PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
8017104-5	1994	The three yeast genes are also functionally related as overexpression of HES1 or KES1 alleviated the tryptophan-transport defect in kes1 delta or osh1 delta mutants, respectively.	Tryptophan	101-111	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	81-85
8017104-5	1994	The three yeast genes are also functionally related as overexpression of HES1 or KES1 alleviated the tryptophan-transport defect in kes1 delta or osh1 delta mutants, respectively.	Tryptophan	101-111	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	132-136
31836520-3	2020	In silico computations demonstrated the compounds possess good membrane permeability and can bind within active sites of known 20-hydroxycholesterol targets (e.g. Smoothened and yeast Osh4) and some other sterol-binding proteins (human LXRbeta and STARD1; yeast START-kins Lam4S2 and Lam2S2).	20-hydroxycholesterol	127-148	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	184-188
31836520-3	2020	In silico computations demonstrated the compounds possess good membrane permeability and can bind within active sites of known 20-hydroxycholesterol targets (e.g. Smoothened and yeast Osh4) and some other sterol-binding proteins (human LXRbeta and STARD1; yeast START-kins Lam4S2 and Lam2S2).	Sterols	142-148	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	184-188
25165144-0	2014	Osh4p is needed to reduce the level of phosphatidylinositol-4-phosphate on secretory vesicles as they mature.	phosphatidylinositol 4-phosphate	39-71	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	0-5
29782498-7	2018	Indeed, deletion of either OSH4, which encodes a sterol/phosphatidylinositol-4-phosphate (PI4P) exchange protein, or SAC1, which encodes a PI4P phosphatase, caused synthetic lethality in Delta-s-tether cells due to disruptions in redundant PI4P and phospholipid regulatory pathways.	-4-phosphate	76-88	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	27-31
29487131-7	2018	Of note, the sterol content in the mitochondrial fraction was significantly decreased in vivo after Osh4 inactivation in a genetic background in which all the other OSH genes were deleted.	Sterols	13-19	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	100-104
26928592-6	2016	OSBP and Osh4p organize a counterflow transport of lipids whereby sterols are exchanged for the phosphoinositide PI4P, which is used as a fuel to drive sterol transport.	phosphoinositide pi4p	96-117	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	9-14
26928592-6	2016	OSBP and Osh4p organize a counterflow transport of lipids whereby sterols are exchanged for the phosphoinositide PI4P, which is used as a fuel to drive sterol transport.	Sterols	66-72	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	9-14
26466678-6	2015	Deletion of KES1 suppresses plasma membrane-missorting defects and the accumulation of intracellular ergosterol in drs2 mutants.	Ergosterol	101-111	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	12-16
31347760-0	2020	The anti-fungal beta-sitosterol targets the yeast oxysterol-binding protein Osh4.	gamma-sitosterol	16-31	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	76-80
31347760-4	2020	RESULTS: beta-Sitosterol (200 mug mL-1 ) is toxic against yeast cells expressing only Osh4 (an oxysterol-binding protein) and harbouring a upc2-1 mutation (which enables sterol uptake), but not against yeast strains expressing all seven Osh proteins and harbouring a upc2-1 mutation.	gamma-sitosterol	9-24	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	86-90
31347760-4	2020	RESULTS: beta-Sitosterol (200 mug mL-1 ) is toxic against yeast cells expressing only Osh4 (an oxysterol-binding protein) and harbouring a upc2-1 mutation (which enables sterol uptake), but not against yeast strains expressing all seven Osh proteins and harbouring a upc2-1 mutation.	Sterols	18-24	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	86-90
31347760-6	2020	The deletion of COQ1 (a gene known to be highly induced upon deletion of OSH4) enhances the toxicity of beta-sitosterol in yeast cells expressing only Osh4 and harbouring the upc2-1 mutation.	gamma-sitosterol	104-119	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	73-77
31347760-6	2020	The deletion of COQ1 (a gene known to be highly induced upon deletion of OSH4) enhances the toxicity of beta-sitosterol in yeast cells expressing only Osh4 and harbouring the upc2-1 mutation.	gamma-sitosterol	104-119	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	151-155
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.	gamma-sitosterol	34-49	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.	gamma-sitosterol	34-49	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	129-133
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
