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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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Pleiotropic Actions of Aldehyde Reductase (AKR1A).

Metabolites

Fujii J, Homma T, Miyata S, Takahashi M.
PMID: 34073440
Metabolites. 2021 May 26;11(6). doi: 10.3390/metabo11060343.

We provide an overview of the physiological roles of aldehyde reductase (AKR1A) and also discuss the functions of aldose reductase (AKR1B) and other family members when necessary. Many types of aldehyde compounds are cytotoxic and some are even carcinogenic....

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Fujii J, Homma T, Miyata S, et al. Pleiotropic Actions of Aldehyde Reductase (AKR1A). Metabolites. 2021;11(6)doi: 10.3390/metabo11060343.
Fujii, J., Homma, T., Miyata, S., & Takahashi, M. (2021). Pleiotropic Actions of Aldehyde Reductase (AKR1A). Metabolites, 11(6), . https://doi.org/10.3390/metabo11060343
Fujii, Junichi, et al. "Pleiotropic Actions of Aldehyde Reductase (AKR1A)." Metabolites vol. 11,6 (2021). doi: https://doi.org/10.3390/metabo11060343
Fujii J, Homma T, Miyata S, Takahashi M. Pleiotropic Actions of Aldehyde Reductase (AKR1A). Metabolites. 2021 May 26;11(6). doi: 10.3390/metabo11060343. PMID: 34073440; PMCID: PMC8227408.
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Microbial synthesis of propane by engineering valine pathway and aldehyde-deformylating oxygenase.

Biotechnology for biofuels

Zhang L, Liang Y, Wu W, Tan X, Lu X.
PMID: 27042209
Biotechnol Biofuels. 2016 Apr 01;9:80. doi: 10.1186/s13068-016-0496-z. eCollection 2016.

BACKGROUND: Propane, a major component of liquid petroleum gas (LPG) derived from fossil fuels, has widespread applications in vehicles, cooking, and ambient heating. Given the concerns about fossil fuel depletion and carbon emission, exploiting alternative and renewable source of...

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Zhang L, Liang Y, Wu W, et al. Microbial synthesis of propane by engineering valine pathway and aldehyde-deformylating oxygenase. Biotechnol Biofuels. 2016;9:80doi: 10.1186/s13068-016-0496-z.
Zhang, L., Liang, Y., Wu, W., Tan, X., & Lu, X. (2016). Microbial synthesis of propane by engineering valine pathway and aldehyde-deformylating oxygenase. Biotechnology for biofuels, 980. https://doi.org/10.1186/s13068-016-0496-z
Zhang, Lei, et al. "Microbial synthesis of propane by engineering valine pathway and aldehyde-deformylating oxygenase." Biotechnology for biofuels vol. 9 (2016): 80. doi: https://doi.org/10.1186/s13068-016-0496-z
Zhang L, Liang Y, Wu W, Tan X, Lu X. Microbial synthesis of propane by engineering valine pathway and aldehyde-deformylating oxygenase. Biotechnol Biofuels. 2016 Apr 01;9:80. doi: 10.1186/s13068-016-0496-z. eCollection 2016. PMID: 27042209; PMCID: PMC4818529.
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Structures of human and porcine aldehyde reductase: an enzyme implicated in diabetic complications.

Acta crystallographica. Section D, Biological crystallography

El-Kabbani O, Green NC, Lin G, Carson M, Narayana SV, Moore KM, Flynn TG, DeLucas LJ.
PMID: 15299353
Acta Crystallogr D Biol Crystallogr. 1994 Nov 01;50:859-68. doi: 10.1107/S0907444994005275.

The crystal structures of porcine and human aldehyde reductase, an enzyme implicated in complications of diabetes, have been determined by X-ray diffraction methods. The crystallographic R factor for the refined porcine aldehyde reductase model is 0.19 at 2.8 A...

