메뉴 건너뛰기




Volumn 73, Issue 10, 2007, Pages 3371-3379

Functional expression of human dihydroorotate dehydrogenase (DHODH) in pyr4 mutants of Ustilago maydis allows target validation of DHODH inhibitors in vivo

Author keywords

[No Author keywords available]

Indexed keywords

CYTOSTATIC DRUGS; FUNCTIONAL EXPRESSION; PYRIMIDINE; TARGETING SIGNAL;

EID: 34249684322     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.02569-06     Document Type: Article
Times cited : (26)

References (58)
  • 3
    • 14644431768 scopus 로고    scopus 로고
    • The origin of dihydroorotate dehydrogenase genes of kinetoplastids, with special reference to their biological significance and adaptation to anaerobic, parasitic conditions
    • Annoura, T., T. Nara, T. Makiuchi, T. Hashimoto, and T. Aoki. 2005. The origin of dihydroorotate dehydrogenase genes of kinetoplastids, with special reference to their biological significance and adaptation to anaerobic, parasitic conditions. J. Mol. Evol. 60:113-127.
    • (2005) J. Mol. Evol , vol.60 , pp. 113-127
    • Annoura, T.1    Nara, T.2    Makiuchi, T.3    Hashimoto, T.4    Aoki, T.5
  • 4
    • 0032145981 scopus 로고    scopus 로고
    • Expression, purification, and characterization of histidine-tagged rat and human flavoenzyme dihydroorotate dehydrogenase
    • Bader, B., W. Knecht, M. Fries, and M. Löffler. 1998. Expression, purification, and characterization of histidine-tagged rat and human flavoenzyme dihydroorotate dehydrogenase. Protein Expr. Purif. 13:414-422.
    • (1998) Protein Expr. Purif , vol.13 , pp. 414-422
    • Bader, B.1    Knecht, W.2    Fries, M.3    Löffler, M.4
  • 5
    • 20444470318 scopus 로고    scopus 로고
    • High-throughput screening for potent and selective inhibitors of Plasmodium falciparum dihydroorotate dehydrogenase
    • Baldwin, J., C. H. Michnoff, N. A. Malmquist, J. White, M. G. Roth, P. K. Rathod, and M. A. Phillips. 2005. High-throughput screening for potent and selective inhibitors of Plasmodium falciparum dihydroorotate dehydrogenase. J. Biol. Chem. 280:21847-21853.
    • (2005) J. Biol. Chem , vol.280 , 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
  • 6
    • 0024268093 scopus 로고
    • Cloning of the PYR3 gene of Ustilago maydis and its use in DNA transformation
    • Banks, G. R., and S. Y. Taylor. 1988. Cloning of the PYR3 gene of Ustilago maydis and its use in DNA transformation. Mol. Cell. Biol. 8:5417-5424.
    • (1988) Mol. Cell. Biol , vol.8 , pp. 5417-5424
    • Banks, G.R.1    Taylor, S.Y.2
  • 7
    • 0029616733 scopus 로고
    • Genetics of Ustilago maydis, a fungal pathogen that induces tumors in maize
    • Banuett, F. 1995. Genetics of Ustilago maydis, a fungal pathogen that induces tumors in maize. Annu. Rev. Genet. 29:179-208.
    • (1995) Annu. Rev. Genet , vol.29 , pp. 179-208
    • Banuett, F.1
  • 8
    • 0000451727 scopus 로고
    • Different alleles of Ustilago maydis are necessary for maintenance of filamentous growth but not for meiosis
    • Banuett, F., and I. Herskowitz. 1989. Different alleles of Ustilago maydis are necessary for maintenance of filamentous growth but not for meiosis. Proc. Natl. Acad. Sci. USA 86:5878-5882.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5878-5882
    • Banuett, F.1    Herskowitz, I.2
  • 9
    • 0039021706 scopus 로고    scopus 로고
    • The activity of Escherichia coli dihydroorotate dehydrogenase is dependent on a conserved loop identified by sequence homology, mutagenesis, and limited proteolysis
    • Björnberg, O., A. C. Gruner, P. Roepstorff, and K. F. Jensen. 1999. The activity of Escherichia coli dihydroorotate dehydrogenase is dependent on a conserved loop identified by sequence homology, mutagenesis, and limited proteolysis. Biochemistry 38:2899-2908.
