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Gene Review

GLUD1  -  glutamate dehydrogenase 1

Bos taurus

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Disease relevance of GLUD1


High impact information on GLUD1


Chemical compound and disease context of GLUD1


Biological context of GLUD1


Anatomical context of GLUD1


Associations of GLUD1 with chemical compounds


Other interactions of GLUD1


Analytical, diagnostic and therapeutic context of GLUD1


  1. The structure of bovine glutamate dehydrogenase provides insights into the mechanism of allostery. Peterson, P.E., Smith, T.J. Structure (1999) [Pubmed]
  2. Molecular gene cloning, expression, and characterization of bovine brain glutamate dehydrogenase. Kim, D.W., Eum, W.S., Jang, S.H., Yoon, C.S., Kim, Y.H., Choi, S.H., Choi, H.S., Kim, S.Y., Kwon, H.Y., Kang, J.H., Kwon, O.S., Cho, S.W., Park, J., Choi, S.Y. J. Biochem. Mol. Biol. (2003) [Pubmed]
  3. Selection, expression, and nucleotide sequencing of the glutamate dehydrogenase gene of Peptostreptococcus asaccharolyticus. Snedecor, B., Chu, H., Chen, E. J. Bacteriol. (1991) [Pubmed]
  4. Biochemical indicators of liver injury in calves with experimental fascioliasis. Anderson, P.H., Berrett, S., Brush, P.J., Hebert, C.N., Parfitt, J.W., Patterson, D.S. Vet. Rec. (1977) [Pubmed]
  5. Glutamate dehydrogenase in Reye's syndrome. Evidence for the presence of an altered enzyme in serum with increased susceptibility to inhibition by GTP. Holt, J.T., Arvan, D.A., Mayer, T., Smith, T.J., Bell, J.E. Biochim. Biophys. Acta (1983) [Pubmed]
  6. Radiation inactivation of glutamate dehydrogenase hexamer: lack of energy transfer between subunits. Kempner, E.S., Miller, J.H. Science (1983) [Pubmed]
  7. Carbonyl oxygen exchange evidence of imine formation in the glutamate dehydrogenase reaction and identification of the "occult role" of NADPH. Fisher, H.F., Viswanathan, T.S. Proc. Natl. Acad. Sci. U.S.A. (1984) [Pubmed]
  8. Partial amino-acid sequence of NAD-specific glutamate dehydrogenase of Neurospora crassa. Austen, B.M., Nyc, J.F., Degani, Y., Smith, E.L. Proc. Natl. Acad. Sci. U.S.A. (1975) [Pubmed]
  9. Identification of an NAD+ binding site of brain glutamate dehydrogenase isoproteins by photoaffinity labeling. Cho, S.W., Yoon, H.Y., Ahn, J.Y., Choi, S.Y., Kim, T.U. J. Biol. Chem. (1998) [Pubmed]
  10. Field study of dairy cows with reduced appetite in early lactation: clinical examinations, blood and rumen fluid analyses. Steen, A. Acta Vet. Scand. (2001) [Pubmed]
  11. Concentrations of isometamidium chloride (Samorin) in sera of Zebu cattle which showed evidence of hepatotoxicity following frequent trypanocidal treatments. Eisler, M.C., Stevenson, P., Munga, L., Smyth, J.B. J. Vet. Pharmacol. Ther. (1997) [Pubmed]
  12. Partial amino acid sequence of the glutamate dehydrogenase of human liver and a revision of the sequence of the bovine enzyme. Julliard, J.H., Smith, E.L. J. Biol. Chem. (1979) [Pubmed]
  13. Structures of bovine glutamate dehydrogenase complexes elucidate the mechanism of purine regulation. Smith, T.J., Peterson, P.E., Schmidt, T., Fang, J., Stanley, C.A. J. Mol. Biol. (2001) [Pubmed]
