PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
2557328-7	1989	The inositol also contained a mixture of fatty acids (16:0, 18:0, 18:1, 20:4, 22:0) located on a site other than the C2 position since the FBP was susceptible to PI-PLC cleavage.	Inositol	4-12	phospholipase C beta 1	Homo sapiens	162-168	
21035488-3	2011	PLCbeta1 is a key player in the regulation of nuclear inositol lipid signaling, and, as discussed above, its function could also be involved in nuclear structure because it hydrolyses PtdIns(4,5)P2, a well accepted regulator of chromatin remodelling.	Inositol	54-62	phospholipase C beta 1	Homo sapiens	0-8	
30896816-1	2019	Four phospholipase C beta (PLCB) isoforms, PLCB1, PLCB2, PLCB3 and PLCB4, have been previously investigated regarding their roles in the metabolism of inositol lipids and cancer.	Inositol	151-159	phospholipase C beta 1	Homo sapiens	43-48	
2826256-3	1987	We have now tested the specificity of various nucleotides in regulating PIC activity in the absence or presence of the hormone cholecystokinin (CCK-8) in saponin-permeabilized [3H]inositol-labelled Flow 9000 cells.	Inositol	180-188	phospholipase C beta 1	Homo sapiens	72-75	
8037672-2	1994	Chemical and enzymic degradation studies have suggested that the PI-PLC resistance of AP is due to inositol acylation of its glycosylphosphatidylinositol (GPI) anchor.	Inositol	99-107	phospholipase C beta 1	Homo sapiens	65-71	
9367761-1	1997	The X-ray crystal structure of the phosphatidylinositol-specific phospholipase C (PI-PLC) from the human pathogen Listeria monocytogenes has been determined both in free form at 2.0 A resolution, and in complex with the competitive inhibitor myo-inositol at 2.6 A resolution.	Inositol	242-254	phospholipase C beta 1	Homo sapiens	35-80	
9367761-1	1997	The X-ray crystal structure of the phosphatidylinositol-specific phospholipase C (PI-PLC) from the human pathogen Listeria monocytogenes has been determined both in free form at 2.0 A resolution, and in complex with the competitive inhibitor myo-inositol at 2.6 A resolution.	Inositol	242-254	phospholipase C beta 1	Homo sapiens	82-88	
9003188-1	1997	Three inositol 1,2-(cyclic)-phosphate analogs, inositol cyclic phosphonates with different stereochemistry at the C-2 position of the inositol ring, have been synthesized as water-soluble inhibitors of phosphatidylinositol-specific phospholipase C (PI-PLC).	Inositol	6-14	phospholipase C beta 1	Homo sapiens	202-247	
9003188-4	1997	(i) Only the analog with the same stereochemistry at the C-2 position of the inositol ring as the natural substrate, myo-inositol 1,2-(cyclic)-phosphate (cIP), exhibits effective inhibition of PI-PLC.	Inositol	77-85	phospholipase C beta 1	Homo sapiens	193-199	
11331006-1	2001	Phosphatidylinositol-specific phospholipase C (PI-PLC) catalyzes the cleavage of the P-O bond in phosphatidylinositol via intramolecular nucleophilic attack of the 2-hydroxyl group of inositol on the phosphorus atom.	Inositol	12-20	phospholipase C beta 1	Homo sapiens	47-53	
8037672-8	1994	The delayed appearance of PI-PLC resistance was unexpected as previous studies have suggested that candidate GPI-anchor precursors are PI-PLC-resistant as a result of inositol acylation.	Inositol	167-175	phospholipase C beta 1	Homo sapiens	26-32	
8037672-8	1994	The delayed appearance of PI-PLC resistance was unexpected as previous studies have suggested that candidate GPI-anchor precursors are PI-PLC-resistant as a result of inositol acylation.	Inositol	167-175	phospholipase C beta 1	Homo sapiens	135-141	
2138615-12	1990	This paper shows that the single difference between P2 and P3, and the basis for the PI-PLC insusceptibility of P3, is a fatty acid, ester-linked to the inositol residue in P3.	Inositol	153-161	phospholipase C beta 1	Homo sapiens	85-91