메뉴 건너뛰기




Volumn 190, Issue 11, 2008, Pages 3808-3816

Cloning, solubilization, and characterization of squalene synthase from Thermosynechococcus elongatus BP-1

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; DETERGENT; FARNESYL DIPHOSPHATE; GLYCEROL; HOPANOID; MAGNESIUM ION; RECOMBINANT ENZYME; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SQUALENE; SQUALENE SYNTHASE; ZARAGOZIC ACID A;

EID: 44349097602     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.01939-07     Document Type: Article
Times cited : (61)

References (58)
  • 1
    • 0017821357 scopus 로고
    • Squalene synthetase. Solubilization from yeast microsomes of a phospholipid-requiring enzyme
    • Agnew, W. S., and G. Popjak. 1978. Squalene synthetase. Solubilization from yeast microsomes of a phospholipid-requiring enzyme. J. Biol. Chem. 253: 4574-4583.
    • (1978) J. Biol. Chem , vol.253 , pp. 4574-4583
    • Agnew, W.S.1    Popjak, G.2
  • 5
    • 0028841895 scopus 로고
    • Discovery, biosynthesis, and mechanism of action of the zaragozic acids: Potent inhibitors of squalene synthase
    • Bergstrom, J. D., C. Dufresne, G. F. Bills, M. Nallin-Omstead, and K. Byrne. 1995. Discovery, biosynthesis, and mechanism of action of the zaragozic acids: potent inhibitors of squalene synthase. Annu. Rev. Microbiol. 49:607-639.
    • (1995) Annu. Rev. Microbiol , vol.49 , pp. 607-639
    • Bergstrom, J.D.1    Dufresne, C.2    Bills, G.F.3    Nallin-Omstead, M.4    Byrne, K.5
  • 6
    • 0027518332 scopus 로고    scopus 로고
    • Bergstrom, J. D., M. M. Kurtz, D. J. Rew, A. M. Amend, J. D. Karkas, R. G. Bostedor, V. S. Bansal, C. Dufresne, F. L. Van Middlesworth, O. D. Hensens, J. M. Liesch, D. L. Zink, K. E. Wilson, J. Onishi, J. A. Milligan, G. Bills, L. Kaplan, M. Nallin Omstead, R. G. Jenkins, L. Huang, M. S. Meinz, L. Quinn, R. W. Burg, Y. L. Kong, S. Mochales, M. Mojena, I. Martin, F. Pelaez, M. T. Diez, and A. W. Alberts. 1993. Zaragozic acids: a family of fungal metabolites that are picomolar competitive inhibitors of squalene synthase. Proc. Natl. Acad. Sci. USA 90:80-84.
    • Bergstrom, J. D., M. M. Kurtz, D. J. Rew, A. M. Amend, J. D. Karkas, R. G. Bostedor, V. S. Bansal, C. Dufresne, F. L. Van Middlesworth, O. D. Hensens, J. M. Liesch, D. L. Zink, K. E. Wilson, J. Onishi, J. A. Milligan, G. Bills, L. Kaplan, M. Nallin Omstead, R. G. Jenkins, L. Huang, M. S. Meinz, L. Quinn, R. W. Burg, Y. L. Kong, S. Mochales, M. Mojena, I. Martin, F. Pelaez, M. T. Diez, and A. W. Alberts. 1993. Zaragozic acids: a family of fungal metabolites that are picomolar competitive inhibitors of squalene synthase. Proc. Natl. Acad. Sci. USA 90:80-84.
  • 7
    • 0027176916 scopus 로고
    • Hopanoid lipids compose the Frankia vesicle envelope, presumptive barrier of oxygen diffusion to nitrogenase
    • Berry, A. M., O. T. Harriott, R. A. Moreau, S. F. Osman, D. R. Benson, and A. D. Jones. 1993. Hopanoid lipids compose the Frankia vesicle envelope, presumptive barrier of oxygen diffusion to nitrogenase. Proc. Natl. Acad. Sci. USA 90:6091-6094.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6091-6094
    • Berry, A.M.1    Harriott, O.T.2    Moreau, R.A.3    Osman, S.F.4    Benson, D.R.5    Jones, A.D.6
  • 8
    • 0021977216 scopus 로고
    • Synthesis of allylic and homoallylic isoprenoid pyrophosphates
    • Davissen, V. J., A. B. Woodside, and C. D. Poulter. 1985. Synthesis of allylic and homoallylic isoprenoid pyrophosphates. Methods Enzymol. 110:130-144.
