Characterization of the allosteric binding pocket of human liver fructose-1,6-bisphosphatase by protein crystallography and inhibitor activity studies

This publication has 20 references indexed in Scilit:

• Structural aspects of the allosteric inhibition of fructose-1,6-bisphosphatase by AMP: the binding of both the substrate analog 2,5-anhydro-D-glucitol 1,6-bisphosphate and catalytic metal ions monitored by x-ray crystallography
  Biochemistry, 1995
• Toward a Mechanism for the Allosteric Transition of Pig Kidney Fructose-1,6-Bisphosphatase
  Journal of Molecular Biology, 1994
• The CCP4 suite: programs for protein crystallography
  Acta Crystallographica Section D-Biological Crystallography, 1994
• PROCHECK: a program to check the stereochemical quality of protein structures
  Journal of Applied Crystallography, 1993
• Crystallographic studies of the catalytic mechanism of the neutral form of fructose-1,6-bisphosphatase
  Biochemistry, 1993
• Conformational transition of fructose-1,6-bisphosphatase: structure comparison between the AMP complex (T form) and the fructose 6-phosphate complex (R form)
  Biochemistry, 1991
• Improved methods for building protein models in electron density maps and the location of errors in these models
  Acta Crystallographica Section A Foundations of Crystallography, 1991
• Contribution of Gluconeogenesis to Overall Glucose Output in Diabetic and Nondiabetic Men
  Annals of Medicine, 1990
• HORMONAL REGULATION OF HEPATIC GLUCONEOGENESIS AND GLYCOLYSIS
  Annual Review of Biochemistry, 1988
• Precursors in the biosynthesis of purine nucleotides. The crystal structures of 5-amino-1-β-D-riboluranosylimidazole-4-carboxamide (AICAR) and its 5'-(dihydrogen phosphate)
  Acta Crystallographica Section B: Structural Science, Crystal Engineering and Materials, 1979