PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
22447923-4	2012	Rgd1p was mislocalized in mutants specifically altered for Golgi apparatus-based phosphatidylinositol 4-P [PtdIns(4)P] synthesis and for PtdIns(4,5)P(2) production at the plasma membrane.	phosphatidylinositol 4-p	81-105	GTPase-activating protein RGD1	Saccharomyces cerevisiae S288C	0-5
22447923-4	2012	Rgd1p was mislocalized in mutants specifically altered for Golgi apparatus-based phosphatidylinositol 4-P [PtdIns(4)P] synthesis and for PtdIns(4,5)P(2) production at the plasma membrane.	phosphatidylinositol 4-phosphate	107-117	GTPase-activating protein RGD1	Saccharomyces cerevisiae S288C	0-5
22447923-4	2012	Rgd1p was mislocalized in mutants specifically altered for Golgi apparatus-based phosphatidylinositol 4-P [PtdIns(4)P] synthesis and for PtdIns(4,5)P(2) production at the plasma membrane.	Phosphatidylinositol 4,5-Diphosphate	137-152	GTPase-activating protein RGD1	Saccharomyces cerevisiae S288C	0-5
22447923-6	2012	Rgd1p may associate with post-Golgi vesicles by binding to PtdIns(4)P and then be transported by secretory vesicles to the plasma membrane.	phosphatidylinositol 4-phosphate	59-69	GTPase-activating protein RGD1	Saccharomyces cerevisiae S288C	0-5
21143383-6	2011	In the tos2Delta strain, the amount of GTP-bound Rho3p was increased, suggesting an influence of Tos2p on Rgd1p activity in vivo.	Guanosine Triphosphate	39-42	GTPase-activating protein RGD1	Saccharomyces cerevisiae S288C	106-111
21215255-0	2011	Evidence for specific interaction between the RhoGAP domain from the yeast Rgd1 protein and phosphoinositides.	Phosphatidylinositols	92-109	GTPase-activating protein RGD1	Saccharomyces cerevisiae S288C	75-79
21215255-3	2011	Phosphoinositides discriminate between the GTPase activities of Rho3p and Rho4p through Rgd1p and specifically stimulate the RhoGAP activity of Rgd1p on Rho4p.	Phosphatidylinositols	0-17	GTPase-activating protein RGD1	Saccharomyces cerevisiae S288C	88-93
21215255-3	2011	Phosphoinositides discriminate between the GTPase activities of Rho3p and Rho4p through Rgd1p and specifically stimulate the RhoGAP activity of Rgd1p on Rho4p.	Phosphatidylinositols	0-17	GTPase-activating protein RGD1	Saccharomyces cerevisiae S288C	144-149
21215255-6	2011	By gel filtration and circular dichroism we provide the first evidences for a specific interaction between a RhoGAP domain (the RhoGAP domain of Rgd1p) and phosphoinositides.	Phosphatidylinositols	156-173	GTPase-activating protein RGD1	Saccharomyces cerevisiae S288C	145-150
29280056-0	2018	Assignment of 1H, 13C and 15N resonances and secondary structure of the Rgd1-RhoGAP domain.	Hydrogen	14-16	GTPase-activating protein RGD1	Saccharomyces cerevisiae S288C	72-76
29280056-0	2018	Assignment of 1H, 13C and 15N resonances and secondary structure of the Rgd1-RhoGAP domain.	13c	18-21	GTPase-activating protein RGD1	Saccharomyces cerevisiae S288C	72-76
29280056-0	2018	Assignment of 1H, 13C and 15N resonances and secondary structure of the Rgd1-RhoGAP domain.	15n	26-29	GTPase-activating protein RGD1	Saccharomyces cerevisiae S288C	72-76
29280056-3	2018	Rgd1p is recruited to the membrane through interactions with phosphoinositide lipids, which bind the two isolated domains and stimulate the RhoGAP activity on Rho4p.	phosphoinositide lipids	61-84	GTPase-activating protein RGD1	Saccharomyces cerevisiae S288C	0-5
28760887-0	2017	Structural evidence of a phosphoinositide-binding site in the Rgd1-RhoGAP domain.	Phosphatidylinositols	25-41	GTPase-activating protein RGD1	Saccharomyces cerevisiae S288C	62-66
28760887-3	2017	Phosphoinositides not only bind Rgd1p, but also stimulate its GAP activity on the membrane-anchored form of Rho4p.	Phosphatidylinositols	0-17	GTPase-activating protein RGD1	Saccharomyces cerevisiae S288C	32-37
28760887-5	2017	In the Rgd1p-F-BAR domain, a phosphoinositide-binding site has been recently characterized.	Phosphatidylinositols	29-45	GTPase-activating protein RGD1	Saccharomyces cerevisiae S288C	7-12
28760887-6	2017	We report here the X-ray structure of the Rgd1p-RhoGAP domain, identify by NMR spectroscopy and confirm by docking simulations, a new but cryptic phosphoinositide-binding site, comprising contiguous A1, A1" and B helices.	Phosphatidylinositols	146-162	GTPase-activating protein RGD1	Saccharomyces cerevisiae S288C	42-47