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El-Kabbani O, Green NC, Lin G, et al. Structures of human and porcine aldehyde reductase: an enzyme implicated in diabetic complications. Acta Crystallogr D Biol Crystallogr. 1994;50:859-68doi: 10.1107/S0907444994005275.
El-Kabbani, O., Green, N. C., Lin, G., Carson, M., Narayana, S. V., Moore, K. M., Flynn, T. G., & DeLucas, L. J. (1994). Structures of human and porcine aldehyde reductase: an enzyme implicated in diabetic complications. Acta crystallographica. Section D, Biological crystallography, 50859-68. https://doi.org/10.1107/S0907444994005275
El-Kabbani, O, et al. "Structures of human and porcine aldehyde reductase: an enzyme implicated in diabetic complications." Acta crystallographica. Section D, Biological crystallography vol. 50 (1994): 859-68. doi: https://doi.org/10.1107/S0907444994005275
El-Kabbani O, Green NC, Lin G, Carson M, Narayana SV, Moore KM, Flynn TG, DeLucas LJ. Structures of human and porcine aldehyde reductase: an enzyme implicated in diabetic complications. Acta Crystallogr D Biol Crystallogr. 1994 Nov 01;50:859-68. doi: 10.1107/S0907444994005275. PMID: 15299353.
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Crystallization and preliminary structure determination of porcine aldehyde reductase from two crystal forms.

Acta crystallographica. Section D, Biological crystallography

El-Kabbani O, Sthanam L, Narayana VL, Moore KM, Green NC, Flynn TG, Delucas LJ.
PMID: 15299508
Acta Crystallogr D Biol Crystallogr. 1993 Sep 01;49:490-6. doi: 10.1107/S0907444993004044.

Aldehyde reductase from porcine kidney has been crystallized from buffered ammonium sulfate solutions. Two crystal forms are monoclinic, space group P2(1), with a = 56.2, b = 98.1, c = 73.2 A, beta = 112.5 degrees and a =...

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El-Kabbani O, Sthanam L, Narayana VL, et al. Crystallization and preliminary structure determination of porcine aldehyde reductase from two crystal forms. Acta Crystallogr D Biol Crystallogr. 1993;49:490-6doi: 10.1107/S0907444993004044.
El-Kabbani, O., Sthanam, L., Narayana, V. L., Moore, K. M., Green, N. C., Flynn, T. G., & Delucas, L. J. (1993). Crystallization and preliminary structure determination of porcine aldehyde reductase from two crystal forms. Acta crystallographica. Section D, Biological crystallography, 49490-6. https://doi.org/10.1107/S0907444993004044
El-Kabbani, O, et al. "Crystallization and preliminary structure determination of porcine aldehyde reductase from two crystal forms." Acta crystallographica. Section D, Biological crystallography vol. 49 (1993): 490-6. doi: https://doi.org/10.1107/S0907444993004044
El-Kabbani O, Sthanam L, Narayana VL, Moore KM, Green NC, Flynn TG, Delucas LJ. Crystallization and preliminary structure determination of porcine aldehyde reductase from two crystal forms. Acta Crystallogr D Biol Crystallogr. 1993 Sep 01;49:490-6. doi: 10.1107/S0907444993004044. PMID: 15299508.
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Purification and Properties of an NADPH-Aldose Reductase (Aldehyde Reductase) from Euonymus japonica Leaves.

Plant physiology

Negm FB.
PMID: 16664750
Plant Physiol. 1986 Apr;80(4):972-7. doi: 10.1104/pp.80.4.972.

The enzyme aldose (aldehyde) reductase was partially purified (142-fold) and characterized from Euonymus japonica leaves. The reductase, a dimer, had an average molecular weight of 67,000 as determined by gel filtration on Sephadex G-100. The enzyme was NADPH specific...

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Negm FB. Purification and Properties of an NADPH-Aldose Reductase (Aldehyde Reductase) from Euonymus japonica Leaves. Plant Physiol. 1986;80(4):972-7doi: 10.1104/pp.80.4.972.
Negm, F. B. (1986). Purification and Properties of an NADPH-Aldose Reductase (Aldehyde Reductase) from Euonymus japonica Leaves. Plant physiology, 80(4), 972-7. https://doi.org/10.1104/pp.80.4.972
Negm, F B. "Purification and Properties of an NADPH-Aldose Reductase (Aldehyde Reductase) from Euonymus japonica Leaves." Plant physiology vol. 80,4 (1986): 972-7. doi: https://doi.org/10.1104/pp.80.4.972
Negm FB. Purification and Properties of an NADPH-Aldose Reductase (Aldehyde Reductase) from Euonymus japonica Leaves. Plant Physiol. 1986 Apr;80(4):972-7. doi: 10.1104/pp.80.4.972. PMID: 16664750; PMCID: PMC1075239.
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Occurrence of multiple ethyl 4-chloro-3-oxobutanoate-reducing enzymes in Candida magnoliae.