    • (1999) Biochemistry , vol.38 , pp. 2899-2908
    • Björnberg, O.1    Gruner, A.C.2    Roepstorff, P.3    Jensen, K.F.4
  • 10
    • 0034964905 scopus 로고    scopus 로고
    • Ustilago maydis: A valuable model system for the study of fungal dimorphism and virulence
    • Bölker, M. 2001. Ustilago maydis: a valuable model system for the study of fungal dimorphism and virulence. Microbiology 147:1395- 1401.
    • (2001) Microbiology , vol.147 , pp. 1395-1401
    • Bölker, M.1
  • 11
    • 0030451029 scopus 로고    scopus 로고
    • Isolation of a carbon source-regulated gene from Ustilago maydis
    • Bottin, A., J. Kämper, and R. Kahmann. 1996. Isolation of a carbon source-regulated gene from Ustilago maydis. Mol. Gen. Genet. 253:342-352.
    • (1996) Mol. Gen. Genet , vol.253 , pp. 342-352
    • Bottin, A.1    Kämper, J.2    Kahmann, R.3
  • 12
    • 0026690437 scopus 로고
    • Inhibition of dihydroorotate dehydrogenase activity by brequinar sodium
    • Chen, S. F., F. W. Perrella, D. L. Behrens, and L. M. Papp. 1992. Inhibition of dihydroorotate dehydrogenase activity by brequinar sodium. Cancer Res. 52:3521-3527.
    • (1992) Cancer Res , vol.52 , pp. 3521-3527
    • Chen, S.F.1    Perrella, F.W.2    Behrens, D.L.3    Papp, L.M.4
  • 13
    • 0036851697 scopus 로고    scopus 로고
    • Inhibitors of de novo nucleotide biosynthesis as drugs
    • Christopherson, R. I., S. D. Lyons, and P. K. Wilson. 2002. Inhibitors of de novo nucleotide biosynthesis as drugs. Acc. Chem. Res. 35:961-971.
    • (2002) Acc. Chem. Res , vol.35 , pp. 961-971
    • Christopherson, R.I.1    Lyons, S.D.2    Wilson, P.K.3
  • 14
    • 0033807651 scopus 로고    scopus 로고
    • Immunocytochemical detection of mitochondrial dihydroorotate dehydrogenase in human spermatozoa
    • Dietz, C., E. Hinsch, and M. Löffler. 2000. Immunocytochemical detection of mitochondrial dihydroorotate dehydrogenase in human spermatozoa. Int. J. Androl. 23:294-299.
    • (2000) Int. J. Androl , vol.23 , pp. 294-299
    • Dietz, C.1    Hinsch, E.2    Löffler, M.3
  • 15
    • 34249685538 scopus 로고
    • Coenzyme Q. XX. Isolation of coenzymes Q9 and Q10 from two Basidiomycetes
    • Erickson, R. E., K. S. Brown, Jr., D. E. Wolf, and K. Folkers. 1960. Coenzyme Q. XX. Isolation of coenzymes Q9 and Q10 from two Basidiomycetes. Arch. Biochem. Biophys. 90:314-317.
    • (1960) Arch. Biochem. Biophys , vol.90 , pp. 314-317
    • Erickson, R.E.1    Brown Jr., K.S.2    Wolf, D.E.3    Folkers, K.4
  • 16
    • 0029585361 scopus 로고
    • Importance of ribonucleotide availability to proliferating T-lymphocytes from healthy humans. Disproportionate expansion of pyrimidine pools and contrasting effects of de novo synthesis inhibitors
    • Fairbanks, L. D., M. Bofill, K. Ruckemann, and H. A. Simmonds. 1995. Importance of ribonucleotide availability to proliferating T-lymphocytes from healthy humans. Disproportionate expansion of pyrimidine pools and contrasting effects of de novo synthesis inhibitors. J. Biol. Chem. 270:29682-29689.
