PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
18377932-4	2008	Equilibrium and steered molecular dynamics (MD) simulations of Osh4 were carried out to characterize the mechanism of cholesterol exchange.	Cholesterol	118-129	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	63-67	
18937371-0	2009	Binding and release of cholesterol in the Osh4 protein of yeast.	Cholesterol	23-34	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	42-46	
18937371-3	2009	Molecular dynamics (MD) simulations are used to study the binding of cholesterol to Osh4 at the atomic level.	Cholesterol	69-80	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	84-88	
18937371-10	2009	Steered MD was used to determine details of the mechanism used by Osh4 to release cholesterol to the cytoplasm.	Cholesterol	82-93	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	66-70	
16136145-2	2005	Here we report the structure of the full-length yeast ORP Osh4 (also known as Kes1) at 1.5-1.9 A resolution in complexes with ergosterol, cholesterol, and 7-, 20- and 25-hydroxycholesterol.	Cholesterol	138-149	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	58-62	
16136145-2	2005	Here we report the structure of the full-length yeast ORP Osh4 (also known as Kes1) at 1.5-1.9 A resolution in complexes with ergosterol, cholesterol, and 7-, 20- and 25-hydroxycholesterol.	Cholesterol	138-149	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	78-82	
31347760-7	2020	Molecular modelling suggests that beta-sitosterol binds to Osh4 and the binding mode is similar to the binding of cholesterol to Osh4.	Cholesterol	114-125	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	59-63	
31347760-7	2020	Molecular modelling suggests that beta-sitosterol binds to Osh4 and the binding mode is similar to the binding of cholesterol to Osh4.	Cholesterol	114-125	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	129-133	
16585271-4	2006	We demonstrate that a representative member of this family, Osh4p/Kes1p, specifically facilitates the nonvesicular transfer of cholesterol and ergosterol between membranes in vitro.	Cholesterol	127-138	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	60-65	
16585271-4	2006	We demonstrate that a representative member of this family, Osh4p/Kes1p, specifically facilitates the nonvesicular transfer of cholesterol and ergosterol between membranes in vitro.	Cholesterol	127-138	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	66-71