PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
1654325-0	1991	A short sequence responsible for both phosphoinositide binding and actin binding activities of cofilin.	Phosphatidylinositols	38-54	cofilin 1	Homo sapiens	95-102	
1654325-2	1991	Both abilities of cofilin can be inhibited by phosphoinositides such as phosphatidylinositol, phosphatidylinositol 4-monophosphate, and phosphatidylinositol 4,5-bisphosphate (PIP2).	Phosphatidylinositols	46-63	cofilin 1	Homo sapiens	18-25	
1654325-2	1991	Both abilities of cofilin can be inhibited by phosphoinositides such as phosphatidylinositol, phosphatidylinositol 4-monophosphate, and phosphatidylinositol 4,5-bisphosphate (PIP2).	Phosphatidylinositols	72-92	cofilin 1	Homo sapiens	18-25	
29073094-2	2017	Membrane phosphoinositides, especially phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2], regulate the activities of many actin-binding proteins (ABPs), including profilin, cofilin, Dia2, N-WASP, ezrin, and moesin, but the underlying molecular mechanisms have remained elusive.	Phosphatidylinositols	9-26	cofilin 1	Homo sapiens	173-180	
29073094-7	2017	Profilin and cofilin display transient, low-affinity interactions with phosphoinositide-rich membranes, whereas F-actin assembly factors Dia2 and N-WASP reside on phosphoinositide-rich membranes for longer periods to perform their functions.	Phosphatidylinositols	71-87	cofilin 1	Homo sapiens	13-20	
19029335-0	2008	Cofilin is a pH sensor for actin free barbed end formation: role of phosphoinositide binding.	Phosphatidylinositols	68-84	cofilin 1	Homo sapiens	0-7	
19029335-6	2008	Cofilin activity is inhibited by phosphoinositide binding, and we found that phosphoinositide binding is pH-dependent for wild-type cofilin, with decreased binding at a higher pH.	Phosphatidylinositols	33-49	cofilin 1	Homo sapiens	0-7	
19029335-6	2008	Cofilin activity is inhibited by phosphoinositide binding, and we found that phosphoinositide binding is pH-dependent for wild-type cofilin, with decreased binding at a higher pH.	Phosphatidylinositols	77-93	cofilin 1	Homo sapiens	0-7	
19029335-6	2008	Cofilin activity is inhibited by phosphoinositide binding, and we found that phosphoinositide binding is pH-dependent for wild-type cofilin, with decreased binding at a higher pH.	Phosphatidylinositols	77-93	cofilin 1	Homo sapiens	132-139	
19029335-7	2008	In contrast, phosphoinositide binding by cofilin-H133A is attenuated and pH insensitive.	Phosphatidylinositols	13-29	cofilin 1	Homo sapiens	41-48	
12451591-0	2003	Products of phosphoinositide specific phospholipase C can trigger dephosphorylation of cofilin in chemoattractant stimulated neutrophils.	Phosphatidylinositols	12-28	cofilin 1	Homo sapiens	87-94	
2160454-0	1990	Inhibition of the interactions of cofilin, destrin, and deoxyribonuclease I with actin by phosphoinositides.	Phosphatidylinositols	90-107	cofilin 1	Homo sapiens	34-41