochrome c binds to approximately 9 negatively charged DMPG molecules, independent of the cytochrome c oxidase content in the reconstituted system.	dimyristoylphosphatidylglycerol	81-85	cytochrome c, somatic	Homo sapiens	24-36
9548943-6	1998	Monitoring DMPG-d5 in mixed DMPC/DMPG bilayers revealed a direct electrostatic interaction of DMPG with the protein, where positively charged lysine residues located at the tail domain of myosin provide the necessary sites for the interaction to occur.	dimyristoylphosphatidylglycerol	11-15	myosin heavy chain 14	Homo sapiens	188-194
9548943-6	1998	Monitoring DMPG-d5 in mixed DMPC/DMPG bilayers revealed a direct electrostatic interaction of DMPG with the protein, where positively charged lysine residues located at the tail domain of myosin provide the necessary sites for the interaction to occur.	dimyristoylphosphatidylglycerol	33-37	myosin heavy chain 14	Homo sapiens	188-194
9548943-6	1998	Monitoring DMPG-d5 in mixed DMPC/DMPG bilayers revealed a direct electrostatic interaction of DMPG with the protein, where positively charged lysine residues located at the tail domain of myosin provide the necessary sites for the interaction to occur.	dimyristoylphosphatidylglycerol	33-37	myosin heavy chain 14	Homo sapiens	188-194
9370448-6	1997	Surface binding of the basic lysine peptides strongly reduced the interfacial pK of spin-labeled fatty acid incorporated into the DMPG bilayers, to a greater extent for polylysine than for tetralysine or pentalysine at saturation.	dimyristoylphosphatidylglycerol	130-134	spindlin 1	Homo sapiens	84-88
12232625-4	1996	The induction intensity of different kinds of lipids on colicin E(1) was in the following order: DMPG>DMPE>DMPC.	dimyristoylphosphatidylglycerol	97-101	small nucleolar RNA, H/ACA box 73A	Homo sapiens	64-68
8968592-9	1996	The miscibility in DMPG/DPPC and DMPA/DPPC mixtures differs remarkably because, for DMPG/DPPC, delta rho = rho l -rho g is negative, whereas for DMPA/DPPC this difference is positive.	dimyristoylphosphatidylglycerol	19-23	ras homolog family member G	Homo sapiens	114-119
8968592-9	1996	The miscibility in DMPG/DPPC and DMPA/DPPC mixtures differs remarkably because, for DMPG/DPPC, delta rho = rho l -rho g is negative, whereas for DMPA/DPPC this difference is positive.	dimyristoylphosphatidylglycerol	84-88	ras homolog family member G	Homo sapiens	114-119
8794774-5	1996	Isothermal titration calorimetry of the interaction between DMPG and rhG-CSF indicates that the binding is saturable and involves 10 lipids/rhG-CSF.	dimyristoylphosphatidylglycerol	60-64	colony stimulating factor 2	Homo sapiens	73-76
8794774-5	1996	Isothermal titration calorimetry of the interaction between DMPG and rhG-CSF indicates that the binding is saturable and involves 10 lipids/rhG-CSF.	dimyristoylphosphatidylglycerol	60-64	colony stimulating factor 2	Homo sapiens	144-147
9384676-7	1995	MLVs composed of DMPC/DMPG (7:3) and SUVs composed of DPPC/DSPC (1:1) displayed high capacity for binding to caprylated TNF-SAM2.	dimyristoylphosphatidylglycerol	22-26	tumor necrosis factor	Homo sapiens	120-123
7548075-3	1995	The ESR spectra of phosphatidylglycerol spin-labeled at position 5 of the sn-2 chain indicate that association of alpha-lactalbumin with dimyristoyl phosphatidylglycerol bilayers increases the chain mobility at temperatures in the lipid gel phase, restricts the chain mobility at temperatures corresponding to the lipid fluid phase, and abolishes the cooperative lipid chain-melting transition.	dimyristoylphosphatidylglycerol	137-169	lactalbumin alpha	Homo sapiens	114-131