    • (1995) J. Biol. Chem , vol.270 , pp. 29682-29689
    • Fairbanks, L.D.1    Bofill, M.2    Ruckemann, K.3    Simmonds, H.A.4
  • 17
    • 34249672826 scopus 로고    scopus 로고
    • Feldbrügge, M., M. Bölker, G. Steinberg, J. Kämper, and R. Kahmann. 2006. Regulatory and structural networks orchestrating mating, dimorphism, cell shape, and pathogenesis in Ustilago maydis, p. 375-392. In U. Kües and R. Fischer (ed.), Mycota, 2nd ed., 1. Springer, Berlin, Germany.
    • Feldbrügge, M., M. Bölker, G. Steinberg, J. Kämper, and R. Kahmann. 2006. Regulatory and structural networks orchestrating mating, dimorphism, cell shape, and pathogenesis in Ustilago maydis, p. 375-392. In U. Kües and R. Fischer (ed.), Mycota, 2nd ed., vol. 1. Springer, Berlin, Germany.
  • 18
    • 0037148779 scopus 로고    scopus 로고
    • De novo pyrimidine biosynthesis is required for virulence of Toxoplasma gondii
    • Fox, B. A., and D. J. Bzik. 2002. De novo pyrimidine biosynthesis is required for virulence of Toxoplasma gondii. Nature 415:926-929.
    • (2002) Nature , vol.415 , pp. 926-929
    • Fox, B.A.1    Bzik, D.J.2
  • 20
    • 0029050136 scopus 로고
    • Inhibition of dihydroorotate dehydrogenase by the immunosuppressive agent leflunomide
    • Greene, S., K. Watanabe, J. Braatz-Trulson, and L. Lou. 1995. Inhibition of dihydroorotate dehydrogenase by the immunosuppressive agent leflunomide. Biochem. Pharmacol. 50:861-867.
    • (1995) Biochem. Pharmacol , vol.50 , pp. 861-867
    • Greene, S.1    Watanabe, K.2    Braatz-Trulson, J.3    Lou, L.4
  • 21
    • 0029744679 scopus 로고    scopus 로고
    • Identification of a new antifungal target site through a dual biochemical and molecular-genetics approach
    • Gustafson, G., G. Davis, C. Waldron, A. Smith, and M. Henry. 1996. Identification of a new antifungal target site through a dual biochemical and molecular-genetics approach. Curr. Genet. 30:159-165.
    • (1996) Curr. Genet , vol.30 , pp. 159-165
    • Gustafson, G.1    Davis, G.2    Waldron, C.3    Smith, A.4    Henry, M.5
  • 22
    • 20444468864 scopus 로고    scopus 로고
    • Contribution of horizontal gene transfer to the evolution of Saccharomyces cerevisiae
    • Hall, C., S. Brachat, and F. S. Dietrich. 2005. Contribution of horizontal gene transfer to the evolution of Saccharomyces cerevisiae. Eukaryot. Cell 4:1102-1115.
    • (2005) Eukaryot. Cell , vol.4 , pp. 1102-1115
    • Hall, C.1    Brachat, S.2    Dietrich, F.S.3
  • 23
    • 0024455485 scopus 로고
    • Possible mode of action of toltrazuril: Studies on two Eimeria species and mammalian and Ascaris suum enzymes
    • Harder, A., and A. Haberkorn. 1989. Possible mode of action of toltrazuril: studies on two Eimeria species and mammalian and Ascaris suum enzymes. Parasitol. Res. 76:8-12.
    • (1989) Parasitol. Res , vol.76 , pp. 8-12
    • Harder, A.1    Haberkorn, A.2
  • 24
    • 0034122123 scopus 로고    scopus 로고
    • Leflunomide: An immunomodulatory drug for the treatment of rheumatoid arthritis and other autoimmune diseases
    • Herrmann, M. L., R. Schleyerbach, and B. J. Kirschbaum. 2000. Leflunomide: an immunomodulatory drug for the treatment of rheumatoid arthritis and other autoimmune diseases. Immunopharmacology 47:273-289.
    • (2000) Immunopharmacology , vol.47 , pp. 273-289
    • Herrmann, M.L.1    Schleyerbach, R.2    Kirschbaum, B.J.3
  • 25
    • 0013820169 scopus 로고
    • Radiation sensitive mutants of Ustilago maydis
    • Holliday, R. 1965. Radiation sensitive mutants of Ustilago maydis. Mutat. Res. 2:557-559.
