33
Views
7
CrossRef citations to date
0
Altmetric
Review

Inhibitors of inosine monophosphate dehydrogenase as potential chemotherapeutic agents

Pages 1161-1170 | Published online: 25 Feb 2005

Bibliography

  • LIU Y, BOHN SA, SHERLEY JL: Inosine 5'-monophosphate dehydrogenase is a rate-determining factor for p53-dependent growth regulation. Ma. Biol. Cell (1998) 9:15–28.
  • •Demonstrates the importance of IMPDH inhibition in cancer.
  • SAUNDERS JO, RAYBUCK SA: Inosine monophosphate dehydrogenase: consideration of structure, kinetics, and therapeutic potential. In: Annual Reports in Medicinal Chemistry Doherty AM (Ed.), Academic Press, San Diego, USA (2000):201–209.
  • COLLART F, HUBERMAN E: Cloning and sequence analysis of the human and Chinese hamster inosine-5'-monophosphate dehydrogenase cDNA. j Biol. Chem. (1988) 263: 15769–15772.
  • CARR SF, PAPP E, WU JC, NATSUMEDA Y: Characterization of human type land type II IMP dehydrogenase. Bia. Chem. (1993) 268:27286–2729.
  • GU JJ, STEGMANN S, GATHY K et al.: Inhibition of T lymphocyte activation in mice heterozygous for loss of the IMPDHII gene. J. Clin. Invest. (2000) 106:599–606.
  • •Demonstrates the importance of IMPDH type II gene for activation of lymphocytes.
  • BARNES BJ, EAKIN AE, IZYDORE RA, HALL IH: Selective inhibition of human Molt-4 leukemia type II inosine 5'-monophosphate dehydrogenase by the 1,5-diazabicyclo [3.1.01hexana-2,4-diones. Biochemistry (2000) 39:13641–13650.
  • ••The demonstration of specific inhibition ofIMPDH type II.
  • COLBY TD, VENDERVEEN K, STRICKLER MD, MARKHAM GD, GOLDSTEIN BM: Crystal structure of human type II inosine monophosphate dehydrogenase: implications for ligand binding and drug design. Proc. Nati Acad. Sci. USA.(1999) 96:3531-3536. Details the crystal structure of human IMPDH type II and discissues the differences between the two isoforms.
  • DIGITS JA, HEDSTROM L: Drug selectivity is determined by coupling across the NAD site of IMP dehydrogenase. Biochemistry (2000) 39:1771–1777.
  • •Describes the importance of NAD site for inhibition of IMPDH.
  • DIGITS JA, HEDSTROM L: Species-specific inhibition of inosine 5'-monophosphate dehydrogenase by mycophenolic acid. Biochemistry (1999) 38:15388–15397.
  • NIMMERSGERN E, FOX T, FLEMING MA, THOMSON JA: Conformational changes and stabilization of inosine 5'-monophosphate dehydrogenase associated with ligand binding and inhibition by mycophenolic acid. j Biol. Chem. (1996) 271: 19421–19427.
  • WANG W, HEDSTROM L: Kinetic mechanism of human inosine 5'-monophosphate dehydrogenase type II: random addition of substrates and ordered release of products. Biochemistry (1997) 36:8479–8483.
  • FLEMING MA, CHAMBERS SP, CONELLY PR et al.: Inhibition of IMPDH by mycophenolic acid: dissection of forward and reverse pathways using capillary electrophoresis. Biochemistry (1996) 35:6990-6997. 38:4691–4700.
  • •Details the crystal structure of IMPDH from other than human sources. Comparison with the human enzyme shows the possibility of specific inhibition of these enzymes.
  • YE D, LEE CH, QUEENER SF: Differential splicing of Pneumocistis carinli f. sp. caniiii inosine 5'-monophosphate dehydrogenase pre-mRNA. Gene (2001) 263:151–158.
  • •As 14.
  • MCMILLAN FM, CAHOON M, WHITE A, HEDSTROM L, PETSKO GA, RINGE D: Crystal structure at 2.4 A resolution of Borrelia burgdorktiinosine 5'-monophosphate dehydrogenase: evidence of a substrate-induced hinged-lid motion by loop 6. Biochemistry (2000) 39:4533-4542. As 14.
  • WHITBY FG, LUECKE H, KUHN P et al.: Crystal structure of Tritrichomortas foetus inosine-5'-monophosphate dehydrogenase and the enzyme-product complex. Biochemistry (1997) 36:10666-10674. As 14.
  • SINTCHAK MD, NIMMESGERN E: The structure of inosine 5'-monophosphate dehydrogenase and the design of novel inhibitors. branurtophannacology (2000) 47:163–184.