    • (1985) Methods Enzymol , vol.110 , pp. 130-144
    • Davissen, V.J.1    Woodside, A.B.2    Poulter, C.D.3
  • 9
    • 16344389152 scopus 로고    scopus 로고
    • Primary intermediate in the photocycle of a blue-light sensory BLUF FAD-protein, TII0078, of Thermosynechococcus elongatus BP-1
    • Fukushima, Y., K. Okajima, Y. Shibata, M. Ikeuchi, and S. Itoh. 2005. Primary intermediate in the photocycle of a blue-light sensory BLUF FAD-protein, TII0078, of Thermosynechococcus elongatus BP-1. Biochemistry 44: 5149-5158.
    • (2005) Biochemistry , vol.44 , pp. 5149-5158
    • Fukushima, Y.1    Okajima, K.2    Shibata, Y.3    Ikeuchi, M.4    Itoh, S.5
  • 10
    • 0032524330 scopus 로고    scopus 로고
    • Function-structure studies and identification of three enzyme domains involved in the catalytic activity in rat hepatic squalene synthase
    • Gu, P., Y. Ishii, T. A. Spencer, and I. Shechter. 1998. Function-structure studies and identification of three enzyme domains involved in the catalytic activity in rat hepatic squalene synthase. J. Biol. Chem. 273:12515-12525.
    • (1998) J. Biol. Chem , vol.273 , pp. 12515-12525
    • Gu, P.1    Ishii, Y.2    Spencer, T.A.3    Shechter, I.4
  • 11
    • 0344815737 scopus 로고
    • Extent of N-terminal methionine excision from Escherichia coli proteins is governed by the side-chain length of the penultimate amino acid
    • Hirel, P. H., M. J. Schmitter, P. Dessen, G. Fayat, and S. Blanquet. 1989. Extent of N-terminal methionine excision from Escherichia coli proteins is governed by the side-chain length of the penultimate amino acid. Proc. Natl. Acad. Sci. USA 86:8247-8251.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 8247-8251
    • Hirel, P.H.1    Schmitter, M.J.2    Dessen, P.3    Fayat, G.4    Blanquet, S.5
  • 12
    • 0028848861 scopus 로고
    • Molecular cloning and functional expression of a cDNA for mouse squalene synthase
    • Inoue, T., T. Osumi, and S. Hata. 1995. Molecular cloning and functional expression of a cDNA for mouse squalene synthase. Biochim. Biophys. Acta 1260:49-54.
    • (1995) Biochim. Biophys. Acta , vol.1260 , pp. 49-54
    • Inoue, T.1    Osumi, T.2    Hata, S.3
  • 13
    • 0037465699 scopus 로고    scopus 로고
    • Bacterial phytoene synthase: Molecular cloning, expression, and characterization of Erwinia herbicola phytoene synthase
    • Iwata-Reuyl, D., S. K. Math, S. B. Desai, and C. D. Poulter. 2003. Bacterial phytoene synthase: molecular cloning, expression, and characterization of Erwinia herbicola phytoene synthase. Biochemistry 42:3359-3365.