    • (1965) Mutat. Res , vol.2 , pp. 557-559
    • Holliday, R.1
  • 27
    • 0003081753 scopus 로고    scopus 로고
    • Evolutionary and functional families of dihydroorotate dehydrogenases
    • Jensen, K. F., and O. Björnberg. 1998. Evolutionary and functional families of dihydroorotate dehydrogenases. Paths Pyrimidines 6:20-28.
    • (1998) Paths Pyrimidines , vol.6 , pp. 20-28
    • Jensen, K.F.1    Björnberg, O.2
  • 28
    • 0018823799 scopus 로고
    • Pyrimidine nucleotide biosynthesis in animals: Genes, enzymes, and regulation of UMP biosynthesis
    • Jones, M. E. 1980. Pyrimidine nucleotide biosynthesis in animals: genes, enzymes, and regulation of UMP biosynthesis. Annu. Rev. Biochem. 49:253-279.
    • (1980) Annu. Rev. Biochem , vol.49 , pp. 253-279
    • Jones, M.E.1
  • 30
    • 33750597877 scopus 로고    scopus 로고
    • Kämper, J, R. Kahmann, M. Bölker, L.-J. Ma, T. Brefort, B. J. Saville, F. Banuett, J. W. Kronstad, S. E. Gold, O. Muller, M. H. Perlin, H. A. B. Wosten, R. de Vries, J. Ruiz-Herrera, C. G. Reynaga-Pena, K. Snetselaar, M. McCann, J. Perez-Martin, M. Feldbrügge, C. W. Basse, G. Steinberg, J. I. Ibeas, W. Holloman, P. Guzman, M. Farman, J. E. Stajich, R. Sentandreu, J. M. Gonzalez-Prieto, J. C. Kennell, L. Molina, J. Schirawski, A. Mendoza-Mendoza, D. Greilinger, K. Munch, N. Rössel, M. Scherer, M. Vranes, O. Ladendorf, V. Vincon, U. Fuchs, B. Sandrock, S. Meng, E. C. H. Ho, M. J. Cahill, K. J. Boyce, J. Klose, S. J. Klosterman, H. J. Deelstra, L. Ortiz-Castellanos, W. Li, P. Sanchez-Alonso, P. H. Schreier, I. Häuser-Hahn, M. Vaupel, E. Koopmann, G. Friedrich, H. Voss, T. Schlüter, J. Margolis, D. Platt, C. Swimmer, A. Gnirke, F. Chen, V. Vysotskaia, G. Mannhaupt, U. Güldener, M. Münsterkötter, D. Haase, M. Oesterheld, H.-W. Mewes, E. W. Ma
    • Kämper, J., R. Kahmann, M. Bölker, L.-J. Ma, T. Brefort, B. J. Saville, F. Banuett, J. W. Kronstad, S. E. Gold, O. Muller, M. H. Perlin, H. A. B. Wosten, R. de Vries, J. Ruiz-Herrera, C. G. Reynaga-Pena, K. Snetselaar, M. McCann, J. Perez-Martin, M. Feldbrügge, C. W. Basse, G. Steinberg, J. I. Ibeas, W. Holloman, P. Guzman, M. Farman, J. E. Stajich, R. Sentandreu, J. M. Gonzalez-Prieto, J. C. Kennell, L. Molina, J. Schirawski, A. Mendoza-Mendoza, D. Greilinger, K. Munch, N. Rössel, M. Scherer, M. Vranes, O. Ladendorf, V. Vincon, U. Fuchs, B. Sandrock, S. Meng, E. C. H. Ho, M. J. Cahill, K. J. Boyce, J. Klose, S. J. Klosterman, H. J. Deelstra, L. Ortiz-Castellanos, W. Li, P. Sanchez-Alonso, P. H. Schreier, I. Häuser-Hahn, M. Vaupel, E. Koopmann, G. Friedrich, H. Voss, T. Schlüter, J. Margolis, D. Platt, C. Swimmer, A. Gnirke, F. Chen, V. Vysotskaia, G. Mannhaupt, U. Güldener, M. Münsterkötter, D. Haase, M. Oesterheld, H.-W. Mewes, E. W. Mauceli, D. DeCaprio, C. M. Wade, J. Butler, S. Young, D. B. Jaffe, S. Calvo, C. Nusbaum, J. Galagan, and B. W. Birren. 2006. Insights from the genome of the biotrophic fungal plant pathogen Ustilago maydis. Nature 444:97-101.
