메뉴 건너뛰기




Volumn 51, Issue 6, 2007, Pages 2123-2129

Kinetic characterization of squalene synthase from Trypanosoma cruzi: Selective inhibition by quinuclidine derivatives

Author keywords

[No Author keywords available]

Indexed keywords

FARNESYL DIPHOSPHATE; NICOTINAMIDE ADENINE DINUCLEOTIDE; QUINUCLIDINE DERIVATIVE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SQUALENE SYNTHASE;

EID: 34250162861     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/AAC.01454-06     Document Type: Article
Times cited : (57)

References (28)
  • 2
    • 0032892735 scopus 로고    scopus 로고
    • Detection of live Trypanosoma cruzi in tissues of infected mice by using histochemical stain for beta-galactosidase
    • Buckner, F. S., A. J. Wilson, and W. C. Van Voorhis. 1999. Detection of live Trypanosoma cruzi in tissues of infected mice by using histochemical stain for beta-galactosidase. Infect. Immun. 67:403-409.
    • (1999) Infect. Immun , vol.67 , pp. 403-409
    • Buckner, F.S.1    Wilson, A.J.2    Van Voorhis, W.C.3
  • 4
    • 0032518190 scopus 로고    scopus 로고
    • Molecular characterization of tobacco squalene synthase and regulation in response to fungal elicitor
    • Devarenne, T. P., D. H. Shin, K. Back, S. Yin, and J. Chappell. 1998. Molecular characterization of tobacco squalene synthase and regulation in response to fungal elicitor. Arch. Biochem. Biophys. 349:205-215.
    • (1998) Arch. Biochem. Biophys , vol.349 , pp. 205-215
    • Devarenne, T.P.1    Shin, D.H.2    Back, K.3    Yin, S.4    Chappell, J.5
  • 5
    • 0030973773 scopus 로고    scopus 로고
    • Sterol biosynthesis inhibitors: Potential chemotherapeutics against Chagas disease
    • Docampo, R., and G. A. Schmunis. 1997. Sterol biosynthesis inhibitors: potential chemotherapeutics against Chagas disease. Parasitol. Today 13:129-130.
    • (1997) Parasitol. Today , vol.13 , pp. 129-130
    • Docampo, R.1    Schmunis, G.A.2
  • 6
    • 0025996074 scopus 로고
    • Isolation and primary structure of the ERG9 gene of Saccharomyces cerevisiae encoding squalene synthetase
    • Fegueur, M., L. Richard, A. D. Charles, and F. Karst. 1991. Isolation and primary structure of the ERG9 gene of Saccharomyces cerevisiae encoding squalene synthetase. Curr. Genet. 20:365-372.
    • (1991) Curr. Genet , vol.20 , pp. 365-372
    • Fegueur, M.1    Richard, L.2    Charles, A.D.3    Karst, F.4
  • 8
    • 0031453756 scopus 로고    scopus 로고
    • cDNA cloning of squalene synthase genes from mono- and dicotyledonous plants, and expression of the gene in rice
    • Hata, S., K. Sanmiya, H. Kouchi, M. Matsuoka, N. Yamamoto, and K. Izui. 1997. cDNA cloning of squalene synthase genes from mono- and dicotyledonous plants, and expression of the gene in rice. Plant Cell Physiol. 38:1409-1413.
    • (1997) Plant Cell Physiol , vol.38 , pp. 1409-1413
    • Hata, S.1    Sanmiya, K.2    Kouchi, H.3    Matsuoka, M.4    Yamamoto, N.5    Izui, K.6
  • 9
    • 0025745086 scopus 로고
    • Molecular cloning and characterization of the yeast gene for squalene synthetase