    • (2003) Biochemistry , vol.42 , pp. 3359-3365
    • Iwata-Reuyl, D.1    Math, S.K.2    Desai, S.B.3    Poulter, C.D.4
  • 14
    • 0037205875 scopus 로고    scopus 로고
    • Recombinant squalene synthase. Synthesis of non-head-to-tail isoprenoids in the absence of NADPH
    • Jarstfer, M. B., D. L. Zhang, and C. D. Poulter. 2002. Recombinant squalene synthase. Synthesis of non-head-to-tail isoprenoids in the absence of NADPH. J. Am. Chem. Soc. 124:8834-8845.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 8834-8845
    • Jarstfer, M.B.1    Zhang, D.L.2    Poulter, C.D.3
  • 15
    • 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
  • 16
    • 0026862454 scopus 로고
    • Localization and distribution of hopanoids in membrane systems of the cyanobacterium Synechocystis PCC 6714
    • Jurgens, U. J., P. Simonin, and M. Rohmer. 1992. Localization and distribution of hopanoids in membrane systems of the cyanobacterium Synechocystis PCC 6714. FEMS Microbiol. Lett. 71:285-288.
    • (1992) FEMS Microbiol. Lett , vol.71 , pp. 285-288
    • Jurgens, U.J.1    Simonin, P.2    Rohmer, M.3
  • 18
    • 0023644544 scopus 로고
    • Squalene synthetase. Solubilization and partial purification of squalene synthetase, copurification of presqualene pyrophosphate and squalene synthetase activities
    • Kuswik-Rabiega, G., and H. C. Rilling. 1987. Squalene synthetase. Solubilization and partial purification of squalene synthetase, copurification of presqualene pyrophosphate and squalene synthetase activities. J. Biol. Chem. 262:1505-1509.
    • (1987) J. Biol. Chem , vol.262 , pp. 1505-1509
    • Kuswik-Rabiega, G.1    Rilling, H.C.2
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0028967667 scopus 로고
    • Inhibition of mammalian squalene synthetase activity by zaragozic acid A is a result of competitive inhibition followed by mechanism-based irreversible inactivation
    • Lindsey, S., and H. J. Harwood. 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.
    • (1995) J. Biol. Chem , vol.270 , pp. 9083-9096
    • Lindsey, S.1    Harwood, H.J.2
  • 21
    • 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
  • 22
    • 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
  • 24
    • 0028366125 scopus 로고
    • Yeast squalene synthase. A mechanism for addition of substrates and activation by NADPH
    • Mookhtiar, K. A., S. S. Kalinowski, D. Zhang, and C. D. Poulter. 1994. Yeast squalene synthase. A mechanism for addition of substrates and activation by NADPH. J. Biol. Chem. 269:11201-11207.
    • (1994) J. Biol. Chem , vol.269 , pp. 11201-11207
    • Mookhtiar, K.A.1    Kalinowski, S.S.2    Zhang, D.3    Poulter, C.D.4
  • 27
    • 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
  • 28
    • 0032550805 scopus 로고    scopus 로고
    • Expression of an active phytoene synthase from Erwinia uredovora and biochemical properties of the enzyme
    • Neudert, U., I. M. Martínez-Férez, P. D. Fraser, and G. Sandmann. 1998. Expression of an active phytoene synthase from Erwinia uredovora and biochemical properties of the enzyme. Biochim. Biophys. Acta 1392:51-58.
    • (1998) Biochim. Biophys. Acta , vol.1392 , pp. 51-58
    • Neudert, U.1    Martínez-Férez, I.M.2    Fraser, P.D.3    Sandmann, G.4
  • 29
    • 12944270421 scopus 로고    scopus 로고
    • Ng, W. V., S. P. Kennedy, G. G. Mahairas, B. Berquist, M. Pan, H. D. Shukla, S. R. Lasky, N. S. Baliga, V. Thorsson, J. Sbrogna, S. Swartzell, D. Weir, J. Hall, T. A. Dahl, R. Welti, Y. A. Goo, B. Leithauser, K. Keller, R. Cruz, M. J. Danson, D. W. Hough, D. G. Maddocks, P. E. Jablonski, M. P. Krebs, C. M. Angevine, H. Dale, T. A. Isenbarger, R. F. Peck, M. Pohlschroder, J. L. Spudich, K. W. Jung, M. Alam, T. Freitas, S. Hou, C. J. Daniels, P. P. Dennis, A. D. Omer, H. Ebhardt, T. M. Lowe, P. Liang, M. Riley, L. Hood, and S. DasSarma. 2000. Genome sequence of Halobacterium species NRC-1. Proc. Natl. Acad. Sci. USA 97:12176-12181.
