Works about NAD (Coenzyme)
Results: 2315
Chemical synthesis, in vitro testing, and in silico Nampt-based molecular docking of novel aniline aromatic ring-substituted 2-aminothiazole analogs.
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- Canadian Journal of Physiology & Pharmacology, 2025, v. 103, n. 3, p. 75, doi. 10.1139/cjpp-2024-0211
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NAD+ Boosting Through NRH Supplementation Enhances Treatment Efficacy in EOC In Vitro.
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- International Journal of Molecular Sciences, 2025, v. 26, n. 4, p. 1719, doi. 10.3390/ijms26041719
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Selective Determination of Nicotinamide Adenine Dinucleotide (NADH) on Screen-Printed Polyethylene Terephthalate (PET) Electrodes Modified with a Reduced Graphene Oxide (rGO), Gold Nanoparticle (AuNP), and Poly-Methylene Blue Nanocomposite.
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- Analytical Letters, 2025, v. 58, n. 7, p. 1151, doi. 10.1080/00032719.2024.2356247
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Caireticulin Inhibits Prion Protein PrP-(23-98) Aggregation in Vitro.
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- Bioscience, Biotechnology & Biochemistry, 2011, v. 75, n. 8, p. 1625, doi. 10.1271/bbb.110287
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Purification and Characterization of an NADH-Dependent Alcohol Dehydrogenase from candida maris for the Synthesis of Optically Active 1-(Pyridyl)ethanol Derivatives.
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- Bioscience, Biotechnology & Biochemistry, 2011, v. 75, n. 6, p. 1055, doi. 10.1271/bbb.100528
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Application of an Electrochemical NAD<sup>+</sup> Recycling System Involving a String-Like Carbon Fiber to an Enzyme Reactor.
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- Bioscience, Biotechnology & Biochemistry, 2010, v. 74, n. 9, p. 1931, doi. 10.1271/bbb.100347
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Melanogenesis Inhibition Due to NADH.
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- Bioscience, Biotechnology & Biochemistry, 2010, v. 74, n. 9, p. 1777, doi. 10.1271/bbb.90965
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Improvement of Coenzyme Q<sub>10</sub> Production by Increasing the NADH/NAD<sup>+</sup> Ratio in Agrobacterium tumefaciens.
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- Bioscience, Biotechnology & Biochemistry, 2010, v. 74, n. 4, p. 895, doi. 10.1271/bbb.100034
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Repeated Batch Production of Theanine by Coupled Fermentation with Energy Transfer Using Membrane-Enclosed γ-Glutamylmethylamide Synthetase and Dried Yeast Cells.
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- Bioscience, Biotechnology & Biochemistry, 2009, v. 73, n. 12, p. 2800, doi. 10.1271/bbb.90647
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Cofactor Recycling for Selective Enzymatic Biotransformation of Cinnamaldehyde to Cinnamyl Alcohol.
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- Bioscience, Biotechnology & Biochemistry, 2009, v. 73, n. 5, p. 1224, doi. 10.1271/bbb.90025
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A New Family of D-2-Hydroxyacid Dehydrogenases That Comprises D-Mandelate Dehydrogenases and 2-Ketopantoate Reductases.
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- Bioscience, Biotechnology & Biochemistry, 2008, v. 72, n. 4, p. 1087, doi. 10.1271/bbb.70827
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Characterization of a Dihydrolipoyl Dehydrogenase Having Diaphorase Activity of Clostridium kluyveri.
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- Bioscience, Biotechnology & Biochemistry, 2008, v. 72, n. 4, p. 982, doi. 10.1271/bbb.70724
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Structure and Function of NAD Kinase and NADP Phosphatase: Key Enzymes That Regulate the Intracellular Balance of NAD(H) and NADP(H).
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- Bioscience, Biotechnology & Biochemistry, 2008, v. 72, n. 4, p. 919, doi. 10.1271/bbb.70738
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Increased Expression of Hypothalamic NADPH-Diaphorase Neurons in Mice with Iron Supplement.
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- Bioscience, Biotechnology & Biochemistry, 2005, v. 69, n. 10, p. 1978, doi. 10.1271/bbb.69.1978
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Analysis of Bacterial Glucose Dehydrogenase Homologs from Thermoacidophilic Archaeon Thermoplasma acidophilum: Finding and Characterization of Aldohexose Dehydrogenase.
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- Bioscience, Biotechnology & Biochemistry, 2004, v. 68, n. 12, p. 2451, doi. 10.1271/bbb.68.2451
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Coenzyme Specificity of Enzymes in the Oxidative Pentose Phosphate Pathway of Gluconobacter oxydans.
