메뉴 건너뛰기




Volumn 10, Issue 3, 2010, Pages 226-239

Plasmodium dihydroorotate dehydrogenase: A promising target for novel anti-malarial chemotherapy

Author keywords

Dihydroorotate dehydrogenase; Drug discovery; Malaria; Plasmodium; Pyrimidine biosynthesis

Indexed keywords

AMIDE; ANTIMALARIAL AGENT; BENZAMIDE DERIVATIVE; DIHYDROOROTATE DEHYDROGENASE; DSM 74; NAPHTHYL GROUP; PYRIMIDINE; PYRIMIDINE DERIVATIVE; THIOPHENE DERIVATIVE; TRIAZOLE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 77953773127     PISSN: 18715265     EISSN: None     Source Type: Journal    
DOI: 10.2174/187152610791163336     Document Type: Article
Times cited : (199)

References (87)
  • 2
    • 39849106369 scopus 로고    scopus 로고
    • The limits and intensity of Plasmodium falciparum transmission: Implications for malaria control and elimination worldwide
    • Guerra, C.A.; Gikandi, P.W.; Tatem, A.J.; Noor, A.M.; Smith, D.L.; Hay, S.I.; Snow, R.W. The limits and intensity of Plasmodium falciparum transmission: implications for malaria control and elimination worldwide. PLoS Med., 2008, 5(2), e38.
    • (2008) PLoS Med. , vol.5 , Issue.2
    • Guerra, C.A.1    Gikandi, P.W.2    Tatem, A.J.3    Noor, A.M.4    Smith, D.L.5    Hay, S.I.6    Snow, R.W.7
  • 3
    • 55049131325 scopus 로고    scopus 로고
    • Challenges facing drug development for malaria
    • Craft, J.C. Challenges facing drug development for malaria. Curr. Opin. Microbiol., 2008, 11(5), 428-433.
    • (2008) Curr. Opin. Microbiol. , vol.11 , Issue.5 , pp. 428-433
    • Craft, J.C.1
  • 4
    • 2142659388 scopus 로고    scopus 로고
    • Antimalarial drug resistance
    • White, N.J. Antimalarial drug resistance. J. Clin. Invest., 2004, 113(8), 1084-1092.
    • (2004) J. Clin. Invest. , vol.113 , Issue.8 , pp. 1084-1092
    • White, N.J.1
  • 5
    • 0030829371 scopus 로고    scopus 로고
    • Variations in frequencies of drug resistance in Plasmodium falciparum
    • Rathod, P.K.; McErlean, T.; Lee, P.C. Variations in frequencies of drug resistance in Plasmodium falciparum. Proc. Natl. Acad. Sci. USA, 1997, 94(7), 9389-9393.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , Issue.7 , pp. 9389-9393
    • Rathod, P.K.1    McErlean, T.2    Lee, P.C.3
  • 6
    • 57649119910 scopus 로고    scopus 로고
    • The role of anti-malarial drugs in eliminating malaria
    • White, N.J. The role of anti-malarial drugs in eliminating malaria. Malar. J., 2008, 11(7) (Suppl 1), S8.
    • (2008) Malar. J. , vol.11 , Issue.7 SUPPL 1
    • White, N.J.1
  • 7
    • 42549101925 scopus 로고    scopus 로고
    • Artesunate for the treatment of severe falciparum malaria
    • Rosenthal, P.J. Artesunate for the treatment of severe falciparum malaria. N. Engl. J. Med., 2008, 358(17), 1829-1836.
    • (2008) N. Engl. J. Med. , vol.358 , Issue.17 , pp. 1829-1836
    • Rosenthal, P.J.1
  • 9
    • 34548126497 scopus 로고    scopus 로고
    • Drug discovery for malaria: A very challenging and timely endeavor
    • Gelb, M.H. Drug discovery for malaria: a very challenging and timely endeavor. Curr. Opin. Chem. Biol., 2007, 11(4), 440-445.
    • (2007) Curr. Opin. Chem. Biol. , vol.11 , Issue.4 , pp. 440-445
    • Gelb, M.H.1
  • 10
    • 67349124872 scopus 로고    scopus 로고
    • The global portfolio of new antimalarial medicines under development
    • Olliaro, P.; Wells, T.N. The global portfolio of new antimalarial medicines under development. Clin. Pharmacol. Ther., 2009, 85(6), 584-595.
    • (2009) Clin. Pharmacol. Ther. , vol.85 , Issue.6 , pp. 584-595
    • Olliaro, P.1    Wells, T.N.2
  • 12
    • 0026605065 scopus 로고
    • Site of action of the antimalarial hydroxynaphthoquinone, 2-[trans-4-(4'-chlorophenyl) cyclohexyl]-3-hydroxy-1,4-naphthoquinone (566C80)
    • Fry, M.; Pudney, M. Site of action of the antimalarial hydroxynaphthoquinone, 2-[trans-4-(4'-chlorophenyl) cyclohexyl]-3-hydroxy-1,4-naphthoquinone (566C80). Biochem. Pharmacol., 1992, 43(7), 1545-1553.