  14. Structural studies on ADP activation of mammalian glutamate dehydrogenase and the evolution of regulation. Banerjee, S., Schmidt, T., Fang, J., Stanley, C.A., Smith, T.J. Biochemistry (2003) [Pubmed]
  15. A new affinity label for guanosine nucleotide sites in proteins. Pal, P.K., Reischer, R.J., Wechter, W.J., Colman, R.F. J. Biol. Chem. (1978) [Pubmed]
  16. Regulation of glutamate dehydrogenase by Mg2+ and magnification of leucine activation by Mg2+. Fahien, L.A., Teller, J.K., Macdonald, M.J., Fahien, C.M. Mol. Pharmacol. (1990) [Pubmed]
  17. Purification and properties of the soluble carnitine palmitoyltransferase from bovine liver mitochondria. Ramsay, R.R., Derrick, J.P., Friend, A.S., Tubbs, P.K. Biochem. J. (1987) [Pubmed]
  18. Quantitative ultrastructural localization of glutamate dehydrogenase in the rat cerebellar cortex. Rothe, F., Brosz, M., Storm-Mathisen, J. Neuroscience (1995) [Pubmed]
  19. The interaction of phospholipid membranes and detergents with glutamate dehydrogenase. Nemat-Gorgani, M., Dodd, G. Eur. J. Biochem. (1977) [Pubmed]
  20. The interaction of phospholipid membranes and detergents with glutamate dehydrogenase. Nemat-Gorgani, M., Dodd, G. Eur. J. Biochem. (1977) [Pubmed]
  21. Nicotinamide adenine dinucleotide-specific glutamate dehydrogenase of Neurospora. IV. The COOH-terminal 669 residues of the peptide chain; comparison with other glutamate dehydrogenases. Austen, B.M., Haberland, M.E., Nyc, J.F., Smith, E.L. J. Biol. Chem. (1977) [Pubmed]
  22. Effect of aspartate on complexes between glutamate dehydrogenase and various aminotransferases. Fahien, L.A., Hsu, S.L., Kmiotek, E. J. Biol. Chem. (1977) [Pubmed]
  23. Effects of level of feed intake and Fusarium toxin-contaminated wheat on rumen fermentation as well as on blood and milk parameters in cows. Seeling, K., Lebzien, P., Dänicke, S., Spilke, J., Südekum, K.H., Flachowsky, G. Journal of animal physiology and animal nutrition. (2006) [Pubmed]
  24. Antibodies against the bovine brain glutamate binding protein. Roy, S., Michaelis, E.K. J. Neurochem. (1984) [Pubmed]
  25. Conformations of nicotinamide coenzymes bound to dehydrogenases determined by transferred nuclear Overhauser effects. Levy, H.R., Ejchart, A., Levy, G.C. Biochemistry (1983) [Pubmed]
  26. Complexes between mitochondrial enzymes and either citrate synthase or glutamate dehydrogenase. Fahien, L.A., Kmiotek, E. Arch. Biochem. Biophys. (1983) [Pubmed]
  27. Comparison of the primary structure of nuclear and mitochondrial glutamate dehydrogenase from bovine liver. McDaniel, H.G. Arch. Biochem. Biophys. (1995) [Pubmed]
  28. Identification of bovine glutamate dehydrogenase as an RNA-binding protein. Preiss, T., Hall, A.G., Lightowlers, R.N. J. Biol. Chem. (1993) [Pubmed]
  29. The allosteric mechanism of bovine liver glutamate dehydrogenase. Evidence from circular-dichroism studies for a conformational change in the ternary complex enzyme-(oxidized nicotinamide-adenine dinucleotide)-glutarate. Chen, S.S., Engel, P.C. Biochem. J. (1977) [Pubmed]
  30. Purification of glutamate dehydrogenase from ox brain and liver. Evidence that commercially available preparations of the enzyme from ox liver have suffered proteolytic cleavage. McCarthy, A.D., Walker, J.M., Tipton, K.F. Biochem. J. (1980) [Pubmed]
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