PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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 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 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 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 9265648-0 1997 Gelsolin modulates phospholipase C activity in vivo through phospholipid binding. Phospholipids 60-72 gelsolin Homo sapiens 0-8 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 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 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 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 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 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