PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
21329368-7	2011	Alternatively, the overlapping helix 10 C-terminal domains of apoA-I were observed to be extremely mobile or "promiscuous", transiently exposing limited hydrocarbon regions of PL.	Hydrocarbons	153-164	apolipoprotein A1	Homo sapiens	62-68	
9819208-5	1998	Above this threshold concentration, apoA-I penetrates within the monolayer (i.e., part of apoA-I crosses the PL polar headgroup/hydrocarbon chain interface).	Hydrocarbons	128-139	apolipoprotein A1	Homo sapiens	36-42	
19167289-5	2009	Of significance, the conformations of the overlapping N- and C-terminal domains of apoA-I in the particles were unusually mobile, exposing hydrocarbon regions of the phospholipid to solvent; a lack of buried interhelical salt bridges in the terminal domains correlated with increased mobility.	Hydrocarbons	139-150	apolipoprotein A1	Homo sapiens	83-89	
9819208-5	1998	Above this threshold concentration, apoA-I penetrates within the monolayer (i.e., part of apoA-I crosses the PL polar headgroup/hydrocarbon chain interface).	Hydrocarbons	128-139	apolipoprotein A1	Homo sapiens	90-96	
3918999-4	1985	The activation of lecithin:cholesterol acyltransferase by apo-A-I and -A-IV differed, depending upon the nature of the hydrocarbon chains of the sn-L-alpha-phosphatidylcholine acyl donor.	Hydrocarbons	119-130	apolipoprotein A1	Homo sapiens	58-75	
167813-3	1975	The activation by apoA-I and apoC-I differed, depending upon the nature of the hydrocarbon chains of phosphatidylcholine acyl donor.	Hydrocarbons	79-90	apolipoprotein A1	Homo sapiens	18-24	
6783071-9	1981	A large change was observed in a protein vibrational band at 1340 cm-1 for pure vs. complexed apoA-I, indicating that protein hydrocarbon side chains are immobilized by lipid binding.	Hydrocarbons	126-137	apolipoprotein A1	Homo sapiens	94-100