메뉴 건너뛰기




Volumn 55, Issue , 2004, Pages 429-457

Biosynthesis and accumulation of sterols

Author keywords

Arabidopsis thaliana; cDNA cloning and expression in yeast; EMS and T DNA insertional mutations; Inhibitors; Sterol metabolism

Indexed keywords

ARABIDOPSIS PROTEIN; ENZYME; PHYTOSTEROL; STEROL;

EID: 3242670779     PISSN: 15435008     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.arplant.55.031903.141616     Document Type: Review
Times cited : (336)

References (146)
  • 1
    • 12044254693 scopus 로고
    • Enzymatic cyclization of squalene and oxidosqualene to sterols and triterpenes
    • Abe I, Rohmer M, Prestwich GD. 1993. Enzymatic cyclization of squalene and oxidosqualene to sterols and triterpenes. Chem. Rev. 93:2189-206
    • (1993) Chem. Rev. , vol.93 , pp. 2189-2206
    • Abe, I.1    Rohmer, M.2    Prestwich, G.D.3
  • 4
    • 0033946944 scopus 로고    scopus 로고
    • Triterpene alcohol and sterol ferulates from rice bran and their anti-inflammatory effects
    • Akihisa T, Yasukawa K, Yamaura M, Ukiya M, Kimura Y, et al. 2000. Triterpene alcohol and sterol ferulates from rice bran and their anti-inflammatory effects. J. Agric. Food Chem. 48:2313-19
    • (2000) J. Agric. Food Chem. , vol.48 , pp. 2313-2319
    • Akihisa, T.1    Yasukawa, K.2    Yamaura, M.3    Ukiya, M.4    Kimura, Y.5
  • 6
    • 0344942508 scopus 로고    scopus 로고
    • Reducation of cholesterol and glycoalkaloid levels in transgenic potato plants by overexpression of a type 1 sterol methyltransferase cDNA
    • Arnqvist L, Dutta PC, Jonsson L, Sitbon F. 2003. Reducation of cholesterol and glycoalkaloid levels in transgenic potato plants by overexpression of a type 1 sterol methyltransferase cDNA. Plant Physiol. 131:1792-99
    • (2003) Plant Physiol. , vol.131 , pp. 1792-1799
    • Arnqvist, L.1    Dutta, P.C.2    Jonsson, L.3    Sitbon, F.4
  • 7
    • 0025866521 scopus 로고
    • Cloning, disruption and sequence of the gene encoding yeast C-5 sterol desaturase
    • Arthington BA, Bennett LG, Skatrud PL, Guynn CJ, Barbuch RJ, et al. 1991. Cloning, disruption and sequence of the gene encoding yeast C-5 sterol desaturase. Gene. 102:39-44
    • (1991) Gene , vol.102 , pp. 39-44
    • Arthington, B.A.1    Bennett, L.G.2    Skatrud, P.L.3    Guynn, C.J.4    Barbuch, R.J.5
  • 8
    • 0025987273 scopus 로고
    • Nucleotide sequence of the gene encoding yeast C-8 sterol isomerase
    • Arthington BA, Hoskins J, Skatrud PL, Bard M. 1991. Nucleotide sequence of the gene encoding yeast C-8 sterol isomerase. Gene 107:173-74
    • (1991) Gene , vol.107 , pp. 173-174
    • Arthington, B.A.1    Hoskins, J.2    Skatrud, P.L.3    Bard, M.4
  • 9
    • 0031470336 scopus 로고    scopus 로고
    • Cloning of cDNAs or genes encoding enzymes of sterol biosynthesis from plants and other eukaryotes: Heterologous expression and complementation analysis of mutations for functional characterization
    • Bach TJ, Benveniste P. 1997. Cloning of cDNAs or genes encoding enzymes of sterol biosynthesis from plants and other eukaryotes: heterologous expression and complementation analysis of mutations for functional characterization. Prog. Lipid Res. 36:197-226
    • (1997) Prog. Lipid Res. , vol.36 , pp. 197-226
    • Bach, T.J.1    Benveniste, P.2
  • 10
    • 0031079568 scopus 로고    scopus 로고
    • Cloning and expression in Escherichia coli of the obtusifoliol 14α-demethylase of Sorghum bicolor (L.) Moench, a cytochrome P450 orthologous to the sterol 14α-demethylases (CYP51) from fungi and mammals
    • Bak S, Kahn RA, Olsen CE, Halkier BA. 1997. Cloning and expression in Escherichia coli of the obtusifoliol 14α-demethylase of Sorghum bicolor (L.) Moench, a cytochrome P450 orthologous to the sterol 14α-demethylases (CYP51) from fungi and mammals. Plant J. 11:191-201
    • (1997) Plant J. , vol.11 , pp. 191-201
    • Bak, S.1    Kahn, R.A.2    Olsen, C.E.3    Halkier, B.A.4
  • 11
    • 0030033387 scopus 로고    scopus 로고
    • Cloning and characterization of ERG25, the Saccharomyces cerevisiae gene encoding C-4 sterol methyl oxidase