31347760-8	2020	CONCLUSION: Our results indicate that the concentrations of beta-sitosterol, and Osh4, as well as its homologues within cells, are most likely the main determinants of beta-sitosterol toxicity.	gamma-sitosterol	168-183	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	81-85
25165144-4	2014	We show here that in yeast the oxysterol-binding proteins Osh1-Osh7 are collectively needed to maintain the normal distribution of PI4P and that Osh4p is critical in this function.	Oxysterols	31-40	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	145-150
20925360-0	2010	Sterol binding and membrane lipid attachment to the Osh4 protein of yeast.	Sterols	0-6	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	52-56
22712517-6	2012	Survival studies after exposure to lethal H2O2 doses using yeast strains bearing a gene deletion corresponding to proteins associated to lipid and vesicle traffic demonstrated for the first time that down-regulation of Kes1p, Vps4p and Ynl010wp and up-regulation of Atp1 and Atp2 increases resistance to H2O2.	Hydrogen Peroxide	304-308	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	219-224
20729555-1	2010	The Saccharomyces cerevisiae protein Kes1/Osh4 is a member of the enigmatic family of oxysterol-binding proteins found throughout Eukarya united by a beta-barrel structure that binds sterols and oxysterols.	Sterols	183-190	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	37-41
20729555-1	2010	The Saccharomyces cerevisiae protein Kes1/Osh4 is a member of the enigmatic family of oxysterol-binding proteins found throughout Eukarya united by a beta-barrel structure that binds sterols and oxysterols.	Sterols	183-190	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	42-46
20729555-2	2010	In this study, we determined that phosphoinositides are the major determinant in membranes that facilitate Kes1 association both in vitro and in cells.	Phosphatidylinositols	34-51	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	107-111
20729555-3	2010	Increased expression of Kes1 in yeast cells decreased the levels of both phosphatidylinositol 4-phosphate (PI4P) and phosphatidylinositol 3-phosphate (PI3P).	phosphatidylinositol 4-phosphate	73-105	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	24-28
20729555-3	2010	Increased expression of Kes1 in yeast cells decreased the levels of both phosphatidylinositol 4-phosphate (PI4P) and phosphatidylinositol 3-phosphate (PI3P).	phosphatidylinositol 3-phosphate	117-149	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	24-28
23593226-0	2013	The yeast oxysterol binding protein Kes1 maintains sphingolipid levels.	Sphingolipids	51-63	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	36-40
23593226-2	2013	The Saccharomyces cerevisiae oxysterol binding protein family member Kes1 (also known as Osh4) also binds phosphoinositides on a distinct surface of the protein from the conserved binding pocket.	Phosphatidylinositols	106-123	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	69-73
23593226-2	2013	The Saccharomyces cerevisiae oxysterol binding protein family member Kes1 (also known as Osh4) also binds phosphoinositides on a distinct surface of the protein from the conserved binding pocket.	Phosphatidylinositols	106-123	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	89-93
23593226-3	2013	In this study, we determine that the oxysterol binding protein family member Kes1 is required to maintain the ratio of complex sphingolipids and levels of ceramide, sphingosine-phosphate and sphingosine.	Sphingolipids	127-140	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	77-81
23593226-3	2013	In this study, we determine that the oxysterol binding protein family member Kes1 is required to maintain the ratio of complex sphingolipids and levels of ceramide, sphingosine-phosphate and sphingosine.	Ceramides	155-163	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	77-81
23593226-3	2013	In this study, we determine that the oxysterol binding protein family member Kes1 is required to maintain the ratio of complex sphingolipids and levels of ceramide, sphingosine-phosphate and sphingosine.	sphingosine phosphate	165-186	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	77-81
23593226-3	2013	In this study, we determine that the oxysterol binding protein family member Kes1 is required to maintain the ratio of complex sphingolipids and levels of ceramide, sphingosine-phosphate and sphingosine.	Sphingosine	165-176	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	77-81
22712517-6	2012	Survival studies after exposure to lethal H2O2 doses using yeast strains bearing a gene deletion corresponding to proteins associated to lipid and vesicle traffic demonstrated for the first time that down-regulation of Kes1p, Vps4p and Ynl010wp and up-regulation of Atp1 and Atp2 increases resistance to H2O2.	Hydrogen Peroxide	42-46	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	219-224