    • Ng, W. V., S. P. Kennedy, G. G. Mahairas, B. Berquist, M. Pan, H. D. Shukla, S. R. Lasky, N. S. Baliga, V. Thorsson, J. Sbrogna, S. Swartzell, D. Weir, J. Hall, T. A. Dahl, R. Welti, Y. A. Goo, B. Leithauser, K. Keller, R. Cruz, M. J. Danson, D. W. Hough, D. G. Maddocks, P. E. Jablonski, M. P. Krebs, C. M. Angevine, H. Dale, T. A. Isenbarger, R. F. Peck, M. Pohlschroder, J. L. Spudich, K. W. Jung, M. Alam, T. Freitas, S. Hou, C. J. Daniels, P. P. Dennis, A. D. Omer, H. Ebhardt, T. M. Lowe, P. Liang, M. Riley, L. Hood, and S. DasSarma. 2000. Genome sequence of Halobacterium species NRC-1. Proc. Natl. Acad. Sci. USA 97:12176-12181.
  • 30
    • 20144366218 scopus 로고    scopus 로고
    • Cyanobacterial non-mevalonate pathway: (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase interacts with ferredoxin in Thermosynechococcus elongatus BP-1
    • Okada. K., and T. Hase. 2005. Cyanobacterial non-mevalonate pathway: (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase interacts with ferredoxin in Thermosynechococcus elongatus BP-1. J. Biol. Chem. 280:20672-20679.
    • (2005) J. Biol. Chem , vol.280 , pp. 20672-20679
    • Okada, K.1    Hase, T.2
  • 31
    • 0023515798 scopus 로고
    • Prokaryotic hopanoids and other polyterpenoid sterol surrogates
    • Ourisson, G., M. Rohmer, and K. Poralla. 1987. Prokaryotic hopanoids and other polyterpenoid sterol surrogates. Annu. Rev. Microbiol. 41:301-333.
    • (1987) Annu. Rev. Microbiol , vol.41 , pp. 301-333
    • Ourisson, G.1    Rohmer, M.2    Poralla, K.3
  • 32
    • 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.
  • 33
    • 1842328052 scopus 로고    scopus 로고
    • Squalene-hopene cyclase from Bradyrhizobium japonicum: Cloning, expression, sequence analysis, and comparison to other triterpenoid cyclases
    • Perzl, M., P. Muller, K. Poralla, and E. L. Kannenberg. 1997. Squalene-hopene cyclase from Bradyrhizobium japonicum: cloning, expression, sequence analysis, and comparison to other triterpenoid cyclases. Microbiology 143:1235-1242.
    • (1997) Microbiology , vol.143 , pp. 1235-1242
    • Perzl, M.1    Muller, P.2    Poralla, K.3    Kannenberg, E.L.4
  • 34
    • 0003693962 scopus 로고    scopus 로고
    • Cloning of conserved genes from Zymomonas mobilis and Bradyrhizobium japonicum that function in the biosynthesis of hopanoid lipids
    • Perzl, M., I. G. Reipen, S. Schmitz, K. Poralla, H. Sahm, G. A. Sprenger, and E. L. Kannenberg. 1998. Cloning of conserved genes from Zymomonas mobilis and Bradyrhizobium japonicum that function in the biosynthesis of hopanoid lipids. Biochim. Biophys. Acta 1393:108-118.
    • (1998) Biochim. Biophys. Acta , vol.1393 , pp. 108-118
    • Perzl, M.1    Reipen, I.G.2    Schmitz, S.3    Poralla, K.4    Sahm, H.5    Sprenger, G.A.6    Kannenberg, E.L.7
  • 35
    • 0032895029 scopus 로고    scopus 로고
    • HMG-CoA reductase regulation: Use of structurally diverse first half-reaction squalene synthetase inhibitors to characterize the site of mevalonate-derived nonsterol regulator production in cultured IM-9 cells
    • Petras, S. F., S. Lindsey, and H. J. Harwood. 1999. HMG-CoA reductase regulation: use of structurally diverse first half-reaction squalene synthetase inhibitors to characterize the site of mevalonate-derived nonsterol regulator production in cultured IM-9 cells. J. Lipid Res. 40:24-38.