    • Bard M, Bruner DA, Pierson CA, Lees ND, Biermann B, et al. 1996. Cloning and characterization of ERG25, the Saccharomyces cerevisiae gene encoding C-4 sterol methyl oxidase. Proc. Natl. Acad. Sci. USA 93:186-90
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 186-190
    • Bard, M.1    Bruner, D.A.2    Pierson, C.A.3    Lees, N.D.4    Biermann, B.5
  • 14
    • 85052213872 scopus 로고
    • Target sites of sterol biosynthesis inhibitors in plants
    • W Koellers, CRC Press
    • Benveniste P, Rahier A. 1992. Target sites of sterol biosynthesis inhibitors in plants. In Target Sites of Fungicide Action, ed. W Koellers, pp. 207-25. CRC Press
    • (1992) Target Sites of Fungicide Action , pp. 207-225
    • Benveniste, P.1    Rahier, A.2
  • 15
    • 0025893858 scopus 로고
    • Molecular cloning an characterization of two distinct hsp85 sequences from the steroid responsive fungus Achlya ambisexualis
    • Blunt SA, Silver JC. 1991. Molecular cloning an characterization of two distinct hsp85 sequences from the steroid responsive fungus Achlya ambisexualis. Curr. Genet. 19:383-88
    • (1991) Curr. Genet. , vol.19 , pp. 383-388
    • Blunt, S.A.1    Silver, J.C.2
  • 16
    • 0037238414 scopus 로고    scopus 로고
    • Steroid biosynthesis in prokaryotes: Identification of myxobacterial steroids and cloning of the first bacterial 2.3(S)-oxidosqualene cyclase from the mycobacterium Stigmatella aurantiaca
    • Bode HB, Zeggel B, Silakowski B, Wenzel SC, Reichenbach H, et al. 2003. Steroid biosynthesis in prokaryotes: identification of myxobacterial steroids and cloning of the first bacterial 2.3(S)-oxidosqualene cyclase from the mycobacterium Stigmatella aurantiaca. Mol. Microbiol. 47:471-81
    • (2003) Mol. Microbiol. , vol.47 , pp. 471-481
    • Bode, H.B.1    Zeggel, B.2    Silakowski, B.3    Wenzel, S.C.4    Reichenbach, H.5
  • 18
    • 0028873790 scopus 로고
    • Sterol acyl transferase and steryl ester hydrolase activities in a tobacco mutant which overproduces sterols
    • Bouvier-Navé P, Benveniste P. 1995. Sterol acyl transferase and steryl ester hydrolase activities in a tobacco mutant which overproduces sterols. Plant Sci. 110:11-19
    • (1995) Plant Sci. , vol.110 , pp. 11-19
    • Bouvier-Navé, P.1    Benveniste, P.2
  • 19
    • 0033971564 scopus 로고    scopus 로고
    • Expression in yeast and tobacco of plant cDNAs encoding acyl CoA:diacylglycerol acyltransferase
    • Bouvier-Navé P, Benveniste P, Oelkers P, Sturley SL, Schaller H. 2000. Expression in yeast and tobacco of plant cDNAs encoding acyl CoA:diacylglycerol acyltransferase. Eur. J. Biochem. 267:85-96
    • (2000) Eur. J. Biochem. , vol.267 , pp. 85-96
    • Bouvier-Navé, P.1    Benveniste, P.2    Oelkers, P.3    Sturley, S.L.4    Schaller, H.5
  • 20
    • 0032528942 scopus 로고    scopus 로고
    • Two families of sterol methyltransferases are involved in the first and the second methylation steps of plant sterol biosynthesis
    • Bouvier-Navé P, Husselstein T, Benveniste P. 1998. Two families of sterol methyltransferases are involved in the first and the second methylation steps of plant sterol biosynthesis. Eur. J. Biochem. 256:88-96
    • (1998) Eur. J. Biochem. , vol.256 , pp. 88-96
    • Bouvier-Navé, P.1    Husselstein, T.2    Benveniste, P.3
  • 21
    • 0030908496 scopus 로고    scopus 로고
    • Identification of cDNAs encoding sterol methyl-transferases involved in the second methylation step of plant sterol biosynthesis
    • Bouvier-Navé P, Husselstein T, Desprez T, Benveniste P. 1997. Identification of cDNAs encoding sterol methyl-transferases involved in the second methylation step of plant sterol biosynthesis. Eur. J. Biochem. 246:518-29
    • (1997) Eur. J. Biochem. , vol.246 , pp. 518-529
    • Bouvier-Navé, P.1    Husselstein, T.2    Desprez, T.3    Benveniste, P.4
  • 23
    • 0038235573 scopus 로고    scopus 로고
    • Virus-induced silencing of sterol biosynthetic genes: Identification of a Nicotiana tabacum L. obtusifoliol-14α-demethylase (CYP51) by genetic manipulation of the sterol biosynthetic pathway in Nicotiana benthamiana L.