8068622-0	1994	Thermotropic behavior of dimyristoylphosphatidylglycerol and its interaction with cytochrome c.	dimyristoylphosphatidylglycerol	25-56	cytochrome c, somatic	Homo sapiens	82-94
7918481-1	1994	The interaction of the actin-binding protein filamin with mixtures of zwitterionic and anionic phospholipids (DMPC, DMPG, PC, PS) was studied in reconstituted lipid monolayers and bilayers.	dimyristoylphosphatidylglycerol	116-120	filamin C	Homo sapiens	45-52
7918481-5	1994	Mixed DMPC/DMPG LUVETs showed a linear decrease of the main phase transition enthalpy and a significant shift in temperature for the solidus and liquidus lines with increasing mole fractions of reconstituted filamin.	dimyristoylphosphatidylglycerol	11-15	filamin C	Homo sapiens	208-215
8068622-1	1994	The thermotropic behavior of dimyristoylphosphatidylglycerol (DMPG) in the absence and presence of cytochrome c under low-salt conditions has been investigated using differential scanning calorimetry (DSC), 31P nuclear magnetic resonance (31P NMR), electron spin resonance (ESR), viscosity, light scattering, and electron microscopy.	dimyristoylphosphatidylglycerol	62-66	cytochrome c, somatic	Homo sapiens	99-111
8068622-15	1994	Calorimetric titration studies of the binding of cytochrome c to DMPG indicate that protein binding is coupled cooperatively to changes in the state of the lipid.	dimyristoylphosphatidylglycerol	65-69	cytochrome c, somatic	Homo sapiens	49-61
2223804-7	1990	In mixtures of DMPG and DPPC, the selectivity of PLP for the acidic phospholipid DMPG was maintained, but was lower than that observed for L-alpha-PS.	dimyristoylphosphatidylglycerol	15-19	proteolipid protein 1	Homo sapiens	49-52
8373787-11	1993	NMR relaxation time measurements in the headgroup and chain region of DMPG and DMPC suggest that the lateral diffusion coefficient of the acidic lipid decreases significantly due to the coupling with MBP while the zwitterionic DMPC is not affected.	dimyristoylphosphatidylglycerol	70-74	myelin basic protein	Homo sapiens	200-203
1654089-3	1991	The gel-to-fluid-phase transition of dimyristoylphosphatidylglycerol induces shifts in the conformational and coordination equilibria of the bound cytochrome c, as recorded by the resonance Raman spectra in the fingerprint and marker band regions.	dimyristoylphosphatidylglycerol	37-68	cytochrome c, somatic	Homo sapiens	147-159
7690591-1	1993	The interaction of two complementary fragments of myelin basic protein from bovine spinal cord with bilayers of dimyristoylphosphatidylglycerol has been studied by broad line 2H and 31P NMR.	dimyristoylphosphatidylglycerol	112-143	myelin basic protein	Bos taurus	50-70
1798016-1	1991	It was found that DMPG liposomes are capable of binding a much higher amount of CsA than those prepared from DMPC.	dimyristoylphosphatidylglycerol	18-22	ERCC excision repair 8, CSA ubiquitin ligase complex subunit	Homo sapiens	80-83
1798016-2	1991	Furthermore, while CsA associated with DMPG was embedded within the hydrophobic region of phospholipids, CsA associated with DMPC was excluded from the hydrophobic region and was entrapped in the hydrophilic region of these liposomes.	dimyristoylphosphatidylglycerol	39-43	ERCC excision repair 8, CSA ubiquitin ligase complex subunit	Homo sapiens	19-22
1941434-5	1991	When liposomes were prepared from pure dimyristoylphosphatidylglycerol (DMPG), 30.7 mol of DMPG were required to bind 1 mol of CsA.	dimyristoylphosphatidylglycerol	39-70	ERCC excision repair 8, CSA ubiquitin ligase complex subunit	Homo sapiens	127-130
