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Association of polymorphism in the alcohol dehydrogenase 2 gene with alcohol-related organ injuries, especially liver cirrhosis.

Addiction biology

Yamauchi M.
PMID: 26734820
Addict Biol. 1998 Apr;3(2):151-7. doi: 10.1080/13556219872218.

The class I hepatic alcohol dehydrogenases (ADHs) are primarily responsible for ethanol metabolism in humans. Genetic polymorphism at the ADH2 locus results in the inheritance of isozymes of strikingly different catalytic properties. In European and Caucasian American populations, β1,...

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Yamauchi M. Association of polymorphism in the alcohol dehydrogenase 2 gene with alcohol-related organ injuries, especially liver cirrhosis. Addict Biol. 1998;3(2):151-7doi: 10.1080/13556219872218.
Yamauchi, M. (1998). Association of polymorphism in the alcohol dehydrogenase 2 gene with alcohol-related organ injuries, especially liver cirrhosis. Addiction biology, 3(2), 151-7. https://doi.org/10.1080/13556219872218
Yamauchi, M. "Association of polymorphism in the alcohol dehydrogenase 2 gene with alcohol-related organ injuries, especially liver cirrhosis." Addiction biology vol. 3,2 (1998): 151-7. doi: https://doi.org/10.1080/13556219872218
Yamauchi M. Association of polymorphism in the alcohol dehydrogenase 2 gene with alcohol-related organ injuries, especially liver cirrhosis. Addict Biol. 1998 Apr;3(2):151-7. doi: 10.1080/13556219872218. PMID: 26734820.
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A comparative multidimensional LC-MS proteomic analysis reveals mechanisms for furan aldehyde detoxification in Thermoanaerobacter pseudethanolicus 39E.

Biotechnology for biofuels

Clarkson SM, Hamilton-Brehm SD, Giannone RJ, Engle NL, Tschaplinski TJ, Hettich RL, Elkins JG.
PMID: 25506391
Biotechnol Biofuels. 2014 Dec 03;7(1):165. doi: 10.1186/s13068-014-0165-z. eCollection 2014.

BACKGROUND: Chemical and physical pretreatment of lignocellulosic biomass improves substrate reactivity for increased microbial biofuel production, but also restricts growth via the release of furan aldehydes, such as furfural and 5-hydroxymethylfurfural (5-HMF). The physiological effects of these inhibitors on...

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Clarkson SM, Hamilton-Brehm SD, Giannone RJ, et al. A comparative multidimensional LC-MS proteomic analysis reveals mechanisms for furan aldehyde detoxification in Thermoanaerobacter pseudethanolicus 39E. Biotechnol Biofuels. 2014;7(1):165doi: 10.1186/s13068-014-0165-z.
Clarkson, S. M., Hamilton-Brehm, S. D., Giannone, R. J., Engle, N. L., Tschaplinski, T. J., Hettich, R. L., & Elkins, J. G. (2014). A comparative multidimensional LC-MS proteomic analysis reveals mechanisms for furan aldehyde detoxification in Thermoanaerobacter pseudethanolicus 39E. Biotechnology for biofuels, 7(1), 165. https://doi.org/10.1186/s13068-014-0165-z
Clarkson, Sonya M, et al. "A comparative multidimensional LC-MS proteomic analysis reveals mechanisms for furan aldehyde detoxification in Thermoanaerobacter pseudethanolicus 39E." Biotechnology for biofuels vol. 7,1 (2014): 165. doi: https://doi.org/10.1186/s13068-014-0165-z
Clarkson SM, Hamilton-Brehm SD, Giannone RJ, Engle NL, Tschaplinski TJ, Hettich RL, Elkins JG. A comparative multidimensional LC-MS proteomic analysis reveals mechanisms for furan aldehyde detoxification in Thermoanaerobacter pseudethanolicus 39E. Biotechnol Biofuels. 2014 Dec 03;7(1):165. doi: 10.1186/s13068-014-0165-z. eCollection 2014. PMID: 25506391; PMCID: PMC4265447.
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Two NAD-dependent alcohol dehydrogenases (E.C. 1.1.1.1) in callus cultures of wheat, rye and triticale.

TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik

Suseelan KN, Bhatia CR, Eapen S.
PMID: 24270533
Theor Appl Genet. 1982 Mar;62(1):45-8. doi: 10.1007/BF00276281.