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- Bioscience, Biotechnology & Biochemistry, 2003, v. 67, n. 12, p. 2648, doi. 10.1271/bbb.67.2648
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Volatilization of Mercury by an Iron Oxidation Enzyme System in a Highly Mercury-resistant Acidithiobacillus ferrooxidans Strain MON-1.
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- Bioscience, Biotechnology & Biochemistry, 2003, v. 67, n. 7, p. 1537, doi. 10.1271/bbb.67.1537
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Purification and Characterization of Two NAD-Dependent Alcohol Dehydrogenases (ADHs) Induced in the Quinoprotein ADH-Deficient Mutant of Acetobacter pasteurianus SKU1108.
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- Bioscience, Biotechnology & Biochemistry, 2003, v. 67, n. 5, p. 958, doi. 10.1271/bbb.67.958
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Functionalized Metal‐Organic Framework for NADH Regeneration by Hydrogen in a Redox Flow Bioreactor.
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- Chemistry - A European Journal, 2024, v. 30, n. 58, p. 1, doi. 10.1002/chem.202401893
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A Prebiotic Pathway to Nicotinamide Adenine Dinucleotide.
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- Chemistry - A European Journal, 2024, v. 30, n. 48, p. 1, doi. 10.1002/chem.202402055
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A Magnesium Binding Site And The Anomeric Effect Regulate The Abiotic Redox Chemistry Of Nicotinamide Nucleotides.
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- Chemistry - A European Journal, 2024, v. 30, n. 35, p. 1, doi. 10.1002/chem.202400411
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Antibactericidal Ir(III) and Ru(II) Complexes with Phosphine‐Alkaloid Conjugate and Their Interactions with Biomolecules: A Case of N‐Methylphenethylamine.
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- Chemistry - A European Journal, 2023, v. 29, n. 62, p. 1, doi. 10.1002/chem.202301603
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NAD(P)H:Quinone Acceptor Oxidoreductase 1 (NQO1) Activatable Salicylamide H<sup>+</sup>/Cl<sup>−</sup> Transporters.
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- Chemistry - A European Journal, 2023, v. 29, n. 51, p. 1, doi. 10.1002/chem.202301412
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Hantzsch Ester as Efficient and Economical NAD(P)H Mimic for In Vitro Bioredox Reactions.
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- Chemistry - A European Journal, 2023, v. 29, n. 45, p. 1, doi. 10.1002/chem.202301180
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Pyrimidoquinazolinophenanthroline Opens Next Chapter in Design of Bridging Ligands for Artificial Photosynthesis**.
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- Chemistry - A European Journal, 2022, v. 28, n. 51, p. 1, doi. 10.1002/chem.202200766
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Controlled Biocatalytic Synthesis of a Metal Nanoparticle‐Enzyme Hybrid: Demonstration for Catalytic H<sub>2</sub>‐driven NADH Recycling.
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- Angewandte Chemie, 2024, v. 136, n. 27, p. 1, doi. 10.1002/ange.202404024
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Photoswitchable PROTACs for Reversible and Spatiotemporal Regulation of NAMPT and NAD<sup>+</sup>.
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- Angewandte Chemie, 2024, v. 136, n. 12, p. 1, doi. 10.1002/ange.202315997
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NADH Photosynthesis System with Affordable Electron Supply and Inhibited NADH Oxidation.
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- Angewandte Chemie, 2023, v. 135, n. 42, p. 1, doi. 10.1002/ange.202310238
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Co‐encapsulating Cofactor and Enzymes in Hydrogen‐Bonded Organic Frameworks for Multienzyme Cascade Reactions with Cofactor Recycling.
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- Angewandte Chemie, 2023, v. 135, n. 42, p. 1, doi. 10.1002/ange.202308562
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Enzyme‐Compatible Core‐Shell Nanoreactor for in Situ H<sub>2</sub>‐Driven NAD(P)H Regeneration.
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- Angewandte Chemie, 2023, v. 135, n. 39, p. 1, doi. 10.1002/ange.202309929
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ATP‐Independent and Cell‐Free Biosynthesis of β‐Hydroxy Acids Using Vinyl Esters as Smart Substrates.
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- Angewandte Chemie, 2023, v. 135, n. 13, p. 1, doi. 10.1002/ange.202218312
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A Versatile Chemoenzymatic Nanoreactor that Mimics NAD(P)H Oxidase for the In Situ Regeneration of Cofactors.