1941434-5	1991	When liposomes were prepared from pure dimyristoylphosphatidylglycerol (DMPG), 30.7 mol of DMPG were required to bind 1 mol of CsA.	dimyristoylphosphatidylglycerol	72-76	ERCC excision repair 8, CSA ubiquitin ligase complex subunit	Homo sapiens	127-130
1941434-5	1991	When liposomes were prepared from pure dimyristoylphosphatidylglycerol (DMPG), 30.7 mol of DMPG were required to bind 1 mol of CsA.	dimyristoylphosphatidylglycerol	91-95	ERCC excision repair 8, CSA ubiquitin ligase complex subunit	Homo sapiens	127-130
1941434-7	1991	In DMPG liposomes, CsA was found in hydrocarbon chains adjacent to the polar head group, while in liposomes prepared from phosphatidylglycerol containing mixed fatty acids, CsA was associated with the polar head group region without penetrating the hydrocarbon chains of phosphatidylglycerol.	dimyristoylphosphatidylglycerol	3-7	ERCC excision repair 8, CSA ubiquitin ligase complex subunit	Homo sapiens	19-22
1710494-4	1991	Electron spin resonance (ESR) spectra of phosphatidylglycerol spin-labeled at position n = 5 in the sn-2 chain showed that complexation of MBP with the PLP-DMPG recombinants leads to a decrease in lipid chain mobility to an extent which correlates with the degree of MBP binding.	dimyristoylphosphatidylglycerol	156-160	myelin basic protein	Bos taurus	139-142
1710494-4	1991	Electron spin resonance (ESR) spectra of phosphatidylglycerol spin-labeled at position n = 5 in the sn-2 chain showed that complexation of MBP with the PLP-DMPG recombinants leads to a decrease in lipid chain mobility to an extent which correlates with the degree of MBP binding.	dimyristoylphosphatidylglycerol	156-160	proteolipid protein 1	Bos taurus	152-155
1710494-4	1991	Electron spin resonance (ESR) spectra of phosphatidylglycerol spin-labeled at position n = 5 in the sn-2 chain showed that complexation of MBP with the PLP-DMPG recombinants leads to a decrease in lipid chain mobility to an extent which correlates with the degree of MBP binding.	dimyristoylphosphatidylglycerol	156-160	myelin basic protein	Bos taurus	267-270
1710494-5	1991	At low DMPG:PLP ratios, the perturbations of lipid mobility by both proteins are mutually enhanced.	dimyristoylphosphatidylglycerol	7-11	proteolipid protein 1	Bos taurus	12-15
1710494-6	1991	In single recombinants of PLP with DMPG, the ESR spectra of phosphatidylglycerol spin-labeled at position n = 14 in the sn-2 chain indicated that approximately 10 lipids/protein are motionally restricted by direct contact with the intramembranous surface of the protein.	dimyristoylphosphatidylglycerol	35-39	proteolipid protein 1	Bos taurus	26-29
1710494-7	1991	This number is in agreement with earlier results for reconstitutions of PLP in dimyristoylphosphatidylcholine (DMPC) [Brophy, P. J., Horvath, L. I., & Marsh, D. (1984) Biochemistry 23, 860-865] and is consistent with a hexameric arrangement of the PLP molecules in DMPG bilayers.	dimyristoylphosphatidylglycerol	269-273	proteolipid protein 1	Bos taurus	72-75
2123484-0	1990	Thermodynamics of the binding of human apolipoprotein A-I to dimyristoylphosphatidylglycerol.	dimyristoylphosphatidylglycerol	61-92	apolipoprotein A1	Homo sapiens	39-57
2123484-1	1990	The interaction of human serum apolipoprotein A-I with dimyristoylphosphatidylglycerol was analyzed by isothermal titration calorimetry.	dimyristoylphosphatidylglycerol	55-86	apolipoprotein A1	Homo sapiens	31-49
