PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 17343998-1 2007 Methanol and ethanol are primarily metabolized through the alcohol dehydrogenase (ADH) system in adults. Methanol 0-8 aldo-keto reductase family 1 member A1 Homo sapiens 59-80 17343998-1 2007 Methanol and ethanol are primarily metabolized through the alcohol dehydrogenase (ADH) system in adults. Methanol 0-8 aldo-keto reductase family 1 member A1 Homo sapiens 82-85 11172179-2 2001 The inhibition of alcohol dehydrogenase is fundamental to the treatment of methanol poisoning. Methanol 75-83 aldo-keto reductase family 1 member A1 Homo sapiens 18-39 15578220-4 2005 Methanol is metabolised in the liver by alcohol dehydrogenase to the toxic metabolites formaldehyde and formic acid. Methanol 0-8 aldo-keto reductase family 1 member A1 Homo sapiens 40-61 15578220-6 2005 We report on the use of fomepizole (4-methylpyrazole),a new and potent inhibitor of alcohol dehydrogenase, in a 3-year-old boy after the intake of a toxic amount of methanol. Methanol 165-173 aldo-keto reductase family 1 member A1 Homo sapiens 84-105 16035197-1 2005 OBJECTIVE: Methanol is metabolized by alcohol dehydrogenase to formaldehyde, and further to formic acid, which is responsible for the toxicity in methanol poisoning. Methanol 11-19 aldo-keto reductase family 1 member A1 Homo sapiens 38-59 16035197-1 2005 OBJECTIVE: Methanol is metabolized by alcohol dehydrogenase to formaldehyde, and further to formic acid, which is responsible for the toxicity in methanol poisoning. Methanol 146-154 aldo-keto reductase family 1 member A1 Homo sapiens 38-59 16035197-2 2005 Fomepizole (4-methylpyrazole) is a potent competitive inhibitor of alcohol dehydrogenase and is used as an antidote to treat methanol poisonings. Methanol 125-133 aldo-keto reductase family 1 member A1 Homo sapiens 67-88 11327890-0 2001 Modeling the active site chemistry of liver alcohol dehydrogenase: mononuclear zinc methanol and N,N-dimethylformamide complexes of a nitrogen/sulfur ligand possessing an internal hydrogen bond donor. Methanol 84-92 aldo-keto reductase family 1 member A1 Homo sapiens 44-65 11172179-3 2001 We performed a multicenter study to evaluate fomepizole, an inhibitor of alcohol dehydrogenase, in the treatment of patients with methanol poisoning. Methanol 130-138 aldo-keto reductase family 1 member A1 Homo sapiens 73-94 34310047-0 2021 Low Temperature Methanol-Water Reforming over the Alcohol Dehydrogenase and Immobilized Ruthenium Complex. Methanol 16-24 aldo-keto reductase family 1 member A1 Homo sapiens 50-71 10782245-7 2000 This result reflected the inhibition of methanol oxidation by alcohol-dehydrogenase, when the plasma ethanol concentration was above 1 g.L-1. Methanol 40-48 aldo-keto reductase family 1 member A1 Homo sapiens 62-83 9806434-0 1998 In vitro studies of human alcohol dehydrogenase inhibition in the process of methanol and ethylene glycol oxidation. Methanol 77-85 aldo-keto reductase family 1 member A1 Homo sapiens 26-47 9730571-3 1998 Normal anion gap has been reported in some cases of concomitant methanol and ethanol ingestion, where the high serum levels of ethanol inhibited the metabolism of methanol by alcohol dehydrogenase. Methanol 64-72 aldo-keto reductase family 1 member A1 Homo sapiens 175-196 9730571-3 1998 Normal anion gap has been reported in some cases of concomitant methanol and ethanol ingestion, where the high serum levels of ethanol inhibited the metabolism of methanol by alcohol dehydrogenase. Methanol 163-171 aldo-keto reductase family 1 member A1 Homo sapiens 175-196 1776249-2 1991 Endogenously formed or consumed methanol is almost exclusively metabolized by alcohol dehydrogenase. Methanol 32-40 aldo-keto reductase family 1 member A1 Homo sapiens 78-99 11192467-6 2000 Although the roles of alcohol dehydrogenase inhibition with ethanol or fomepizole and hemodialysis are clear in the case of toxic ingestions of methanol and ethylene glycol, they remain poorly defined for butoxyethanol poisoning. Methanol 144-152 aldo-keto reductase family 1 member A1 Homo sapiens 22-43 9398786-1 1997 Treatment of human methanol poisoning with the alcohol dehydrogenase inhibitor, 4-methylpyrazole (fomepizole), has not been previously described. Methanol 19-27 aldo-keto reductase family 1 member A1 Homo sapiens 47-68 1759354-1 1991 The studies of peculiarities of aliphatic alcohol metabolism in etiopathogenesis of acute poisoning with methyl alcohol and ethilenglicol have shown that it was reasonable to apply the inhibitors of alcoholdehydrogenase as a specific antidote in emergency therapy. Methanol 105-119 aldo-keto reductase family 1 member A1 Homo sapiens 199-219 2053487-0 1991 Kinetics and mechanism of methanol and formaldehyde interconversion and formaldehyde oxidation catalyzed by liver alcohol dehydrogenase. Methanol 26-34 aldo-keto reductase family 1 member A1 Homo sapiens 114-135 34310047-6 2021 We employ the alcohol dehydrogenase (ADH) and coenzyme I (NAD + ) for methanol catalytic dehydrogenation at low temperature, which could generate formaldehyde and reductive coenzyme I (NADH). Methanol 70-78 