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T Ikuta et al.
Proceedings of the National Academy of Sciences of the United States of America, 83(3), 634-638 (1986-02-01)
Class I human alcohol dehydrogenase (ADH; alcohol:NAD+ oxidoreductase, EC 1.1.1.1) consists of several homo- and heterodimers of alpha, beta, and gamma subunits that are governed by the ADH1, ADH2, and ADH3 loci. We previously cloned a full length of cDNA
Brian J Gibbons et al.
Biochemistry, 43(39), 12555-12562 (2004-09-29)
Formamides are aldehyde analogues that have demonstrated potent and selective inhibition of human alcohol dehydrogenase isoenzymes. The alphaalpha, beta(1)beta(1), gamma(2)gamma(2), and sigmasigma isoforms have all been found to be strongly inhibited by substituted formamides. In this paper, the structure of
Kinetics and equilibria in the liver alcohol dehydrogenase system.
H THEORELL
Advances in enzymology and related subjects of biochemistry, 20, 31-49 (1958-01-01)
P Strömberg et al.
Biochemical and biophysical research communications, 278(3), 544-549 (2000-11-30)
The human ADH5 gene was reported to lack the last exon compared to other mammalian ADHs and consequently should be expressed as a truncated protein. Here we show with PCR amplification of 3'-cDNA ends that the ADH5 gene harbors the
Armando Moreno-Cermeño et al.
Biochimica et biophysica acta, 1833(12), 3326-3337 (2013-10-09)
Frataxin is a mitochondrial protein involved in iron metabolism whose deficiency in humans causes Friedreich ataxia. We performed transcriptomic and proteomic analyses of conditional Yeast Frataxin Homologue (Yfh1) mutants (tetO7-YFH1) to investigate metabolic remodeling upon Yfh1 depletion. These studies revealed
Thi Hong Tuoi Do et al.
Chemico-biological interactions, 206(2), 117-125 (2013-09-13)
The development of alcoholic liver diseases depends on the ability of hepatocyte to proliferate and differentiate in the case of alcohol-induced injury. Our previous work showed an inhibitory effect of alcohol on hepatocyte proliferation. However, the effect of alcohol on
M A Satre et al.
The Journal of biological chemistry, 269(22), 15606-15612 (1994-06-03)
A novel human alcohol dehydrogenase (ADH) gene called ADH7 has been characterized and determined to encode class IV ADH, an ADH isozyme which is very active as a retinol dehydrogenase. A nearly full-length cDNA for ADH7 was isolated from a
N B Gubergrits et al.
Terapevticheskii arkhiv, 86(2), 49-55 (2014-04-29)
To study the gene polymorphisms of alcohol dehydrogenase (ADH), aldehyde dehydrogenase (ALDH), and cytochrome CYP2E1 in patients with alcoholic chronic pancreatitis (ACP) and to compare them with laboratory and instrumental findings. Seventy-two patients with ACP and 80 healthy individuals were
Diya Alsafadi et al.
Extremophiles : life under extreme conditions, 17(1), 115-122 (2012-11-28)
The effect of various organic solvents on the catalytic activity, stability and substrate specificity of alchohol dehydrogenase from Haloferax volcanii (HvADH2) was evaluated. The HvADH2 showed remarkable stability and catalysed the reaction in aqueous-organic medium containing dimethyl sulfoxide (DMSO) and
Dong-hyuk Heo et al.
The Journal of biological chemistry, 288(51), 36676-36690 (2013-11-08)
The RNA polymerase II (RNApII) C-terminal domain (CTD)-interacting domain (CID) proteins are involved in two distinct RNApII termination pathways and recognize different phosphorylated forms of CTD. To investigate the role of differential CTD-CID interactions in the choice of termination pathway
M Yasunami et al.
Genomics, 7(2), 152-158 (1990-06-01)
The class I alcohol dehydrogenases (ADH; EC 1.1.1.1) play a key role in hepatic alcohol catabolism. Three human class I ADH genes, ADH1, ADH2, and ADH3, which encode the alpha, beta, and gamma subunits respectively, have been isolated and mapped
R Kaiser et al.
Biochemistry, 27(4), 1132-1140 (1988-02-23)
The primary structure of class III alcohol dehydrogenase (dimeric with chi subunits) from human liver has been determined by peptide analyses. The protein chain is a clearly distinct type of subunit distantly related to those of both human class I
M S Niederhut et al.
Protein science : a publication of the Protein Society, 10(4), 697-706 (2001-03-29)
In contrast with other animal species, humans possess three distinct genes for class I alcohol dehydrogenase and show polymorphic variation in the ADH1B and ADH1C genes. The three class I alcohol dehydrogenase isoenzymes share approximately 93% sequence identity but differ
Geetha Durairaj et al.
RNA (New York, N.Y.), 20(2), 133-142 (2013-12-12)
Mdm30, an F-box protein in yeast, has been recently shown to promote mRNA export. However, it remains unknown how Mdm30 facilitates mRNA export. Here, we show that Mdm30 targets the Sub2 component of the TREX (Transcription/Export) complex for ubiquitylation and
Peter Huppke et al.
Experimental neurology, 320, 112958-112958 (2019-05-28)
We identified a homozygous missense mutation in the gene encoding NAD synthesizing enzyme NMNAT2 in two siblings with childhood onset polyneuropathy with erythromelalgia. No additional homozygotes for this rare allele, which leads to amino acid substitution T94M, were present among
L O Hedén et al.