2123484-2	1990	Binding of the apolipoprotein A-I to large unilamellar vesicles of dimyristoylphosphatidylglycerol, a negatively charged phospholipid, is characterized by thermodynamic parameters which are invariant over the 30-40 degrees C temperature range.	dimyristoylphosphatidylglycerol	67-98	apolipoprotein A1	Homo sapiens	15-33
2123484-10	1990	The binding isotherms for the high affinity binding of the apolipoprotein A-I to large unilammelar vesicles of dimyristoylphosphatidylglycerol, over the temperature range 30-40 degrees C, gave an enthalpy change of 1.43 +/- 0.07 kcal/mol of protein and a free energy change of -5.91 +/- 0.04 kcal/mol of protein for the binding of the protein to a cluster of 25 +/- 2 lipid molecules.	dimyristoylphosphatidylglycerol	111-142	apolipoprotein A1	Homo sapiens	59-77
2223804-7	1990	In mixtures of DMPG and DPPC, the selectivity of PLP for the acidic phospholipid DMPG was maintained, but was lower than that observed for L-alpha-PS.	dimyristoylphosphatidylglycerol	81-85	proteolipid protein 1	Homo sapiens	49-52
2162758-1	1990	Resonance Raman spectra have been recorded from ferri-cytochrome c bound to phospholipid vesicles composed of dimyristoyl phosphatidylglycerol (DMPG), dioleoyl phosphatidylglycerol (DOPG) or dioleoyl phosphatidylglycerol-dioleoyl phosphatidylcholine (DOPG-DOPC) (70:30 mole/mole).	dimyristoylphosphatidylglycerol	110-142	cytochrome c, somatic	Homo sapiens	54-66
2252889-2	1990	We studied the interaction of transferrin receptors (of cell line Molt-4) with mixed model membranes as a function of lipid chain length (phospholipids with C14:0 and C18:1 hydrocarbon chains) and of the surface charge of the membrane using mixtures of C14:0 lecithin (DMPC) with C14:0 phosphatidylglycerol (DMPG) and C14:0 phosphatidylserine (DMPS).	dimyristoylphosphatidylglycerol	308-312	transferrin	Homo sapiens	30-41
1710494-0	1991	Lipid-protein and protein-protein interactions in double recombinants of myelin proteolipid apoprotein and myelin basic protein with dimyristoylphosphatidylglycerol.	dimyristoylphosphatidylglycerol	133-164	myelin basic protein	Bos taurus	107-127
1710494-1	1991	The integral proteolipid apoprotein (PLP) from bovine spinal cord has been reconstituted in dimyristoylphosphatidylglycerol (DMPG) bilayers, and the mutual interactions on binding the peripheral myelin basic protein (MBP) have been studied.	dimyristoylphosphatidylglycerol	92-123	proteolipid protein 1	Bos taurus	37-40
1710494-1	1991	The integral proteolipid apoprotein (PLP) from bovine spinal cord has been reconstituted in dimyristoylphosphatidylglycerol (DMPG) bilayers, and the mutual interactions on binding the peripheral myelin basic protein (MBP) have been studied.	dimyristoylphosphatidylglycerol	125-129	proteolipid protein 1	Bos taurus	37-40
1710494-2	1991	Quantitation of protein and lipid contents in the MBP-PLP-DMPG double recombinants at different PLP:DMPG ratios led to the conclusion that MBP binds only to the DMPG lipid headgroups and is hindered from interaction with the first shell of lipids surrounding the PLP.	dimyristoylphosphatidylglycerol	58-62	proteolipid protein 1	Bos taurus	54-57
1710494-2	1991	Quantitation of protein and lipid contents in the MBP-PLP-DMPG double recombinants at different PLP:DMPG ratios led to the conclusion that MBP binds only to the DMPG lipid headgroups and is hindered from interaction with the first shell of lipids surrounding the PLP.	dimyristoylphosphatidylglycerol	58-62	myelin basic protein	Bos taurus	139-142