Two NAD-dependent alcohol dehydrogenases ADH-1 and ADH-2, under independent genetic control of genes designated as Adh-1 and Adh-2 located on chromosomes 4A, 4B and 4D, have been reported in aestivum wheat (Hart 1980). Only ADH-1 is expressed in developing...

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Suseelan KN, Bhatia CR, Eapen S. Two NAD-dependent alcohol dehydrogenases (E.C. 1.1.1.1) in callus cultures of wheat, rye and triticale. Theor Appl Genet. 1982;62(1):45-8doi: 10.1007/BF00276281.
Suseelan, K. N., Bhatia, C. R., & Eapen, S. (1982). Two NAD-dependent alcohol dehydrogenases (E.C. 1.1.1.1) in callus cultures of wheat, rye and triticale. TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik, 62(1), 45-8. https://doi.org/10.1007/BF00276281
Suseelan, K N, et al. "Two NAD-dependent alcohol dehydrogenases (E.C. 1.1.1.1) in callus cultures of wheat, rye and triticale." TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik vol. 62,1 (1982): 45-8. doi: https://doi.org/10.1007/BF00276281
Suseelan KN, Bhatia CR, Eapen S. Two NAD-dependent alcohol dehydrogenases (E.C. 1.1.1.1) in callus cultures of wheat, rye and triticale. Theor Appl Genet. 1982 Mar;62(1):45-8. doi: 10.1007/BF00276281. PMID: 24270533.
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The interaction of 1-anilino-8-naphthalene sulphonate with yeast alcohol dehydrogenase.

FEBS letters

Dickinson FM.
PMID: 11945803
FEBS Lett. 1971 Jun 02;15(1):17-20. doi: 10.1016/0014-5793(71)80068-6.

No abstract available.

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Dickinson FM. The interaction of 1-anilino-8-naphthalene sulphonate with yeast alcohol dehydrogenase. FEBS Lett. 1971;15(1):17-20doi: 10.1016/0014-5793(71)80068-6.
Dickinson, F. M. (1971). The interaction of 1-anilino-8-naphthalene sulphonate with yeast alcohol dehydrogenase. FEBS letters, 15(1), 17-20. https://doi.org/10.1016/0014-5793(71)80068-6
Dickinson, F M.. "The interaction of 1-anilino-8-naphthalene sulphonate with yeast alcohol dehydrogenase." FEBS letters vol. 15,1 (1971): 17-20. doi: https://doi.org/10.1016/0014-5793(71)80068-6
Dickinson FM. The interaction of 1-anilino-8-naphthalene sulphonate with yeast alcohol dehydrogenase. FEBS Lett. 1971 Jun 02;15(1):17-20. doi: 10.1016/0014-5793(71)80068-6. PMID: 11945803.
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Gender differences in drug therapy.

American journal of therapeutics

Khosla S, Somberg JC.
PMID: 11862230
Am J Ther. 1996 Oct;3(10):735-9. doi: 10.1097/00045391-199610000-00010.

Patient response to drug therapy is affected by multiple factors, including age, renal function, diet, smoking, congestive heart failure and gender. However, the data on gender differences in pharmacotherapy are limited, predominantly because women are excluded from clinical research...

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Khosla S, Somberg JC. Gender differences in drug therapy. Am J Ther. 1996;3(10):735-9doi: 10.1097/00045391-199610000-00010.
Khosla, S., & Somberg, J. C. (1996). Gender differences in drug therapy. American journal of therapeutics, 3(10), 735-9. https://doi.org/10.1097/00045391-199610000-00010
Khosla, S, and Somberg, J C. "Gender differences in drug therapy." American journal of therapeutics vol. 3,10 (1996): 735-9. doi: https://doi.org/10.1097/00045391-199610000-00010
Khosla S, Somberg JC. Gender differences in drug therapy. Am J Ther. 1996 Oct;3(10):735-9. doi: 10.1097/00045391-199610000-00010. PMID: 11862230.
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Alcohol dehydrogenase ADH2-1 and ADH2-2 allelic isoforms in the Russian population correlate with type of alcoholic disease.

Addiction biology

Ogurtsov PP, Garmash IV, Miandina GI, Guschin AE, Itkes AV, Moiseev VS.
PMID: 11900616
Addict Biol. 2001 Sep;6(4):377-383. doi: 10.1080/13556210020077109.