  • 31
    • 0033990195 scopus 로고    scopus 로고
    • Kinetics of inhibition of human and rat dihydroorotate dehydrogenase by atovaquone, lawsone derivatives, brequinar sodium and polyporic acid
    • Knecht, W., J. Henseling, and M. Löffler. 2000. Kinetics of inhibition of human and rat dihydroorotate dehydrogenase by atovaquone, lawsone derivatives, brequinar sodium and polyporic acid. Chem. Biol. Interact. 124: 61-76.
    • (2000) Chem. Biol. Interact , vol.124 , pp. 61-76
    • Knecht, W.1    Henseling, J.2    Löffler, M.3
  • 32
    • 0344653661 scopus 로고    scopus 로고
    • Species-related inhibition of human and rat dihydroorotate dehydrogenase by immunosuppressive isoxazol and cinchoninic acid derivatives
    • Knecht, W., and M. Löffler. 1998. Species-related inhibition of human and rat dihydroorotate dehydrogenase by immunosuppressive isoxazol and cinchoninic acid derivatives. Biochem. Pharmacol. 56:1259-1264.
    • (1998) Biochem. Pharmacol , vol.56 , pp. 1259-1264
    • Knecht, W.1    Löffler, M.2
  • 33
    • 0024616567 scopus 로고
    • Isolation of two alleles of the b locus of Ustilago maydis
    • Kronstad, J. W., and S. A. Leong. 1989. Isolation of two alleles of the b locus of Ustilago maydis. Proc. Natl. Acad. Sci. USA 86:978-982.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 978-982
    • Kronstad, J.W.1    Leong, S.A.2
  • 34
    • 0001553686 scopus 로고
    • The natural occurrence of coenzyme Q. and related compounds
    • Lester, R. L., and F. L. Crane. 1959. The natural occurrence of coenzyme Q. and related compounds. J. Biol. Chem. 234:2169-2175.
    • (1959) J. Biol. Chem , vol.234 , pp. 2169-2175
    • Lester, R.L.1    Crane, F.L.2
  • 35
    • 27144526423 scopus 로고    scopus 로고
    • Yeast evolution and comparative genomics
    • Liti, G., and E. J. Louis. 2005. Yeast evolution and comparative genomics. Annu. Rev. Microbiol. 59:135-153.
    • (2005) Annu. Rev. Microbiol , vol.59 , pp. 135-153
    • Liti, G.1    Louis, E.J.2
  • 36
    • 0034650342 scopus 로고    scopus 로고
    • Structures of human dihydroorotate dehydrogenase in complex with anti-proliferative agents
    • Liu, S., E. A. Neidhardt, T. H. Grossman, T. Ocain, and J. Clardy. 2000. Structures of human dihydroorotate dehydrogenase in complex with anti-proliferative agents. Structure 8:25-33.
    • (2000) Structure , vol.8 , pp. 25-33
    • Liu, S.1    Neidhardt, E.A.2    Grossman, T.H.3    Ocain, T.4    Clardy, J.5
  • 38
    • 0030761388 scopus 로고    scopus 로고
    • Dihydroorotat-ubiquinone oxidoreductase links mitochondria in the biosynthesis of pyrimidine nucleotides
    • Löffler, M., J. Jöckel, G. Schuster, and C. Becker. 1997. Dihydroorotat-ubiquinone oxidoreductase links mitochondria in the biosynthesis of pyrimidine nucleotides. Mol. Cell. Biochem. 174:125-129.