    • (1992) Biochem. Pharmacol. , vol.43 , Issue.7 , pp. 1545-1553
    • Fry, M.1    Pudney, M.2
  • 14
    • 0032781364 scopus 로고    scopus 로고
    • Resistance mutations reveal the atovaquone-binding domain of cytochrome b in malaria parasites
    • Srivastava, I.; Morrisey, J.; Darrouzet, E.; Daldal, F.; Vaidya, A. Resistance mutations reveal the atovaquone-binding domain of cytochrome b in malaria parasites. Mol. Microbiol., 1999, 33(4), 704-711.
    • (1999) Mol. Microbiol. , vol.33 , Issue.4 , pp. 704-711
    • Srivastava, I.1    Morrisey, J.2    Darrouzet, E.3    Daldal, F.4    Vaidya, A.5
  • 15
    • 0031052025 scopus 로고    scopus 로고
    • Atovaquone, a broad spectrum antiparasitic drug, collapses mitochondrial membrane potential in a malarial parasite
    • Srivastava, I.; Rottenberg, H.; Vaidya, A. Atovaquone, a broad spectrum antiparasitic drug, collapses mitochondrial membrane potential in a malarial parasite. J. Biol. Chem., 1997, 272(7), 3961-3966.
    • (1997) J. Biol. Chem. , vol.272 , Issue.7 , pp. 3961-3966
    • Srivastava, I.1    Rottenberg, H.2    Vaidya, A.3
  • 16
    • 33845984935 scopus 로고    scopus 로고
    • Targeting purine and pyrimidine metabolism in human apicomplexan parasites
    • Hyde, J.E. Targeting purine and pyrimidine metabolism in human apicomplexan parasites. Curr. Drug Targets, 2007, 8(1), 31-47.
    • (2007) Curr. Drug Targets , vol.8 , Issue.1 , pp. 31-47
    • Hyde, J.E.1
  • 17
    • 0030865068 scopus 로고    scopus 로고
    • dCTP levels are maintained in Plasmodium falciparum subjected to pyrimidine deficiency or excess
    • Seymour, K.K.; Yeo, A.E.; Rieckmann, K.H.; Christopherson, R.I. dCTP levels are maintained in Plasmodium falciparum subjected to pyrimidine deficiency or excess. Ann. Trop. Med. Parasitol., 1997, 91(6), 603-9.
    • (1997) Ann. Trop. Med. Parasitol. , vol.91 , Issue.6 , pp. 603-609
    • Seymour, K.K.1    Yeo, A.E.2    Rieckmann, K.H.3    Christopherson, R.I.4
  • 18
    • 0028109373 scopus 로고
    • The effects of antimalarials on the Plasmodium falciparum dihydroorotate dehydrogenase
    • Ittarat, I.; Asawamahasakda, W.; Meshnick, S.R. The effects of antimalarials on the Plasmodium falciparum dihydroorotate dehydrogenase. Exp. Parasitol., 1994, 79(1), 50-56.
    • (1994) Exp. Parasitol. , vol.79 , Issue.1 , pp. 50-56
    • Ittarat, I.1    Asawamahasakda, W.2    Meshnick, S.R.3
  • 19
    • 33847398001 scopus 로고    scopus 로고
    • Specific role of mitochondrial electron transport in blood-stage Plasmodium falciparum
    • Painter, H. J.; Morrisey, J. M.; Mather, M. W.; Vaidya, A. B. Specific role of mitochondrial electron transport in blood-stage Plasmodium falciparum. Nature, 2007, 446(7131), 88-91.
    • (2007) Nature , vol.446 , Issue.7131 , pp. 88-91
    • Painter, H.J.1    Morrisey, J.M.2    Mather, M.W.3    Vaidya, A.B.4
  • 20
    • 70349536103 scopus 로고    scopus 로고
    • Mitochondrial Evolution and Functions in Malaria Parasites
    • Vaidya, A.B.; Mather, M.W. Mitochondrial Evolution and Functions in Malaria Parasites. Annu. Rev. Microbiol., 2009, 63, 249-267.
    • (2009) Annu. Rev. Microbiol. , vol.63 , pp. 249-267
    • Vaidya, A.B.1    Mather, M.W.2
  • 21
    • 0034019568 scopus 로고    scopus 로고
    • Potent and selective activity of a combination of thymidine and 1843U89, a folate-based thymidylate synthase inhibitor, against Plasmodium falciparum
    • Jiang, L.; Lee, P.C.; White, J.; Rathod, P.K. Potent and selective activity of a combination of thymidine and 1843U89, a folate-based thymidylate synthase inhibitor, against Plasmodium falciparum. Antimicrob. Agents Chemother., 2000, 44(4), 1047-1050.
    • (2000) Antimicrob. Agents Chemother. , vol.44 , Issue.4 , pp. 1047-1050
    • Jiang, L.1    Lee, P.C.2    White, J.3    Rathod, P.K.4
  • 22
    • 0024400016 scopus 로고
    • Selective activity of 5-fluoroorotic acid against Plasmodium falciparum in vitro
    • Rathod, P.K.; Khatri, A.; Hubbert, T.; Milhous, W.K. Selective activity of 5-fluoroorotic acid against Plasmodium falciparum in vitro. Antimicrobial. Agents Chemother., 1989, 33(7), 1090-1094.
