Effect of additives on the crystallization of glutamate dehydrogenase from Clostridium symbiosum: Evidence for a ligand-induced conformational change

This publication has 13 references indexed in Scilit:

• Subunit assembly and active site location in the structure of glutamate dehydrogenase
  Proteins-Structure Function and Bioinformatics, 1992
• The partial amino acid sequence of the NAD -dependent glutamate dehydrogenase of Clostridium symbiosum: implications for the evolution and structural basis of coenzyme specificity
  Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1991
• Identification of three essential lysine residues probably involved in substrate binding of the NAD+ - dependent glutamate dehydrogenase of Clostridium symbiosum
  Biochemical Society Transactions, 1988
• Multiple interactions of lysine-128 of Escherichia coli glutamate dehydrogenase revealed by site-directed mutagenesis studies
  Protein Engineering, Design and Selection, 1988
• Crystallization of an NAD+-dependent glutamate dehydrogenase from Clostridium symbiosum
  Journal of Molecular Biology, 1985
• Complete nucleotide sequence of theEscherichia coli gdhAgene
  Nucleic Acids Research, 1983
• l-Glutamic acid dehydrogenase
  International Journal of Biochemistry, 1981
• Slow conformational changes of a Neurospora glutamate dehydrogenase studied by protein fluorescence
  Biochemical Journal, 1974
• Association behaviour of rat liver glutamate dehydrogenase
  FEBS Letters, 1972
• L-Glutamate Dehydrogenases* *Research work cited in this review which originates in the author's laboratory was supported in part by research grant AM 13332, United States Public Health Service and research grant GB 26583X from the National Science Foundation.
  Current Topics in Cellular Regulation, 1971