    • Burger C, Rondet S, Benveniste P, Schaller H. 2003. Virus-induced silencing of sterol biosynthetic genes: identification of a Nicotiana tabacum L. obtusifoliol-14α-demethylase (CYP51) by genetic manipulation of the sterol biosynthetic pathway in Nicotiana benthamiana L. J. Exp. Bot. 54:1675-83
    • (2003) J. Exp. Bot. , vol.54 , pp. 1675-1683
    • Burger, C.1    Rondet, S.2    Benveniste, P.3    Schaller, H.4
  • 24
    • 0033152101 scopus 로고    scopus 로고
    • Optimized expression and catalytical properties of a wheat obtusifoliol 14α-demethylase (CYP51) expressed in yeast. Complementation of erg11 yeast mutants by wheat CYP51
    • Cabello-Hurtado F, Taton M, Forthoffer N, Bak S, Kahn R, et al. 1999. Optimized expression and catalytical properties of a wheat obtusifoliol 14α-demethylase (CYP51) expressed in yeast. Complementation of erg11 yeast mutants by wheat CYP51. Eur. J. Biochem. 262:435-46
    • (1999) Eur. J. Biochem. , vol.262 , pp. 435-446
    • Cabello-Hurtado, F.1    Taton, M.2    Forthoffer, N.3    Bak, S.4    Kahn, R.5
  • 25
    • 0036741602 scopus 로고    scopus 로고
    • The identification of CVP1 reveals a role for sterols in vascular patterning
    • Carland FM, Fujioka S, Takatsuto S, Yoshida S, Nelson T. 2002. The identification of CVP1 reveals a role for sterols in vascular patterning. Plant Cell. 14:2045-58
    • (2002) Plant Cell. , vol.14 , pp. 2045-2058
    • Carland, F.M.1    Fujioka, S.2    Takatsuto, S.3    Yoshida, S.4    Nelson, T.5
  • 26
    • 0035028604 scopus 로고    scopus 로고
    • Brassinosteroids, microtubules and cell elongation in Arabidopsis thaliana. II. Effects of brassinosteroids on microtubules and cell elongation in the bull mutant
    • Catterou M, Dubois F, Schaller H, Aubanelle L, Vilcot B, et al. 2001. Brassinosteroids, microtubules and cell elongation in Arabidopsis thaliana. II. Effects of brassinosteroids on microtubules and cell elongation in the bull mutant. Planta 212:673-83
    • (2001) Planta , vol.212 , pp. 673-683
    • Catterou, M.1    Dubois, F.2    Schaller, H.3    Aubanelle, L.4    Vilcot, B.5
  • 27
    • 0033102093 scopus 로고    scopus 로고
    • The Arabidopsis dwarf1 mutant is defective in the conversion of 24-methylene-cholesterol to campesterol in brassinosteroid biosynthesis
    • Choe S, Dilkes BP, Gregory BD, Ross AS, Yuan H, et al. 1999. The Arabidopsis dwarf1 mutant is defective in the conversion of 24-methylene- cholesterol to campesterol in brassinosteroid biosynthesis. Plant Physiol. 119:897-907
    • (1999) Plant Physiol. , vol.119 , pp. 897-907
    • Choe, S.1    Dilkes, B.P.2    Gregory, B.D.3    Ross, A.S.4    Yuan, H.5
  • 28
    • 6544274717 scopus 로고    scopus 로고
    • The Arabidopsis dwf7/ste1 mutant is defective in the Δ7-sterol C-5 desaturation step leading to brassinosteroid biosynthesis
    • Choe S, Noguchi T, Fujioka S, Takatsuto S, Tissier CP, et al. 1999. The Arabidopsis dwf7/ste1 mutant is defective in the Δ7-sterol C-5 desaturation step leading to brassinosteroid biosynthesis. Plant Cell. 11:207-21
    • (1999) Plant Cell. , vol.11 , pp. 207-221
    • Choe, S.1    Noguchi, T.2    Fujioka, S.3    Takatsuto, S.4    Tissier, C.P.5
  • 29
    • 0034028486 scopus 로고    scopus 로고
    • Lesions in the sterol Δ7-reductase gene of Arabidopsis cause dwarfism due to a block in brassinosteroid biosynthesis
    • Choe S, Tanaka A, Noguchi T, Fujioka S, Takatsuto S, et al. 2000. Lesions in the sterol Δ7-reductase gene of Arabidopsis cause dwarfism due to a block in brassinosteroid biosynthesis. Plant J. 21:431-43
    • (2000) Plant J. , vol.21 , pp. 431-443
    • Choe, S.1    Tanaka, A.2    Noguchi, T.3    Fujioka, S.4    Takatsuto, S.5
  • 30
    • 0034710593 scopus 로고    scopus 로고
    • Plant development: A role for sterols in embryogenesis
    • Clouse SD. 2000. Plant development: a role for sterols in embryogenesis. Curr. Biol. 10:601-4
    • (2000) Curr. Biol. , vol.10 , pp. 601-604
    • Clouse, S.D.1
  • 31