    • Jennings, S. M., Y. H. Tsay, T. M. Fisch, and G. W. Robinson. 1991. Molecular cloning and characterization of the yeast gene for squalene synthetase. Proc. Natl. Acad. Sci. USA 88:6038-6042.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 6038-6042
    • Jennings, S.M.1    Tsay, Y.H.2    Fisch, T.M.3    Robinson, G.W.4
  • 10
    • 1842847404 scopus 로고    scopus 로고
    • Cloning and expression of squalene synthase cDNA from hot pepper (Capsicum annuum L.)
    • Lee, J. H., Y. H. Yoon, H. Y. Kim, D. H. Shin, D. U. Kim, I. J. Lee, and K. U. Kim. 2002. Cloning and expression of squalene synthase cDNA from hot pepper (Capsicum annuum L.). Mol. Cells 13:436-443.
    • (2002) Mol. Cells , vol.13 , pp. 436-443
    • Lee, J.H.1    Yoon, Y.H.2    Kim, H.Y.3    Shin, D.H.4    Kim, D.U.5    Lee, I.J.6    Kim, K.U.7
  • 11
    • 85177001248 scopus 로고    scopus 로고
    • Lindsey, S., and H. J. Harwood, Jr. 1995. Inhibition of mammalian squalene synthetase activity by zaragozic acid A is a result of competitive inhibition followed by mechanism-based irreversible inactivation. J. Biol. Chem. 270:9083-9096.
    • Lindsey, S., and H. J. Harwood, Jr. 1995. Inhibition of mammalian squalene synthetase activity by zaragozic acid A is a result of competitive inhibition followed by mechanism-based irreversible inactivation. J. Biol. Chem. 270:9083-9096.
  • 12
    • 0027487993 scopus 로고
    • Overexpression, purification, and kinetic characterization of a carboxyl-terminal-truncated yeast squalene synthetase
    • LoGrasso, P. V., D. A. Soltis, and B. R. Boettcher. 1993. Overexpression, purification, and kinetic characterization of a carboxyl-terminal-truncated yeast squalene synthetase. Arch. Biochem. Biophys. 307:193-199.
    • (1993) Arch. Biochem. Biophys , vol.307 , pp. 193-199
    • LoGrasso, P.V.1    Soltis, D.A.2    Boettcher, B.R.3
  • 13
    • 0026808513 scopus 로고
    • Molecular cloning, expression, and characterization of the cDNA for the rat hepatic squalene synthase
    • McKenzie, T. L., G. Jiang, J. R. Straubhaar, D. G. Conrad, and I. Shechter. 1992. Molecular cloning, expression, and characterization of the cDNA for the rat hepatic squalene synthase. J. Biol. Chem. 267:21368- 21374.
    • (1992) J. Biol. Chem , vol.267 , pp. 21368-21374
    • McKenzie, T.L.1    Jiang, G.2    Straubhaar, J.R.3    Conrad, D.G.4    Shechter, I.5
  • 15
    • 0028929919 scopus 로고
    • Cloning, expression, and characterization of cDNAs encoding Arabidopsis thaliana squalene synthase
    • Nakashima, T., T. Inoue, A. Oka, T. Nishino, T. Osumi, and S. Hata. 1995. Cloning, expression, and characterization of cDNAs encoding Arabidopsis thaliana squalene synthase. Proc. Natl. Acad. Sci. USA 92:2328-2332.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2328-2332
    • Nakashima, T.1    Inoue, T.2    Oka, A.3    Nishino, T.4    Osumi, T.5    Hata, S.6
  • 17
    • 0034730724 scopus 로고    scopus 로고
    • Pandit, J., D. E. Danley, G. K. Schulte, S. Mazzalupo, T. A. Pauly, C. M. Hayward, E. S. Hamanaka, J. F. Thompson, and H. J. Harwood, Jr. 2000. Crystal structure of human squalene synthase. A key enzyme in cholesterol biosynthesis. J. Biol. Chem. 275:30610-30617.
