PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
29058294-7	2017	from a tryptophan codon (TAT) to a histidine codon (CAT).	Histidine	35-44	catalase	Homo sapiens	52-55	
12142-1	1976	V. Ethoxyformylation of histidine and tyrosine residues of catalase with diethylpyrocarbonate.	Histidine	24-33	catalase	Homo sapiens	59-67	
12142-2	1976	In order to elucidate the possible roles of histidine and tyrosine residues of catalase [EC 1.11.1.6] in maintaining the quaternary structure and catalatic activity, diethylpyrocarbonate modification experiments were carried out.	Histidine	44-53	catalase	Homo sapiens	79-87	
12142-8	1976	More EF-His residues were formed by the reaction of diethyl pyrocarbonate with cyanoethylated (CE)-catalase monomer (subunit) than with CE-catalase tetramer.	Histidine	8-11	catalase	Homo sapiens	99-107	
12142-8	1976	More EF-His residues were formed by the reaction of diethyl pyrocarbonate with cyanoethylated (CE)-catalase monomer (subunit) than with CE-catalase tetramer.	Histidine	8-11	catalase	Homo sapiens	139-147	
28409923-0	2017	The Catalase Activity of Catalase-Peroxidases Is Modulated by Changes in the pKa of the Distal Histidine.	Histidine	95-104	catalase	Homo sapiens	4-12	
28409923-0	2017	The Catalase Activity of Catalase-Peroxidases Is Modulated by Changes in the pKa of the Distal Histidine.	Histidine	95-104	catalase	Homo sapiens	25-33	
24412336-4	2014	Some amino acids namely arginine, glycine and histidine showed good retention of catalase functionality after spray drying and subsequent storage stress.	Histidine	46-55	catalase	Homo sapiens	81-89	
8205256-4	1994	Sequence analysis of the coding exons of the androgen receptor gene from the patients revealed a single nucleotide substitution at position 2881 in exon G, resulting in the conversion of arginine (CGT) to histidine (CAT) at amino acid position 840 in the hormone-binding domain of the androgen receptor.	Histidine	205-214	catalase	Homo sapiens	216-219	
23871971-6	2013	The change in the relative position of His 74 to heme induced by the variation of secondary structure is considered to be the major reason for the reduction of CAT activity.	Histidine	39-42	catalase	Homo sapiens	160-163	
19199251-5	2009	RESULTS: A missense mutation of GAT>CAT was identified at codon 1441 of the COL1A1 gene from the family, which resulted in the replacement of aspartic acid by histidine (D1441H).	Histidine	159-168	catalase	Homo sapiens	36-39	
16417235-8	2006	UVA irradiation of low phototype reconstructed epidermis and of U937 through synthetic pheomelanin induced a modification in the electrophoretic properties of native catalase, which was counteracted by histidine, a quencher of singlet oxygen.	Histidine	202-211	catalase	Homo sapiens	166-174	
16450583-5	2006	The mutation of codon 840 CGT (arginine) to CAT (histidine) of AR gene led to the infertility in the patients.	Histidine	49-58	catalase	Homo sapiens	44-47	
16450583-7	2006	The clinical phenotype of theirs presented more deleteriously than and different from the one reported before, though they had the same mutation of codon 840 CGT (arginine) to CAT (histidine) of AR gene, which was very different from the mutation of 840 CGT (arginine) to TGT (cysteine) at the same codon.	Histidine	181-190	catalase	Homo sapiens	176-179	
8593088-10	1995	The catalase photoinactivation by tetracycline was not eliminated by L-histidine or comparatively high concentrations of mannitol but was entirely eliminated by ethanol used in relatively low concentrations.	Histidine	69-80	catalase	Homo sapiens	4-12	
16513636-4	2006	A close look at the hydrogen-bonding possibilities around the distal His in cAOS suggested that the imidazole ring is rotated by 180 degrees relative to that of catalase because of the hydrogen bond between Thr-66 and the distal His-67.	Histidine	69-72	catalase	Homo sapiens	161-169	
16513636-4	2006	A close look at the hydrogen-bonding possibilities around the distal His in cAOS suggested that the imidazole ring is rotated by 180 degrees relative to that of catalase because of the hydrogen bond between Thr-66 and the distal His-67.	Histidine	229-232	catalase	Homo sapiens	161-169	
16309371-15	2005	These are close to amino acids that are important for the binding of heme to catalase, 44 (Val) and 72-75 (Arg, Val, Val, His).	Histidine	122-125	catalase	Homo sapiens	77-85	
11270626-5	2001	The TEMPONE signal intensity was weakened significantly in the presence of beta-carotene and histidine in a concentration-dependent manner, but was not at all decreased by mannitol, Mn-superoxide dismutase and catalase.	Histidine	93-102	catalase	Homo sapiens	210-218	
9189046-3	1997	A point mutation was identified in all of them at position 101 of the gene for alpha-TTP, where histidine (CAT) was replaced with glutamine (CAG).	Histidine	96-105	catalase	Homo sapiens	107-110	
7566022-8	1995	RESULTS: The patient was homozygous for a point mutation that replaces histidine (CAT) with glutamine (CAG) at position 101 of the gene for the alpha-tocopherol-transfer protein.	Histidine	71-80	catalase	Homo sapiens	82-85	
8400271-7	1993	We detected the in-frame deletion of the trinucleotide CAT, encoding histidine 469, two amino acid residues to the N-terminal side of the abnormal proteolytic cleavage site between residues 470 and 471.	Histidine	69-78	catalase	Homo sapiens	55-58	
7913773-5	1994	Further analysis of the father and members of other arms of the kindred revealed a different mutation (C insertion: CAT-->CCAT), resulting in a frameshift beginning at amino acid #107 (His-->Pro) and truncation of the protein at codon #119 of the mature protein.	Histidine	185-188	catalase	Homo sapiens	116-119	
7866410-0	1994	Marked zinc activation of ester hydrolysis by a mutation, 67-His (CAT) to Arg (CGT), in the active site of human carbonic anhydrase I.	Histidine	61-64	catalase	Homo sapiens	66-69	
2349545-1	1990	I: Impaired heparin binding caused by an Arg47 to his (CGT to CAT) substitution.	Histidine	50-53	catalase	Homo sapiens	62-65