PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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 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 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 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 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 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 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 19-23 myosin heavy chain 14 Homo sapiens 140-146 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 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 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 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