    • (1999) J. Lipid Res , vol.40 , pp. 24-38
    • Petras, S.F.1    Lindsey, S.2    Harwood, H.J.3
  • 36
    • 0002869606 scopus 로고
    • Biosynthesis of non-head-to-tail terpenes. Formation of 1′-1 and 1′-3 linkages
    • Poulter, C. D. 1990. Biosynthesis of non-head-to-tail terpenes. Formation of 1′-1 and 1′-3 linkages. Acc. Chem. Res. 23:70-77.
    • (1990) Acc. Chem. Res , vol.23 , pp. 70-77
    • Poulter, C.D.1
  • 37
    • 0000680126 scopus 로고
    • Conversion of farnesyl pyrophosphate to squalene
    • J. W. Porter and S. L. Spurgeon ed, Wiley, New York, NY
    • Poulter, C. D., and H. C. Rilling. 1981. Conversion of farnesyl pyrophosphate to squalene, p. 413-441. In J. W. Porter and S. L. Spurgeon (ed.), Biosynthesis of isoprenoid compounds, vol. 1. Wiley, New York, NY.
    • (1981) Biosynthesis of isoprenoid compounds , vol.1 , pp. 413-441
    • Poulter, C.D.1    Rilling, H.C.2
  • 39
    • 0034701004 scopus 로고    scopus 로고
    • Squalene synthase: Steady-state, pre-steady-state, and isotope-trapping studies
    • Radisky, E. S., and C. D. Poulter. 2000. Squalene synthase: steady-state, pre-steady-state, and isotope-trapping studies. Biochemistry 39:1748-1760.
    • (2000) Biochemistry , vol.39 , pp. 1748-1760
    • Radisky, E.S.1    Poulter, C.D.2
  • 40
    • 0028817559 scopus 로고
    • Zymomonas mobilis squalene-hopene cyclase gene (shc): Cloning, DNA sequence analysis, and expression in Escherichia coli
    • Reipen, I. G., K. Poralla, H. Sahm, and G. A. Sprenger. 1995. Zymomonas mobilis squalene-hopene cyclase gene (shc): cloning, DNA sequence analysis, and expression in Escherichia coli. Microbiology 141:155-161.
    • (1995) Microbiology , vol.141 , pp. 155-161
    • Reipen, I.G.1    Poralla, K.2    Sahm, H.3    Sprenger, G.A.4
  • 41
    • 0027312026 scopus 로고
    • Conservation between human and fungal squalene synthetases: Similarities in structure, function, and regulation
    • Robinson, G. W., Y. H. Tsay, B. K. Kienzle, C. A. Smith-Monroy, and R. W. Bishop. 1993. Conservation between human and fungal squalene synthetases: similarities in structure, function, and regulation. Mol. Cell. Biol. 13: 2706-2717.
    • (1993) Mol. Cell. Biol , vol.13 , pp. 2706-2717
    • Robinson, G.W.1    Tsay, Y.H.2    Kienzle, B.K.3    Smith-Monroy, C.A.4    Bishop, R.W.5
  • 42
    • 0021259115 scopus 로고
    • Distribution of hopanoid triterpenes in prokaryotes
    • Rohmer, M., P. Bouvier-Nave, and G. Ourisson. 1984. Distribution of hopanoid triterpenes in prokaryotes. J. Gen. Microbiol. 130:1137-1150.
    • (1984) J. Gen. Microbiol , vol.130 , pp. 1137-1150
    • Rohmer, M.1    Bouvier-Nave, P.2    Ourisson, G.3
  • 43
    • 0019560891 scopus 로고
    • The formation of cyclic sesquiterpenes from farnesyl pyrophosphate by prenyltransferase
    • Saito, A., and H. C. Rilling. 1981. The formation of cyclic sesquiterpenes from farnesyl pyrophosphate by prenyltransferase. Arch. Biochem. Biophys. 208:508-511.
