PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
3936545-9	1985	In a model HDL composed of DMPC and apoA-I, the lateral diffusion of a pyrene-labeled cholesterol was dramatically changed at the Tc whereas little change was observed in that of a pyrene-labeled PC.	pyrene	71-77	apolipoprotein A1	Homo sapiens	36-42	
3936545-9	1985	In a model HDL composed of DMPC and apoA-I, the lateral diffusion of a pyrene-labeled cholesterol was dramatically changed at the Tc whereas little change was observed in that of a pyrene-labeled PC.	pyrene	181-187	apolipoprotein A1	Homo sapiens	36-42	
33718538-0	2021	Dataset on pyrene-labelled apolipoprotein A-I, model development and fitting to monitor oligomeric species of its lipid-free form.	pyrene	11-17	apolipoprotein A1	Homo sapiens	27-45	
33444627-0	2021	Analysis of pyrene-labelled apolipoprotein A-I oligomerization in solution: Spectra deconvolution and changes in P-value and excimer formation.	pyrene	12-18	apolipoprotein A1	Homo sapiens	28-46	
33718538-1	2021	This article contains data for the self-association of pyrene-labelled single Cys-mutants of apolipoprotein A-I (apoA-I).	pyrene	55-61	apolipoprotein A1	Homo sapiens	93-111	
33718538-1	2021	This article contains data for the self-association of pyrene-labelled single Cys-mutants of apolipoprotein A-I (apoA-I).	pyrene	55-61	apolipoprotein A1	Homo sapiens	113-119	
33718538-2	2021	Mathematical models were developed to characterise the self-association events at different cysteine positions on apoA-I obtained as a function of protein concentration based on the multi-parametric spectrum of pyrene, particularly P-value and excimer emissions.	pyrene	211-217	apolipoprotein A1	Homo sapiens	114-120	
19786567-6	2010	The results of fluorescence experiments with pyrene-labeled apoA-I are consistent with the N-terminal helix bundle domain interacting with proteins resident on the HDL particle surface.	pyrene	45-51	apolipoprotein A1	Homo sapiens	60-66	
18831538-5	2008	Taking advantage of a significant increase in fluorescence when a pyrene-labeled helix is in contact with the lipid surface, we monitored the behaviors of the N- and C-terminal helices upon binding of apoA-I to egg PC small unilamellar vesicles.	pyrene	66-72	apolipoprotein A1	Homo sapiens	201-207	
18831538-6	2008	Comparison of the binding isotherms for pyrene-labeled apoA-I as well as a C-terminal helical peptide suggests that an increase in surface concentration of apoA-I causes dissociation of the N-terminal helix from the surface leaving the C-terminal helix attached.	pyrene	40-46	apolipoprotein A1	Homo sapiens	55-61	
18831538-6	2008	Comparison of the binding isotherms for pyrene-labeled apoA-I as well as a C-terminal helical peptide suggests that an increase in surface concentration of apoA-I causes dissociation of the N-terminal helix from the surface leaving the C-terminal helix attached.	pyrene	40-46	apolipoprotein A1	Homo sapiens	156-162	
16671566-2	2005	Incubation of erythrocyte membranes with apolipoprotein A-I was accompanied by significant changes in biophysical characteristics of a fluorescent probe pyrene in the hydrophobic membrane region and a decrease in Na+/K(+)-ATPase activity.	pyrene	153-159	apolipoprotein A1	Homo sapiens	41-59