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Aldo-keto reductase family 1, member A1

Alcohol Dehydrogenase
Top mentioned proteins: CAN, Alcohol Dehydrogenase, ACID, HAD, AGE
Papers on Alcohol Dehydrogenase
Efficient PCR-Based Amplification of Diverse Alcohol Dehydrogenase Genes from Metagenomes for Improving Biocatalysis: Screening of Gene-Specific Amplicons from Metagenomes.
Kurokawa et al., Toyama, Japan. In Appl Environ Microbiol, 15 Nov 2014
We used this approach to isolate alcohol dehydrogenase (adh) genes from metagenomes based on the Leifsonia species adh gene (lsadh), the enzyme product of which can produce various chiral alcohols.
The Activity of Alcohol Dehydrogenase (ADH) Isoenzymes and Aldehyde Dehydrogenase (ALDH) in the Sera of Patients with Brain Cancer.
Szmitkowski et al., BiaƂystok, Poland. In Neurochem Res, 10 Nov 2014
UNLABELLED: Human brain tissue contains various alcohol dehydrogenase (ADH) isoenzymes and possess also aldehyde dehydrogenase (ALDH) activity.
Engineering of Highly Selective Variants of Parvibaculum lavamentivorans Alcohol Dehydrogenase.
Leggewie et al., Monheim, Germany. In Chembiochem, 22 Oct 2014
We present the development of highly selective variants of the Parvibaculum lavamentivorans alcohol dehydrogenase.
Structural Studies of Cinnamoyl-CoA Reductase and Cinnamyl-Alcohol Dehydrogenase, Key Enzymes of Monolignol Biosynthesis.
Wang et al., Ardmore, United States. In Plant Cell, 12 Oct 2014
UNLABELLED: The enzymes cinnamoyl-CoA reductase (CCR) and cinnamyl alcohol dehydrogenase (CAD) catalyze the two key reduction reactions in the conversion of cinnamic acid derivatives into monolignol building blocks for lignin polymers in plant cell walls.
Enantiocomplementary Yarrowia lipolytica Oxidoreductases: Alcohol Dehydrogenase 2 and Short Chain Dehydrogenase/Reductase.
Winkler et al., Graz, Austria. In Biomolecules, 2012
Herein, we cloned and overexpressed the Zn-dependent alcohol dehydrogenase ADH2 from Yarrowia lipolytica in Escherichia coli.
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.
[Possible interaction between ethanol and drugs and their significance for drug therapy in the elderly].
Lesch et al., Vienna, Austria. In Wien Klin Wochenschr, 2001
Alcohol dehydrogenase (ADH), acetaldehydede hydrogenase (ALDH) and cytochrome P450 2E1 are the enzymes responsible for the metabolism of ethanol.
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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