  • •As 14.
  • TAM RC, RAMASAMY K, BARD J, PAI B, LIM B, AVERETT DR: The ribavirin analog ICN 17261 demonstrates reduced toxicity and antiviral effects with retention of both immunomodulatory activity and reduction of Hepatitis-induced serum alanine aminotransferase levels. Antlinicrob. Agents Chemother. (2000) 44:1276–1283.
  • KERR KM, HEDSTROM L: The roles of conserved carboxylate residues in IMP dehydrogenase and identification of a transition state analog. Biochemistry (1997) 36:13365–13373.
  • •Mechanisn of action of hredinin, used in clinics as an immunosuppresssant, is discussed.
  • MINAKAWA N, MTSUDA A: Mechanism-based design of inosine 5'-monophosphate dehydrogenase inhibitors: synthesis and biological activities of 5-ethynyl 1 13 ribofuranosylimidazole-4-carboxamide (EICAR) and its derivatives. Cun: Med. Chem. (1999) 6:615–628.
  • FRANKLIN TJ, JACOBS VN, JONES G, PLE P: Human collorectal carcinoma cells in vitro as a means to assess the metabolism of analogues of mycophenolic acid. Drug Metabolism Disp. (1997) 25:367–370.
  • MARKLAND W, MCQUAID TJ, JAIN J, KWONG AD. Broad-spectrum antiviral activity of the IMP dehydrogenase inhibitor VX-497: a comparison with ribavirin and demonstration of antiviral additivity with alpha interferon. Antimicrob. Agents Chemother. (2000) 44:859–866.
  • •Antiviral activity of VX-497 is discussed. This Vertex compound is in Phase II clinical trials.
  • EDELSON S: Vertex: a small bump in the road. BioCentury (2001) 5:A6.
  • 25.FRANKLIN TJ, MORRIS WP JACOBS VN et al.: A novel series of non-nucleoside inhibitors of inosine 5'-monophosphate dehydrogenase with immunosuppressive activity. Biochem. Pharmacol. (1999) 58:867–876.
  • ••A novel class of inhibitors of IMPDH arediscovered.
  • GEBEYEHU G, MARQUEZ VE, VAN COTT A et al: Ribavirin, tiazofurin, selenazofurin: mononucleotides and nicotinamide adenine dinucleotide analogues. Synthesis, structure, and interactions with IMP dehydrogenase. Med. Chem. (1985) 28:99–105.
  • FRANCHETTI E MARCHETTI S, CAPPELLACCI L et al: Synthesis, conformational analysis, and biological activity of C-thioribonucleosides related to tiazofurin. j Med. Chem. (2000) 43:1264–1270.
  • FRANCHETTI E MARCHETTI S, CAPELLACCI L et al: A new C-nucleoside analogue of tiazofurin: synthesis and biological evaluation 2-13-ribofuranosylimidazole-4-carbox-amide (imidazofurin). Bioorg. Med. Chem. Lett. (2001) 11:67–69.
  • RAUKO P, NOVOTNY L, DOVINOVA I, HUNAKOVA L, SZEKERES T, JAYARAM HN: Antitumor activity of benzamide riboside and its combination with cis-platin and staurosporine. Eur. Pharm. Sci. (2001) 12:387–394.
  • LESIAK K, WATANABE KA, MAJUMDAR A et al.: Synthesis of nonhydrolyzable analogues of thiazole-4-carboxamide and benzamide adenine dinucleotide containing fluorine atom at the C2' of adenine nucleoside: induction of K562 differentiation and inosine monophosphate dehydrogenase inhibitory activity. j Med. Chem. (1997) 40:2533–2538.
  • •Novel bis(phosphonate) analogues of NAD under development in Pharmasset are described.
  • SINTCHAK MD, FLEMING MA, FUTER 0 et al: Structure and mechanism of inosine monophosphate dehydrogenase in complex with the immunosuppressant mycophenolic acid. Cell (1996) 85:921–930.
  • •Mechanisn of action of mycophenolic acid, used in clinics as an immunosuppresssant, is discussed.
  • LESIAK K,WATANABE KA, MAJUMDAR A et al.: Synthesis of a methylenebis(phosphonate) analogue of mycophenolic adenine dinucleotide: a glucuronidation-resistant MAD analogue of NAD. j Med. Chem. (1998) 41:618–622.
  • •As 30.
  • PANKIEWICZ KW, MALINOWSKI K, JAYARAM HN, LESIAK-WATANABE K, WATANABE KA. Novel mycophenolic adenine bis(phosphonate)s as potential immunosuppressants. Curr. Med. Chem. (1999) 6:629–634.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.