PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
11577104-8	2001	We conclude that gelsolin plays a key role in recruitment of signaling proteins to the plasma membrane through phospholipid-protein interactions and by regulation of their phosphorylation status through its association with PTP-PEST.	Phospholipids	111-123	gelsolin	Homo sapiens	17-25	
12592377-8	2003	These results suggest that gelsolin suppressed the activation of PKCs involved in phospholipid signalling pathways, inhibiting cell proliferation and tumorigenicity.	Phospholipids	82-94	gelsolin	Homo sapiens	27-35	
10210201-2	1999	It interacts with phospholipids and we previously showed that phosphatidylinositol 4,5-bisphosphate promotes phosphorylation of gelsolin by the tyrosine kinase c-Src.	Phospholipids	18-31	gelsolin	Homo sapiens	128-136	
9265648-0	1997	Gelsolin modulates phospholipase C activity in vivo through phospholipid binding.	Phospholipids	60-72	gelsolin	Homo sapiens	0-8	
2855803-7	1988	A structure-function analysis of gelsolin indicates that its N-terminal half is primarily responsible for severing actin filaments, and elucidates mechanisms by which Ca2+ and phospholipid may regulate gelsolin functions.	Phospholipids	176-188	gelsolin	Homo sapiens	33-41	
1847925-9	1991	The sequence homology and similar functional domain structure suggest a common structural basis for the calcium- and phospholipid-regulated actin-severing properties shared by adseverin, gelsolin, and villin.	Phospholipids	117-129	gelsolin	Homo sapiens	187-195	
2538463-4	1989	This study correlates tests of gelsolin"s severing function with quasielastic light scattering measurements of the size of mixed lipid particles and shows that the previously demonstrated diminution of the maximal effect of PIP2 in micellar form by aggregation of the micelles or mixing with other phospholipids is not the result of an absolute requirement for small lipid particles, but rather the masking of critical sites by aggregation, by sequestration in multilamellar vesicles, or by dilution of the polyphosphoinositides below a critical concentration.	Phospholipids	298-311	gelsolin	Homo sapiens	31-39	
2538463-7	1989	Experiments with bilayer-forming phospholipids or with Triton X-100 indicate that a critical number of PIP2 molecules may be required for incipient effects on a gelsolin molecule.	Phospholipids	33-46	gelsolin	Homo sapiens	161-169	
8744948-1	1996	Based on previous studies demonstrating activation of phosphatidylinositol 3-hydroxyl kinase (PI3-kinase) and stimulation of a change in cell shape, we examined the effect of osteopontin on the association of phospholipids with gelsolin, an actin-capping/severing protein.	Phospholipids	209-222	gelsolin	Homo sapiens	228-236	
2855803-7	1988	A structure-function analysis of gelsolin indicates that its N-terminal half is primarily responsible for severing actin filaments, and elucidates mechanisms by which Ca2+ and phospholipid may regulate gelsolin functions.	Phospholipids	176-188	gelsolin	Homo sapiens	202-210	
29363700-0	2018	Optically sensing phospholipid induced coil-helix transitions in the phosphoinositide-binding motif of gelsolin.	Phospholipids	18-30	gelsolin	Homo sapiens	103-111	
21545139-0	2011	1-Palmitoyl-2-(9"-oxononanoyl)-sn-glycero-3-phosphocholine, an oxidized phospholipid, accelerates Finnish type familial gelsolin amyloidosis in vitro.	Phospholipids	72-84	gelsolin	Homo sapiens	120-128