Journal of bioscience and bioengineering

Wada M, Kawabata H, Yoshizumi A, Kataoka M, Nakamori S, Yasohara Y, Kizaki N, Hasegawa J, Shimizu S.
PMID: 16232441
J Biosci Bioeng. 1999;87(2):144-8. doi: 10.1016/s1389-1723(99)89003-3.

Multiple ethyl 4-chloro-3-oxobutanoate (COBE)-reducing enzymes were isolated from a cell-free extract of Candida magnoliae. A NADPH-dependent COBE-reducing enzyme, distinct from the carbonyl reductase and aldehyde reductase previously reported, was purified to homogeneity using five steps, including polyethylene glycol treatment....

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Wada M, Kawabata H, Yoshizumi A, et al. Occurrence of multiple ethyl 4-chloro-3-oxobutanoate-reducing enzymes in Candida magnoliae. J Biosci Bioeng. 1999;87(2):144-8doi: 10.1016/s1389-1723(99)89003-3.
Wada, M., Kawabata, H., Yoshizumi, A., Kataoka, M., Nakamori, S., Yasohara, Y., Kizaki, N., Hasegawa, J., & Shimizu, S. (1999). Occurrence of multiple ethyl 4-chloro-3-oxobutanoate-reducing enzymes in Candida magnoliae. Journal of bioscience and bioengineering, 87(2), 144-8. https://doi.org/10.1016/s1389-1723(99)89003-3
Wada, M, et al. "Occurrence of multiple ethyl 4-chloro-3-oxobutanoate-reducing enzymes in Candida magnoliae." Journal of bioscience and bioengineering vol. 87,2 (1999): 144-8. doi: https://doi.org/10.1016/s1389-1723(99)89003-3
Wada M, Kawabata H, Yoshizumi A, Kataoka M, Nakamori S, Yasohara Y, Kizaki N, Hasegawa J, Shimizu S. Occurrence of multiple ethyl 4-chloro-3-oxobutanoate-reducing enzymes in Candida magnoliae. J Biosci Bioeng. 1999;87(2):144-8. doi: 10.1016/s1389-1723(99)89003-3. PMID: 16232441.
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Characterization of the Kluyveromyces marxianus strain DMB1 YGL157w gene product as a broad specificity NADPH-dependent aldehyde reductase.

AMB Express

Akita H, Watanabe M, Suzuki T, Nakashima N, Hoshino T.
PMID: 25852994
AMB Express. 2015 Mar 03;5:17. doi: 10.1186/s13568-015-0104-9. eCollection 2015.

The open reading frame YGL157w in the genome of the yeast Kluyveromyces marxianus strain DMB1 encodes a putative uncharacterized oxidoreductase. However, this protein shows 46% identity with the Saccharomyces cerevisiae S288c NADPH-dependent methylglyoxal reductase, which exhibits broad substrate specificity...