1710494-2	1991	Quantitation of protein and lipid contents in the MBP-PLP-DMPG double recombinants at different PLP:DMPG ratios led to the conclusion that MBP binds only to the DMPG lipid headgroups and is hindered from interaction with the first shell of lipids surrounding the PLP.	dimyristoylphosphatidylglycerol	100-104	myelin basic protein	Bos taurus	139-142
1710494-2	1991	Quantitation of protein and lipid contents in the MBP-PLP-DMPG double recombinants at different PLP:DMPG ratios led to the conclusion that MBP binds only to the DMPG lipid headgroups and is hindered from interaction with the first shell of lipids surrounding the PLP.	dimyristoylphosphatidylglycerol	100-104	myelin basic protein	Bos taurus	139-142
2475162-3	1989	When the spin-labeled MBP was reacted with lipid vesicles consisting of DSPG, DPPG, and DMPG, most of the spin-label was motionally restricted in the gel phase, with a correlation time greater than 10(-8)s. The motion increased with increasing temperature and was sensitive to the lipid phase transition.	dimyristoylphosphatidylglycerol	88-92	myelin basic protein	Homo sapiens	22-25
34547703-2	2021	We studied the aggregates formed by beta2GPI with the anionic phospholipids palmitoyloleoylphosphatidyl glycerol, dimyristoylphosphatidyl glycerol, dipalmitoylphosphatidyl glycerol and cardiolipin using small angle X-ray scattering.	dimyristoylphosphatidylglycerol	114-146	apolipoprotein H	Homo sapiens	36-44
35616927-5	2022	alpha-Synuclein did not interact with zwitterionic 1,2-dimyristoyl-sn-glycero-3-phosphocholine lipids but interacted strongly with anionic 1,2-dimyristoyl-sn-glycero-3-phospho(1"-rac-glycerol) lipids, eventually leading to membrane disruption.	dimyristoylphosphatidylglycerol	139-191	synuclein alpha	Homo sapiens	0-15
2482075-0	1989	Spin-label ESR studies on the interaction of bovine spinal cord myelin basic protein with dimyristoylphosphatidylglycerol dispersions.	dimyristoylphosphatidylglycerol	90-121	myelin basic protein	Bos taurus	64-84
2482075-1	1989	Electron spin resonance (ESR) spectroscopy and chemical binding assays were used to study the interaction of bovine spinal cord myelin basic protein (MBP) with dimyristoylphosphatidylglycerol (DMPG) membranes.	dimyristoylphosphatidylglycerol	160-191	myelin basic protein	Bos taurus	128-148
2482075-1	1989	Electron spin resonance (ESR) spectroscopy and chemical binding assays were used to study the interaction of bovine spinal cord myelin basic protein (MBP) with dimyristoylphosphatidylglycerol (DMPG) membranes.	dimyristoylphosphatidylglycerol	160-191	myelin basic protein	Bos taurus	150-153
2482075-1	1989	Electron spin resonance (ESR) spectroscopy and chemical binding assays were used to study the interaction of bovine spinal cord myelin basic protein (MBP) with dimyristoylphosphatidylglycerol (DMPG) membranes.	dimyristoylphosphatidylglycerol	193-197	myelin basic protein	Bos taurus	128-148
2482075-1	1989	Electron spin resonance (ESR) spectroscopy and chemical binding assays were used to study the interaction of bovine spinal cord myelin basic protein (MBP) with dimyristoylphosphatidylglycerol (DMPG) membranes.	dimyristoylphosphatidylglycerol	193-197	myelin basic protein	Bos taurus	150-153
2482075-2	1989	Increasing binding of MBP to DMPG bilayers resulted in an increasing motional restriction of PG spin-labeled at the C-5 atom position in the acyl chain, up to a maximum degree of association of 1 MBP molecule per 36 lipid molecules.	dimyristoylphosphatidylglycerol	29-33	myelin basic protein	Bos taurus	22-25