    • (1997) Mol. Cell. Biochem , vol.174 , pp. 125-129
    • Löffler, M.1    Jöckel, J.2    Schuster, G.3    Becker, C.4
  • 39
    • 20044380139 scopus 로고    scopus 로고
    • Loftus, B. J, E. Fung, P. Roncaglia, D. Rowley, P. Amedeo, D. Bruno, J. Vamathevan, M. Miranda, I. J. Anderson, J. A. Fraser, J. E. Allen, I. E. Bosdet, M. R. Brent, R. Chiu, T. L. Doering, M. J. Donlin, C. A. D'Souza, D. S. Fox, V. Grinberg, J. Fu, M. Fukushima, B. J. Haas, J. C. Huang, G. Janbon, S. J. Jones, H. L. Koo, M. I. Krzywinski, J. K. Kwon-Chung, K. B. Lengeler, R. Maiti, M. A. Marra, R. E. Marra, C. A. Mathewson, T. G. Mitchell, M. Pertea, F. R. Riggs, S. L. Salzberg, J. E. Schein, A. Shvartsbeyn, H. Shin, M. Shumway, C. A. Specht, B. B. Suh, A. Tenney, T. R. Utterback, B. L. Wickes, J. R. Wortman, N. H. Wye, J. W. Kronstad, J. K. Lodge, J. Heitman, R. W. Davis, C. M. Fraser, and R. W. Hyman. 2005. The genome of the basidiomycetous yeast and human pathogen Cryptococcus neoformans. Science 307:1321-1324
    • Loftus, B. J., E. Fung, P. Roncaglia, D. Rowley, P. Amedeo, D. Bruno, J. Vamathevan, M. Miranda, I. J. Anderson, J. A. Fraser, J. E. Allen, I. E. Bosdet, M. R. Brent, R. Chiu, T. L. Doering, M. J. Donlin, C. A. D'Souza, D. S. Fox, V. Grinberg, J. Fu, M. Fukushima, B. J. Haas, J. C. Huang, G. Janbon, S. J. Jones, H. L. Koo, M. I. Krzywinski, J. K. Kwon-Chung, K. B. Lengeler, R. Maiti, M. A. Marra, R. E. Marra, C. A. Mathewson, T. G. Mitchell, M. Pertea, F. R. Riggs, S. L. Salzberg, J. E. Schein, A. Shvartsbeyn, H. Shin, M. Shumway, C. A. Specht, B. B. Suh, A. Tenney, T. R. Utterback, B. L. Wickes, J. R. Wortman, N. H. Wye, J. W. Kronstad, J. K. Lodge, J. Heitman, R. W. Davis, C. M. Fraser, and R. W. Hyman. 2005. The genome of the basidiomycetous yeast and human pathogen Cryptococcus neoformans. Science 307:1321-1324.
  • 40
    • 0036155407 scopus 로고    scopus 로고
    • RNA interference (RNAi) inhibits growth of Plasmodium falciparum
    • McRobert, L., and G. A. McConkey. 2002. RNA interference (RNAi) inhibits growth of Plasmodium falciparum. Mol. Biochem. Parasitol. 119:273-278.
    • (2002) Mol. Biochem. Parasitol , vol.119 , pp. 273-278
    • McRobert, L.1    McConkey, G.A.2
  • 41
    • 0016736770 scopus 로고
    • Radiation-sensitive pyrimidine auxotrophs of Ustilago maydis. I. Isolation and characterization of mutants
    • Moore, P. D. 1975. Radiation-sensitive pyrimidine auxotrophs of Ustilago maydis. I. Isolation and characterization of mutants. Mutat. Res. 28:355-366.
    • (1975) Mutat. Res , vol.28 , pp. 355-366
    • Moore, P.D.1
  • 42
    • 0016705926 scopus 로고
    • Radiation-sensitive pyrimidine auxotrophs of Ustilago maydis. II. A study of repair mechanisms and UV recovery in pyr I
    • Moore, P. D. 1975. Radiation-sensitive pyrimidine auxotrophs of Ustilago maydis. II. A study of repair mechanisms and UV recovery in pyr I. Mutat. Res. 28:367-380.