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Akita H, Watanabe M, Suzuki T, et al. Characterization of the Kluyveromyces marxianus strain DMB1 YGL157w gene product as a broad specificity NADPH-dependent aldehyde reductase. AMB Express. 2015;5:17doi: 10.1186/s13568-015-0104-9.
Akita, H., Watanabe, M., Suzuki, T., Nakashima, N., & Hoshino, T. (2015). Characterization of the Kluyveromyces marxianus strain DMB1 YGL157w gene product as a broad specificity NADPH-dependent aldehyde reductase. AMB Express, 517. https://doi.org/10.1186/s13568-015-0104-9
Akita, Hironaga, et al. "Characterization of the Kluyveromyces marxianus strain DMB1 YGL157w gene product as a broad specificity NADPH-dependent aldehyde reductase." AMB Express vol. 5 (2015): 17. doi: https://doi.org/10.1186/s13568-015-0104-9
Akita H, Watanabe M, Suzuki T, Nakashima N, Hoshino T. Characterization of the Kluyveromyces marxianus strain DMB1 YGL157w gene product as a broad specificity NADPH-dependent aldehyde reductase. AMB Express. 2015 Mar 03;5:17. doi: 10.1186/s13568-015-0104-9. eCollection 2015. PMID: 25852994; PMCID: PMC4385108.
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Purification and Characterization of Aldehyde Reductase from Leuconostoc dextranicum.

Bioscience, biotechnology, and biochemistry

Nakajima N, Nakamura K, Sumi H, Matsuyama A, Esaki N, Soda K.
PMID: 27316898
Biosci Biotechnol Biochem. 1993 Jan;57(1):160-1. doi: 10.1271/bbb.57.160.

No abstract available.

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Nakajima N, Nakamura K, Sumi H, et al. Purification and Characterization of Aldehyde Reductase from Leuconostoc dextranicum. Biosci Biotechnol Biochem. 1993;57(1):160-1doi: 10.1271/bbb.57.160.
Nakajima, N., Nakamura, K., Sumi, H., Matsuyama, A., Esaki, N., & Soda, K. (1993). Purification and Characterization of Aldehyde Reductase from Leuconostoc dextranicum. Bioscience, biotechnology, and biochemistry, 57(1), 160-1. https://doi.org/10.1271/bbb.57.160
Nakajima, N, et al. "Purification and Characterization of Aldehyde Reductase from Leuconostoc dextranicum." Bioscience, biotechnology, and biochemistry vol. 57,1 (1993): 160-1. doi: https://doi.org/10.1271/bbb.57.160
Nakajima N, Nakamura K, Sumi H, Matsuyama A, Esaki N, Soda K. Purification and Characterization of Aldehyde Reductase from Leuconostoc dextranicum. Biosci Biotechnol Biochem. 1993 Jan;57(1):160-1. doi: 10.1271/bbb.57.160. PMID: 27316898.
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Virtual screening of epalrestat mimicking selective ALR2 inhibitors from natural product database: auto pharmacophore, ADMET prediction and molecular dynamics approach.

Journal of biomolecular structure & dynamics

Choudhary S, Silakari O.
PMID: 33480327
J Biomol Struct Dyn. 2021 Jan 22;1-19. doi: 10.1080/07391102.2021.1875878. Epub 2021 Jan 22.

Epalrestat is the only effective aldose reductase (ALR2) inhibitor available in the market for the treatment of diabetic neuropathy. Clinical effectiveness of epalrestat in diabetic neuropathy encouraged us to develop some more ALR2 inhibitors with a better therapeutic profile....

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Choudhary S, Silakari O. Virtual screening of epalrestat mimicking selective ALR2 inhibitors from natural product database: auto pharmacophore, ADMET prediction and molecular dynamics approach. J Biomol Struct Dyn. 2021;1-19doi: 10.1080/07391102.2021.1875878.
Choudhary, S., & Silakari, O. (2021). Virtual screening of epalrestat mimicking selective ALR2 inhibitors from natural product database: auto pharmacophore, ADMET prediction and molecular dynamics approach. Journal of biomolecular structure & dynamics, 1-19. https://doi.org/10.1080/07391102.2021.1875878
Choudhary, Shalki, and Silakari, Om. "Virtual screening of epalrestat mimicking selective ALR2 inhibitors from natural product database: auto pharmacophore, ADMET prediction and molecular dynamics approach." Journal of biomolecular structure & dynamics vol. (2021): 1-19. doi: https://doi.org/10.1080/07391102.2021.1875878
Choudhary S, Silakari O. Virtual screening of epalrestat mimicking selective ALR2 inhibitors from natural product database: auto pharmacophore, ADMET prediction and molecular dynamics approach. J Biomol Struct Dyn. 2021 Jan 22;1-19. doi: 10.1080/07391102.2021.1875878. Epub 2021 Jan 22. PMID: 33480327.
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RNA sequencing reveals metabolic and regulatory changes leading to more robust fermentation performance during short-term adaptation of Saccharomyces cerevisiae to lignocellulosic inhibitors.

