1. Baker P, et al. 1997. Determinants of Substrate Specificity in the Superfamily of Amino Acid Dehydrogenases. Biochemistry 36, 16109-16115.
  2. Banerjee, S, et al. 2003. Structural Studies on ADP Activation of Mammalian Glutamate Dehydrogenase and the Evolution of Regulation. Biochemistry 42, 3446-3456.
  3. Biesecker, G; et al. 1977. Sequence and Structure of Glyceraldehyde 3-Phosphate from Bacillus stearothermophilus. Nature, 266: 328-33.
  4. Consalvi, V et al. 2000. Thermal unfolding and conformational stability of the recombinant domain II of glutamate dehydrogenase from the hyperthermophile Thermotoga maritime Protein Engineering. 13(7), 501-507.
  5. Goda, S, et al. 2005. Intersubunit Interaction Induced by Subunit Rearrangement is Essential for the Catalytic Activity of the Hyperthermophilic Glutamate Dehydrogenase from Pyrobaculum islandicum. Biochemistry, 44(46), 15304-15313.
  6. Hurley, James H.; Dean, Anthony M.; Koshland, Daniel E.; Stroud, Robert M.  Catalytic Mechanism of NADP+ Dependent Dehydrogenase: Implications from the Structures of Magnesium-Isocitrate and NADP+ Complexes.  Biochemistry 1991, 30, 8671-8678.
  7. Kim, Yong-Ou; Koh, Ho-Jin; Kim, Seok-Hyung; Jo, Seung-Hee; Huh, Jae-Wook; Jeong, Kyu-Shik; Lee, Insong J.; Song, Byoung J.; Huh, Tae-Lin. Identification and Functional Characterization of a Novel, Tissue-specific NAD+ dependent Isocitrate Dehydrogenase Beta-subunit Isoform.  Journal of Biochemistry 1999, 274, 36866-36875.
  8. Mescar, Andrew D., Stoddard, Barry L., Koshland, Daniel E Jr.  Orbital Steering in the Catalytic Power of Enzymes: Small structural Changes with Large Catalytic Consequences. Science 1997, 277 pp. 202.
  9. Nakasako, M, 2001. Large-Scale Domain Movements and Hydration Structure Changes in the Active-Site Cleft of Unligated Glutamate Dehydrogenase from Thermococcus profundus Studied by Cryogenic X-ray Crystal Structure Analysis and Small-Angle X-ray Scattering. Biochemistry 40, 3069-3079.
  10. Saukri, A.; et al. 1989.  Role of Histidine 176 Residue in Glyceraldehyde 3- Phosphate Dehydrogenase as Probed by Site Directed Mutagenesis. Biochemistry, 28(6): 2586-2592.
  11. Skarzynksy, T.; et al. 1987. Structure of Holo Glyceraldehyde 3-Phosphate Dehydrogenase from Bacillus stearothermophilus at 1.8 A Resolution. J. Mol. Biol, 193(1): 171-187.
  12. Song, S.; 1999. Structure of the Active Site of Glyceraldehyde 3-Phosphate Dehydrogenase. J. Mol. Biol, 287(4): 719-25.
  13. Stillman T.J, et al. 1993. Conformational Flexibility in Glutamate Dehydrogenase Role of Water in Substrate Recognition and Catalysis. J. Mol. Biol, 234(4): 1131-1139.
  14. Stoddard, Barry L.; Koshland, Daniel E. Jr.  1993. Structure of Isocitrate Dehydrogenase with Isocitrate, Nicotinamide Adenine dinucleotide Phosphate, and Calcium at 2.5-A Resolution: A Pseudo-Michaelis Ternary Structure.  Biochemistry, 32, 9310-9316.
  15. Stryer (Ed.). Biochemistry (5th Ed.) 2002. W.H. Freeman and Company, New York. 
  16. Tanner, John J.; Hecht, Ralph M.; Krause Kurt L.  Determinants of Enzyme Thermostability Observed in the Molecular Structure of Thermus aquaticus D-Glyceraldehyde-3-phosphate Dehydrogenase at 2.5 A Resolution.  Biochemistry 1996, 35(8), 2597-2609. 
  17. A Medical Terminology Dictionary Published at the Dept. of Medical Oncology, University of Newcastle upon Tyne © Copyright 1997-2005
  18. Protein Data Bank
  19. Wikipedia, the free encyclopedia,
  20. The Medical Biochemistry Page,

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