    • (1989) Antimicrobial. Agents Chemother. , vol.33 , Issue.7 , pp. 1090-1094
    • Rathod, P.K.1    Khatri, A.2    Hubbert, T.3    Milhous, W.K.4
  • 23
    • 0026510588 scopus 로고
    • Molecular targets of 5-fluoroorotate in the human malaria parasite, Plasmodium falciparum
    • Rathod, P.K.; Leffers, N.P.; Young, R.D. Molecular targets of 5-fluoroorotate in the human malaria parasite, Plasmodium falciparum. Antimicrobial. Agents Chemother., 1992, 36(4), 704-711.
    • (1992) Antimicrobial. Agents Chemother. , vol.36 , Issue.4 , pp. 704-711
    • Rathod, P.K.1    Leffers, N.P.2    Young, R.D.3
  • 24
    • 0028295332 scopus 로고
    • Suceptibility of Plasmodium falciparum to a combination of thymidine and ICI D1694, a quinazoline antifolate directed at thymidylate synthase
    • Rathod, P.K.; Reshmi, S. Suceptibility of Plasmodium falciparum to a combination of thymidine and ICI D1694, a quinazoline antifolate directed at thymidylate synthase. Antimicrobial. Agents Chemother., 1994, 38(3), 476-480.
    • (1994) Antimicrobial. Agents Chemother. , vol.38 , Issue.3 , pp. 476-480
    • Rathod, P.K.1    Reshmi, S.2
  • 25
    • 0020596784 scopus 로고
    • Orotidylate-metabolizing enzymes of the human malarial parasite, Plasmodium falciparum, differ from host cell enzymes
    • Rathod, P.K.; Reyes, P., Orotidylate-metabolizing enzymes of the human malarial parasite, Plasmodium falciparum, differ from host cell enzymes. J. Biol. Chem., 1983, 258(5), 2852-2855.
    • (1983) J. Biol. Chem. , vol.258 , Issue.5 , pp. 2852-2855
    • Rathod, P.K.1    Reyes, P.2
  • 27
    • 0028943370 scopus 로고
    • Purification, characterization and localization of mitochondrial dihydroorotate dehydrogenase in Plasmodium falciparum, human malarial parasite
    • Krungkrai, J. Purification, characterization and localization of mitochondrial dihydroorotate dehydrogenase in Plasmodium falciparum, human malarial parasite. Biochim. Biophys. Acta, 1995, 1243(3), 351-360.
    • (1995) Biochim. Biophys. Acta , vol.1243 , Issue.3 , pp. 351-360
    • Krungkrai, J.1
  • 28
    • 0026533662 scopus 로고
    • Antimalarial activity of orotate analogs that inhibit dihdroorotase and dihydroorotate dehydrogenase
    • Krungkrai, J.; Krungkrai, S.R.; Phakanont, K. Antimalarial activity of orotate analogs that inhibit dihdroorotase and dihydroorotate dehydrogenase. Biochem. Pharmacol., 1992, 43(6), 1295-1301.
    • (1992) Biochem. Pharmacol. , vol.43 , Issue.6 , pp. 1295-1301
    • Krungkrai, J.1    Krungkrai, S.R.2    Phakanont, K.3
  • 29
    • 0027216320 scopus 로고
    • The dihydroorotate dehydrogenase gene homologue of Plasmodium falciparum
    • LeBlanc, S.B.; Wilson, C.M. The dihydroorotate dehydrogenase gene homologue of Plasmodium falciparum. Mol. Biochem. Parasitol., 1993, 60(2), 349-352.
    • (1993) Mol. Biochem. Parasitol. , vol.60 , Issue.2 , pp. 349-352
    • LeBlanc, S.B.1    Wilson, C.M.2
  • 30
    • 0034739441 scopus 로고    scopus 로고
    • Evolutionary implications of the mosaic pyrimidine-biosynthetic pathway in eukaryotes
    • Nara, T.; Hshimoto, T.; Aoki, T. Evolutionary implications of the mosaic pyrimidine-biosynthetic pathway in eukaryotes. Gene, 2000, 257(2), 209-222.
    • (2000) Gene , vol.257 , Issue.2 , pp. 209-222
    • Nara, T.1    Hshimoto, T.2    Aoki, T.3
  • 31
    • 0014740189 scopus 로고
    • Incorporatin of radioactive precursors into DNA and RNA of Plasmodium knowlesi
    • Gutteridge, W.E.; Trigg, P.I. Incorporatin of radioactive precursors into DNA and RNA of Plasmodium knowlesi. J. Protozool., 1970, 17(1), 89-96.
