PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8223953-2	1993	When [32P]orthophosphate-labelled human neutrophils were treated with C. botulinum C2 toxin, [32P]ADP-ribosylated gelsolin-actin was precipitated with anti-gelsolin antibody.	Phosphates	10-24	gelsolin	Homo sapiens	114-122	
8617730-0	1996	Binding of phosphate, aluminum fluoride, or beryllium fluoride to F-actin inhibits severing by gelsolin.	Phosphates	11-20	gelsolin	Homo sapiens	95-103	
8617730-3	1996	We examined whether the enrichment of phosphate on filamentous ADP-actin might modulate the severing activity of gelsolin, a protein previously shown to bind differently to ATP and ADP actin monomers.	Phosphates	38-47	gelsolin	Homo sapiens	113-121	
8617730-4	1996	Binding of phosphate, or the phosphate analogs aluminum fluoride and beryllium fluoride, to actin filaments reduces their susceptibility to severing by gelsolin.	Phosphates	11-20	gelsolin	Homo sapiens	152-160	
8617730-4	1996	Binding of phosphate, or the phosphate analogs aluminum fluoride and beryllium fluoride, to actin filaments reduces their susceptibility to severing by gelsolin.	Phosphates	29-38	gelsolin	Homo sapiens	152-160	
8223953-2	1993	When [32P]orthophosphate-labelled human neutrophils were treated with C. botulinum C2 toxin, [32P]ADP-ribosylated gelsolin-actin was precipitated with anti-gelsolin antibody.	Phosphates	10-24	gelsolin	Homo sapiens	156-164	
1645651-1	1991	Binding of biological phosphate compounds to actin was investigated by the effect of these compounds on the critical concentration of the pointed ends of gelsolin-capped actin filaments.	Phosphates	22-31	gelsolin	Homo sapiens	154-162	
3607065-3	1987	Phosphate has an almost identical effect on the critical monomer concentration of the pointed ends of gelsolin-capped actin filaments in the presence of ATP.	Phosphates	0-9	gelsolin	Homo sapiens	102-110