2482075-2	1989	Increasing binding of MBP to DMPG bilayers resulted in an increasing motional restriction of PG spin-labeled at the C-5 atom position in the acyl chain, up to a maximum degree of association of 1 MBP molecule per 36 lipid molecules.	dimyristoylphosphatidylglycerol	29-33	myelin basic protein	Bos taurus	196-199
2482076-4	1989	The saturation binding stoichiometries of the two fragments were found to sum to that of the MBP, having values of 11, 24, and 36 mol of DMPG/mol of protein for F2, F1, and the MBP, respectively.	dimyristoylphosphatidylglycerol	137-141	myelin basic protein	Bos taurus	93-96
2482077-1	1989	The selectivity of interaction between bovine spinal cord myelin basic protein (MBP) and eight different spin-labeled lipid species in complexes with dimyristoylphosphatidylglycerol (DMPG) and between spin-labeled phosphatidylglycerol and spin-labeled phosphatidylcholine in complexes of MBP with various mixtures of DMPG and dimyristoylphosphatidylcholine (DMPC) has been studied by electron spin resonance (ESR) spectroscopy.	dimyristoylphosphatidylglycerol	150-181	myelin basic protein	Bos taurus	58-78
2482077-1	1989	The selectivity of interaction between bovine spinal cord myelin basic protein (MBP) and eight different spin-labeled lipid species in complexes with dimyristoylphosphatidylglycerol (DMPG) and between spin-labeled phosphatidylglycerol and spin-labeled phosphatidylcholine in complexes of MBP with various mixtures of DMPG and dimyristoylphosphatidylcholine (DMPC) has been studied by electron spin resonance (ESR) spectroscopy.	dimyristoylphosphatidylglycerol	150-181	myelin basic protein	Bos taurus	80-83
2482077-1	1989	The selectivity of interaction between bovine spinal cord myelin basic protein (MBP) and eight different spin-labeled lipid species in complexes with dimyristoylphosphatidylglycerol (DMPG) and between spin-labeled phosphatidylglycerol and spin-labeled phosphatidylcholine in complexes of MBP with various mixtures of DMPG and dimyristoylphosphatidylcholine (DMPC) has been studied by electron spin resonance (ESR) spectroscopy.	dimyristoylphosphatidylglycerol	183-187	myelin basic protein	Bos taurus	58-78
2482077-1	1989	The selectivity of interaction between bovine spinal cord myelin basic protein (MBP) and eight different spin-labeled lipid species in complexes with dimyristoylphosphatidylglycerol (DMPG) and between spin-labeled phosphatidylglycerol and spin-labeled phosphatidylcholine in complexes of MBP with various mixtures of DMPG and dimyristoylphosphatidylcholine (DMPC) has been studied by electron spin resonance (ESR) spectroscopy.	dimyristoylphosphatidylglycerol	183-187	myelin basic protein	Bos taurus	80-83
3233207-19	1988	In DMPG the sn-1 C = O group seems to be more accessible to water, indicating a different conformation of the glycerol backbone.	dimyristoylphosphatidylglycerol	3-7	solute carrier family 38 member 3	Homo sapiens	12-16
3597388-1	1987	The secondary structure of a hydrophobic myelin protein (lipophilin), reconstituted with dimyristoylphosphatidylcholine or dimyristoylphosphatidylglycerol, was investigated by Fourier-transform infrared spectroscopy.	dimyristoylphosphatidylglycerol	123-154	proteolipid protein 1	Homo sapiens	57-67
2443163-0	1987	Fourier transform infrared spectroscopic investigation of the interaction between myelin basic protein and dimyristoylphosphatidylglycerol bilayers.	dimyristoylphosphatidylglycerol	107-138	myelin basic protein	Homo sapiens	82-102
