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Aldo-keto reductase family 1, member A1

Alcohol Dehydrogenase
Top mentioned proteins: CAN, Alcohol Dehydrogenase, HAD, ACID, AGE
Papers on Alcohol Dehydrogenase
Increasing Anaerobic Acetate Consumption and Ethanol Yields in Saccharomyces cerevisiae with NADPH-Specific Alcohol Dehydrogenase.
Zelle et al., United States. In Appl Environ Microbiol, 01 Jan 2016
However, the original metabolic pathway devised to convert acetate to ethanol uses NADH-specific acetylating acetaldehyde dehydrogenase and alcohol dehydrogenase and quickly becomes constrained by limited NADH availability, even when glycerol formation is abolished.
Alcohol Dehydrogenase-1B (rs1229984) and Aldehyde Dehydrogenase-2 (rs671) Genotypes and Alcoholic Ketosis Are Associated with the Serum Uric Acid Level in Japanese Alcoholic Men.
Maruyama et al., Saitama, Japan. In Alcohol Alcohol, 04 Dec 2015
AIMS: To identify determinants of hyperuricemia in alcoholics.
Slowed Diffusion and Excluded Volume Both Contribute to the Effects of Macromolecular Crowding on Alcohol Dehydrogenase Steady-State Kinetics.
Slade et al., New York City, United States. In Biochemistry, 29 Oct 2015
Dextran has a weaker effect on the Michaelis-Menten kinetic parameters of yeast alcohol dehydrogenase (YADH) than its small molecule counterpart, glucose.
Genetic susceptibility factors for alcohol-induced chronic pancreatitis.
Simon et al., Greifswald, Germany. In Pancreatology, Jul 2015
Smaller studies in ethnically defined populations have found that not only polymorphism in proteins involved in the metabolism of ethanol, such as Alcohol Dehydrogenase and Aldehyde Dehydrogenase, can confer a risk for developing chronic pancreatitis but also mutations that had previously been reported in association with idiopathic pancreatitis, such as SPINK1 mutations.
Enhanced Stability and Reusability of Alcohol Dehydrogenase Covalently Immobilized on Magnetic Graphene Oxide Nanocomposites.
Chen et al., In J Nanosci Nanotechnol, Feb 2015
In this study, Magnetic GO (MGO) nanocomposites were synthesized according to covalent binding of amino Fe3O4 nanoparticles onto the GO surface and the as-made nanocomposites were successfully applied as supports for the immobilization of alcohol dehydrogenase (ADH).
Impact of multiple Alcohol Dehydrogenase gene polymorphisms on risk of laryngeal, esophageal, gastric and colorectal cancers in Chinese Han population.
Jin et al., Xi'an, China. In Am J Cancer Res, Dec 2014
Previous study had identified several single nucleotide polymorphisms (SNPs) of Alcohol Dehydrogenase (ADH) genes associated with UADT cancers in European and Japanese populations.
Natural alcohol exposure: is ethanol the main substrate for alcohol dehydrogenases in animals?
Riveros-Rosas et al., Mexico. In Chem Biol Interact, 2011
Alcohol dehydrogenase (ADH) activity is widely distributed in all phyla.
Polymorphism of ethanol-metabolism genes and alcoholism: correlation of allelic variations with the pharmacokinetic and pharmacodynamic consequences.
Yin et al., Taipei, Taiwan. In Chem Biol Interact, 2009
Alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) are the principal enzymes responsible for metabolism of ethanol.
[Alcohol dehydrogenase and aldehyde dehydrogenase in malignant diseases--Part II].
Szmitkowski et al., In Pol Merkur Lekarski, 2008
Heavy alcohol consumption is associated with increased risk of cancers including digestive tract, liver, pancreas, colorectum and breast.
Sub1A is an ethylene-response-factor-like gene that confers submergence tolerance to rice.
Mackill et al., Davis, United States. In Nature, 2006
japonica conferred enhanced tolerance to the plants, downregulation of Sub1C and upregulation of Alcohol dehydrogenase 1 (Adh1), indicating that Sub1A-1 is a primary determinant of submergence tolerance.
Influence of genetic variations of ethanol-metabolizing enzymes on phenotypes of alcohol-related disorders.
Mochizuki et al., Yokosuka, Japan. In Ann N Y Acad Sci, 2004
Alcohol dehydrogenase (ADH) and aldehyde dehydrogenase-2 (ALDH2) play central roles in the metabolism of ethanol and its metabolite, acetaldehyde, in the liver.
Cosuppression of nonhomologous transgenes in Drosophila involves mutually related endogenous sequences.
Birchler et al., Columbia, United States. In Cell, 1999
Here we demonstrate that two nonhomologous reciprocal fusion genes, white-Alcohol dehydrogenase (w-Adh) and Adh-w, exhibit cosuppression using the endogenous Adh sequence as an intermediary.
Cosuppression in Drosophila: gene silencing of Alcohol dehydrogenase by white-Adh transgenes is Polycomb dependent.
Birchler et al., Columbia, United States. In Cell, 1997
When two to six copies of a white promoter-Alcohol dehydrogenase (Adh) reporter fusion gene are introduced into the genome, the expression is progressively reduced both in larvae and adults rather than the expected gene dosage effect.
A molecular basis for heterosis.
Laughner et al., In Science, 1969
Alcohol dehydrogenase allodimers composed of an unstable active subunit and a stable but inactive subunit are both active and stable.
Alcohol Dehydrogenase in Drosophila melanogaster: Isozymes and Genetic Variants.
Murphy et al., In Science, 1965
Alcohol dehydrogenase, in Drosophila melanogaster homozygous for the alleles Adh(F) or Adh(S), is found in three electrophoretically different forms.
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