The frequency ADH2-2 allele in the Moscow urban population and a correlation between the ADH2-2 allele, alcoholic dependence without cirrhosis, symptomatic alcoholic cirrhosis and status on hepatitis B and C infection have been studied. One hundred and twenty-three inhabitants...

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Ogurtsov PP, Garmash IV, Miandina GI, et al. Alcohol dehydrogenase ADH2-1 and ADH2-2 allelic isoforms in the Russian population correlate with type of alcoholic disease. Addict Biol. 2001;6(4):377-383doi: 10.1080/13556210020077109.
Ogurtsov, P. P., Garmash, I. V., Miandina, G. I., Guschin, A. E., Itkes, A. V., & Moiseev, V. S. (2001). Alcohol dehydrogenase ADH2-1 and ADH2-2 allelic isoforms in the Russian population correlate with type of alcoholic disease. Addiction biology, 6(4), 377-383. https://doi.org/10.1080/13556210020077109
Ogurtsov, Pavel P., et al. "Alcohol dehydrogenase ADH2-1 and ADH2-2 allelic isoforms in the Russian population correlate with type of alcoholic disease." Addiction biology vol. 6,4 (2001): 377-383. doi: https://doi.org/10.1080/13556210020077109
Ogurtsov PP, Garmash IV, Miandina GI, Guschin AE, Itkes AV, Moiseev VS. Alcohol dehydrogenase ADH2-1 and ADH2-2 allelic isoforms in the Russian population correlate with type of alcoholic disease. Addict Biol. 2001 Sep;6(4):377-383. doi: 10.1080/13556210020077109. PMID: 11900616.
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Fate of oxygen losses from Typha domingensis (Typhaceae) and Cladium jamaicense (Cyperaceae) and consequences for root metabolism.

American journal of botany

Chabbi A, McKee KL, Mendelssohn IA.
PMID: 10947992
Am J Bot. 2000 Aug;87(8):1081-90.

The objective of this work was to determine whether radial oxygen loss (ROL) from roots of Typha domingensis and Cladium jamaicense creates an internal oxygen deficiency or, conversely, indicates adequate internal aeration and leakage of excess oxygen to the...

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Chabbi A, McKee KL, Mendelssohn IA. Fate of oxygen losses from Typha domingensis (Typhaceae) and Cladium jamaicense (Cyperaceae) and consequences for root metabolism. Am J Bot. 2000;87(8):1081-90
Chabbi, A., McKee, K. L., & Mendelssohn, I. A. (2000). Fate of oxygen losses from Typha domingensis (Typhaceae) and Cladium jamaicense (Cyperaceae) and consequences for root metabolism. American journal of botany, 87(8), 1081-90.
Chabbi, A, et al. "Fate of oxygen losses from Typha domingensis (Typhaceae) and Cladium jamaicense (Cyperaceae) and consequences for root metabolism." American journal of botany vol. 87,8 (2000): 1081-90.
Chabbi A, McKee KL, Mendelssohn IA. Fate of oxygen losses from Typha domingensis (Typhaceae) and Cladium jamaicense (Cyperaceae) and consequences for root metabolism. Am J Bot. 2000 Aug;87(8):1081-90. PMID: 10947992.
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Asymmetric Electroreduction of Ketone and Aldehyde Derivatives to the Corresponding Alcohols Using Alcohol Dehydrogenase as an Electrocatalyst.

The Journal of organic chemistry

Yuan R, Watanabe S, Kuwabata S, Yoneyama H.
PMID: 11671588
J Org Chem. 1997 Apr 18;62(8):2494-2499. doi: 10.1021/jo9620573.

Asymmetric electroreduction of ketone and aldehyde derivatives was examined for two electrochemical reduction systems using alcohol dehydrogenase (ADH) as an electrocatalyst. The reaction system A is concerned with reduction of substrates catalyzed by ADH coupled with regeneration of cofactors...

