PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8906563-2	1996	Correlation with metabolism of membrane phospholipids suggests that PKC-alpha and MARCKS may be required to mediate phosphatidylcholine turnover stimulated by phorbol ester (beta-TPA).	Phosphatidylcholines	116-135	myristoylated alanine rich protein kinase C substrate	Homo sapiens	82-88	
8906563-8	1996	Thus, induced differentiation of human neuroblastoma cells involved increased expression of PKC-alpha and MARCKS and synthesis of phosphatidylcholine, consistent with involvement of PKC-alpha and MARCKS in regulation of phosphatidylcholine turnover during neurite growth.	Phosphatidylcholines	220-239	myristoylated alanine rich protein kinase C substrate	Homo sapiens	196-202	
15298909-2	2004	We used a well-characterized peptide corresponding to the basic effector domain of myristoylated alanine-rich C kinase substrate, MARCKS(151-175), that was fluorescently labeled with Alexa488, and measured its binding to large unilamellar vesicles (diameter approximately 100 nm) composed of phosphatidylcholine and phosphatidylserine or phosphatidylinositol 4,5-bisphosphate.	Phosphatidylcholines	292-311	myristoylated alanine rich protein kinase C substrate	Homo sapiens	130-136	
12670959-4	2003	Measurements of cross-relaxation rates in two-dimensional nuclear Overhauser enhancement spectroscopy NMR experiments show that the five Phe rings of MARCKS-(151-175) penetrate into the acyl chain region of phosphatidylcholine bilayers containing phosphatidylglycerol or PI(4,5)P2.	Phosphatidylcholines	207-226	myristoylated alanine rich protein kinase C substrate	Homo sapiens	150-156	
10504221-4	1999	Deuterium NMR in membranes containing phosphatidylcholine (PC) and phosphatidylserine (PS) indicates that this peptide, MARCKS(151-175), partially penetrates the membrane interface when bound and alters the effective charge density on the membrane interface by approximately 2 charges per bound peptide.	Phosphatidylcholines	38-57	myristoylated alanine rich protein kinase C substrate	Homo sapiens	120-126	
9601059-2	1998	Previously we showed that stimulation of phosphatidylcholine (PtdCho) synthesis by PMA in SK-N-MC human neuroblastoma cells required overexpression of MARCKS, whereas PKCalpha alone was insufficient.	Phosphatidylcholines	41-60	myristoylated alanine rich protein kinase C substrate	Homo sapiens	151-157	
9601059-2	1998	Previously we showed that stimulation of phosphatidylcholine (PtdCho) synthesis by PMA in SK-N-MC human neuroblastoma cells required overexpression of MARCKS, whereas PKCalpha alone was insufficient.	Phosphatidylcholines	62-68	myristoylated alanine rich protein kinase C substrate	Homo sapiens	151-157	
9601059-10	1998	Our results show that MARCKS is an essential link in the PKC-mediated activation of PtdCho-specific PLD in these cells and that the stimulation of PtdCho synthesis by PMA is a secondary response.	Phosphatidylcholines	84-90	myristoylated alanine rich protein kinase C substrate	Homo sapiens	22-28	
8627336-0	1996	Overexpression of MARCKS, but not protein kinase C-alpha, increases phorbol ester-stimulated synthesis of phosphatidylcholine in human SK-N-MC neuroblastoma cells.	Phosphatidylcholines	106-125	myristoylated alanine rich protein kinase C substrate	Homo sapiens	18-24	
8627336-2	1996	In five clones with a less than fivefold increase in MARCKS protein level, the synthesis of PtdCho from [methyl-3H] choline was stimulated 1.88-2.34-fold in the presence of 100-200 nM TPA.	Phosphatidylcholines	92-98	myristoylated alanine rich protein kinase C substrate	Homo sapiens	53-59	
7964753-9	1994	Of these proteins, only MARCKS appears to be correlated with phorbol ester stimulation of phosphatidylcholine turnover in these cells.	Phosphatidylcholines	90-109	myristoylated alanine rich protein kinase C substrate	Homo sapiens	24-30