    • 0036743364 scopus 로고    scopus 로고
    • Arabidopsis mutants reveal multiple roles for sterols in plant development
    • Clouse SD. 2002. Arabidopsis mutants reveal multiple roles for sterols in plant development. Plant Cell. 14:1995-2000
    • (2002) Plant Cell. , vol.14 , pp. 1995-2000
    • Clouse, S.D.1
  • 32
    • 0027146637 scopus 로고
    • Isolation of an Arabidopsis thaliana gene encoding cycloartenol synthase by functional expression in a yeast mutant lacking lanosterol synthase by the use of a chromatographic screen
    • Corey EJ, Matsuda SPT, Bartel B. 1993. Isolation of an Arabidopsis thaliana gene encoding cycloartenol synthase by functional expression in a yeast mutant lacking lanosterol synthase by the use of a chromatographic screen. Proc. Natl. Acad. Sci. USA 90:11628-32
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 11628-11632
    • Corey, E.J.1    Matsuda, S.P.T.2    Bartel, B.3
  • 33
    • 0040102451 scopus 로고
    • Sterol and ecdysteroid profiles of Serratula tinctoria L.: Plant and cell cultures producing steroids
    • Corio-Costet MF, Chapuis L, Mouillet JF, Delbecque JP. 1993. Sterol and ecdysteroid profiles of Serratula tinctoria L.: plant and cell cultures producing steroids. Insect Biochem. Molec. Biol. 23:175-80
    • (1993) Insect Biochem. Molec. Biol. , vol.23 , pp. 175-180
    • Corio-Costet, M.F.1    Chapuis, L.2    Mouillet, J.F.3    Delbecque, J.P.4
  • 34
    • 0034485767 scopus 로고    scopus 로고
    • Spatial and temporal patterns of GUS expression directed by 5′ regions of the Arabidopsis thaliana farnesyl diphosphate synthase genes FPS1 and FPS2
    • Cunillera N, Boronat A, Ferrer A. 2000. Spatial and temporal patterns of GUS expression directed by 5′ regions of the Arabidopsis thaliana farnesyl diphosphate synthase genes FPS1 and FPS2. Plant Mol. Biol. 44:747-58
    • (2000) Plant Mol. Biol. , vol.44 , pp. 747-758
    • Cunillera, N.1    Boronat, A.2    Ferrer, A.3
  • 35
    • 0035834373 scopus 로고    scopus 로고
    • Functional identification of sterol-4α-methyl oxidase cDNAs from Arabidopsis thaliana by complementation of a yeast erg25 mutant lacking sterol-4α-methyl oxidation
    • Darnet S, Bard M, Rahier A. 2001. Functional identification of sterol-4α-methyl oxidase cDNAs from Arabidopsis thaliana by complementation of a yeast erg25 mutant lacking sterol-4α-methyl oxidation. FEBS Letters. 508:39-43
    • (2001) FEBS Letters , vol.508 , pp. 39-43
    • Darnet, S.1    Bard, M.2    Rahier, A.3
  • 36
    • 0038487267 scopus 로고    scopus 로고
    • Enzymologycal properties of sterol-C4-melhyl oxidase of yeast sterol biosynthesis
    • Darnet S, Rahier A. 2003. Enzymologycal properties of sterol-C4-melhyl oxidase of yeast sterol biosynthesis. Biochim. Biophys. Acta. 1633:106-17
    • (2003) Biochim. Biophys. Acta , vol.1633 , pp. 106-117
    • Darnet, S.1    Rahier, A.2
  • 37
    • 0032428659 scopus 로고    scopus 로고
    • PCR cloning and detection of point mutations in the eburicol 14α-demethylase (CYP51) gene from Erysiphe graminis f. sp. hordei, a "recalcitrant" fungus
    • Delye C, Bousset L, Corio-Costet MF. 1998. PCR cloning and detection of point mutations in the eburicol 14α-demethylase (CYP51) gene from Erysiphe graminis f. sp. hordei, a "recalcitrant" fungus. Curr. Genet. 34:399-403
    • (1998) Curr. Genet. , vol.34 , pp. 399-403
    • Delye, C.1    Bousset, L.2    Corio-Costet, M.F.3
  • 39
    • 0033949584 scopus 로고    scopus 로고
    • Sterol Methyl Transferase 1 controls the level of cholesterol in plants
    • Diener AC, Li H, Zhou WX, Whoriskey WJ, Nes WD, et al. 2000. STEROL METHYL TRANSFERASE 1 controls the level of cholesterol in plants. Plant Cell. 12:853-70
    • (2000) Plant Cell. , vol.12 , pp. 853-870
    • Diener, A.C.1    Li, H.2    Zhou, W.X.3    Whoriskey, W.J.4    Nes, W.D.5
  • 40
    • 0013410490 scopus 로고
    • Steryl fatty acyl esters in plants
    • Dyas L, Goad LJ. 1993. Steryl fatty acyl esters in plants. Phytochemistry 34:17-29
