메뉴 건너뛰기




Volumn 172, Issue 2, 2010, Pages 152-155

Susceptibility of Plasmodium falciparum to glutamate dehydrogenase inhibitors-A possible new antimalarial target

Author keywords

Anti oxidant defences; Antimalarial; Enzyme inhibition; Glutamate dehydrogenase; Isophthalic acid; Plasmodium falciparum

Indexed keywords

ANTIMALARIAL AGENT; ENZYME INHIBITOR; GLUTAMATE DEHYDROGENASE INHIBITOR; ISOPHTHALIC ACID; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UNCLASSIFIED DRUG;

EID: 77953026455     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molbiopara.2010.04.002     Document Type: Article
Times cited : (20)

References (22)
  • 2
    • 1542528978 scopus 로고
    • Malaria: a role for reactive oxygen species in parasite killing and host pathology.
    • London: Richelieu.
    • Buffinton GD, Hunt NH, Cowden WB, Clark IA. Malaria: a role for reactive oxygen species in parasite killing and host pathology. Free Rad Cell Dam Dis;1986:201-20. London: Richelieu.
    • (1986) Free Rad Cell Dam Dis , pp. 201-20
    • Buffinton, G.D.1    Hunt, N.H.2    Cowden, W.B.3    Clark, I.A.4
  • 3
    • 4444359792 scopus 로고    scopus 로고
    • Redox and antioxidant systems of the malaria parasite Plasmodium falciparum
    • Müller S. Redox and antioxidant systems of the malaria parasite Plasmodium falciparum. Mol Microbiol 2004, 53:1291-1305.
    • (2004) Mol Microbiol , vol.53 , pp. 1291-1305
    • Müller, S.1
  • 4
    • 0024379872 scopus 로고
    • NADPH production by the malarial parasite Plasmodium falciparum
    • Vander Jagt D.L., Hunsaker L.A., Kibirige M., Campos N.M. NADPH production by the malarial parasite Plasmodium falciparum. Blood 1989, 74:471-474.
    • (1989) Blood , vol.74 , pp. 471-474
    • Vander Jagt, D.L.1    Hunsaker, L.A.2    Kibirige, M.3    Campos, N.M.4
  • 6
    • 0032403885 scopus 로고    scopus 로고
    • Glutamate dehydrogenase, the marker protein of Plasmodium falciparum. Cloning, expression and characterization of the malarial enzyme
    • Wagner J.T., Lüdemann H., Färber P.M., Lottspeich F., Krauth-Siegel R.L. Glutamate dehydrogenase, the marker protein of Plasmodium falciparum. Cloning, expression and characterization of the malarial enzyme. Eur J Biochem 1996, 258:813-819.
    • (1996) Eur J Biochem , vol.258 , pp. 813-819
    • Wagner, J.T.1    Lüdemann, H.2    Färber, P.M.3    Lottspeich, F.4    Krauth-Siegel, R.L.5
  • 7
    • 77953026938 scopus 로고    scopus 로고
    • To what extent is it possible to design selective glutamate dehydrogenase inhibitors? MSc thesis,
    • Song Y. To what extent is it possible to design selective glutamate dehydrogenase inhibitors? MSc thesis, University College Dublin; 2005.
    • (2005) University College Dublin
    • Song, Y.1
  • 8
    • 19444372583 scopus 로고    scopus 로고
    • The crystal structure of Plasmodium falciparum glutamate dehydrogenase, a putative target for novel antimalarial drugs
    • Werner C., Stubbs M.T., Krauth-Siegel R.L., Klebe G. The crystal structure of Plasmodium falciparum glutamate dehydrogenase, a putative target for novel antimalarial drugs. J Mol Biol 2005, 349:597-607.
    • (2005) J Mol Biol , vol.349 , pp. 597-607
    • Werner, C.1    Stubbs, M.T.2    Krauth-Siegel, R.L.3    Klebe, G.4
  • 9
    • 0036304611 scopus 로고    scopus 로고
    • The structure of apo human glutamate dehydrogenase details subunit communication and allostery
    • Smith T.J., Schmidt T., Fang J., Wu J., Siuzdak G., Stanley C.A. The structure of apo human glutamate dehydrogenase details subunit communication and allostery. J Mol Biol 2002, 318:765-777.
    • (2002) J Mol Biol , vol.318 , pp. 765-777
    • Smith, T.J.1    Schmidt, T.2    Fang, J.3    Wu, J.4    Siuzdak, G.5    Stanley, C.A.6
  • 10
    • 0006541738 scopus 로고
    • L-Glutamic acid dehydrogenase: structural requirements for substrate competition: effect of thyroxine
    • Caughey W.S., Smiley J.D., Hellerman L. l-Glutamic acid dehydrogenase: structural requirements for substrate competition: effect of thyroxine. J Biol Chem 1957, 224:591-607.