    • (1970) J. Protozool. , vol.17 , Issue.1 , pp. 89-96
    • Gutteridge, W.E.1    Trigg, P.I.2
  • 34
    • 0032763963 scopus 로고    scopus 로고
    • Leflunomide, a novel immunomodulator for the treatment of active rheumatoid arthritis
    • Goldenberg, M.M. Leflunomide, a novel immunomodulator for the treatment of active rheumatoid arthritis. Clin. Ther., 1999, 21(11), 1837-1852.
    • (1999) Clin. Ther. , vol.21 , Issue.11 , pp. 1837-1852
    • Goldenberg, M.M.1
  • 35
    • 0034122123 scopus 로고    scopus 로고
    • Leflunomide: An immunomodulatory drug for the treatment of rheumatoid arthritis and other autoimmune diseases
    • Herrmann, M.L.; Schleyerbach, R.; Kirschbaum, B.J. Leflunomide: an immunomodulatory drug for the treatment of rheumatoid arthritis and other autoimmune diseases. Immunopharmacology, 2000, 47(2-3), 273-289.
    • (2000) Immunopharmacology , vol.47 , Issue.2-3 , pp. 273-289
    • Herrmann, M.L.1    Schleyerbach, R.2    Kirschbaum, B.J.3
  • 36
    • 2442590862 scopus 로고    scopus 로고
    • New drugs for rheumatoid arthritis
    • Olsen, N.J.; Stein, C.M. New drugs for rheumatoid arthritis. N. Engl. J. Med., 2004, 350(21), 2167-2179.
    • (2004) N. Engl. J. Med. , vol.350 , Issue.21 , pp. 2167-2179
    • Olsen, N.J.1    Stein, C.M.2
  • 37
    • 0030032806 scopus 로고    scopus 로고
    • The immunosuppressive metabolite of leflunomide is a potent inhibitor of human dihydroorotate dehydrogenase
    • Davis, J.P.; Cain, G.A.; Pitts, W.J.; Magolda, R.L.; Copeland, R.A. The immunosuppressive metabolite of leflunomide is a potent inhibitor of human dihydroorotate dehydrogenase. Biochemistry, 1996, 35(4), 1270-1273.
    • (1996) Biochemistry , vol.35 , Issue.4 , pp. 1270-1273
    • Davis, J.P.1    Cain, G.A.2    Pitts, W.J.3    Magolda, R.L.4    Copeland, R.A.5
  • 39
    • 0029050136 scopus 로고
    • Inhibition of dihydroorotate dehydrogenase by the immunosppressive agent leflunomide
    • Greene, S.; Watanabe, K.; Braatz-Trulson, J.; Lou, L. Inhibition of dihydroorotate dehydrogenase by the immunosppressive agent leflunomide. Biochem. Pharmacol., 1995, 50, 861-867.
    • (1995) Biochem. Pharmacol. , vol.50 , pp. 861-867
    • Greene, S.1    Watanabe, K.2    Braatz-Trulson, J.3    Lou, L.4
  • 42
    • 0033621879 scopus 로고    scopus 로고
    • Redoxal as a new lead structure for dihydroorotate dehydrogenase inhibitors: A kinetic study of the inhibition mechanism
    • Knecht, W.; Loffler, M. Redoxal as a new lead structure for dihydroorotate dehydrogenase inhibitors: a kinetic study of the inhibition mechanism. FEBS Lett., 2000, 467(1), 27-30.
    • (2000) FEBS Lett. , vol.467 , Issue.1 , pp. 27-30
    • Knecht, W.1    Loffler, M.2
  • 44
    • 0022445044 scopus 로고
    • Mechanism of action of the novel anticancer agent 6-fluoro-2-(2'-fluoro-1,1'-biphenyl-4-yl)-3-methyl-4-quinolinecarbo xylic acid sodium salt (NSC 368390): Inhibition of de novo pyrimidine nucleotide biosynthesis
    • Chen, S.F.; Ruben, R.L.; Dexter, D.L. Mechanism of action of the novel anticancer agent 6-fluoro-2-(2'-fluoro-1,1'-biphenyl-4-yl)-3-methyl-4-quinolinecarbo xylic acid sodium salt (NSC 368390): inhibition of de novo pyrimidine nucleotide biosynthesis. Cancer Res., 1986, 46(10), 5014-5019.
    • (1986) Cancer Res. , vol.46 , Issue.10 , pp. 5014-5019
    • Chen, S.F.1    Ruben, R.L.2    Dexter, D.L.3
  • 45
    • 0025331551 scopus 로고
    • In vivo inhibition of the pyrimidine de novo enzyme dihydroorotic acid dehydrogenase by brequinar sodium (DUP-785; NSC 368390) in mice and patients
    • Peters, G.J.; Schwartsmann, G.; Nadal, J.C.; Laurensse, E.J.; van Groeningen, C.J.; van der Vijgh, W.J.; Pinedo, H.M. In vivo inhibition of the pyrimidine de novo enzyme dihydroorotic acid dehydrogenase by brequinar sodium (DUP-785; NSC 368390) in mice and patients. Cancer Res., 1990, 50(15), 4644-4649.