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Yuan R, Watanabe S, Kuwabata S, et al. Asymmetric Electroreduction of Ketone and Aldehyde Derivatives to the Corresponding Alcohols Using Alcohol Dehydrogenase as an Electrocatalyst. J Org Chem. 1997;62(8):2494-2499doi: 10.1021/jo9620573.
Yuan, R., Watanabe, S., Kuwabata, S., & Yoneyama, H. (1997). Asymmetric Electroreduction of Ketone and Aldehyde Derivatives to the Corresponding Alcohols Using Alcohol Dehydrogenase as an Electrocatalyst. The Journal of organic chemistry, 62(8), 2494-2499. https://doi.org/10.1021/jo9620573
Yuan, Ruo, et al. "Asymmetric Electroreduction of Ketone and Aldehyde Derivatives to the Corresponding Alcohols Using Alcohol Dehydrogenase as an Electrocatalyst." The Journal of organic chemistry vol. 62,8 (1997): 2494-2499. doi: https://doi.org/10.1021/jo9620573
Yuan R, Watanabe S, Kuwabata S, Yoneyama H. Asymmetric Electroreduction of Ketone and Aldehyde Derivatives to the Corresponding Alcohols Using Alcohol Dehydrogenase as an Electrocatalyst. J Org Chem. 1997 Apr 18;62(8):2494-2499. doi: 10.1021/jo9620573. PMID: 11671588.
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Design and Synthesis of Transition State Analogs for Induction of Hydride Transfer Catalytic Antibodies.

The Journal of organic chemistry

Schröer J, Sanner M, Reymond JL.
PMID: 11671707
J Org Chem. 1997 May 16;62(10):3220-3229. doi: 10.1021/jo962179v.

Alcohol dehydrogenases and related aldehyde reductase enzymes catalyze the oxidation of alcohols to aldehydes and the simultaneous reduction of a nicotinamide derivative (NAD(+) or NADP(+)) to the corresponding 1,4-dihydronicotinamide. Herein we report the design and synthesis of a stable...

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Schröer J, Sanner M, Reymond JL. Design and Synthesis of Transition State Analogs for Induction of Hydride Transfer Catalytic Antibodies. J Org Chem. 1997;62(10):3220-3229doi: 10.1021/jo962179v.
Schröer, J., Sanner, M., & Reymond, J. L. (1997). Design and Synthesis of Transition State Analogs for Induction of Hydride Transfer Catalytic Antibodies. The Journal of organic chemistry, 62(10), 3220-3229. https://doi.org/10.1021/jo962179v
Schröer, Josef, et al. "Design and Synthesis of Transition State Analogs for Induction of Hydride Transfer Catalytic Antibodies." The Journal of organic chemistry vol. 62,10 (1997): 3220-3229. doi: https://doi.org/10.1021/jo962179v
Schröer J, Sanner M, Reymond JL. Design and Synthesis of Transition State Analogs for Induction of Hydride Transfer Catalytic Antibodies. J Org Chem. 1997 May 16;62(10):3220-3229. doi: 10.1021/jo962179v. PMID: 11671707.
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Regulation of alcohol dehydrogenase gene expression in barley aleurone by gibberellin and abscisic acid.

Physiologia plantarum

MacNicol PK, Jacobsen JV.
PMID: 11299019
Physiol Plant. 2001 Apr;111(4):533-539. doi: 10.1034/j.1399-3054.2001.1110414.x.

The expression of the Adh1 gene (alcohol dehydrogenase, EC 1.1.1.1) was studied in the aleurone layer of barley (Hordeum vulgare cv. Himalaya). Expression increased markedly during grain development at the levels of activity, enzyme protein and mRNA. mRNA content,...

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MacNicol PK, Jacobsen JV. Regulation of alcohol dehydrogenase gene expression in barley aleurone by gibberellin and abscisic acid. Physiol Plant. 2001;111(4):533-539doi: 10.1034/j.1399-3054.2001.1110414.x.
MacNicol, P. K., & Jacobsen, J. V. (2001). Regulation of alcohol dehydrogenase gene expression in barley aleurone by gibberellin and abscisic acid. Physiologia plantarum, 111(4), 533-539. https://doi.org/10.1034/j.1399-3054.2001.1110414.x
MacNicol, Peter K., and Jacobsen, John V.. "Regulation of alcohol dehydrogenase gene expression in barley aleurone by gibberellin and abscisic acid." Physiologia plantarum vol. 111,4 (2001): 533-539. doi: https://doi.org/10.1034/j.1399-3054.2001.1110414.x
MacNicol PK, Jacobsen JV. Regulation of alcohol dehydrogenase gene expression in barley aleurone by gibberellin and abscisic acid. Physiol Plant. 2001 Apr;111(4):533-539. doi: 10.1034/j.1399-3054.2001.1110414.x. PMID: 11299019.
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Hypoxic and Anoxic Induction of Alcohol Dehydrogenase in Roots and Shoots of Seedlings of Zea mays (Adh Transcripts and Enzyme Activity).