28760887-10	2017	Solid-state NMR spectroscopy experiments confirm the membrane interaction of the Rgd1p-RhoGAP domain upon the addition of PtdIns(4,5)P2 and indicate a slight membrane destabilization in the presence of the two partners.	Phosphatidylinositol 4,5-Diphosphate	122-135	GTPase-activating protein RGD1	Saccharomyces cerevisiae S288C	81-86
18845541-0	2008	Phosphoinositides affect both the cellular distribution and activity of the F-BAR-containing RhoGAP Rgd1p in yeast.	Phosphatidylinositols	0-17	GTPase-activating protein RGD1	Saccharomyces cerevisiae S288C	100-105
18845541-4	2008	We demonstrate here that phospholipids discriminate between the GTPase activities of Rho3p and Rho4p through Rgd1p and specifically stimulate the RhoGAP activity on Rho4p.	Phospholipids	25-38	GTPase-activating protein RGD1	Saccharomyces cerevisiae S288C	109-114
18845541-6	2008	The F-BAR region binds to phosphoinositides in vitro and also plays a key role in the localization of Rgd1p to the bud tip and neck during the cell cycle.	Phosphatidylinositols	26-43	GTPase-activating protein RGD1	Saccharomyces cerevisiae S288C	102-107
18845541-7	2008	Studies of heat-sensitive mutants lacking phosphatidylinositol 4-phosphate and phosphatidylinositol 4,5-biphosphate suggested that Rgd1p initially binds to Golgi membranes via phosphatidylinositol 4-phosphate and is then transported to the plasma membrane, where it binds phosphatidylinositol 4,5-biphosphate.	phosphatidylinositol 4-phosphate	42-74	GTPase-activating protein RGD1	Saccharomyces cerevisiae S288C	131-136
18845541-7	2008	Studies of heat-sensitive mutants lacking phosphatidylinositol 4-phosphate and phosphatidylinositol 4,5-biphosphate suggested that Rgd1p initially binds to Golgi membranes via phosphatidylinositol 4-phosphate and is then transported to the plasma membrane, where it binds phosphatidylinositol 4,5-biphosphate.	Phosphatidylinositol 4,5-Diphosphate	79-115	GTPase-activating protein RGD1	Saccharomyces cerevisiae S288C	131-136
18845541-7	2008	Studies of heat-sensitive mutants lacking phosphatidylinositol 4-phosphate and phosphatidylinositol 4,5-biphosphate suggested that Rgd1p initially binds to Golgi membranes via phosphatidylinositol 4-phosphate and is then transported to the plasma membrane, where it binds phosphatidylinositol 4,5-biphosphate.	phosphatidylinositol 4-phosphate	176-208	GTPase-activating protein RGD1	Saccharomyces cerevisiae S288C	131-136
18845541-7	2008	Studies of heat-sensitive mutants lacking phosphatidylinositol 4-phosphate and phosphatidylinositol 4,5-biphosphate suggested that Rgd1p initially binds to Golgi membranes via phosphatidylinositol 4-phosphate and is then transported to the plasma membrane, where it binds phosphatidylinositol 4,5-biphosphate.	Phosphatidylinositol 4,5-Diphosphate	272-308	GTPase-activating protein RGD1	Saccharomyces cerevisiae S288C	131-136
18845541-9	2008	Phosphoinositides both regulate the recruitment and trafficking of Rgd1p to membranes via the F-BAR domain and specifically stimulate GTPase-activating protein activity, consistent with functional interplay between lipids, RhoGAP, and its related GTPases in yeast growth.	Phosphatidylinositols	0-17	GTPase-activating protein RGD1	Saccharomyces cerevisiae S288C	67-72
10931290-2	2000	Rgd1p, which displays a conserved FCH-coiled coil-Rho-GAP domain organization, showed a patch-like distribution in the cell, including a localization in growing buds.	fluorocholine	34-37	GTPase-activating protein RGD1	Saccharomyces cerevisiae S288C	0-5
10590461-10	1999	As for mutants altered in PKC pathway, the accumulation of small-budded dead cells in slg1, rgd1 and mid2 after heat shock was prevented by 1 M sorbitol.	Sorbitol	144-152	GTPase-activating protein RGD1	Saccharomyces cerevisiae S288C	92-96
25620000-4	2015	Whereas some F-BAR domains (such as Bzz1p and Hof1p F-BARs) bind equally well to all phospholipids, the F-BAR domain from the RhoGAP Rgd1p preferentially binds phosphoinositides.	Phospholipids	85-98	GTPase-activating protein RGD1	Saccharomyces cerevisiae S288C	133-138
25620000-4	2015	Whereas some F-BAR domains (such as Bzz1p and Hof1p F-BARs) bind equally well to all phospholipids, the F-BAR domain from the RhoGAP Rgd1p preferentially binds phosphoinositides.	Phosphatidylinositols	160-177	GTPase-activating protein RGD1	Saccharomyces cerevisiae S288C	133-138
25620000-5	2015	We determined X-ray crystal structures of F-BAR domains from Hof1p and Rgd1p, the latter bound to an inositol phosphate.	Inositol Phosphates	101-119	GTPase-activating protein RGD1	Saccharomyces cerevisiae S288C	71-76