    • (1990) Cancer Res. , vol.50 , Issue.15 , pp. 4644-4649
    • Peters, G.J.1    Schwartsmann, G.2    Nadal, J.C.3    Laurensse, E.J.4    van Groeningen, C.J.5    van der Vijgh, W.J.6    Pinedo, H.M.7
  • 49
    • 0034650342 scopus 로고    scopus 로고
    • Structures of human dihydroorotate dehydrogenase in complex with antiproliferative agents
    • Liu, S.; Neidhardt, E. A.; Grossman, T. H.; Ocain, T.; Clardy, J. Structures of human dihydroorotate dehydrogenase in complex with antiproliferative agents. Structure, 2000, 8(1), 25-33.
    • (2000) Structure , vol.8 , Issue.1 , pp. 25-33
    • Liu, S.1    Neidhardt, E.A.2    Grossman, T.H.3    Ocain, T.4    Clardy, J.5
  • 50
    • 34250375257 scopus 로고    scopus 로고
    • Detergent-dependent kinetics of truncated Plasmodium falciparum dihydroorotate dehydrogenase
    • Malmquist, N.A.; Baldwin, J.; Phillips, M.A. Detergent-dependent kinetics of truncated Plasmodium falciparum dihydroorotate dehydrogenase. J. Biol. Chem., 2007, 282(17), 12678-12686.
    • (2007) J. Biol. Chem. , vol.282 , Issue.17 , pp. 12678-12686
    • Malmquist, N.A.1    Baldwin, J.2    Phillips, M.A.3
  • 52
    • 0026668882 scopus 로고
    • Divergent evolution of pyrimidine biosynthesis between anaerobic and aerobic yeasts
    • Nagy, M.; Lacroute, F.; Thomas, D. Divergent evolution of pyrimidine biosynthesis between anaerobic and aerobic yeasts. Proc. Natl. Acad. Sci. USA, 1992, 89(19), 8966-8970.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , Issue.19 , pp. 8966-8970
    • Nagy, M.1    Lacroute, F.2    Thomas, D.3
  • 53
    • 0035878763 scopus 로고    scopus 로고
    • Dihydrooxonate is a substrate of dihydroorotate dehydrogenase (DHOD) providing evidence for involvement of cysteine and serine residues in base catalysis
    • Bjornberg, O.; Jordan, D. B.; Palfey, B.A.; Jensen, K.F. Dihydrooxonate is a substrate of dihydroorotate dehydrogenase (DHOD) providing evidence for involvement of cysteine and serine residues in base catalysis. Arch. Biochem. Biophys., 2001, 391(2), 286-294.
    • (2001) Arch. Biochem. Biophys. , vol.391 , Issue.2 , pp. 286-294
    • Bjornberg, O.1    Jordan, D.B.2    Palfey, B.A.3    Jensen, K.F.4
  • 54
    • 0031423109 scopus 로고    scopus 로고
    • Active site of dihydroorotate dehydrogenase A from Lactococcus lactis investigated by chemical modification and mutagenesis
    • Bjornberg, O.; Rowland, P.; Larsen, S.; Jensen, K.F. Active site of dihydroorotate dehydrogenase A from Lactococcus lactis investigated by chemical modification and mutagenesis. Biochemistry, 1997, 36(51), 16197-16205.
    • (1997) Biochemistry , vol.36 , Issue.51 , pp. 16197-16205
    • Bjornberg, O.1    Rowland, P.2    Larsen, S.3    Jensen, K.F.4
  • 55
    • 34248577146 scopus 로고    scopus 로고
    • Interaction of benzoate pyrimidine analogues with class 1A dihydroorotate dehydrogenase from Lactococcus lactis
    • Wolfe, A.E.; Thymark, M.; Gattis, S.G.; Fagan, R.L.; Hu, Y.C.; Johansson, E.; Arent, S.; Larsen, S.; Palfey, B.A. Interaction of benzoate pyrimidine analogues with class 1A dihydroorotate dehydrogenase from Lactococcus lactis. Biochemistry, 2007, 46(19), 5741-5753.
    • (2007) Biochemistry , vol.46 , Issue.19 , pp. 5741-5753
    • Wolfe, A.E.1    Thymark, M.2    Gattis, S.G.3    Fagan, R.L.4    Hu, Y.C.5    Johansson, E.6    Arent, S.7    Larsen, S.8    Palfey, B.A.9
  • 56
    • 0032880511 scopus 로고    scopus 로고
    • Dihydroorotate dehydrogenase B of Enterococcus faecalis. Characterization and insights into chemical mechanism
    • Marcinkeviciene, J.; Tinney, L.M.; Wang, K.H.; Rogers, M.J.; Copeland, R.A. Dihydroorotate dehydrogenase B of Enterococcus faecalis. Characterization and insights into chemical mechanism. Biochemistry, 38(40), 13129-13137.
    • Biochemistry , vol.38 , Issue.40 , pp. 13129-13137
    • Marcinkeviciene, J.1    Tinney, L.M.2    Wang, K.H.3    Rogers, M.J.4    Copeland, R.A.5
  • 57
    • 0010184353 scopus 로고    scopus 로고
    • Structure of roorotate dehydrogenase B: Electron transfer between two flavin groups bridged by a iron-sulphur cluster
    • Rowland, P.; Norager, S.; Jensen, K.F.; Larsen, S. Structure of roorotate dehydrogenase B: electron transfer between two flavin groups bridged by a iron-sulphur cluster. Structure, 2000, 8(12), 1227-1238.