Biotechnology for biofuels

van Dijk M, Rugbjerg P, Nygård Y, Olsson L.
PMID: 34654441
Biotechnol Biofuels. 2021 Oct 15;14(1):201. doi: 10.1186/s13068-021-02049-y.

BACKGROUND: The limited tolerance of Saccharomyces cerevisiae to inhibitors is a major challenge in second-generation bioethanol production, and our understanding of the molecular mechanisms providing tolerance to inhibitor-rich lignocellulosic hydrolysates is incomplete. Short-term adaptation of the yeast in the...

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van Dijk M, Rugbjerg P, Nygård Y, et al. RNA sequencing reveals metabolic and regulatory changes leading to more robust fermentation performance during short-term adaptation of Saccharomyces cerevisiae to lignocellulosic inhibitors. Biotechnol Biofuels. 2021;14(1):201doi: 10.1186/s13068-021-02049-y.
van Dijk, M., Rugbjerg, P., Nygård, Y., & Olsson, L. (2021). RNA sequencing reveals metabolic and regulatory changes leading to more robust fermentation performance during short-term adaptation of Saccharomyces cerevisiae to lignocellulosic inhibitors. Biotechnology for biofuels, 14(1), 201. https://doi.org/10.1186/s13068-021-02049-y
van Dijk, Marlous, et al. "RNA sequencing reveals metabolic and regulatory changes leading to more robust fermentation performance during short-term adaptation of Saccharomyces cerevisiae to lignocellulosic inhibitors." Biotechnology for biofuels vol. 14,1 (2021): 201. doi: https://doi.org/10.1186/s13068-021-02049-y
van Dijk M, Rugbjerg P, Nygård Y, Olsson L. RNA sequencing reveals metabolic and regulatory changes leading to more robust fermentation performance during short-term adaptation of Saccharomyces cerevisiae to lignocellulosic inhibitors. Biotechnol Biofuels. 2021 Oct 15;14(1):201. doi: 10.1186/s13068-021-02049-y. PMID: 34654441; PMCID: PMC8518171.
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Processing of Airborne Green Leaf Volatiles for Their Glycosylation in the Exposed Plants.

Frontiers in plant science

Sugimoto K, Iijima Y, Takabayashi J, Matsui K.
PMID: 34868107
Front Plant Sci. 2021 Nov 16;12:721572. doi: 10.3389/fpls.2021.721572. eCollection 2021.

Green leaf volatiles (GLVs), the common constituents of herbivore-infested plant volatiles (HIPVs), play an important role in plant defense and function as chemical cues to communicate with other individuals in nature. Reportedly, in addition to endogenous GLVs, the absorbance...

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Sugimoto K, Iijima Y, Takabayashi J, et al. Processing of Airborne Green Leaf Volatiles for Their Glycosylation in the Exposed Plants. Front Plant Sci. 2021;12:721572doi: 10.3389/fpls.2021.721572.
Sugimoto, K., Iijima, Y., Takabayashi, J., & Matsui, K. (2021). Processing of Airborne Green Leaf Volatiles for Their Glycosylation in the Exposed Plants. Frontiers in plant science, 12721572. https://doi.org/10.3389/fpls.2021.721572
Sugimoto, Koichi, et al. "Processing of Airborne Green Leaf Volatiles for Their Glycosylation in the Exposed Plants." Frontiers in plant science vol. 12 (2021): 721572. doi: https://doi.org/10.3389/fpls.2021.721572
Sugimoto K, Iijima Y, Takabayashi J, Matsui K. Processing of Airborne Green Leaf Volatiles for Their Glycosylation in the Exposed Plants. Front Plant Sci. 2021 Nov 16;12:721572. doi: 10.3389/fpls.2021.721572. eCollection 2021. PMID: 34868107; PMCID: PMC8636985.
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Showing 1 to 12 of 34 entries