PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
23207165-0	2013	Methanol teratogenicity in mutant mice with deficient catalase activity and transgenic mice expressing human catalase.	Methanol	0-8	catalase	Homo sapiens	54-62	
25723373-6	2015	Some enzymes (dehydrogenases, oxidase, and catalase) are valuable products with high conversion efficiencies and can generate methanol or sequester CO2 as formic acid ex vivo.	Methanol	126-134	catalase	Homo sapiens	30-51	
23207165-4	2013	hCat mice and WTs were similarly susceptible to MeOH-initiated ophthalmic abnormalities and cleft palates.	Methanol	48-52	catalase	Homo sapiens	0-4	
17343998-10	2007	In the perinatal infants, these results suggest that catalase may play a more prominent role in the metabolism of alcohols than does the ADH system and may explain the finding of first-order kinetics in case reports of high methanol and ethanol intoxication.	Methanol	224-232	catalase	Homo sapiens	53-61	
21295602-0	2011	Altered methanol embryopathies in embryo culture with mutant catalase-deficient mice and transgenic mice expressing human catalase.	Methanol	8-16	catalase	Homo sapiens	61-69	
16677702-1	2006	Effect of six organic solvents-methanol, ethanol, propanol, dimethyl sulphoxide (DMSO), N,N-dimethyl formamide (DMF), and glycerol on the conformation and interaction of catalase and anticatalase antibodies were studied with the aim of identifying the solvents in which antigen-antibody interactions are strong.	Methanol	31-39	catalase	Homo sapiens	170-178	
27314787-7	1993	The addition of H2O2 and catalase to the reaction system supplied molecular oxygen for methanol oxidation to formaldehyde by alcohol oxidase.	Methanol	87-95	catalase	Homo sapiens	16-33	
16618987-5	2006	However, at a low concentration of H2O2 and in the presence of a suitable hydrogen donor, e.g. ethanol, methanol, phenol, and others, catalase acts peroxidically, removing H2O2, but oxidizing its substrate (peroxidatic reaction).	Methanol	104-112	catalase	Homo sapiens	134-142	
17009246-6	2006	The activities of superoxide dismutase and catalase were decreased in the brain following methanol exposure, whereas in methanol- and ethanol-coexposed animals there was no significant effect on these enzymes as compared to methanol-exposed animals.	Methanol	90-98	catalase	Homo sapiens	43-51	
4452669-0	1974	Methanol oxidation in a reconstituted system of NADPH-cytochrome c reductase, catalase, and a factor from trypsin digested microsomes.	Methanol	0-8	catalase	Homo sapiens	78-86	
2680403-4	1989	Studies of rates of oxidation of butanol, a specific substrate for alcohol dehydrogenase, and methanol, a substrate for catalase, indicate that peroxidation via catalase supported by H2O2 formed by the peroxisomal beta-oxidation of fatty acids is the predominant pathway of alcohol oxidation in the fasted state.	Methanol	94-102	catalase	Homo sapiens	120-128	
2680403-4	1989	Studies of rates of oxidation of butanol, a specific substrate for alcohol dehydrogenase, and methanol, a substrate for catalase, indicate that peroxidation via catalase supported by H2O2 formed by the peroxisomal beta-oxidation of fatty acids is the predominant pathway of alcohol oxidation in the fasted state.	Methanol	94-102	catalase	Homo sapiens	161-169	
3019241-1	1986	Catalase is an enzyme which can function either in the catabolism of hydrogen peroxide or in the peroxidatic oxidation of small substrates such as ethanol, methanol, or elemental mercury (Hg0).	Methanol	156-164	catalase	Homo sapiens	0-8	
33773249-5	2021	However, excessive methanol (>5 mM) combined with BDE-47 had strong stress on microbial cells, including significant (p < 0.05) increase of reactive oxygen species level, superoxide dismutase activity, catalase activity and malondialdehyde content, even causing 20.65% cell apoptosis and 11.27% death.	Methanol	19-27	catalase	Homo sapiens	202-210	
34070837-6	2021	In HEK-293 cells, the MeOH extract possessed cellular antioxidant effects by attenuating hydrogen peroxide (H2O2)-induced ROS production and increasing catalase, glutathione peroxidase-1 (GPx-1), and glutathione reductase (GRe).	Methanol	22-26	catalase	Homo sapiens	152-160	
4089878-2	1985	In the present report, cyanamide was shown to inhibit the peroxidatic activity of catalase with alcohols such as ethanol or methanol.	Methanol	124-132	catalase	Homo sapiens	82-90	
4988806-0	1969	Role of the intracellular distribution of hepatic catalase in the peroxidative oxidation of methanol.	Methanol	92-100	catalase	Homo sapiens	50-58	
4972129-0	1968	Role of the intracellular distribution of hepatic catalase in the peroxidative oxidation of methanol.	Methanol	92-100	catalase	Homo sapiens	50-58	
31759263-6	2020	The kinetic data in methanol and buffered aqueous solutions correlate well with the results of the test of catalase activity, thus showing that the rate determining step in the catalytic cycle corresponds to the initial reaction of the complexes with H2O2.	Methanol	20-28	catalase	Homo sapiens	107-115