    • (1981) Arch. Biochem. Biophys , vol.208 , pp. 508-511
    • Saito, A.1    Rilling, H.C.2
  • 48
    • 0029973224 scopus 로고    scopus 로고
    • Bacterial triterpenoids of the hopane series from the prochlorophyte Prochlorothrix hollandica and their intracellular localization
    • Simonin, P., U. J. Jurgens, and M. Rohmer. 1996. Bacterial triterpenoids of the hopane series from the prochlorophyte Prochlorothrix hollandica and their intracellular localization. Eur. J. Biochem. 241:865-871.
    • (1996) Eur. J. Biochem , vol.241 , pp. 865-871
    • Simonin, P.1    Jurgens, U.J.2    Rohmer, M.3
  • 49
    • 0027194032 scopus 로고
    • Subcellular localization of squalene synthase in rat hepatic cells. Biochemical and immunochemical evidence
    • Stamellos, K. D., J. E. Shackelford, I. Shechter, G. Jiang, D. Conrad, G. A. Keller, and S. K. Krisans. 1993. Subcellular localization of squalene synthase in rat hepatic cells. Biochemical and immunochemical evidence. J. Biol. Chem. 268:12825-12836.
    • (1993) J. Biol. Chem , vol.268 , pp. 12825-12836
    • Stamellos, K.D.1    Shackelford, J.E.2    Shechter, I.3    Jiang, G.4    Conrad, D.5    Keller, G.A.6    Krisans, S.K.7
  • 50
    • 0027717852 scopus 로고
    • Cloning, expression and characterisation of the cDNA encoding human hepatic squalene synthase, and its relationship to phytoene synthase
    • Summers, C., F. Karst, and A. D. Charles. 1993. Cloning, expression and characterisation of the cDNA encoding human hepatic squalene synthase, and its relationship to phytoene synthase. Gene. 136:185-192.
    • (1993) Gene , vol.136 , pp. 185-192
    • Summers, C.1    Karst, F.2    Charles, A.D.3
  • 52
    • 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.
  • 53
    • 0032579970 scopus 로고    scopus 로고
    • Squalene-hopene cyclase from Methylococcus capsulatus (Bath): A bacterium producing hopanoids and steroids
    • Tippelt, A., L. Jahnke, and K. Poralla. 1998. Squalene-hopene cyclase from Methylococcus capsulatus (Bath): a bacterium producing hopanoids and steroids. Biochim. Biophys. Acta 1391:223-232.
    • (1998) Biochim. Biophys. Acta , vol.1391 , pp. 223-232
    • Tippelt, A.1    Jahnke, L.2    Poralla, K.3
  • 54
    • 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
  • 56
    • 1242274653 scopus 로고    scopus 로고
    • NMR structure of the KaiC-interacting C-terminal domain of KaiA, a circadian clock protein: Implications for KaiA-KaiC interaction
    • Vakonakis, I., J. Sun, T. Wu, A. Holzenburg, S. S. Golden, and A. C. LiWang. 2004. NMR structure of the KaiC-interacting C-terminal domain of KaiA, a circadian clock protein: implications for KaiA-KaiC interaction. Proc. Natl. Acad. Sci. USA 101:1479-1484.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 1479-1484
    • Vakonakis, I.1    Sun, J.2    Wu, T.3    Holzenburg, A.4    Golden, S.S.5    LiWang, A.C.6
  • 57
    • 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
  • 58
    • 0028827701 scopus 로고
    • Biosynthesis of non-head-to-tail isoprenoids. Synthesis of 1′-1 and 1′-3 structures by recombinant yeast squalene synthase
    • Zhang, D., and C. D. Poulter. 1995. Biosynthesis of non-head-to-tail isoprenoids. Synthesis of 1′-1 and 1′-3 structures by recombinant yeast squalene synthase J. Am. Chem. Soc. 117:1641-1642.
    • (1995) J. Am. Chem. Soc , vol.117 , pp. 1641-1642
    • Zhang, D.1    Poulter, C.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.