PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
6509022-2	1984	Upon binding of cofilin, the fluorescence of pyrene-labeled actin under polymerizing conditions is changed into the monomer form, irrespective of whether cofilin is added to actin before or after polymerization.	pyrene	45-51	cofilin 1	Homo sapiens	16-23	
2753044-4	1989	The hexapeptides, DIKKKL and DAIKKL, also inhibited the binding of cofilin to F-actin and affected the fluorescence intensity of pyrene-labeled F-actin and the rate of actin polymerization, like the heptapeptide.	pyrene	129-135	cofilin 1	Homo sapiens	67-74	
26842224-2	2016	The filaments of the fusion protein were functionally similar to actin filaments bound with cofilin in that they did not bind rhodamine-phalloidin, had quenched fluorescence of pyrene attached to Cys374 and showed enhanced susceptibility of the DNase loop to cleavage by subtilisin.	pyrene	177-183	cofilin 1	Homo sapiens	92-99	
29463680-8	2018	Our results indicate that cofilin-induced changes in filament twist propagate only 1-2 subunits from the boundary into the bare actin segment, independently of the boundary polarity (i.e. irrespective of whether or not the bare actin segment flanks the pointed or barbed-end side of the boundary) and the pyrene fluorophore labeling of actin.	pyrene	305-311	cofilin 1	Homo sapiens	26-33	
15670604-1	2005	I have monitored equilibrium binding of human cofilin to rabbit skeletal muscle (alpha) and human non-muscle (85% beta, 15% gamma) actin filaments from the quenching of pyrene actin fluorescence.	pyrene	169-175	cofilin 1	Homo sapiens	46-53	
12023237-5	2002	Saturation binding of cofilin prevents pyrene fluorescence enhancement normally associated with actin polymerization.	pyrene	39-45	cofilin 1	Homo sapiens	22-29