PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
10496983-3	1999	A similar lack of modification was also found in actin from the yeast Candida albicans, while rabbit muscle actin revealed the expected 3-methylhistidine residue.	3-methylhistidine	136-153	actin	Oryctolagus cuniculus	108-113	
1446680-10	1992	In methylation experiments employing the fusion actin in the form of inclusion bodies, 3-methylhistidine is the major product, as is the case when soluble muscle or non-muscle actin is used.	3-methylhistidine	87-104	actin	Oryctolagus cuniculus	48-53	
1446680-10	1992	In methylation experiments employing the fusion actin in the form of inclusion bodies, 3-methylhistidine is the major product, as is the case when soluble muscle or non-muscle actin is used.	3-methylhistidine	87-104	actin	Oryctolagus cuniculus	176-181	
4249861-0	1970	Biological activity and the 3-methylhistidine content of actin and myosin.	3-methylhistidine	28-45	actin	Oryctolagus cuniculus	57-62	
4249861-5	1970	The 3-methylhistidine content of actin was similar in all of the types of muscle from which it was isolated.	3-methylhistidine	4-21	actin	Oryctolagus cuniculus	33-38	
4249861-7	1970	The 3-methylhistidine of rabbit actin is localized in a single tryptic peptide that was readily modified during fractionation procedures.	3-methylhistidine	4-21	actin	Oryctolagus cuniculus	32-37	
4249861-11	1970	During photooxidation G-actin lost completely the ability to polymerize to the F form before all the 3-methylhistidine was destroyed.	3-methylhistidine	101-118	actin	Oryctolagus cuniculus	24-29