2443163-3	1987	The association of myelin basic protein with DMPG results in a broadening of the lipid phase transition, accompanied by an increase in the conformational order of the acyl chains at temperatures below the phase transition.	dimyristoylphosphatidylglycerol	45-49	myelin basic protein	Homo sapiens	19-39
33743025-8	2021	This work shows how ATR-FTIR used together with polarized light was successfully used to characterize structurally two CPs (RSKSWPgKQ and RSKSWXC10KQ) in solution and upon interaction with negatively charged membranes of DMPG, assessing the formation and orientation of tubular structures (SCPNs) that were shown to be enhanced by the presence of the lipid membrane.	dimyristoylphosphatidylglycerol	221-225	ATR serine/threonine kinase	Homo sapiens	20-23
1182173-1	1975	Calorimetric experiments showed a marked effect of Ca2+ and Mg2+ on the thermotropic behaviour of dimyristoyl phosphatidylglycerol.	dimyristoylphosphatidylglycerol	98-130	mucin 7, secreted	Homo sapiens	60-63
1182173-8	1975	A Ca2+- and Mg2+-induced shift in the transition temperature and an increase in the enthalpy change was also observed in a 1:1 mixture of dimyristoyl phosphatidylglycerol and dimyristoyl phosphatidylcholine.	dimyristoylphosphatidylglycerol	138-170	mucin 7, secreted	Homo sapiens	12-15
1182173-13	1975	The leak of ions from liposomes of a 1:1 mixture of dimyristoyl phosphatidylglycerol and dimyristoyl phosphatidylcholine in the vicinity of the phase transition temperature was considerably less in the presence of Ca2+ than in the presence of Mg2+.	dimyristoylphosphatidylglycerol	52-84	mucin 7, secreted	Homo sapiens	243-246
1182173-15	1975	It is concluded that there is a correlation between the calorimetric data and the permeability properties of dimyristoyl phosphatidylglycerol-containing bilayers with respect to the influence of Ca2+ and Mg2+.	dimyristoylphosphatidylglycerol	109-141	mucin 7, secreted	Homo sapiens	204-207
3097001-6	1986	This is again in contrast to apo A-I recombinants with DMPG which show no calorimetrically detectable thermal denaturation, at least in a temperature range up to 100 degrees C. Also circular dichroism data indicate high resistance of apo A-I to thermal unfolding in the presence of DMPG.	dimyristoylphosphatidylglycerol	55-59	apolipoprotein A1	Homo sapiens	29-36
3097001-6	1986	This is again in contrast to apo A-I recombinants with DMPG which show no calorimetrically detectable thermal denaturation, at least in a temperature range up to 100 degrees C. Also circular dichroism data indicate high resistance of apo A-I to thermal unfolding in the presence of DMPG.	dimyristoylphosphatidylglycerol	282-286	apolipoprotein A1	Homo sapiens	234-241
3097001-8	1986	In contrast, complexes of apo A-I with DMPG and other acidic phospholipids may be thermodynamically stable over a wide temperature range greater than or equal to Tc.	dimyristoylphosphatidylglycerol	39-43	apolipoprotein A1	Homo sapiens	26-33
3097001-10	1986	Both apo A-I X DMPC and apo A-I X DMPG complexes form lipoprotein particles having a discoidal shape.	dimyristoylphosphatidylglycerol	34-38	apolipoprotein A1	Homo sapiens	24-31
3786805-1	1986	We have previously demonstrated the partial protection of the rat liver by 16,16-dmPGE2 (DMPG) against a number of hepatotoxins including carbon tetrachloride (CCl4).	dimyristoylphosphatidylglycerol	89-93	C-C motif chemokine ligand 4	Rattus norvegicus	160-164
