PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
1420910-9	1992	The sliding velocities of actin over copolymers of modified and unmodified myosins in the motility assay were slowest with rigor-modified myosin and most rapid with SH2-labeled myosin.	copolymers	37-47	myosin heavy chain 14	Homo sapiens	75-81	
1420910-9	1992	The sliding velocities of actin over copolymers of modified and unmodified myosins in the motility assay were slowest with rigor-modified myosin and most rapid with SH2-labeled myosin.	copolymers	37-47	myosin heavy chain 14	Homo sapiens	138-144	
3500954-2	1987	The stability of copolymers of phosphorylated and dephosphorylated myosin was, however, unknown.	copolymers	17-27	myosin heavy chain 14	Homo sapiens	67-73	
3500954-4	1987	Copolymers were typically formed by dialyzing monomeric mixtures into filament-forming buffer but, unexpectedly, could also be formed within minutes of mixing preformed rod and myosin minifilaments.	copolymers	0-10	myosin heavy chain 14	Homo sapiens	177-183	
3685024-3	1987	This observation provides a possible explanation for the behavior of copolymers of dephosphorylated and phosphorylated myosin in the presence of nucleotide.	copolymers	69-79	myosin heavy chain 14	Homo sapiens	119-125	
22643837-7	2012	Copolymers of WT and increasing amounts of the mutant actins led to a reduced stimulation of the myosin ATPase.	copolymers	0-10	myosin heavy chain 14	Homo sapiens	97-103	
28888060-5	2017	When we used a mixture of actin filaments and copolymers of actin and acto-S1dC, a chimeric protein of actin and the myosin motor domain, HMM-GFP preferentially formed clusters along the copolymers.	copolymers	46-56	myosin heavy chain 14	Homo sapiens	117-123