21819498-1	2011	Oxysterol-binding protein (OSBP)-related protein Kes1/ Osh4p is implicated in nonvesicular sterol transfer between membranes in Saccharomyces cerevisiae.	Sterols	3-9	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	49-53
21819498-1	2011	Oxysterol-binding protein (OSBP)-related protein Kes1/ Osh4p is implicated in nonvesicular sterol transfer between membranes in Saccharomyces cerevisiae.	Sterols	3-9	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	55-60
21819498-7	2011	We propose that in response to sterol binding and release Osh4p promotes efficient exocytosis through the co-ordinate regulation of Sac1p, a phosphoinositide 4-phosphate (PI4P) phosphatase, and the exocyst complex.	Sterols	31-37	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	58-63
20729555-4	2010	Phosphoinositide and sterol bindings by Kes1 were necessary for Kes1 to decrease the level of PI4P but not PI3P.	Phosphatidylinositols	0-16	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	40-44
20729555-4	2010	Phosphoinositide and sterol bindings by Kes1 were necessary for Kes1 to decrease the level of PI4P but not PI3P.	Phosphatidylinositols	0-16	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	64-68
20729555-4	2010	Phosphoinositide and sterol bindings by Kes1 were necessary for Kes1 to decrease the level of PI4P but not PI3P.	Sterols	21-27	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	40-44
20729555-4	2010	Phosphoinositide and sterol bindings by Kes1 were necessary for Kes1 to decrease the level of PI4P but not PI3P.	Sterols	21-27	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	64-68
20729555-6	2010	Sterol and phosphoinositide binding by Kes1 both contributed to its regulation of Snc1 trafficking.	Sterols	0-6	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	39-43
20729555-6	2010	Sterol and phosphoinositide binding by Kes1 both contributed to its regulation of Snc1 trafficking.	Phosphatidylinositols	11-27	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	39-43
20925360-1	2010	Osh4 is an oxysterol-binding protein homologue found in yeast that is essential for the intracellular transport of sterols and cell life.	Sterols	115-122	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	0-4
20925360-2	2010	In this study, molecular dynamics simulations were used to investigate the binding of ergosterol, 25-hydroxycholesterol, and lipid moieties to Osh4.	Ergosterol	86-96	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	143-147
20925360-2	2010	In this study, molecular dynamics simulations were used to investigate the binding of ergosterol, 25-hydroxycholesterol, and lipid moieties to Osh4.	25-hydroxycholesterol	98-119	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	143-147
20925360-3	2010	The binding energies between both sterols and Osh4 were dominated by van der Waals interactions with residues within the sterol binding pocket, and were further stabilized by water-mediated interactions with polar residues at the bottom of the binding pocket (W46, Q96, Y97, N165, Q181).	Sterols	34-41	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	46-50
20925360-3	2010	The binding energies between both sterols and Osh4 were dominated by van der Waals interactions with residues within the sterol binding pocket, and were further stabilized by water-mediated interactions with polar residues at the bottom of the binding pocket (W46, Q96, Y97, N165, Q181).	Water	175-180	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	46-50
20925360-5	2010	Possible lipid binding sites on the surface of Osh4 were identified by docking four lipid moieties modeled from different lipid head groups (phosphatidylcholine, phosphatidylserine, phosphatidylinositol(4,5)biphosphate, and phosphatidylinositol(3,4,5)triphosphate).	Phosphatidylcholines	141-160	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	47-51
20925360-5	2010	Possible lipid binding sites on the surface of Osh4 were identified by docking four lipid moieties modeled from different lipid head groups (phosphatidylcholine, phosphatidylserine, phosphatidylinositol(4,5)biphosphate, and phosphatidylinositol(3,4,5)triphosphate).	Phosphatidylserines	162-180	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	47-51
20925360-5	2010	Possible lipid binding sites on the surface of Osh4 were identified by docking four lipid moieties modeled from different lipid head groups (phosphatidylcholine, phosphatidylserine, phosphatidylinositol(4,5)biphosphate, and phosphatidylinositol(3,4,5)triphosphate).	Phosphatidylinositol 4,5-Diphosphate	182-218	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	47-51
20925360-5	2010	Possible lipid binding sites on the surface of Osh4 were identified by docking four lipid moieties modeled from different lipid head groups (phosphatidylcholine, phosphatidylserine, phosphatidylinositol(4,5)biphosphate, and phosphatidylinositol(3,4,5)triphosphate).	phosphatidylinositol 3,4,5-triphosphate	224-263	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	47-51
