PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
28802697-5	2017	The MP1-lipid membrane interaction was studied using Langmuir phosphatidylcholine and phosphatidylserine (PS) monolayers as model membrane systems.	Phosphatidylserines	86-104	pitrilysin metallopeptidase 1	Homo sapiens	4-7	
28802697-5	2017	The MP1-lipid membrane interaction was studied using Langmuir phosphatidylcholine and phosphatidylserine (PS) monolayers as model membrane systems.	Phosphatidylserines	106-108	pitrilysin metallopeptidase 1	Homo sapiens	4-7	
28802697-6	2017	PS was chosen since this negatively charged lipid was found predominantly on the outer leaflet of tumor cells, and it enhances MP1 activity for PS-containing membranes to a greater extent than for other negatively charged lipids.	Phosphatidylserines	0-2	pitrilysin metallopeptidase 1	Homo sapiens	127-130	
28802697-6	2017	PS was chosen since this negatively charged lipid was found predominantly on the outer leaflet of tumor cells, and it enhances MP1 activity for PS-containing membranes to a greater extent than for other negatively charged lipids.	Phosphatidylserines	144-146	pitrilysin metallopeptidase 1	Homo sapiens	127-130	
28802697-7	2017	MP1 incorporated into anionic PS monolayers, which show a liquid-expanded (LE) phase or LE-liquid-condensed (LC) phase coexistence, up to lipid-packing densities higher than those of cell membranes.	Phosphatidylserines	30-32	pitrilysin metallopeptidase 1	Homo sapiens	0-3	
28274844-3	2017	In agreement with this requirement, phosphatidylserine lipids are translocated to the outer leaflet of cells, and are available for MP1 binding, depending on the presence of liquid-ordered domains.	Phosphatidylserines	36-54	pitrilysin metallopeptidase 1	Homo sapiens	132-135	
28274844-4	2017	Here, we investigated the effect of PS on MP1 activity when this lipid is reconstituted in membranes of giant or large liposomes with different lipid-phase states.	Phosphatidylserines	36-38	pitrilysin metallopeptidase 1	Homo sapiens	42-45	
28274844-8	2017	Based on our findings, we propose that the physicochemical properties of cancer cell membranes, which possess a much higher concentration of PS than normal cells, renders them susceptible to MP1 binding and lytic pore formation.	Phosphatidylserines	141-143	pitrilysin metallopeptidase 1	Homo sapiens	191-194	
26331251-8	2015	Therefore, PS and PE lipids synergistically combine to enhance membrane poration by MP1, implying that the combined enrichment of both these lipids in the outer leaflet of cancer cells is highly significant for MP1"s anticancer action.	Phosphatidylserines	11-13	pitrilysin metallopeptidase 1	Homo sapiens	84-87	
26331251-8	2015	Therefore, PS and PE lipids synergistically combine to enhance membrane poration by MP1, implying that the combined enrichment of both these lipids in the outer leaflet of cancer cells is highly significant for MP1"s anticancer action.	Phosphatidylserines	11-13	pitrilysin metallopeptidase 1	Homo sapiens	211-214