    • (1993) Phytochemistry , vol.34 , pp. 17-29
    • Dyas, L.1    Goad, L.J.2
  • 41
    • 14444280650 scopus 로고    scopus 로고
    • Acyl CoA:cholesterol acyltransferase genes and knockout mice
    • Farese RV Jr. 1998. Acyl CoA:cholesterol acyltransferase genes and knockout mice. Curr. Op. Lipidol. 9:119-23
    • (1998) Curr. Op. Lipidol. , vol.9 , pp. 119-123
    • Farese Jr., R.V.1
  • 43
    • 0001612646 scopus 로고
    • A 24-methylene lophenol C-28 methyl transferase from suspension cultures of bramble cells
    • Fonteneau P, Hartmann MA, Benveniste P. 1977. A 24-methylene lophenol C-28 methyl transferase from suspension cultures of bramble cells. Plant Sci. Lett. 10:147-55
    • (1977) Plant Sci. Lett. , vol.10 , pp. 147-155
    • Fonteneau, P.1    Hartmann, M.A.2    Benveniste, P.3
  • 44
    • 0032506001 scopus 로고    scopus 로고
    • Characterization of the Saccharomyces cerevisiae ERG26 gene encoding the C-3 sterol dehydrogenase (C-4 decarboxylase) involved in sterol biosynthesis
    • Gachotte D, Barbuch R, Gaylor J, Nickel E, Bard M. 1998. Characterization of the Saccharomyces cerevisiae ERG26 gene encoding the C-3 sterol dehydrogenase (C-4 decarboxylase) involved in sterol biosynthesis. Proc. Natl. Acad. Sci. USA 95:13794-99
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 13794-13799
    • Gachotte, D.1    Barbuch, R.2    Gaylor, J.3    Nickel, E.4    Bard, M.5
  • 47
    • 0033607267 scopus 로고    scopus 로고
    • Characterization of the Saccharomyces cerevisiae ERG27 gene encoding the 3-keto reductase involved in C-4 sterol demethylation
    • Gachotte D, Sen SE, Eckstein J, Barbuch R, Krieger M, et al. 1999. Characterization of the Saccharomyces cerevisiae ERG27 gene encoding the 3-keto reductase involved in C-4 sterol demethylation. Proc. Natl. Acad. Sci. USA 96:12655-60
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 12655-12660
    • Gachotte, D.1    Sen, S.E.2    Eckstein, J.3    Barbuch, R.4    Krieger, M.5
  • 48
    • 0011707346 scopus 로고
    • Partial characterization of steryl ester biosynthesis in spinach leaves
    • Garcia RE, Mudd JB. 1978. Partial characterization of steryl ester biosynthesis in spinach leaves. Plant Physiol. 61:357-60
    • (1978) Plant Physiol. , vol.61 , pp. 357-360
    • Garcia, R.E.1    Mudd, J.B.2
  • 49
    • 0038717630 scopus 로고    scopus 로고
    • Cloning and characterization of the Dictyostelium discoideum cycloartenol synthase cDNA
    • Godzina SM, Lovato MA, Meyer MM, Foster KA, Wilson WK, et al. 2000. Cloning and characterization of the Dictyostelium discoideum cycloartenol synthase cDNA Lipids 35:249-55
    • (2000) Lipids , vol.35 , pp. 249-255
    • Godzina, S.M.1    Lovato, M.A.2    Meyer, M.M.3    Foster, K.A.4    Wilson, W.K.5
  • 50
    • 0028121655 scopus 로고
    • Regulation of sterol content in membranes by subcellular compartmentation of steryl-esters accumulation in a sterol overproduction tobacco mutant
    • Gondet L, Bronner R, Benveniste P. 1994. Regulation of sterol content in membranes by subcellular compartmentation of steryl-esters accumulation in a sterol overproduction tobacco mutant. Plant Physiol. 105:509-18
    • (1994) Plant Physiol. , vol.105 , pp. 509-518
    • Gondet, L.1    Bronner, R.2    Benveniste, P.3
  • 51
    • 0026705642 scopus 로고
    • Regulatory role of microsomal 3-hydroxy-3-methyl-glutaryl-Coenzyme A reductase in a tobacco mutant that overproduces sterols
    • Gondet L, Weber T, Maillot-Vernier P, Benveniste M, Bach TJ. 1992. Regulatory role of microsomal 3-hydroxy-3-methyl-glutaryl-Coenzyme A reductase in a tobacco mutant that overproduces sterols. Biochem. Biophys. Res. Commun. 186:878-93
    • (1992) Biochem. Biophys. Res. Commun. , vol.186 , pp. 878-893
    • Gondet, L.1    Weber, T.2    Maillot-Vernier, P.3    Benveniste, M.4    Bach, T.J.5
  • 53
    • 0031214093 scopus 로고    scopus 로고
    • Characterization of Zea mays endosperm C-24 sterol methyltransferase: One of two types of sterol methyltransferase in higher plants