FEBS letters, 194(2), 327-332 (1986-01-06)
Three different size classes of cDNA clones coding for the beta 1-subunit of human alcohol dehydrogenase (ADH) were characterized from a human liver cDNA library. Clones were identified by hybridization with synthetic oligodeoxyribonucleotides. A total of 2530 nucleotides were determined
Jorge Correale et al.
Journal of immunology (Baltimore, Md. : 1950), 191(7), 3827-3837 (2013-08-27)
We recently demonstrated better outcomes in helminth-infected multiple sclerosis (MS) patients, compared with uninfected ones. The present study evaluates the role of TLR2 and retinoic acid (RA) in parasite-driven protection in MS patients. RA serum levels were significantly higher in
Jonathan Extance et al.
Acta crystallographica. Section D, Biological crystallography, 69(Pt 10), 2104-2115 (2013-10-09)
Bifunctional alcohol/aldehyde dehydrogenase (ADHE) enzymes are found within many fermentative microorganisms. They catalyse the conversion of an acyl-coenzyme A to an alcohol via an aldehyde intermediate; this is coupled to the oxidation of two NADH molecules to maintain the NAD(+)
B Holmquist et al.
Biochemistry, 32(19), 5139-5144 (1993-05-18)
Modification of class III alcohol dehydrogenase (chi chi-ADH) with phenylglyoxal eliminates fatty acid activation by pentanoate and octanoate and concomitantly increases specific activity toward ethanol and 3-methylcrotyl alcohol 2-3-fold. In contrast, chemical modification decreases activity toward S-(hydroxymethyl)glutathione (FDH activity) and
N Y Kedishvili et al.
The Journal of biological chemistry, 270(8), 3625-3630 (1995-02-24)
A full-length 1966-base pair clone of the human class IV alcohol dehydrogenase (sigma-ADH) was isolated from a human stomach cDNA library. The 373-amino acid sigma-ADH encoded by this cDNA was expressed in Escherichia coli. The specific activity of the recombinant
Ladeana W Hillier et al.
Nature, 434(7034), 724-731 (2005-04-09)
Human chromosome 2 is unique to the human lineage in being the product of a head-to-head fusion of two intermediate-sized ancestral chromosomes. Chromosome 4 has received attention primarily related to the search for the Huntington's disease gene, but also for
H von Bahr-Lindström et al.
Biochemistry, 25(9), 2465-2470 (1986-05-06)
Two cDNA clones for human liver alcohol dehydrogenase (ADH) were identified, together covering 1450 nucleotides that contain the cDNA sequence of the ADH1 locus and include a coding region of 1122 nucleotides for the alpha subunit of the enzyme. In
Sarah J Lewis et al.
PloS one, 7(11), e49407-e49407 (2012-11-21)
Observational studies have generated conflicting evidence on the effects of moderate maternal alcohol consumption during pregnancy on offspring cognition mainly reflecting problems of confounding. Among mothers who drink during pregnancy fetal alcohol exposure is influenced not only by mother's intake
Cláudio J R Frazão et al.
Scientific reports, 9(1), 11576-11576 (2019-08-11)
In this work, we describe the construction of a synthetic metabolic pathway enabling direct biosynthesis of 1,3-propanediol (PDO) from glucose via the Krebs cycle intermediate malate. This non-natural pathway extends a previously published synthetic pathway for the synthesis of (L)-2,4-dihydroxybutyrate
Vladimir Leskovac et al.
FEMS yeast research, 2(4), 481-494 (2003-04-19)
This review is a summary of our current knowledge of the structure, function and mechanism of action of the three zinc-containing alcohol dehydrogenases, YADH-1, YADH-2 and YADH-3, in baker's yeast, Saccharomyces cerevisiae. The opening section deals with the substrate specificity
Kavitha Swaminathan et al.
Life sciences, 92(6-7), 325-336 (2013-01-29)
Ethanol metabolism leads to the formation of acetaldehyde and malondialdehyde. Acetaldehyde and malondialdehyde can together form malondialdehyde-acetaldehyde (MAA) adducts. The role of alcohol dehydrogenase (ADH) and cytochrome P4502E1 (CYP2E1) in the formation of MAA-adducts in liver cells has been investigated.
Yu Chen et al.
The Journal of biological chemistry, 288(11), 7506-7518 (2013-01-24)
Autophagy is a conserved feature of lysosome-mediated intracellular degradation. Dysregulated autophagy is implicated as a contributor in neurodegenerative diseases; however, the role of autophagy in retinal degeneration remains largely unknown. Here, we report that the photo-activated visual chromophore, all-trans-retinal, modulated
Gian Paolo Vallerini et al.
Neuroscience, 448, 1-13 (2020-09-14)
Binge drinking is a frequent pattern of ethanol consumption within Alcohol Use Disorders (AUDs). Binge-like ethanol exposure increases Poly(ADP-ribose) polymerase (PARP) expression and activity. PARP enzymes have been implicated in addiction and serve multiple roles in the cell, including gene
Kenta Iitani et al.
Analytical chemistry, 91(15), 9458-9465 (2019-07-10)
We developed a gas-imaging system (sniff-cam) for gaseous ethanol (EtOH) with improved sensitivity. The sniff-cam was applied to measure the extremely low concentration distribution of breath EtOH without the consumption of alcohol, which is related to the activity of the
Molecular cloning and chromosomal localization of the ADH7 gene encoding human class IV (sigma) ADH.
H Yokoyama et al.
Genomics, 31(2), 243-245 (1996-01-15)
The ADH7 gene encoding human Class IV (sigma) alcohol dehydrogenase (ADH) was cloned from a Caucasian genomic DNA library and characterized. It has nine exons and eight introns that span about 22 kb, and its intron insertion is identical to
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