PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15849248-5	2005	In YQR deoxy myoglobin, the mutated Gln(E7)64 is stably H-bonded with the mutated Tyr(B10)29.	Tyrosine	82-85	myoglobin	Physeter catodon	13-22	
1315742-3	1992	Site-specific mutagenesis has been used to prepare all the possible tyrosine----phenylalanine mutants of the recombinant myoglobin, including the three single mutants at Tyr-103, -146, and -151, the three double mutants, and the triple mutant.	Tyrosine	170-173	myoglobin	Physeter catodon	121-130	
15749393-6	2005	Interestingly, formation of the myoglobin dimer, which is known to be formed primarily by cross-linkage of tyrosine-151, was inhibited by the addition of DMPO.	Tyrosine	107-115	myoglobin	Physeter catodon	32-41	
10681426-1	2000	We determined the structure of the photolytic intermediate of a sperm whale myoglobin (Mb) mutant called Mb-YQR [Leu-(B10)-->Tyr; His(E7)-->Gln; Thr(E10)-->Arg] to 1.4-A resolution by ultra-low temperature (20 K) x-ray diffraction.	Tyrosine	128-131	myoglobin	Physeter catodon	76-85	
7757198-5	1995	Since the suicidal interaction of myoglobin with H2O2 forms unstable tyrosine radicals, we suggest that the increased activity of myoglobin on myosin results from an efficient electron transfer between surface tyrosines of myosin and myoglobin but not horseradish peroxidase.	Tyrosine	210-219	myoglobin	Physeter catodon	34-43	
7757198-5	1995	Since the suicidal interaction of myoglobin with H2O2 forms unstable tyrosine radicals, we suggest that the increased activity of myoglobin on myosin results from an efficient electron transfer between surface tyrosines of myosin and myoglobin but not horseradish peroxidase.	Tyrosine	210-219	myoglobin	Physeter catodon	130-139	
7757198-5	1995	Since the suicidal interaction of myoglobin with H2O2 forms unstable tyrosine radicals, we suggest that the increased activity of myoglobin on myosin results from an efficient electron transfer between surface tyrosines of myosin and myoglobin but not horseradish peroxidase.	Tyrosine	210-219	myoglobin	Physeter catodon	130-139	
7757198-6	1995	These conclusions were supported by evidence that sperm whale myoglobin, which contains two active tyrosines--the heme-adjacent (tyrosine-103) and the surface (tyrosine-151), is more active as a mediator of myosin peroxidation than horse heart myoglobin which is devoid of the surface tyrosine.	Tyrosine	99-108	myoglobin	Physeter catodon	62-71	
7757198-6	1995	These conclusions were supported by evidence that sperm whale myoglobin, which contains two active tyrosines--the heme-adjacent (tyrosine-103) and the surface (tyrosine-151), is more active as a mediator of myosin peroxidation than horse heart myoglobin which is devoid of the surface tyrosine.	Tyrosine	99-107	myoglobin	Physeter catodon	62-71	
7757198-6	1995	These conclusions were supported by evidence that sperm whale myoglobin, which contains two active tyrosines--the heme-adjacent (tyrosine-103) and the surface (tyrosine-151), is more active as a mediator of myosin peroxidation than horse heart myoglobin which is devoid of the surface tyrosine.	Tyrosine	129-137	myoglobin	Physeter catodon	62-71	
7757198-6	1995	These conclusions were supported by evidence that sperm whale myoglobin, which contains two active tyrosines--the heme-adjacent (tyrosine-103) and the surface (tyrosine-151), is more active as a mediator of myosin peroxidation than horse heart myoglobin which is devoid of the surface tyrosine.	Tyrosine	129-137	myoglobin	Physeter catodon	62-71	
8349589-0	1993	Kinetics of ligand binding to Pseudoterranova decipiens and Ascaris suum hemoglobins and to Leu-29-->Tyr sperm whale myoglobin mutant.	Tyrosine	104-107	myoglobin	Physeter catodon	120-129	
8349589-11	1993	A mutant of sperm whale myoglobin suggested by sequence alignment of the nematode hemoglobins, Leu-29-->Tyr, did not have kinetic properties similar to them.	Tyrosine	107-110	myoglobin	Physeter catodon	24-33	
8419357-0	1993	The roles of His-64, Tyr-103, Tyr-146, and Tyr-151 in the epoxidation of styrene and beta-methylstyrene by recombinant sperm whale myoglobin.	Tyrosine	21-24	myoglobin	Physeter catodon	131-140	
8419357-0	1993	The roles of His-64, Tyr-103, Tyr-146, and Tyr-151 in the epoxidation of styrene and beta-methylstyrene by recombinant sperm whale myoglobin.	Tyrosine	30-33	myoglobin	Physeter catodon	131-140	
8419357-0	1993	The roles of His-64, Tyr-103, Tyr-146, and Tyr-151 in the epoxidation of styrene and beta-methylstyrene by recombinant sperm whale myoglobin.	Tyrosine	30-33	myoglobin	Physeter catodon	131-140	
1315742-14	1992	The present studies show that the peroxide-generated myoglobin radical readily exchanges between remote loci, including non-tyrosine residues, but protein cross-linking only occurs when radical density is located on Tyr-151.	Tyrosine	124-132	myoglobin	Physeter catodon	53-62	
913393-2	1977	When compared with the high-spin acetate complex, ligands which cause a transition to the low-spin state also cause large perturbations of tyrosine(s) remote from the haem pocket in myoglobin but only minor perturbations of tryptophan (s) in leghaem calobin.	Tyrosine	139-147	myoglobin	Physeter catodon	182-191	
3182873-4	1988	The dityrosine content of the sperm whale myoglobin dimer shows that it is primarily held together by dityrosine cross-links, although more tyrosine residues are lost than are accounted for by dityrosine formation.	Tyrosine	6-14	myoglobin	Physeter catodon	42-51	
3182873-6	1988	The amino acid composition, amino acid sequence, and mass spectrum of the peptide show that cross-linking involves covalent bond formation between Tyr-103 of one myoglobin chain and Tyr-151 of the other.	Tyrosine	147-150	myoglobin	Physeter catodon	162-171	
3182873-6	1988	The amino acid composition, amino acid sequence, and mass spectrum of the peptide show that cross-linking involves covalent bond formation between Tyr-103 of one myoglobin chain and Tyr-151 of the other.	Tyrosine	182-185	myoglobin	Physeter catodon	162-171	
25392956-0	2015	A novel tyrosine-heme C-O covalent linkage in F43Y myoglobin: a new post-translational modification of heme proteins.	Tyrosine	8-16	myoglobin	Physeter catodon	51-60	
25392956-2	2015	We herein report a novel tyrosine-heme covalent C-O bond in an artificially produced sperm whale myoglobin (Mb) mutant, F43Y Mb, which formed spontaneously in vivo between the Tyr43 hydroxy group and the heme 4-vinyl group.	Tyrosine	25-33	myoglobin	Physeter catodon	97-106	
25392956-2	2015	We herein report a novel tyrosine-heme covalent C-O bond in an artificially produced sperm whale myoglobin (Mb) mutant, F43Y Mb, which formed spontaneously in vivo between the Tyr43 hydroxy group and the heme 4-vinyl group.	Tyrosine	25-33	myoglobin	Physeter catodon	108-110