aldo-keto reductase family 1 member A1 Homo sapiens 14-35 34310047-6 2021 We employ the alcohol dehydrogenase (ADH) and coenzyme I (NAD + ) for methanol catalytic dehydrogenation at low temperature, which could generate formaldehyde and reductive coenzyme I (NADH). Methanol 70-78 aldo-keto reductase family 1 member A1 Homo sapiens 37-40 26551875-1 2016 The alcohols, methanol, ethylene glycol and diethylene glycol, have many features in common, the most important of which is the fact that the compounds themselves are relatively non-toxic but are metabolized, initially by alcohol dehydrogenase, to various toxic intermediates. Methanol 14-22 aldo-keto reductase family 1 member A1 Homo sapiens 222-243 34141419-4 2021 Discussion: Methanol is usually rapidly absorbed after ingestion and metabolized by alcohol dehydrogenase (ADH), then distributed to the body water to reach a volume distribution approximately equal to 0.77 L/kg. Methanol 12-20 aldo-keto reductase family 1 member A1 Homo sapiens 84-105 34141419-4 2021 Discussion: Methanol is usually rapidly absorbed after ingestion and metabolized by alcohol dehydrogenase (ADH), then distributed to the body water to reach a volume distribution approximately equal to 0.77 L/kg. Methanol 12-20 aldo-keto reductase family 1 member A1 Homo sapiens 107-110 33539811-0 2021 A novel metabolic disorder in the degradation pathway of endogenous methanol due to a mutation in the gene of alcohol dehydrogenase. Methanol 68-76 aldo-keto reductase family 1 member A1 Homo sapiens 110-131 33539811-1 2021 BACKGROUND: A small amount of methanol is produced endogenously in the human body but it is efficiently metabolized by alcohol dehydrogenase (ADH) and other enzymes, and the products eliminated without harm. Methanol 30-38 aldo-keto reductase family 1 member A1 Homo sapiens 119-140 33539811-1 2021 BACKGROUND: A small amount of methanol is produced endogenously in the human body but it is efficiently metabolized by alcohol dehydrogenase (ADH) and other enzymes, and the products eliminated without harm. Methanol 30-38 aldo-keto reductase family 1 member A1 Homo sapiens 142-145 30360499-3 2018 In recent work we have also shown that the use of alcohol dehydrogenase enzyme as a component of the anodic section of a direct catalytic methanol (or ethanol) fuel cell significantly improves the performance of a simple DMFC device, making it more suitable to measure ethanol (or methanol) in real samples by this cell. Methanol 138-146 aldo-keto reductase family 1 member A1 Homo sapiens 50-71 30360499-3 2018 In recent work we have also shown that the use of alcohol dehydrogenase enzyme as a component of the anodic section of a direct catalytic methanol (or ethanol) fuel cell significantly improves the performance of a simple DMFC device, making it more suitable to measure ethanol (or methanol) in real samples by this cell. Methanol 281-289 aldo-keto reductase family 1 member A1 Homo sapiens 50-71 34247144-15 2021 Both treatments work by blocking the metabolism of methanol by liver alcohol dehydrogenase (ADH). Methanol 51-59 aldo-keto reductase family 1 member A1 Homo sapiens 92-95 3056073-1 1988 4-Methylpyrazole (4-MP), an inhibitor of alcohol dehydrogenase, is a possible future drug for the treatment of methanol and ethylene glycol intoxications and the severe ethanol-disulfiram reaction. Methanol 111-119 aldo-keto reductase family 1 member A1 Homo sapiens 41-62 172084-0 1975 Human liver alcohol dehydrogenase--inhibition of methanol activity by pyrazole, 4-methylpyrazole, 4-hydroxymethylpyrazole and 4-carboxypyrazole. Methanol 49-57 aldo-keto reductase family 1 member A1 Homo sapiens 12-33 14469361-0 1962 Comments on a recent publication by Kini and Cooper which purports to show that alcohol dehydrogenase is responsible for the physiological oxidation of methanol. Methanol 152-160 aldo-keto reductase family 1 member A1 Homo sapiens 80-101 31214899-1 2019 Fomepizole is used as an antidote to treat methanol poisoning due to its selectivity towards alcohol dehydrogenase. Methanol 43-51 aldo-keto reductase family 1 member A1 Homo sapiens 93-114 26915245-6 2016 Fomepizole is the antidote for methanol and ethyleneglycol, blocking alcohol dehydrogenase. Methanol 31-39 aldo-keto reductase family 1 member A1 Homo sapiens 69-90 26208080-6 2015 Alcohol dehydrogenase (EC 1.1.1.1), able to catalyze the conversion of formaldehyde into methanol, was selected as the model enzyme. Methanol 89-97 aldo-keto reductase family 1 member A1 Homo sapiens 0-21 23529657-1 2013 Alcohol dehydrogenase (ADH) catalyzes the final step in the biosynthesis of methanol from CO2. Methanol 76-84 aldo-keto reductase family 1 member A1 Homo sapiens 0-21 23529657-1 2013 Alcohol dehydrogenase (ADH) catalyzes the final step in the biosynthesis of methanol from CO2. Methanol 76-84 aldo-keto reductase family 1 member A1 Homo sapiens 23-26 23529657-7 2013 In the direction of formaldehyde reduction, ADH has an ordered kinetic mechanism with formaldehyde adding to enzyme first and product methanol released last. Methanol 134-142 aldo-keto reductase family 1 member A1 Homo sapiens 44-47