    • (1957) J Biol Chem , vol.224 , pp. 591-607
    • Caughey, W.S.1    Smiley, J.D.2    Hellerman, L.3
  • 11
    • 0022419137 scopus 로고
    • +-dependent glutamate dehydrogenase from Clostridium symbiosum
    • +-dependent glutamate dehydrogenase from Clostridium symbiosum. J Mol Biol 1985, 181:147-149.
    • (1985) J Mol Biol , vol.181 , pp. 147-149
    • Rice, D.W.1    Hornby, D.P.2    Engel, P.C.3
  • 12
    • 0026557303 scopus 로고
    • Subunit assembly and active site location in the structure of glutamate dehydrogenase
    • Baker P.J., Britton K.L., Engel P.C., et al. Subunit assembly and active site location in the structure of glutamate dehydrogenase. Proteins 1992, 12:75-86.
    • (1992) Proteins , vol.12 , pp. 75-86
    • Baker, P.J.1    Britton, K.L.2    Engel, P.C.3
  • 13
    • 0037015614 scopus 로고    scopus 로고
    • Genome sequence of the human malaria parasite Plasmodium falciparum
    • Gardner M.J., Hall N., Fung E., et al. Genome sequence of the human malaria parasite Plasmodium falciparum. Nature 2002, 419:498-511.
    • (2002) Nature , vol.419 , pp. 498-511
    • Gardner, M.J.1    Hall, N.2    Fung, E.3
  • 15
    • 0016631230 scopus 로고
    • Molecular features of organic anion permeability in ox red blood cell
    • Aubert L., Motais R. Molecular features of organic anion permeability in ox red blood cell. J Physiol 1975, 246:159-179.
    • (1975) J Physiol , vol.246 , pp. 159-179
    • Aubert, L.1    Motais, R.2
  • 16
  • 17
    • 0030953287 scopus 로고    scopus 로고
    • A membrane network for nutrient import in red cells infected with the malaria parasite
    • Lauer S.A., Rathod P.K., Ghori N., Haldar K. A membrane network for nutrient import in red cells infected with the malaria parasite. Science 1997, 276:1122-1125.
    • (1997) Science , vol.276 , pp. 1122-1125
    • Lauer, S.A.1    Rathod, P.K.2    Ghori, N.3    Haldar, K.4
  • 18
    • 0033788590 scopus 로고    scopus 로고
    • Nerve tissue-specific (GLUD2) and housekeeping (GLUD1) human glutamate dehydrogenases are regulated by distinct allosteric mechanisms: implications for biological function
    • Plaitakis A., Metaxari M., Shashidharan P. Nerve tissue-specific (GLUD2) and housekeeping (GLUD1) human glutamate dehydrogenases are regulated by distinct allosteric mechanisms: implications for biological function. J Neurochem 2000, 75:1862-1869.
    • (2000) J Neurochem , vol.75 , pp. 1862-1869
    • Plaitakis, A.1    Metaxari, M.2    Shashidharan, P.3
  • 19
    • 0035577286 scopus 로고    scopus 로고
    • Regulation of human glutamate dehydrogenases: implications for glutamate, ammonia and energy metabolism in brain
    • Plaitakis A., Zaganas I. Regulation of human glutamate dehydrogenases: implications for glutamate, ammonia and energy metabolism in brain. J Neurosci Res 2001, 66:899-908.
    • (2001) J Neurosci Res , vol.66 , pp. 899-908
    • Plaitakis, A.1    Zaganas, I.2
  • 21
    • 39449094922 scopus 로고    scopus 로고
    • Isotype expression, post-translational modification and stage-specific production of tubulins in erythrocytic Plasmodium falciparum
    • Fennell B.J., Al-shatr Z.A., Bell A. Isotype expression, post-translational modification and stage-specific production of tubulins in erythrocytic Plasmodium falciparum. Int J Parasitol 2008, 38:527-539.
    • (2008) Int J Parasitol , vol.38 , pp. 527-539
    • Fennell, B.J.1    Al-shatr, Z.A.2    Bell, A.3
  • 22
    • 0027281689 scopus 로고
    • Parasite lactate dehydrogenase as an assay for Plasmodium falciparum drug sensitivity
    • Makler M.T., Ries J.M., Williams J.A., et al. Parasite lactate dehydrogenase as an assay for Plasmodium falciparum drug sensitivity. Am J Trop Med Hyg 1993, 48:739-741.
    • (1993) Am J Trop Med Hyg , vol.48 , pp. 739-741
    • Makler, M.T.1    Ries, J.M.2    Williams, J.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.