    • (2000) Structure , vol.8 , Issue.12 , pp. 1227-1238
    • Rowland, P.1    Norager, S.2    Jensen, K.F.3    Larsen, S.4
  • 58
    • 0028820543 scopus 로고
    • Recombinant human dihydroorotate dehydrogenase: Expression, purification, and characterization of a catalytically functional truncated enzyme
    • Copeland, R.A.; Davis, J.P.; Dowling, R.L.; Lombardo, D.; Murphy, K.B.; Patterson, T.A. Recombinant human dihydroorotate dehydrogenase: expression, purification, and characterization of a catalytically functional truncated enzyme. Arch. Biochem. Biophys., 1995, 323(1), 79-86.
    • (1995) Arch. Biochem. Biophys. , vol.323 , Issue.1 , pp. 79-86
    • Copeland, R.A.1    Davis, J.P.2    Dowling, R.L.3    Lombardo, D.4    Murphy, K.B.5    Patterson, T.A.6
  • 59
    • 33646583490 scopus 로고    scopus 로고
    • Structure of Plasmodium falciparum dihydroorotate dehydrogenase with a bound inhibitor
    • Hurt, D. E.; Widom, J.; Clardy, J. Structure of Plasmodium falciparum dihydroorotate dehydrogenase with a bound inhibitor. Acta Crystallogr. D Biol. Crystallogr., 2006, 62(Pt 3), 312-323.
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , Issue.Pt 3 , pp. 312-323
    • Hurt, D.E.1    Widom, J.2    Clardy, J.3
  • 60
    • 0035836526 scopus 로고    scopus 로고
    • Insight into the chemistry of flavin reduction and oxidation in Escherichia coli dihydroorotate dehydrogenase obtained by rapid reaction studies
    • Palfey, B.A.; Bjornberg, O.; Jensen, K.F. Insight into the chemistry of flavin reduction and oxidation in Escherichia coli dihydroorotate dehydrogenase obtained by rapid reaction studies. Biochemistry, 2001, 40(14), 4381-4390.
    • (2001) Biochemistry , vol.40 , Issue.14 , pp. 4381-4390
    • Palfey, B.A.1    Bjornberg, O.2    Jensen, K.F.3
  • 61
    • 0041433824 scopus 로고    scopus 로고
    • E. coli dihydroorotate dehydrogenase reveals structural and functional distinctions between different classes of dihydroorotate dehydrogenases
    • Norager, S.; Jensen, K. F.; Bjornberg, O.; Larsen, S.,E. coli dihydroorotate dehydrogenase reveals structural and functional distinctions between different classes of dihydroorotate dehydrogenases. Structure, 2002, 10(9), 1211-1223.
    • (2002) Structure , vol.10 , Issue.9 , pp. 1211-1223
    • Norager, S.1    Jensen, K.F.2    Bjornberg, O.3    Larsen, S.4
  • 62
    • 0036830528 scopus 로고    scopus 로고
    • Malarial dihydroorotate dehydrogenase: Substrate and inhibitor specificity
    • Baldwin, J.; Farajallah, A.M.; Malmquist, N.A.; Rathod, P.K.; Phillips, M.A. Malarial dihydroorotate dehydrogenase: substrate and inhibitor specificity. J. Biol. Chem., 2002, 277(44), 41827-41834.
    • (2002) J. Biol. Chem. , vol.277 , Issue.44 , pp. 41827-41834
    • Baldwin, J.1    Farajallah, A.M.2    Malmquist, N.A.3    Rathod, P.K.4    Phillips, M.A.5
  • 63
    • 65649152331 scopus 로고    scopus 로고
    • Structure-based design, synthesis, and characterization of inhibitors of human and Plasmodium falciparum dihydroorotate dehydrogenases
    • Davies, M.; Heikkila, T.; McConkey, G.A.; Fishwick, C.W.; Parsons, M.R.; Johnson, A.P. Structure-based design, synthesis, and characterization of inhibitors of human and Plasmodium falciparum dihydroorotate dehydrogenases. J. Med. Chem., 2009, 52(9), 2683-2693.
    • (2009) J. Med. Chem. , vol.52 , Issue.9 , pp. 2683-2693
    • Davies, M.1    Heikkila, T.2    McConkey, G.A.3    Fishwick, C.W.4    Parsons, M.R.5    Johnson, A.P.6
  • 65
    • 50149091073 scopus 로고    scopus 로고
    • The structures of human dihydroorotate dehydrogenase with and without inhibitor reveal conformational flexibility in the inhibitor and substrate binding sites
    • Walse, B.; Dufe, V.T.; Svensson, B.; Fritzson, I.; Dahlberg, L.; Khairoullina, A.; Wellmar, U.; Al-Karadaghi, S. The structures of human dihydroorotate dehydrogenase with and without inhibitor reveal conformational flexibility in the inhibitor and substrate binding sites. Biochemistry, 2008, 47(34), 8929-8936.
