PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
6849876-1	1983	The interactions of cytochrome b5 with dimyristoylphosphatidylcholine and dipalmitoylphosphatidylcholine lipid bilayers have been studied with high-sensitivity differential scanning calorimetry and fluorescence spectroscopy.	Dimyristoylphosphatidylcholine	39-69	cytochrome b5 type A	Homo sapiens	20-33	
4016089-1	1985	Resonance energy transfer was used to study the structure of cytochrome b5 and its nonpolar segment reconstituted into sonicated vesicles of dimyristoylphosphatidylcholine.	Dimyristoylphosphatidylcholine	141-171	cytochrome b5 type A	Homo sapiens	61-74	
6838895-2	1983	Detergent-solubilized cytochrome b5 in solution and in a reconstituted system with dimyristoyl phosphatidylcholine.	Dimyristoylphosphatidylcholine	83-114	cytochrome b5 type A	Homo sapiens	22-35	
1600082-0	1992	Bilayer structure and physical dynamics of the cytochrome b5 dimyristoylphosphatidylcholine interaction.	Dimyristoylphosphatidylcholine	61-91	cytochrome b5 type A	Homo sapiens	47-60	
1600082-2	1992	Low angle x-ray diffraction has been used to determine the structure of an asymmetrically reconstituted cytochrome b5:DMPC model membrane system.	Dimyristoylphosphatidylcholine	118-122	cytochrome b5 type A	Homo sapiens	104-117	
1600082-7	1992	In these studies, we have obtained a reconstituted cytochrome b5:DMPC bilayer structure at approximately 6.3 A resolution and conclude that the nonpolar peptide does not penetrate beyond the bilayer midplane.	Dimyristoylphosphatidylcholine	65-69	cytochrome b5 type A	Homo sapiens	51-64	
3680211-0	1987	Topography of the C terminus of cytochrome b5 tightly bound to dimyristoylphosphatidylcholine vesicles.	Dimyristoylphosphatidylcholine	63-93	cytochrome b5 type A	Homo sapiens	32-45	
3680211-1	1987	Cytochrome b5 holoenzyme was bound asymmetrically in the tightly bound form to small unilamellar dimyristoylphosphatidylcholine vesicles.	Dimyristoylphosphatidylcholine	97-127	cytochrome b5 type A	Homo sapiens	0-13	
17488074-4	2007	Here, we present the first solid-state NMR studies on holo-cyt b5 in a membrane environment, namely, macroscopically oriented DMPC:DHPC bicelles.	Dimyristoylphosphatidylcholine	126-130	cytochrome b5 type A	Homo sapiens	59-65	
2804107-1	1989	The changes in steady-state fluorescence lifetimes and anisotropy decay parameters, as well as enzyme activities, of dansyl-labeled cytochrome b5 (DNS-cytochrome b5), on interaction with NADH-cytochrome-b5 reductase in DMPC vesicles, have been measured as a function of temperature.	Dimyristoylphosphatidylcholine	219-223	cytochrome b5 type A	Homo sapiens	132-145	
2804107-1	1989	The changes in steady-state fluorescence lifetimes and anisotropy decay parameters, as well as enzyme activities, of dansyl-labeled cytochrome b5 (DNS-cytochrome b5), on interaction with NADH-cytochrome-b5 reductase in DMPC vesicles, have been measured as a function of temperature.	Dimyristoylphosphatidylcholine	219-223	cytochrome b5 type A	Homo sapiens	151-164	
2804107-2	1989	Steady-state fluorescence of DNS-cytochrome b5 in DMPC vesicles with and without cholesterol was increased on interaction with reductase at temperatures both above and below the DMPC phase transition.	Dimyristoylphosphatidylcholine	50-54	cytochrome b5 type A	Homo sapiens	33-46	
2804107-2	1989	Steady-state fluorescence of DNS-cytochrome b5 in DMPC vesicles with and without cholesterol was increased on interaction with reductase at temperatures both above and below the DMPC phase transition.	Dimyristoylphosphatidylcholine	178-182	cytochrome b5 type A	Homo sapiens	33-46