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- Angewandte Chemie, 2022, v. 134, n. 39, p. 1, doi. 10.1002/ange.202206926
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Bioinspired Metalation of the Metal‐Organic Framework MIL‐125‐NH<sub>2</sub> for Photocatalytic NADH Regeneration and Gas‐Liquid‐Solid Three‐Phase Enzymatic CO<sub>2</sub> Reduction.
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- Angewandte Chemie, 2022, v. 134, n. 31, p. 1, doi. 10.1002/ange.202206283
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Profiling of the ADP‐Ribosylome in Living Cells.
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- Angewandte Chemie, 2022, v. 134, n. 18, p. 1, doi. 10.1002/ange.202200977
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Engineering Olefin‐Linked Covalent Organic Frameworks for Photoenzymatic Reduction of CO<sub>2</sub>.
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- Angewandte Chemie, 2022, v. 134, n. 12, p. 1, doi. 10.1002/ange.202200261
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Structural Basis for Inhibition of ROS‐Producing Respiratory Complex I by NADH‐OH.
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- Angewandte Chemie, 2021, v. 133, n. 52, p. 27483, doi. 10.1002/ange.202112165
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Reversible Ratiometric NADH Sensing Using Semiconducting Polymer Dots.
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- Angewandte Chemie, 2021, v. 133, n. 21, p. 12114, doi. 10.1002/ange.202100774
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Implantable Biosupercapacitor Inspired by the Cellular Redox System.
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- Angewandte Chemie, 2021, v. 133, n. 19, p. 10657, doi. 10.1002/ange.202101388
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"NAD‐display": Ultrahigh‐Throughput in Vitro Screening of NAD(H) Dehydrogenases Using Bead Display and Flow Cytometry.
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- Angewandte Chemie, 2021, v. 133, n. 16, p. 9097, doi. 10.1002/ange.202013486
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Enzyme‐Loaded Nanoreactors Enable the Continuous Regeneration of Nicotinamide Adenine Dinucleotide in Artificial Metabolisms.
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- Angewandte Chemie, 2021, v. 133, n. 14, p. 7807, doi. 10.1002/ange.202012023
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Light‐Activated Electron Transfer and Catalytic Mechanism of Carnitine Oxidation by Rieske‐Type Oxygenase from Human Microbiota.
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- Angewandte Chemie, 2021, v. 133, n. 9, p. 4579, doi. 10.1002/ange.202012381
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Biological Nicotinamide Cofactor as a Redox‐Active Motif for Reversible Electrochemical Energy Storage.
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- Angewandte Chemie, 2019, v. 131, n. 47, p. 16920, doi. 10.1002/ange.201906844
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Aerobic Baeyer–Villiger Oxidation Catalyzed by a Flavin‐Containing Enzyme Mimic in Water.
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- Angewandte Chemie, 2018, v. 130, n. 50, p. 16650, doi. 10.1002/ange.201810124
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Nicotinamide Riboside Supplementation Restores Myocardial Nicotinamide Adenine Dinucleotide Levels, Improves Survival, and Promotes Protective Environment Post Myocardial Infarction.
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- Cardiovascular Drugs & Therapy, 2024, v. 38, n. 6, p. 1385, doi. 10.1007/s10557-023-07525-1
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An Investigation into Membrane Bound Redox Carriers Involved in Energy Transduction Mechanism in Brevibacterium linens DSM 20158 with Unsequenced Genome.
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- Journal of Membrane Biology, 2014, v. 247, n. 4, p. 345, doi. 10.1007/s00232-014-9641-4
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Peroxide Reductase Activity of NADH Dehydrogenase in the Presence of an Endogenous 20-kDa Component of an Alkaliphilic Bacillus.
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- Current Microbiology, 2000, v. 41, n. 6, p. 388, doi. 10.1007/s002840010155
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Age-related NADH oxidase (arNOX)-catalyzed oxidative damage to skin proteins.
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- Archives of Dermatological Research, 2014, v. 306, n. 7, p. 645, doi. 10.1007/s00403-014-1472-8
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Studies of the Effects of Antibiotics on the Microflora of the Gastrointestinal Tract by Fluorimetry.
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- Pharmaceutical Chemistry Journal, 2016, v. 50, n. 4, p. 262, doi. 10.1007/s11094-016-1434-x
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Functional characterization of a novel CYP119 variant to explore its biocatalytic potential.
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- Biotechnology & Applied Biochemistry, 2022, v. 69, n. 4, p. 1741, doi. 10.1002/bab.2243
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Construction and characterization of novel bifunctional fusion proteins composed of alcohol dehydrogenase and NADH oxidase with efficient oxidized cofactor regeneration.
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- Biotechnology & Applied Biochemistry, 2022, v. 69, n. 4, p. 1535, doi. 10.1002/bab.2225
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