    • (1975) Mutat. Res , vol.28 , pp. 367-380
    • Moore, P.D.1
  • 43
    • 0026668882 scopus 로고
    • Divergent evolution of pyrimidine biosynthesis between anaerobic and aerobic yeasts
    • Nagy, M., F. Lacroute, and D. Thomas. 1992. Divergent evolution of pyrimidine biosynthesis between anaerobic and aerobic yeasts. Proc. Natl. Acad. Sci. USA 89:8966-8970.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8966-8970
    • Nagy, M.1    Lacroute, F.2    Thomas, D.3
  • 44
    • 0032972509 scopus 로고    scopus 로고
    • PSORT: A program for detecting sorting signals in proteins and predicting their subcellular localization
    • Nakai, K., and P. Horton. 1999. PSORT: a program for detecting sorting signals in proteins and predicting their subcellular localization. Trends Biochem. Sci. 24:34-36.
    • (1999) Trends Biochem. Sci , vol.24 , pp. 34-36
    • Nakai, K.1    Horton, P.2
  • 45
    • 0034739441 scopus 로고    scopus 로고
    • Evolutionary implications of the mosaic pyrimidine-biosynthetic pathway in eukaryotes
    • Nara, T., T. Hshimoto, and T. Aoki. 2000. Evolutionary implications of the mosaic pyrimidine-biosynthetic pathway in eukaryotes. Gene 257:209-222.
    • (2000) Gene , vol.257 , pp. 209-222
    • Nara, T.1    Hshimoto, T.2    Aoki, T.3
  • 46
    • 0041433824 scopus 로고    scopus 로고
    • Nørager, S., K. F. Jensen, O. Björnberg, and S. Larsen. 2002. E. coli dihydroorotate dehydrogenase reveals structural and functional distinctions between different classes of dihydroorotate dehydrogenases. Structure 10: 1211-1223.
    • Nørager, S., K. F. Jensen, O. Björnberg, and S. Larsen. 2002. E. coli dihydroorotate dehydrogenase reveals structural and functional distinctions between different classes of dihydroorotate dehydrogenases. Structure 10: 1211-1223.
  • 47
    • 0002333552 scopus 로고
    • Natural occurrence and distribution of coenzyme Q
    • G. Lenaz ed, John Wiley, London, United Kingdom
    • Ramasarma, T. 1985. Natural occurrence and distribution of coenzyme Q, p. 67-81. In G. Lenaz (ed.), Coenzyme Q. John Wiley, London, United Kingdom.
    • (1985) Coenzyme Q , pp. 67-81
    • Ramasarma, T.1
  • 48
    • 0034070355 scopus 로고    scopus 로고
    • Requirements for the mitochondrial import and localization of dihydroorotate dehydrogenase
    • Rawls, J., W. Knecht, K. Diekert, R. Lill, and M. Löffler. 2000. Requirements for the mitochondrial import and localization of dihydroorotate dehydrogenase. Eur. J. Biochem. 267:2079-2087.
    • (2000) Eur. J. Biochem , vol.267 , pp. 2079-2087
    • Rawls, J.1    Knecht, W.2    Diekert, K.3    Lill, R.4    Löffler, M.5
  • 49
    • 0029379684 scopus 로고
    • Filament-specific expression of a cellulase gene in the dimorphic fungus Ustilago maydis
    • Schauwecker, F., G. Wanner, and R. Kahmann. 1995. Filament-specific expression of a cellulase gene in the dimorphic fungus Ustilago maydis. Biol. Chem. Hoppe-Seyler 376:617-625.
    • (1995) Biol. Chem. Hoppe-Seyler , vol.376 , pp. 617-625
    • Schauwecker, F.1    Wanner, G.2    Kahmann, R.3
  • 50
    • 0025034813 scopus 로고
    • The b alleles of U. maydis, whose combinations program pathogenic development, code for polypeptides containing a homeodomain-related motif
    • Schulz, B., F. Banuett, M. Dahl, R. Schlesinger, W. Schäfer, T. Martin, I. Herskowitz, and R. Kahmann. 1990. The b alleles of U. maydis, whose combinations program pathogenic development, code for polypeptides containing a homeodomain-related motif. Cell 60:295-306.
