PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
16914033-2	2006	CapZ is associated with membranes in cells and it is generally assumed that this interaction is mediated by polyphosphoinositides (PPI) particularly PIP2, which has been characterized in vitro.	Phosphatidylinositol Phosphates	108-129	capping actin protein of muscle Z-line subunit alpha 2	Homo sapiens	0-4	
16914033-2	2006	CapZ is associated with membranes in cells and it is generally assumed that this interaction is mediated by polyphosphoinositides (PPI) particularly PIP2, which has been characterized in vitro.	Phosphatidylinositol Phosphates	131-134	capping actin protein of muscle Z-line subunit alpha 2	Homo sapiens	0-4	
12788695-6	2003	Furthermore, addition of constitutively active D-3 phosphorylated polyphosphoinositides or recombinant PI3-kinase subunits to octylglucoside-permeabilized platelets elicits actin filament barbed end exposure by releasing gelsolin and CapZ from the cytoskeleton.	Phosphatidylinositol Phosphates	66-87	capping actin protein of muscle Z-line subunit alpha 2	Homo sapiens	234-238	
8660341-4	1996	These data suggest S100a0 and polyphosphoinositides bind to the same COOH-terminal region of CapZalpha, thus potentially modulating CapZ activity.	Phosphatidylinositol Phosphates	30-51	capping actin protein of muscle Z-line subunit alpha 2	Homo sapiens	93-97