PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
29879417-1	2018	OSBP binds, extracts and transfers sterols and phosphatidylinositol-4-phosphate (PI(4)P between liposomes, but the sequence of steps at the membrane surface leading to ligand removal is poorly characterized.	pi(4)p	81-87	oxysterol binding protein	Homo sapiens	0-4	
29879417-2	2018	In this study, we used dual polarization interferometry (DPI), a label-free surface analytical technique, to characterize the interaction of recombinant, purified OSBP as it flows over immobilized dioleoyl-phosphatidylcholine (DOPC) bilayers containing PI(4)P, cholesterol or 25-hydroxycholesterol.	pi(4)p	253-259	oxysterol binding protein	Homo sapiens	163-167	
29879417-3	2018	Kinetics of membrane interaction were analyzed for PI(4)P-binding and phosphorylation mutants of OSBP.	pi(4)p	51-57	oxysterol binding protein	Homo sapiens	97-101	
29879417-4	2018	Wild-type OSBP demonstrated a distinctive association with immobilized DOPC bilayers containing 1-8 mol% PI(4)P that was characterized by initial saturable binding followed by desorption, indicative of PI(4)P extraction.	pi(4)p	105-111	oxysterol binding protein	Homo sapiens	10-14	
29879417-4	2018	Wild-type OSBP demonstrated a distinctive association with immobilized DOPC bilayers containing 1-8 mol% PI(4)P that was characterized by initial saturable binding followed by desorption, indicative of PI(4)P extraction.	pi(4)p	202-208	oxysterol binding protein	Homo sapiens	10-14	
29879417-5	2018	In support of this conclusion, an OSBP mutant with impaired binding and extraction of PI(4)P was stably absorbed to PI(4)P-containing membranes, while a pleckstrin homology domain mutant did not associate with PI(4)P-containing membranes.	pi(4)p	86-92	oxysterol binding protein	Homo sapiens	34-38	
29879417-5	2018	In support of this conclusion, an OSBP mutant with impaired binding and extraction of PI(4)P was stably absorbed to PI(4)P-containing membranes, while a pleckstrin homology domain mutant did not associate with PI(4)P-containing membranes.	pi(4)p	116-122	oxysterol binding protein	Homo sapiens	34-38	
29879417-5	2018	In support of this conclusion, an OSBP mutant with impaired binding and extraction of PI(4)P was stably absorbed to PI(4)P-containing membranes, while a pleckstrin homology domain mutant did not associate with PI(4)P-containing membranes.	pi(4)p	116-122	oxysterol binding protein	Homo sapiens	34-38	
29879417-8	2018	These real-time flow studies allow us to dissect the association of OSBP with PI(4)P into discrete components; initial recruitment to PI(4)P membranes by the PH domain, detection and extraction of PI(4)P, and desorption due to ligand depletion.	pi(4)p	78-84	oxysterol binding protein	Homo sapiens	68-72