    • (2008) Biochemistry , vol.47 , Issue.34 , pp. 8929-8936
    • Walse, B.1    Dufe, V.T.2    Svensson, B.3    Fritzson, I.4    Dahlberg, L.5    Khairoullina, A.6    Wellmar, U.7    Al-Karadaghi, S.8
  • 66
    • 70350385202 scopus 로고    scopus 로고
    • Structural plasticity of malaria dihydroorotate dehydrogenase allows selective binding of diverse chemical scaffolds
    • Deng, X.; Gujjar, R.; El Mazouni, F.; Kaminsky, W.; Malmquist, N.A.; Goldsmith, E.J.; Rathod, P.K.; Phillips, M.A. Structural plasticity of malaria dihydroorotate dehydrogenase allows selective binding of diverse chemical scaffolds. J. Biol. Chem., 2009, 284(39), 26999-27009.
    • (2009) J. Biol. Chem. , vol.284 , Issue.39 , pp. 26999-27009
    • Deng, X.1    Gujjar, R.2    El Mazouni, F.3    Kaminsky, W.4    Malmquist, N.A.5    Goldsmith, E.J.6    Rathod, P.K.7    Phillips, M.A.8
  • 67
    • 0344653661 scopus 로고    scopus 로고
    • Species-related inhibition of human and rat dihydroorotate dehydrogenase by immunosuppressive isoxazol and cinchoninic acid derivatives
    • Knecht, W.; Loffler, M. Species-related inhibition of human and rat dihydroorotate dehydrogenase by immunosuppressive isoxazol and cinchoninic acid derivatives. Biochem. Pharmacol., 1998, 56(9), 1259-1264.
    • (1998) Biochem. Pharmacol. , vol.56 , Issue.9 , pp. 1259-1264
    • Knecht, W.1    Loffler, M.2
  • 68
    • 0026690437 scopus 로고
    • Inhibition of dihydroorotate dehydrogenase activity by brequinar sodium
    • Chen, S. F.; Perrella, F. W.; Behrens, D. L.; Papp, L. M., Inhibition of dihydroorotate dehydrogenase activity by brequinar sodium. Cancer Res., 1992, 52 (13), 3521-3527.
    • (1992) Cancer Res. , vol.52 , Issue.13 , pp. 3521-3527
    • Chen, S.F.1    Perrella, F.W.2    Behrens, D.L.3    Papp, L.M.4
  • 72
    • 20444470318 scopus 로고    scopus 로고
    • High-throughput screening for potent and selective inhibitors of Plasmodium falciparum dihydroorotate dehydrogenase
    • Baldwin, J.; Michnoff, C.H.; Malmquist, N.A.; White, J.; Roth, M.G.; Rathod, P.K.; Phillips, M.A. High-throughput screening for potent and selective inhibitors of Plasmodium falciparum dihydroorotate dehydrogenase. J. Biol. Chem., 2005, 280(23), 21847-21853.
    • (2005) J. Biol. Chem. , vol.280 , Issue.23 , pp. 21847-21853
    • Baldwin, J.1    Michnoff, C.H.2    Malmquist, N.A.3    White, J.4    Roth, M.G.5    Rathod, P.K.6    Phillips, M.A.7
  • 73
    • 45749119578 scopus 로고    scopus 로고
    • Triazolopyrimidine-based dihydroorotate dehydrogenase inhibitors with potent and selective activity against the malaria parasite, Plasmodium falciparum
    • Phillips, M.A.; Gujjar, R.; Malmquist, N.A.; White, J.; El Mazouni, F.; Baldwin, J.; Rathod, P.K. Triazolopyrimidine-based dihydroorotate dehydrogenase inhibitors with potent and selective activity against the malaria parasite, Plasmodium falciparum. J. Med. Chem., 2008, 51(12), 3649-3653.
    • (2008) J. Med. Chem. , vol.51 , Issue.12 , pp. 3649-3653
    • Phillips, M.A.1    Gujjar, R.2    Malmquist, N.A.3    White, J.4    El Mazouni, F.5    Baldwin, J.6    Rathod, P.K.7
  • 76
    • 13844317355 scopus 로고    scopus 로고
    • Synthesis of brequinar analogue inhibitors of malaria parasite dihydroorotate dehydrogenase
    • Boa, A.N.; Canavan, S.P.; Hirst, P.R.; Ramsey, C.; Stead, A.M. W.; McConkey, G.A. Synthesis of brequinar analogue inhibitors of malaria parasite dihydroorotate dehydrogenase. Bioorg. Med. Chem., 2005, 13(6), 1945-1967.
