Cryptosporidium parvum IMP Dehydrogenase

This publication has 43 references indexed in Scilit:

• A first glimpse into the pattern and scale of gene transfer in the Apicomplexa
  International Journal for Parasitology, 2004
• Crystal Structure of a Ternary Complex of Tritrichomonas foetus Inosine 5‘-Monophosphate Dehydrogenase: NAD⁺ Orients the Active Site Loop for Catalysis^,
  Biochemistry, 2002
• 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
• Drug Selectivity Is Determined by Coupling Across the NAD⁺ Site of IMP Dehydrogenase
  Biochemistry, 2000
• Species-Specific Inhibition of Inosine 5‘-Monophosphate Dehydrogenase by Mycophenolic Acid
  Biochemistry, 1999
• Efficacy of select antivirals againstCryptosporidium parvumin vitro
  FEMS Microbiology Letters, 1998
• Kinetic Mechanism of Human Inosine 5‘-Monophosphate Dehydrogenase Type II: Random Addition of Substrates and Ordered Release of Products
  Biochemistry, 1997
• Purification of IMP dehydrogenase from rat hepatoma 3924A
  Life Sciences, 1987
• Purification, characterization, and kinetic analysis of inosine 5′-monophosphate dehydrogenase of Tritrichomonas foetus
  Molecular and Biochemical Parasitology, 1987
• The kinetics of enzyme-catalyzed reactions with two or more substrates or products
  Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 1963