20925360-7	2010	Several residues identified in these regions, such as K168, A169, K173, and E412, are either included or adjacent to residues experimentally implicated in Osh4 membrane binding.	6-Aminoindazole	54-58	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	155-159
20925360-7	2010	Several residues identified in these regions, such as K168, A169, K173, and E412, are either included or adjacent to residues experimentally implicated in Osh4 membrane binding.	halofantrine	66-70	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	155-159
20925360-7	2010	Several residues identified in these regions, such as K168, A169, K173, and E412, are either included or adjacent to residues experimentally implicated in Osh4 membrane binding.	guar gum	76-80	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	155-159
20925360-9	2010	Ultimately, understanding how Osh4 attaches to cellular membranes and binds sterol will lead to a clear understanding of how this protein transports sterols between organelles in vivo.	Sterols	76-82	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	30-34
20925360-9	2010	Ultimately, understanding how Osh4 attaches to cellular membranes and binds sterol will lead to a clear understanding of how this protein transports sterols between organelles in vivo.	Sterols	149-156	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	30-34
17428193-5	2007	Molecular modelling suggested that ORP2 has a sterol-binding pocket similar to that of Saccharomyces cerevisiae Osh4p.	Sterols	46-52	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	112-117
20008566-5	2009	Using Osh4p/Kes1p as a representative ORP, we show that ORPs have at least two membrane-binding surfaces; one near the mouth of the sterol-binding pocket and a distal site that can bind a second membrane.	Sterols	132-138	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	6-11
20008566-5	2009	Using Osh4p/Kes1p as a representative ORP, we show that ORPs have at least two membrane-binding surfaces; one near the mouth of the sterol-binding pocket and a distal site that can bind a second membrane.	Sterols	132-138	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	12-17
20008566-6	2009	The distal site is required for the protein to function in cells and, remarkably, regulates the rate at which Osh4p extracts and delivers sterols in a phosphoinositide-dependent manner.	Sterols	138-145	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	110-115
20008566-6	2009	The distal site is required for the protein to function in cells and, remarkably, regulates the rate at which Osh4p extracts and delivers sterols in a phosphoinositide-dependent manner.	Phosphatidylinositols	151-167	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	110-115
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
18377932-2	2008	The crystal structure of one ORP family member, yeast Osh4, is known in apo and sterol-bound states.	Sterols	80-86	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	54-58
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
17938859-4	2008	Recently, three-dimensional crystal structures of Osh4 with and without sterols bound within the core of the protein were determined.	Sterols	72-79	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	50-54
20651827-6	2010	SGA analysis identified a role for Kes1 and Sec14 in regulating the level and function of Golgi PI-4-phosphate (PI-4-P).	phosphatidylinositol 4-phosphate	96-110	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	35-39
20651827-6	2010	SGA analysis identified a role for Kes1 and Sec14 in regulating the level and function of Golgi PI-4-phosphate (PI-4-P).	pi-4-p	112-118	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	35-39
20651827-8	2010	Comparing SGA screens in databases, coupled with genetic and cell biological analyses, further determined that the PI-4-P pool affected by Kes1 is generated by the PI 4-kinase Pik1.	pi-4-p	115-121	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	139-143
20651827-9	2010	An important biological role for Sec14 and Kes1 revealed by SGA is coordinate regulation of the Pik1-generated Golgi PI-4-P pool that in turn is essential for vesicular transport into and out of the trans-Golgi.	pi-4-p	117-123	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	43-47
19403696-1	2009	The oxysterol binding protein homologue Kes1p has been implicated in nonvesicular sterol transport in Saccharomyces cerevisiae.	Sterols	7-13	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	40-45
19403696-3	2009	Here, we show that potential phospholipid translocases in the Drs2/Dnf family (type IV P-type ATPases [P4-ATPases]) are downstream targets of Kes1p repression.	Phospholipids	29-41	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	142-147