    • Grebenok RJ, Galbraith DW, DellaPenna D. 1997. Characterization of Zea mays endosperm C-24 sterol methyltransferase: one of two types of sterol methyltransferase in higher plants. Plant Mol. Biol. 34:891-96
    • (1997) Plant Mol. Biol. , vol.34 , pp. 891-896
    • Grebenok, R.J.1    Galbraith, D.W.2    DellaPenna, D.3
  • 55
    • 0034307463 scopus 로고    scopus 로고
    • The human DIMINUTO:DWARF1 homolog seladin-1 confers resistance to Alzheimer's diseaseassociated neurodegeneration and oxidative stress
    • Greeve I, Hermans-Borgmeyer I, Brellinger C, Kasper D, Gomez-Isla T, et al. 2000. The human DIMINUTO:DWARF1 homolog seladin-1 confers resistance to Alzheimer's diseaseassociated neurodegeneration and oxidative stress. J. Neurosci. 20:7345-52
    • (2000) J. Neurosci. , vol.20 , pp. 7345-7352
    • Greeve, I.1    Hermans-Borgmeyer, I.2    Brellinger, C.3    Kasper, D.4    Gomez-Isla, T.5
  • 56
    • 0032941410 scopus 로고    scopus 로고
    • Serum sterols during stanol ester feeding in a mildy hypercholesterolemic population
    • Gylling H, Puska P, Vartiainen E, Miettinen TA. 1999. Serum sterols during stanol ester feeding in a mildy hypercholesterolemic population. J. Lipid Res. 40:593-600
    • (1999) J. Lipid Res. , vol.40 , pp. 593-600
    • Gylling, H.1    Puska, P.2    Vartiainen, E.3    Miettinen, T.A.4
  • 57
    • 0028355262 scopus 로고
    • SED6 is identical to ERG 6, and encodes a putative methyltransferase required for ergosterol synthesis
    • Hardwick KG, Pelham HR. 1994. SED6 is identical to ERG 6, and encodes a putative methyltransferase required for ergosterol synthesis. Yeast 10:265-69
    • (1994) Yeast , vol.10 , pp. 265-269
    • Hardwick, K.G.1    Pelham, H.R.2
  • 58
    • 0037977901 scopus 로고    scopus 로고
    • Co-ordinate regulation of sterol biosynthesis enzyme activity during accumulation of sterols in developing rape and tobacco seed
    • Harker M, Hellyer A, Clayton JC, Duvoix A, Lanot A, et al. 2003. Co-ordinate regulation of sterol biosynthesis enzyme activity during accumulation of sterols in developing rape and tobacco seed. Planta 216:707-15
    • (2003) Planta , vol.216 , pp. 707-715
    • Harker, M.1    Hellyer, A.2    Clayton, J.C.3    Duvoix, A.4    Lanot, A.5
  • 59
    • 0033610475 scopus 로고    scopus 로고
    • Directed evolution to investigate steric control of enzymatic oxidosqualene cyclization. An isoleucine-co-valine mutation in cycloartenol synthase allows lanosterol and parkeol biosynthesis
    • Hart EA, Hua L, Daer LB, Wilson WK, Pang J, et al. 1999. Directed evolution to investigate steric control of enzymatic oxidosqualene cyclization. An isoleucine-co-valine mutation in cycloartenol synthase allows lanosterol and parkeol biosynthesis. J. Am. Chem. Soc. 121:9887-88
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 9887-9888
    • Hart, E.A.1    Hua, L.2    Daer, L.B.3    Wilson, W.K.4    Pang, J.5
  • 60
    • 3242715266 scopus 로고    scopus 로고
    • Sterol metabolism and function in higher plants
    • Lipid Metabolism and Membrane Biogenesis. ed. G Daum
    • Hartmann MA. 2003. Sterol metabolism and function in higher plants. In Lipid Metabolism and Membrane Biogenesis. Top Curr. Genet (Rev. Ser.), ed. G Daum, pp. 183-211
    • (2003) Top Curr. Genet (Rev. Ser.) , pp. 183-211
    • Hartmann, M.A.1
  • 61
    • 0001154042 scopus 로고
    • Sterol biosynthetic capability of purified membrane fractions from maize coleoptiles
    • Hartmann-Bouillon MA, Benveniste P. 1978. Sterol biosynthetic capability of purified membrane fractions from maize coleoptiles. Photochemistry 17:1037-42
    • (1978) Photochemistry , vol.17 , pp. 1037-1042
    • Hartmann-Bouillon, M.A.1    Benveniste, P.2
  • 62
    • 0016164881 scopus 로고
    • Enzymatic cleavage of the 9β,19-cyclopropane ring of cyclopropyl sterols in bramble tissue cultures
    • Heintz R, Benveniste P. 1974. Enzymatic cleavage of the 9β,19-cyclopropane ring of cyclopropyl sterols in bramble tissue cultures. J. Biol. Chem. 249:4267