    • (1990) Cell , vol.60 , pp. 295-306
    • Schulz, B.1    Banuett, F.2    Dahl, M.3    Schlesinger, R.4    Schäfer, W.5    Martin, T.6    Herskowitz, I.7    Kahmann, R.8
  • 51
    • 0026780940 scopus 로고
    • The Ustilago maydis pyr3 gene: Sequence and transcriptional analysis
    • Spanos, A., N. Kanuga, D. W. Holden, and G. R. Banks. 1992. The Ustilago maydis pyr3 gene: sequence and transcriptional analysis. Gene 117:73-79.
    • (1992) Gene , vol.117 , pp. 73-79
    • Spanos, A.1    Kanuga, N.2    Holden, D.W.3    Banks, G.R.4
  • 53
    • 0015024643 scopus 로고
    • Biosynthetic dihydroorotate dehydrogenase from Lactobacillus bulgaricus
    • Taylor, M. L., W. H. Taylor, D. F. Eames, and C. D. Taylor. 1971. Biosynthetic dihydroorotate dehydrogenase from Lactobacillus bulgaricus. J. Bacteriol. 105:1015-1027.
    • (1971) J. Bacteriol , vol.105 , pp. 1015-1027
    • Taylor, M.L.1    Taylor, W.H.2    Eames, D.F.3    Taylor, C.D.4
  • 54
    • 0023664610 scopus 로고
    • The kinetics of reoxidation of yeast complex III. An evaluation of the Q-cycle
    • Tsai, A. L., J. S. Olson, and G. Palmer. 1987. The kinetics of reoxidation of yeast complex III. An evaluation of the Q-cycle. J. Biol. Chem. 262:8677-8684.
    • (1987) J. Biol. Chem , vol.262 , pp. 8677-8684
    • Tsai, A.L.1    Olson, J.S.2    Palmer, G.3
  • 55
    • 0034823624 scopus 로고    scopus 로고
    • Recombinant expression of N-terminal truncated mutants of the membrane bound mouse, rat and human flavoenzyme dihydroorotate dehydrogenase. A versatile tool to rate inhibitor effects?
    • Ullrich, A., W. Knecht, M. Fries, and M. Löffler. 2001. Recombinant expression of N-terminal truncated mutants of the membrane bound mouse, rat and human flavoenzyme dihydroorotate dehydrogenase. A versatile tool to rate inhibitor effects? Eur. J. Biochem. 268:1861-1868.
    • (2001) Eur. J. Biochem , vol.268 , pp. 1861-1868
    • Ullrich, A.1    Knecht, W.2    Fries, M.3    Löffler, M.4
  • 56
    • 0017133345 scopus 로고
    • The influence of DNA binding protein on the substrate affinities of DNA polymerase from Ustilago maydis: One polymerase implicated in both DNA replication and repair
    • Yarranton, G. T., P. D. Moore, and A. Spanos. 1976. The influence of DNA binding protein on the substrate affinities of DNA polymerase from Ustilago maydis: one polymerase implicated in both DNA replication and repair. Mol. Gen. Genet. 145:215-218.
    • (1976) Mol. Gen. Genet , vol.145 , pp. 215-218
    • Yarranton, G.T.1    Moore, P.D.2    Spanos, A.3
  • 57
    • 33745623955 scopus 로고    scopus 로고
    • Biochemical characterization of recombinant dihydroorotate dehydrogenase from the opportunistic pathogenic yeast Candida albicans
    • Zameitat, E., Z. Gojkovic, W. Knecht, J. Piskur, and M. Löffler. 2006. Biochemical characterization of recombinant dihydroorotate dehydrogenase from the opportunistic pathogenic yeast Candida albicans. FEBS J. 273: 3183-3191.
    • (2006) FEBS J , vol.273 , pp. 3183-3191
    • Zameitat, E.1    Gojkovic, Z.2    Knecht, W.3    Piskur, J.4    Löffler, M.5
  • 58
    • 2942529243 scopus 로고    scopus 로고
    • Two different dihydroorotate dehydrogenases from yeast Saccharomyces kluyveri
    • Zameitat, E., W. Knecht, J. Piskur, and M. Löffler. 2004. Two different dihydroorotate dehydrogenases from yeast Saccharomyces kluyveri. FEBS Lett. 568:129-134.
    • (2004) FEBS Lett , vol.568 , pp. 129-134
    • Zameitat, E.1    Knecht, W.2    Piskur, J.3    Löffler, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.