PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
6436641-0	1984	Methylated lysines and 3-methylhistidine in myosin: tissue and developmental differences.	3-methylhistidine	23-40	myosin heavy chain 14	Homo sapiens	44-50	
6774077-3	1980	Three-methylhistidine (3MH), an unusual amino acid found in actin and myosin, is not further metabolized and is quantitatively excreted following muscle degradation.	3-methylhistidine	23-26	myosin heavy chain 14	Homo sapiens	70-76	
6780020-1	1981	Urinary excretion of the post-translationally modified amino-acid 3-methylhistidine, derived from the contractile proteins actin and myosin, was measured in patients with conditions associated with nitrogen loss.	3-methylhistidine	66-83	myosin heavy chain 14	Homo sapiens	133-139	
7192806-1	1980	3-Methylhistidine (3-MH) excretion reflects the rate of muscle protein catabolism, since 3-MH occurs almost exclusively in muscle actin and myosin and is not reutilized or catabolized.	3-methylhistidine	0-17	myosin heavy chain 14	Homo sapiens	140-146	
7192806-1	1980	3-Methylhistidine (3-MH) excretion reflects the rate of muscle protein catabolism, since 3-MH occurs almost exclusively in muscle actin and myosin and is not reutilized or catabolized.	3-methylhistidine	19-23	myosin heavy chain 14	Homo sapiens	140-146	
4241475-0	1969	Distribution and biological role of 3-methyl-histidine in actin and myosin.	3-methylhistidine	36-54	myosin heavy chain 14	Homo sapiens	68-74	
350635-1	1978	Actin and myosin, the contractile proteins of skeletal muscle, are methylated following peptide bond synthesis, with production of Ntau-methylhistidine (3-methylhistidine, 3-MeHis).	3-methylhistidine	131-151	myosin heavy chain 14	Homo sapiens	10-16	
350635-1	1978	Actin and myosin, the contractile proteins of skeletal muscle, are methylated following peptide bond synthesis, with production of Ntau-methylhistidine (3-methylhistidine, 3-MeHis).	3-methylhistidine	153-170	myosin heavy chain 14	Homo sapiens	10-16	
350635-1	1978	Actin and myosin, the contractile proteins of skeletal muscle, are methylated following peptide bond synthesis, with production of Ntau-methylhistidine (3-methylhistidine, 3-MeHis).	3-methylhistidine	172-179	myosin heavy chain 14	Homo sapiens	10-16	
2050768-1	1991	A method is described for the determination of the 3-methylhistidine content in myofibrilar proteins (myosin and actin) using reversed-phase high-performance liquid chromatography with ultraviolet detection.	3-methylhistidine	51-68	myosin heavy chain 14	Homo sapiens	102-108	
2050768-4	1991	This method allows the detection of picomole amounts of 3-methylhistidine in myosin and actin.	3-methylhistidine	56-73	myosin heavy chain 14	Homo sapiens	77-83	
1702054-2	1990	A comparison of the steady-state turnover of RNA and the proteins actin plus myosin (determined using urinary 3-methylhistidine) in preterm infants and adults showed that preterm infants have about 3 times higher average turnover rates per unit body weight than adults of tRNA and rRNA as well as of actin plus myosin, whereas calculated mRNA turnover was 6 times higher in preterm infants than in adults.	3-methylhistidine	110-127	myosin heavy chain 14	Homo sapiens	77-83	
35234930-2	2022	3-methylhistidine (3-MH) is the by-product of actin and myosin degradation reflecting skeletal muscle turnover.	3-methylhistidine	0-17	myosin heavy chain 14	Homo sapiens	56-62	
35234930-2	2022	3-methylhistidine (3-MH) is the by-product of actin and myosin degradation reflecting skeletal muscle turnover.	3-methylhistidine	19-23	myosin heavy chain 14	Homo sapiens	56-62