    • (1974) J. Biol. Chem. , vol.249 , pp. 4267
    • Heintz, R.1    Benveniste, P.2
  • 63
    • 0039255131 scopus 로고    scopus 로고
    • Composition and role of tapetal lipid bodies in the biogenesis of the pollen coat of Brassica napus
    • Hernandez-Pinzon I, Ross JH, Barnes KA, Damant AP, Murphy DJ. 1999. Composition and role of tapetal lipid bodies in the biogenesis of the pollen coat of Brassica napus. Planta 208:588-98
    • (1999) Planta , vol.208 , pp. 588-598
    • Hernandez-Pinzon, I.1    Ross, J.H.2    Barnes, K.A.3    Damant, A.P.4    Murphy, D.J.5
  • 64
    • 0032399269 scopus 로고    scopus 로고
    • Cloning and characterization of the Arabidopsis thaliana lupeol synthase gene
    • Herrera JBR, Bartel B, Wilson WK, Matsuda SPT. 1998. Cloning and characterization of the Arabidopsis thaliana lupeol synthase gene. Phytochemistry 49:1905-11
    • (1998) Phytochemistry , vol.49 , pp. 1905-1911
    • Herrera, J.B.R.1    Bartel, B.2    Wilson, W.K.3    Matsuda, S.P.T.4
  • 65
    • 0036742742 scopus 로고    scopus 로고
    • Sterol C-24 methyltransferase type 1 controls the flux of carbon into sterol biosynthesis in tobacco seed
    • Holmberg N, Harker M, Gibbard CL, Wallace AD, Clayton JC, et al. 2002. Sterol C-24 methyltransferase type 1 controls the flux of carbon into sterol biosynthesis in tobacco seed. Plant Physiol. 130:303-11
    • (2002) Plant Physiol. , vol.130 , pp. 303-311
    • Holmberg, N.1    Harker, M.2    Gibbard, C.L.3    Wallace, A.D.4    Clayton, J.C.5
  • 66
    • 0030030157 scopus 로고    scopus 로고
    • Transformation of Saccharomyces cerevisiae with a cDNA encoding a sterol C-methyltransferase from Arabidopsis thaliana results in the synthesis of 24-ethyl sterols
    • Husselstein T, Gachotte D, Desprez T, Bard M, Benveniste P. 1996. Transformation of Saccharomyces cerevisiae with a cDNA encoding a sterol C-methyltransferase from Arabidopsis thaliana results in the synthesis of 24-ethyl sterols. FEBS Lett. 381:87-92
    • (1996) FEBS Lett. , vol.381 , pp. 87-92
    • Husselstein, T.1    Gachotte, D.2    Desprez, T.3    Bard, M.4    Benveniste, P.5
  • 67
    • 0032589275 scopus 로고    scopus 로고
    • 7-sterol-C5-desaturase molecular characterization and functional expression of wild type and mutant alleles
    • 7-sterol-C5-desaturase molecular characterization and functional expression of wild type and mutant alleles. Plant Mol. Biol. 39:891-906
    • (1999) Plant Mol. Biol. , vol.39 , pp. 891-906
    • Husselstein, T.1    Schaller, H.2    Gachotte, D.3    Benveniste, P.4
  • 68
    • 0037067996 scopus 로고    scopus 로고
    • Seladin-1 transcription is linked to neuronal degeneration in Alzheimer's disease
    • Iivonen S, Hiltunen M, Alafuzoff I, Mannermaa A, Kerokoski P, et al. 2002. Seladin-1 transcription is linked to neuronal degeneration in Alzheimer's disease. Neuroscience 113:301-10
    • (2002) Neuroscience , vol.113 , pp. 301-310
    • Iivonen, S.1    Hiltunen, M.2    Alafuzoff, I.3    Mannermaa, A.4    Kerokoski, P.5
  • 69
    • 0037032543 scopus 로고    scopus 로고
    • A novel sterol 14alpha-demethylase/ferredoxin fusion protein (MC-CYP51FX) from Methylococcus capsulatus represents a new class of the cytochrome P450 superfamily
    • Jackson CJ, Lamb DC, Marczylo TH, Warrilow AG, Manning NJ, et al. 2002. A novel sterol 14alpha-demethylase/ferredoxin fusion protein (MC-CYP51FX) from Methylococcus capsulatus represents a new class of the cytochrome P450 superfamily. J. Biol. Chem. 277:46959-65
    • (2002) J. Biol. Chem. , vol.277 , pp. 46959-46965
    • Jackson, C.J.1    Lamb, D.C.2    Marczylo, T.H.3    Warrilow, A.G.4    Manning, N.J.5
  • 70
    • 0034659222 scopus 로고    scopus 로고
    • A critical role of sterols in embryonic patterning and meristem programming revealed by the fackel mutants of Arabidopsis thaliana