Plant physiology

Andrews DL, Cobb BG, Johnson JR, Drew MC.
PMID: 12231696
Plant Physiol. 1993 Feb;101(2):407-414. doi: 10.1104/pp.101.2.407.

Alcohol dehydrogenase (ADH) is one of a number of enzymes of glycolysis and fermentation known to be synthesized preferentially under low O2 conditions. We examined levels of Adh1 transcripts and of ADH activity in 5-mm root tips, root axes...

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Andrews DL, Cobb BG, Johnson JR, et al. Hypoxic and Anoxic Induction of Alcohol Dehydrogenase in Roots and Shoots of Seedlings of Zea mays (Adh Transcripts and Enzyme Activity). Plant Physiol. 1993;101(2):407-414doi: 10.1104/pp.101.2.407.
Andrews, D. L., Cobb, B. G., Johnson, J. R., & Drew, M. C. (1993). Hypoxic and Anoxic Induction of Alcohol Dehydrogenase in Roots and Shoots of Seedlings of Zea mays (Adh Transcripts and Enzyme Activity). Plant physiology, 101(2), 407-414. https://doi.org/10.1104/pp.101.2.407
Andrews, D. L., et al. "Hypoxic and Anoxic Induction of Alcohol Dehydrogenase in Roots and Shoots of Seedlings of Zea mays (Adh Transcripts and Enzyme Activity)." Plant physiology vol. 101,2 (1993): 407-414. doi: https://doi.org/10.1104/pp.101.2.407
Andrews DL, Cobb BG, Johnson JR, Drew MC. Hypoxic and Anoxic Induction of Alcohol Dehydrogenase in Roots and Shoots of Seedlings of Zea mays (Adh Transcripts and Enzyme Activity). Plant Physiol. 1993 Feb;101(2):407-414. doi: 10.1104/pp.101.2.407. PMID: 12231696; PMCID: PMC160585.
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Biochemical response of Norway spruce (Picea abies (L.) Karst.) towards 14-month exposure to ozone and acid mist: part I--Effects on polyphenol and monoterpene metabolism.

Environmental pollution (Barking, Essex : 1987)

Heller W, Rosemann D, Osswald WF, Benz B, Schönwitz R, Lohwasser K, Kloos M, Sandermann H.
PMID: 15092291
Environ Pollut. 1990;64(3):353-66. doi: 10.1016/0269-7491(90)90057-j.

Three-year-old clonal Picea abies (L.) Karst. plants, grown either on a sandy (No. 1) or on a calcareous (No. 2) soil, were treated with ozone (100 microg m(-3) and peaks of up to 360 microg m(-3)) and acid mist...

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Heller W, Rosemann D, Osswald WF, et al. Biochemical response of Norway spruce (Picea abies (L.) Karst.) towards 14-month exposure to ozone and acid mist: part I--Effects on polyphenol and monoterpene metabolism. Environ Pollut. 1990;64(3):353-66doi: 10.1016/0269-7491(90)90057-j.
Heller, W., Rosemann, D., Osswald, W. F., Benz, B., Schönwitz, R., Lohwasser, K., Kloos, M., & Sandermann, H. (1990). Biochemical response of Norway spruce (Picea abies (L.) Karst.) towards 14-month exposure to ozone and acid mist: part I--Effects on polyphenol and monoterpene metabolism. Environmental pollution (Barking, Essex : 1987), 64(3), 353-66. https://doi.org/10.1016/0269-7491(90)90057-j
Heller, W, et al. "Biochemical response of Norway spruce (Picea abies (L.) Karst.) towards 14-month exposure to ozone and acid mist: part I--Effects on polyphenol and monoterpene metabolism." Environmental pollution (Barking, Essex : 1987) vol. 64,3 (1990): 353-66. doi: https://doi.org/10.1016/0269-7491(90)90057-j
Heller W, Rosemann D, Osswald WF, Benz B, Schönwitz R, Lohwasser K, Kloos M, Sandermann H. Biochemical response of Norway spruce (Picea abies (L.) Karst.) towards 14-month exposure to ozone and acid mist: part I--Effects on polyphenol and monoterpene metabolism. Environ Pollut. 1990;64(3):353-66. doi: 10.1016/0269-7491(90)90057-j. PMID: 15092291.
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Showing 25 to 36 of 850 entries