    • (2005) Bioorg. Med. Chem. , vol.13 , Issue.6 , pp. 1945-1967
    • Boa, A.N.1    Canavan, S.P.2    Hirst, P.R.3    Ramsey, C.4    Stead, A.M.W.5    McConkey, G.A.6
  • 79
    • 0035916227 scopus 로고    scopus 로고
    • Multiple inhibitor analysis of Brequinar and Leflunomide binding sites on human dihydroorotate dehydrogenase
    • McLean, J.E.; Neidhardt, E.A.; Grossman, T.H.; Hedstrom, L. Multiple inhibitor analysis of Brequinar and Leflunomide binding sites on human dihydroorotate dehydrogenase. Biochemistry, 2001, 40(7), 2194-2200.
    • (2001) Biochemistry , vol.40 , Issue.7 , pp. 2194-2200
    • McLean, J.E.1    Neidhardt, E.A.2    Grossman, T.H.3    Hedstrom, L.4
  • 80
    • 39749179794 scopus 로고    scopus 로고
    • Analysis of flavin oxidation and electron-transfer inhibition in Plasmodium falciparum dihydroorotate dehydrogenase
    • Malmquist, N.A.; Gujjar, R.; Rathod, P.K.; Phillips, M.A., Analysis of flavin oxidation and electron-transfer inhibition in Plasmodium falciparum dihydroorotate dehydrogenase. Biochemistry, 2008, 47(8), 2466-2475.
    • (2008) Biochemistry , vol.47 , Issue.8 , pp. 2466-2475
    • Malmquist, N.A.1    Gujjar, R.2    Rathod, P.K.3    Phillips, M.A.4
  • 81
    • 53549094659 scopus 로고    scopus 로고
    • Carbonic anhydrase inhibitors: Inhibition of Plasmodium falciparum carbonic anhydrase with aromatic/heterocyclic sulfonamides- and studies
    • Krungkrai, J.; Krungkrai, S.R.; Supuran, C.T. Carbonic anhydrase inhibitors: inhibition of Plasmodium falciparum carbonic anhydrase with aromatic/heterocyclic sulfonamides- and studies. Bioorg. Med. Chem. Lett., 2008, 18(20), 5466-5471.
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , Issue.20 , pp. 5466-5471
    • Krungkrai, J.1    Krungkrai, S.R.2    Supuran, C.T.3
  • 82
    • 37549044295 scopus 로고    scopus 로고
    • Dihydroorotase of human malarial parasite Plasmodium falciparum differs from host enzyme
    • Krungkrai, S.R.; Wutipraditkul, N.; Krungkrai, J. Dihydroorotase of human malarial parasite Plasmodium falciparum differs from host enzyme. Biochem. Biophys. Res. Commun., 2008, 366(3), 821-826.
    • (2008) Biochem. Biophys. Res. Commun. , vol.366 , Issue.3 , pp. 821-826
    • Krungkrai, S.R.1    Wutipraditkul, N.2    Krungkrai, J.3
  • 84
    • 13444273194 scopus 로고    scopus 로고
    • A novel enzyme complex of orotate phosphoribosyltransferase and orotidine 5'-monophosphate decarboxylase in human malaria parasite Plasmodium falciparum: Physical association, kinetics, and inhibition characterization
    • Krungkrai, S.R.; DelFraino, B.J.; Smiley, J.A.; Prapunwattana, P.; Mitamura, T.; Horii, T.; Krungkrai, J. A novel enzyme complex of orotate phosphoribosyltransferase and orotidine 5'-monophosphate decarboxylase in human malaria parasite Plasmodium falciparum: physical association, kinetics, and inhibition characterization. Biochemistry, 2005, 44(5), 1643-1652.
    • (2005) Biochemistry , vol.44 , Issue.5 , pp. 1643-1652
    • Krungkrai, S.R.1    DelFraino, B.J.2    Smiley, J.A.3    Prapunwattana, P.4    Mitamura, T.5    Horii, T.6    Krungkrai, J.7
  • 86
    • 39149112528 scopus 로고    scopus 로고
    • Structure-activity relationships of C6-uridine derivatives targeting plasmodia orotidine monophosphate decarboxylase
    • Bello, A.M.; Poduch, E.; Liu, Y.; Wei, L.; Crandall, I.; Wang, X.; Dyanand, C.; Kain, K. C.; Pai, E.F.; Kotra, L.P. Structure-activity relationships of C6-uridine derivatives targeting plasmodia orotidine monophosphate decarboxylase. J. Med. Chem., 2008, 51(3), 439-448.
    • (2008) J. Med. Chem. , vol.51 , Issue.3 , pp. 439-448
    • Bello, A.M.1    Poduch, E.2    Liu, Y.3    Wei, L.4    Crandall, I.5    Wang, X.6    Dyanand, C.7    Kain, K.C.8    Pai, E.F.9    Kotra, L.P.10
  • 87
    • 67949123091 scopus 로고    scopus 로고
    • Transition states of Plasmodium falciparum and human orotate phosphoribosyltransferases
    • Zhang, Y.; Luo, M.; Schramm, V.L. Transition states of Plasmodium falciparum and human orotate phosphoribosyltransferases. J. Am. Chem. Soc., 2009, 131(13), 4685-4694.
    • (2009) J. Am. Chem. Soc. , vol.131 , Issue.13 , pp. 4685-4694
    • Zhang, Y.1    Luo, M.2    Schramm, V.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.