3786805-4	1986	This report details a series of experiments in which the effects of DMPG on CCl4 metabolism was evaluated in the rat.	dimyristoylphosphatidylglycerol	68-72	C-C motif chemokine ligand 4	Rattus norvegicus	76-80
3786805-5	1986	These data indicate that pretreatment with DMPG may reduce the hepatic concentration of the toxic CCl3.	dimyristoylphosphatidylglycerol	43-47	C-C motif chemokine ligand 3	Rattus norvegicus	98-102
3786805-11	1986	We conclude that the rate of CCl4 metabolism may be reduced by pretreatment with DMPG.	dimyristoylphosphatidylglycerol	81-85	C-C motif chemokine ligand 4	Rattus norvegicus	29-33
31048240-8	2019	Our results also show the differential extents of interaction of various CDs (alpha-CD, beta-CD, methyl-beta-CD, and gamma-CD) with DMPG leading to varying degrees of release of the bound-dye molecule.	dimyristoylphosphatidylglycerol	132-136	ACD shelterin complex subunit and telomerase recruitment factor	Homo sapiens	78-86
31048240-8	2019	Our results also show the differential extents of interaction of various CDs (alpha-CD, beta-CD, methyl-beta-CD, and gamma-CD) with DMPG leading to varying degrees of release of the bound-dye molecule.	dimyristoylphosphatidylglycerol	132-136	ACD shelterin complex subunit and telomerase recruitment factor	Homo sapiens	88-95
31048240-8	2019	Our results also show the differential extents of interaction of various CDs (alpha-CD, beta-CD, methyl-beta-CD, and gamma-CD) with DMPG leading to varying degrees of release of the bound-dye molecule.	dimyristoylphosphatidylglycerol	132-136	ACD shelterin complex subunit and telomerase recruitment factor	Homo sapiens	104-111
27503057-3	2016	In this work, we applied an array of neutron scattering methods to study the structure and dynamics of Abeta(1-40) interacting 1,2-dimyristoyl-sn-glycero-3-phosphoglycerol (DMPG) bilayers.	dimyristoylphosphatidylglycerol	173-177	amyloid beta precursor protein	Homo sapiens	103-108
27503057-4	2016	In the structural investigations of lipid bilayer"s response to Abeta binding, Small Angle Neutron Scattering and Neutron Membrane Diffraction revealed that the Abeta anchors firmly to the highly charged DMPG bilayers in the interfacial region between water and hydrocarbon chain, and it doesn"t penetrate deeply into the bilayer.	dimyristoylphosphatidylglycerol	204-208	amyloid beta precursor protein	Homo sapiens	64-69
27503057-4	2016	In the structural investigations of lipid bilayer"s response to Abeta binding, Small Angle Neutron Scattering and Neutron Membrane Diffraction revealed that the Abeta anchors firmly to the highly charged DMPG bilayers in the interfacial region between water and hydrocarbon chain, and it doesn"t penetrate deeply into the bilayer.	dimyristoylphosphatidylglycerol	204-208	amyloid beta precursor protein	Homo sapiens	161-166
25933940-1	2015	The development of a novel, mucus permeating SNEDDS formulation for oral insulin delivery containing a hydrophobic ion pair of insulin/dimyristoyl phosphatidylglycerol (INS/DMPG) is presented.	dimyristoylphosphatidylglycerol	135-167	insulin	Homo sapiens	73-80
25933940-7	2015	The incorporation of INS/DMPG in SNEDDS prevented an initial burst release of insulin.	dimyristoylphosphatidylglycerol	25-29	insulin	Homo sapiens	78-85
25933940-9	2015	According to the reported results, the incorporation of the hydrophobic ion pair of INS/DMPG in SNEDDS could be regarded as a promising strategy for the oral delivery of insulin.	dimyristoylphosphatidylglycerol	88-92	insulin	Homo sapiens	170-177