PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8609911-3	1995	Both fluorescence and dialysis data indicate L-FABP mediated sterol transfer between L-cell fibroblast plasma membranes occurs by a direct membrane effect: First, dansylated-L-FABP (DNS-L-FABP) is bound to L-cell fibroblast plasma membranes as indicated by increased DNS-L-FABP steady state polarization and phase resolved limiting anisotropy.	Sterols	61-67	fatty acid binding protein 1	Homo sapiens	45-51	
8609911-3	1995	Both fluorescence and dialysis data indicate L-FABP mediated sterol transfer between L-cell fibroblast plasma membranes occurs by a direct membrane effect: First, dansylated-L-FABP (DNS-L-FABP) is bound to L-cell fibroblast plasma membranes as indicated by increased DNS-L-FABP steady state polarization and phase resolved limiting anisotropy.	Sterols	61-67	fatty acid binding protein 1	Homo sapiens	174-180	
8609911-3	1995	Both fluorescence and dialysis data indicate L-FABP mediated sterol transfer between L-cell fibroblast plasma membranes occurs by a direct membrane effect: First, dansylated-L-FABP (DNS-L-FABP) is bound to L-cell fibroblast plasma membranes as indicated by increased DNS-L-FABP steady state polarization and phase resolved limiting anisotropy.	Sterols	61-67	fatty acid binding protein 1	Homo sapiens	174-180	
8609911-3	1995	Both fluorescence and dialysis data indicate L-FABP mediated sterol transfer between L-cell fibroblast plasma membranes occurs by a direct membrane effect: First, dansylated-L-FABP (DNS-L-FABP) is bound to L-cell fibroblast plasma membranes as indicated by increased DNS-L-FABP steady state polarization and phase resolved limiting anisotropy.	Sterols	61-67	fatty acid binding protein 1	Homo sapiens	174-180	
8609911-6	1995	However, L-FABP mediated intermembrane sterol transfer did require a sterol binding site on L-FABP.	Sterols	39-45	fatty acid binding protein 1	Homo sapiens	9-15	
8609911-6	1995	However, L-FABP mediated intermembrane sterol transfer did require a sterol binding site on L-FABP.	Sterols	39-45	fatty acid binding protein 1	Homo sapiens	92-98	
8609911-9	1995	The fact that L-FABP interacted with plasma membrane vesicles and required a sterol binding site was consistent with a mode of action whereby L-FABP binds to the membrane prior to releasing sterol from the bilayer.	Sterols	77-83	fatty acid binding protein 1	Homo sapiens	14-20	
8609911-9	1995	The fact that L-FABP interacted with plasma membrane vesicles and required a sterol binding site was consistent with a mode of action whereby L-FABP binds to the membrane prior to releasing sterol from the bilayer.	Sterols	77-83	fatty acid binding protein 1	Homo sapiens	142-148	
8609911-9	1995	The fact that L-FABP interacted with plasma membrane vesicles and required a sterol binding site was consistent with a mode of action whereby L-FABP binds to the membrane prior to releasing sterol from the bilayer.	Sterols	190-196	fatty acid binding protein 1	Homo sapiens	14-20	
8609911-9	1995	The fact that L-FABP interacted with plasma membrane vesicles and required a sterol binding site was consistent with a mode of action whereby L-FABP binds to the membrane prior to releasing sterol from the bilayer.	Sterols	190-196	fatty acid binding protein 1	Homo sapiens	142-148	
8431458-4	1993	L-FABP also binds sterols and stimulates sterol uptake and esterification.	Sterols	18-25	fatty acid binding protein 1	Homo sapiens	0-6	
8431458-4	1993	L-FABP also binds sterols and stimulates sterol uptake and esterification.	Sterols	18-24	fatty acid binding protein 1	Homo sapiens	0-6	
8431458-11	1993	These alterations of plasma membrane structure and composition are consistent with a role for L-FABP in regulating intracellular sterol and fatty acid distribution and thereby membrane lipid domain structure.	Sterols	129-135	fatty acid binding protein 1	Homo sapiens	94-100	
25639618-5	2015	BAs were found to interact with L-FABP with dissociation constants in the narrow range of 0.6-7 mum; however, the diverse substitution patterns of the sterol nucleus and the presence of side-chain conjugation resulted in complexes endowed with various degrees of conformational heterogeneity.	Sterols	151-157	fatty acid binding protein 1	Homo sapiens	32-38