PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
11988466-5	2002	We conclude by considering the hypothesis that proteins such as MARCKS bind a significant fraction of the PIP2 in a cell, helping to sequester it in lateral membrane domains, then release this lipid in response to local signals such as an increased concentration of Ca(++)/calmodulin or activation of protein kinase C.	Phosphatidylinositol 4,5-Diphosphate	106-110	calmodulin 1	Homo sapiens	273-283	
22989896-0	2012	PtdIns(4,5)P2 interacts with CaM binding domains on TRPM3 N-terminus.	Phosphatidylinositol 4,5-Diphosphate	0-13	calmodulin 1	Homo sapiens	29-32	
22643219-5	2012	The calmodulin-deficient channel has a reduced affinity towards PIP2.	Phosphatidylinositol 4,5-Diphosphate	64-68	calmodulin 1	Homo sapiens	4-14	
21883766-3	2011	CaM inhibition increased Rac1 binding to PIP5K and induced an extensive phosphatidylinositol 4,5-bisphosphate (PI4,5P(2) )-positive tubular membrane network.	Phosphatidylinositol 4,5-Diphosphate	72-109	calmodulin 1	Homo sapiens	0-3	
33041849-0	2020	Two KCNQ2 Encephalopathy Variants in the Calmodulin-Binding Helix A Exhibit Dominant-Negative Effects and Altered PIP2 Interaction.	Phosphatidylinositol 4,5-Diphosphate	114-118	calmodulin 1	Homo sapiens	41-51	
9545238-5	1998	Accordingly, the AKAP79 basic regions mediate binding to membrane vesicles containing acidic phospholipids including phosphatidylinositol-4, 5-bisphosphate [PtdIns(4,5)P2] and this binding is regulated by phosphorylation and calcium-calmodulin.	Phosphatidylinositol 4,5-Diphosphate	117-155	calmodulin 1	Homo sapiens	233-243	
9545238-5	1998	Accordingly, the AKAP79 basic regions mediate binding to membrane vesicles containing acidic phospholipids including phosphatidylinositol-4, 5-bisphosphate [PtdIns(4,5)P2] and this binding is regulated by phosphorylation and calcium-calmodulin.	Phosphatidylinositol 4,5-Diphosphate	157-170	calmodulin 1	Homo sapiens	233-243	
2994657-1	1985	The calmodulin antagonists trifluoperazine, chlorpromazine, perphenazine, promazine, tamoxifen and the naphthalene sulfonamide derivatives W7 and W13 increased the level of 32P-incorporation into human platelet PIP and PIP2.	Phosphatidylinositol 4,5-Diphosphate	219-223	calmodulin 1	Homo sapiens	4-14	
9341159-10	1997	We discuss the biological implications of this switch mechanism, speculating that an increase in the level of Ca2+-calmodulin could rapidly release phosphatidylinositol 4, 5-bisphosphate that previous work has suggested is sequestered in lateral domains formed by MARCKS and MARCKS-(151-175).	Phosphatidylinositol 4,5-Diphosphate	148-186	calmodulin 1	Homo sapiens	115-125	
33310856-4	2020	Combined electrophysiology and molecular dynamics network analysis suggest that VSD transition into the fully activated state allows PIP2 to compete with CaM for binding to VSD.	Phosphatidylinositol 4,5-Diphosphate	133-137	calmodulin 1	Homo sapiens	154-157	
27933776-7	2016	The findings show that CaM does stimulate PI3K lipid kinase activity by binding MARCKS and displacing it from PIP2 headgroups, thereby releasing free PIP2 that recruits active PI3K to the membrane and serves as the substrate for the generation of PIP3.	Phosphatidylinositol 4,5-Diphosphate	110-114	calmodulin 1	Homo sapiens	23-26	
32560560-2	2020	The aim of this study was to characterise interactions between the TRP cation channel subfamily melastatin member 4 (TRPM4) and endogenous intracellular modulators-calcium-binding proteins (calmodulin (CaM) and S100A1) and phosphatidylinositol 4, 5-bisphosphate (PIP2).	Phosphatidylinositol 4,5-Diphosphate	223-261	calmodulin 1	Homo sapiens	190-200	
32560560-2	2020	The aim of this study was to characterise interactions between the TRP cation channel subfamily melastatin member 4 (TRPM4) and endogenous intracellular modulators-calcium-binding proteins (calmodulin (CaM) and S100A1) and phosphatidylinositol 4, 5-bisphosphate (PIP2).	Phosphatidylinositol 4,5-Diphosphate	263-267	calmodulin 1	Homo sapiens	190-200	
27933776-5	2016	This study asks whether calmodulin (CaM), which is known to directly bind MARCKS, also stimulates PIP3 production by releasing free PIP2.	Phosphatidylinositol 4,5-Diphosphate	132-136	calmodulin 1	Homo sapiens	24-34	
27933776-5	2016	This study asks whether calmodulin (CaM), which is known to directly bind MARCKS, also stimulates PIP3 production by releasing free PIP2.	Phosphatidylinositol 4,5-Diphosphate	132-136	calmodulin 1	Homo sapiens	36-39	
24349250-13	2013	These results suggest that a rise in intracellular calcium induces a change in the configuration of CaM-KCNQ binding, which leads to the reduction of KCNQ affinity for PIP2 and subsequent current suppression.	Phosphatidylinositol 4,5-Diphosphate	168-172	calmodulin 1	Homo sapiens	100-103	
26359296-3	2015	Live-cell fluorescence energy transfer measurements and direct binding studies indicate that remote coiled-coil formation creates conditions for different CaM interaction modes, each conferring different PIP2 dependency to Kv7.2 channels.	Phosphatidylinositol 4,5-Diphosphate	204-208	calmodulin 1	Homo sapiens	155-158	
26359296-4	2015	Disruption of coiled-coil formation by epilepsy-causing mutation decreases apparent CaM-binding affinity and interrupts CaM influence on PIP2 sensitivity.	Phosphatidylinositol 4,5-Diphosphate	137-141	calmodulin 1	Homo sapiens	120-123	
25543978-8	2015	We found that this region overlaps with previously identified calmodulin and PIP2 binding sites and that S100A1 competes with calmodulin and PIP2 for this binding site.	Phosphatidylinositol 4,5-Diphosphate	141-145	calmodulin 1	Homo sapiens	62-72