17881569-0	2007	The oxysterol binding protein Kes1p regulates Golgi apparatus phosphatidylinositol-4-phosphate function.	phosphatidylinositol 4-phosphate	62-94	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	30-35
17881569-7	2007	Kes1p regulates Golgi apparatus-derived vesicular transport by inhibiting the function of Pik1p-generated Golgi apparatus phosphatidylinositol-4-phosphate (PI-4P).	phosphatidylinositol 4-phosphate	122-154	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	0-5
16141212-5	2005	Of these eight, four are ergosterol-related genes (HEM14, HMG1, KES1, and ERG5).	Ergosterol	25-35	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	64-68
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
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.	Ergosterol	143-153	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.	Ergosterol	143-153	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	66-71
16585271-5	2006	In addition, Osh4p transfers sterols more rapidly between membranes containing phosphoinositides (PIPs), suggesting that PIPs regulate sterol transport by ORPs.	Sterols	29-36	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	13-18
16585271-5	2006	In addition, Osh4p transfers sterols more rapidly between membranes containing phosphoinositides (PIPs), suggesting that PIPs regulate sterol transport by ORPs.	Phosphatidylinositols	79-96	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	13-18
16585271-5	2006	In addition, Osh4p transfers sterols more rapidly between membranes containing phosphoinositides (PIPs), suggesting that PIPs regulate sterol transport by ORPs.	piperidine	98-102	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	13-18
16585271-5	2006	In addition, Osh4p transfers sterols more rapidly between membranes containing phosphoinositides (PIPs), suggesting that PIPs regulate sterol transport by ORPs.	piperidine	121-125	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	13-18
16585271-5	2006	In addition, Osh4p transfers sterols more rapidly between membranes containing phosphoinositides (PIPs), suggesting that PIPs regulate sterol transport by ORPs.	Sterols	29-35	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	13-18
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.	Ergosterol	126-136	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.	Ergosterol	126-136	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	78-82
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
16136145-7	2005	The structure of Osh4 in the absence of ligand exposes potential phospholipid-binding sites that are positioned for membrane docking and sterol exchange.	Phospholipids	65-77	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	17-21
15617515-3	2005	Current data imply that the yeast ORP Kes1p is a negative regulator of Golgi-derived vesicular transport mediated by the essential phosphatidylinositol/phosphatidylcholine transfer protein Sec14p.	Phosphatidylinositols	131-151	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	38-43
15617515-3	2005	Current data imply that the yeast ORP Kes1p is a negative regulator of Golgi-derived vesicular transport mediated by the essential phosphatidylinositol/phosphatidylcholine transfer protein Sec14p.	Phosphatidylcholines	152-171	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	38-43
15617515-5	2005	Recent studies have determined that Kes1p and ORP1S both bind phospholipids as ligands.	Phospholipids	62-75	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	36-41
15617515-9	2005	The results determined that the phospholipid binding domain per se was insufficient for inhibition of vesicular transport by ORP1S, and that transport of carboxypeptidase Y and invertase from the Golgi may be regulated differentially by specific regions of ORP1S/Kes1p.	Phospholipids	32-44	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	263-268
11916983-3	2002	Kes1p, one of seven members of the yeast OSBP family, negatively regulates Golgi complex secretory functions that are dependent on the action of the major yeast phosphatidylinositol/phosphatidylcholine Sec14p.	Phosphatidylinositols	161-181	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	0-5
11916983-3	2002	Kes1p, one of seven members of the yeast OSBP family, negatively regulates Golgi complex secretory functions that are dependent on the action of the major yeast phosphatidylinositol/phosphatidylcholine Sec14p.	Phosphatidylcholines	182-201	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	0-5
11916983-4	2002	We now demonstrate that Kes1p is a peripheral membrane protein of the yeast Golgi complex, that localization to the Golgi complex is required for Kes1p function in vivo, and that targeting of Kes1p to the Golgi complex requires binding to a phosphoinositide pool generated via the action of the Pik1p, but not the Stt4p, PtdIns 4-kinase.	Phosphatidylinositols	241-257	oxysterol-binding protein KES1	Saccharomyces cerevisiae S288C	24-29