Crystal Structure of Tritrichomonas foetus Inosine Monophosphate Dehydrogenase in Complex with the Inhibitor Ribavirin Monophosphate Reveals a Catalysis-dependent Ion-binding Site

This publication has 33 references indexed in Scilit:

• Crystal Structure at 2.4 Å Resolution of Borrelia burgdorferi Inosine 5‘-Monophosphate Dehydrogenase: Evidence of a Substrate-Induced Hinged-Lid Motion by Loop 6^,
  Biochemistry, 2000
• Crystal structure of human type II inosine monophosphate dehydrogenase: Implications for ligand binding and drug design
  Proceedings of the National Academy of Sciences, 1999
• Characteristics and Crystal Structure of Bacterial Inosine-5‘-monophosphate Dehydrogenase^,
  Biochemistry, 1999
• Acid−Base Catalysis in the Chemical Mechanism of Inosine Monophosphate Dehydrogenase
  Biochemistry, 1999
• Kinetic Mechanism of Tritrichomonas foetus Inosine 5‘-Monophosphate Dehydrogenase
  Biochemistry, 1999
• Crystal Structure ofTritrichomonas foetusInosine-5‘-monophosphate Dehydrogenase and the Enzyme−Product Complex
  Biochemistry, 1997
• Kinetic Mechanism of Human Inosine 5‘-Monophosphate Dehydrogenase Type II: Random Addition of Substrates and Ordered Release of Products
  Biochemistry, 1997
• The structure of a domain common to archaebacteria and the homocystinuria disease protein
  Trends in Biochemical Sciences, 1997
• Structure and Mechanism of Inosine Monophosphate Dehydrogenase in Complex with the Immunosuppressant Mycophenolic Acid
  Cell, 1996
• Preliminary X‐ray crystallographic analysis of Tritrichomonas foetus inosine‐5′‐monophosphate dehydrogenase
  Proteins-Structure Function and Bioinformatics, 1995