    • Pandit, J., D. E. Danley, G. K. Schulte, S. Mazzalupo, T. A. Pauly, C. M. Hayward, E. S. Hamanaka, J. F. Thompson, and H. J. Harwood, Jr. 2000. Crystal structure of human squalene synthase. A key enzyme in cholesterol biosynthesis. J. Biol. Chem. 275:30610-30617.
  • 21
    • 0031822964 scopus 로고    scopus 로고
    • Thompson, J. F., D. E. Danley, S. Mazzalupo, P. M. Milos, M. E. Lira, and H. J. Harwood, Jr. 1998. Truncation of human squalene synthase yields active, crystallizable protein. Arch. Biochem. Biophys. 350:283-290.
    • Thompson, J. F., D. E. Danley, S. Mazzalupo, P. M. Milos, M. E. Lira, and H. J. Harwood, Jr. 1998. Truncation of human squalene synthase yields active, crystallizable protein. Arch. Biochem. Biophys. 350:283-290.
  • 22
    • 0036234361 scopus 로고    scopus 로고
    • Chemotherapy of Chagas disease
    • Urbina, J. A. 2002. Chemotherapy of Chagas disease. Curr. Pharm. Des. 8:287-295.
    • (2002) Curr. Pharm. Des , vol.8 , pp. 287-295
    • Urbina, J.A.1
  • 24
    • 3042570789 scopus 로고    scopus 로고
    • In vitro and in vivo activities of E5700 and ER-119884, two novel orally active squalene synthase inhibitors, against Trypanosoma cruzi
    • Urbina, J. A., J. L. Concepcion, A. Caldera, G. Payares, C. Sanoja, T. Otomo, and H. Hiyoshi. 2004. In vitro and in vivo activities of E5700 and ER-119884, two novel orally active squalene synthase inhibitors, against Trypanosoma cruzi. Antimicrob. Agents Chemother. 48:2379-2387.
    • (2004) Antimicrob. Agents Chemother , vol.48 , pp. 2379-2387
    • Urbina, J.A.1    Concepcion, J.L.2    Caldera, A.3    Payares, G.4    Sanoja, C.5    Otomo, T.6    Hiyoshi, H.7
  • 25
    • 0036860240 scopus 로고    scopus 로고
    • Squalene synthase as a chemotherapeutic target in Trypanosoma cruzi and Leishmania mexicana
    • Urbina, J. A., J. L. Concepcion, S. Rangel, G. Visbal, and R. Lira. 2002. Squalene synthase as a chemotherapeutic target in Trypanosoma cruzi and Leishmania mexicana. Mol. Biochem. Parasitol. 125:35-45.
    • (2002) Mol. Biochem. Parasitol , vol.125 , pp. 35-45
    • Urbina, J.A.1    Concepcion, J.L.2    Rangel, S.3    Visbal, G.4    Lira, R.5
  • 26
    • 0142227145 scopus 로고    scopus 로고
    • Specific chemotherapy of Chagas disease: Controversies and advances
    • Urbina, J. A., and R. Docampo. 2003. Specific chemotherapy of Chagas disease: controversies and advances. Trends Parasitol. 19:495-501.
    • (2003) Trends Parasitol , vol.19 , pp. 495-501
    • Urbina, J.A.1    Docampo, R.2
  • 27
    • 34250174670 scopus 로고    scopus 로고
    • WHO. 2002. The world health report. World Health Organization, Geneva, Switzerland.
    • WHO. 2002. The world health report. World Health Organization, Geneva, Switzerland.
  • 28
    • 0027177510 scopus 로고
    • Yeast squalene synthase: Expression, purification, and characterization of soluble recombinant enzyme
    • Zhang, D., S. M. Jennings, G. W. Robinson, and C. D. Poulter. 1993. Yeast squalene synthase: expression, purification, and characterization of soluble recombinant enzyme. Arch. Biochem. Biophys. 304:133-143.
    • (1993) Arch. Biochem. Biophys , vol.304 , pp. 133-143
    • Zhang, D.1    Jennings, S.M.2    Robinson, G.W.3    Poulter, C.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.