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nad and methylmalonic acid

nad has been researched along with methylmalonic acid in 5 studies

Research

Studies (5)

TimeframeStudies, this research(%)All Research%
pre-19903 (60.00)18.7374
1990's0 (0.00)18.2507
2000's0 (0.00)29.6817
2010's2 (40.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Hämäläinen, MM1
Fleischer, S; Fritzsche, TM; McIntyre, JO; Trommer, WE1
el Kebbaj, MS; Gaudemer, Y; Latruffe, N1
Branlant, G; Stines-Chaumeil, C; Talfournier, F1
Hoque, MM; Kanazawa, H; Kawai, G; Kondo, J; Suzuki, K; Takénaka, A; Tsunoda, M; Yamamoto, T1

Other Studies

5 other study(ies) available for nad and methylmalonic acid

ArticleYear
Organic aciduria in rats fed high amounts of xylitol or sorbitol.
    Toxicology and applied pharmacology, 1987, Sep-15, Volume: 90, Issue:2

    Topics: Animals; Body Weight; Citrates; Citric Acid; Cytoplasm; Gas Chromatography-Mass Spectrometry; Hydrogen-Ion Concentration; Ketoglutaric Acids; Malates; Male; Malonates; Methylmalonic Acid; NAD; Oxalates; Oxalic Acid; Rats; Rats, Inbred Strains; Sorbitol; Xylitol

1987
Complex formation between nucleotides and D-beta-hydroxybutyrate dehydrogenase studied by fluorescence and EPR spectroscopy.
    Biochimica et biophysica acta, 1984, Dec-07, Volume: 791, Issue:2

    Topics: Animals; Cattle; Electron Spin Resonance Spectroscopy; Energy Transfer; Glycerol; Hydrogen-Ion Concentration; Hydroxybutyrate Dehydrogenase; Kinetics; Liposomes; Methylmalonic Acid; NAD; Phosphatidylcholines; Spectrometry, Fluorescence; Spin Labels; Sulfites

1984
Evidence for the presence of one carboxyl group in the catalytic center of D-beta-hydroxybutyrate dehydrogenase. Inactivation and binding studies with carbodiimide reagents.
    Biochimica et biophysica acta, 1984, Sep-25, Volume: 789, Issue:3

    Topics: Animals; Apoenzymes; Carbodiimides; Dicyclohexylcarbodiimide; Ethyldimethylaminopropyl Carbodiimide; Glycine; Hydroxybutyrate Dehydrogenase; Kinetics; Methylmalonic Acid; Mitochondria, Liver; NAD; Oxidation-Reduction; Phospholipids; Rats

1984
Methylmalonate-semialdehyde dehydrogenase from Bacillus subtilis: substrate specificity and coenzyme A binding.
    The Journal of biological chemistry, 2011, Jun-24, Volume: 286, Issue:25

    Topics: Aldehydes; Amino Acid Sequence; Amino Acid Substitution; Animals; Bacillus subtilis; Biocatalysis; Coenzyme A; Enzyme Stability; Esterification; Humans; Kinetics; Methylmalonate-Semialdehyde Dehydrogenase (Acylating); Methylmalonic Acid; Molecular Sequence Data; Mutation; NAD; Protein Binding; Rats; Substrate Specificity

2011
Structural insights into the catalytic reaction trigger and inhibition of D-3-hydroxybutyrate dehydrogenase.
    Acta crystallographica. Section F, Structural biology communications, 2016, Volume: 72, Issue:Pt 7

    Topics: 3-Hydroxybutyric Acid; Alcaligenes faecalis; Amino Acid Motifs; Bacterial Proteins; Catalytic Domain; Crystallography, X-Ray; Enzyme Inhibitors; Gene Expression; Glutamine; Hydrogen Bonding; Hydrophobic and Hydrophilic Interactions; Hydroxybutyrate Dehydrogenase; Malonates; Methylmalonic Acid; Models, Molecular; NAD; Protein Binding; Protein Conformation, alpha-Helical; Protein Conformation, beta-Strand; Protein Interaction Domains and Motifs; Protein Multimerization; Protein Subunits; Recombinant Proteins; Substrate Specificity; Tyrosine

2016