    • Jang YC, Fujioka S, Tasaka M, Seto H, Takatsuto S, et al. 2000. A critical role of sterols in embryonic patterning and meristem programming revealed by the fackel mutants of Arabidopsis thaliana. Genes Dev. 14:1485-97
    • (2000) Genes Dev. , vol.14 , pp. 1485-1497
    • Jang, Y.C.1    Fujioka, S.2    Tasaka, M.3    Seto, H.4    Takatsuto, S.5
  • 71
    • 0035859360 scopus 로고    scopus 로고
    • Trypanosome and animal lanosterol synthases use different catalytic motifs
    • Joubert BM, Buckner FS, Matsuda SP. 2001. Trypanosome and animal lanosterol synthases use different catalytic motifs. Org. Lett. 3:1957-60
    • (2001) Org. Lett. , vol.3 , pp. 1957-1960
    • Joubert, B.M.1    Buckner, F.S.2    Matsuda, S.P.3
  • 72
    • 0028179364 scopus 로고
    • Widespread occurrence of three sequence motifs in diverse S-adenosylmethionine-dependent methyltransferases suggests a common structure for these enzymes
    • Kagan RM, Clarke S. 1994. Widespread occurrence of three sequence motifs in diverse S-adenosylmethionine-dependent methyltransferases suggests a common structure for these enzymes. Arch. Biochem. Biophys. 310:417-27
    • (1994) Arch. Biochem. Biophys. , vol.310 , pp. 417-427
    • Kagan, R.M.1    Clarke, S.2
  • 73
    • 0022981279 scopus 로고
    • Isolation of a cytochrome P-450 structural gene from Saccharomyces cerevisiae
    • Kalb VF, Loper JC, Dey CR, Woods CW, Sutter TR. 1986. Isolation of a cytochrome P-450 structural gene from Saccharomyces cerevisiae. Gene 45:237-45
    • (1986) Gene , vol.45 , pp. 237-245
    • Kalb, V.F.1    Loper, J.C.2    Dey, C.R.3    Woods, C.W.4    Sutter, T.R.5
  • 74
    • 0035374351 scopus 로고    scopus 로고
    • The sonic hedgehog receptor patched associates with caveolin-1 in cholesterol-rich microdomains of the plasma membrane
    • Karpen HE, Bukowski JT, Hughes T, Gratton JP, Sessa WC, et al. 2001. The sonic hedgehog receptor patched associates with caveolin-1 in cholesterol-rich microdomains of the plasma membrane. J. Biol. Chem. 276:19503-11
    • (2001) J. Biol. Chem. , vol.276 , pp. 19503-19511
    • Karpen, H.E.1    Bukowski, J.T.2    Hughes, T.3    Gratton, J.P.4    Sessa, W.C.5
  • 75
    • 0037097340 scopus 로고    scopus 로고
    • Abnormal sterol metabolism in a patient with Antley-Bixler syndrome and ambiguous genitalia
    • Kelley RI, Kratz LE, Glaser RL, Netzloff ML, Wolf LM, et al. 2002. Abnormal sterol metabolism in a patient with Antley-Bixler syndrome and ambiguous genitalia. Am. J. Med. Genet. 110:95-102
    • (2002) Am. J. Med. Genet. , vol.110 , pp. 95-102
    • Kelley, R.I.1    Kratz, L.E.2    Glaser, R.L.3    Netzloff, M.L.4    Wolf, L.M.5
  • 76
    • 0012466695 scopus 로고    scopus 로고
    • Inhibition of sonic hedgehog autoprocessing in cultured mammalian cells by sterol deprivation
    • Guy RK. 2000. Inhibition of sonic hedgehog autoprocessing in cultured mammalian cells by sterol deprivation. Proc. Nat. Acad. Sci USA 97:7307-12
    • (2000) Proc. Nat. Acad. Sci USA , vol.97 , pp. 7307-7312
    • Guy, R.K.1
  • 77
    • 0032192096 scopus 로고    scopus 로고
    • The Arabidopsis DIMINUTO/DWARF1 gene encodes a protein involved in steroid synthesis
    • Klahre U, Noguchi T, Fujioka S, Takatsuto S, Yokota T, et al. 1998. The Arabidopsis DIMINUTO/DWARF1 gene encodes a protein involved in steroid synthesis. Plant Cell. 10:1677-10
    • (1998) Plant Cell. , vol.10 , pp. 1677-1710
    • Klahre, U.1    Noguchi, T.2    Fujioka, S.3    Takatsuto, S.4    Yokota, T.5
  • 78
    • 0034741032 scopus 로고    scopus 로고
    • Obtusifoliol 14α-demethylase (CYP51) antisense Arabidopsis shows slow growth and long life
    • Kushiro M, Nakano T, Sato K, Yamagishi K, Asami T, et al. 2001. Obtusifoliol 14α-demethylase (CYP51) antisense Arabidopsis shows slow growth and long life. Biochem. Biophys. Res. Communic. 285:98-104
    • (2001) Biochem. Biophys. Res. Communic. , vol.285 , pp. 98-104
    • Kushiro, M.1    Nakano, T.2    Sato, K.3    Yamagishi, K.4    Asami, T.5
  • 80
    • 0029873330 scopus 로고    scopus 로고
    • A role for brassinosteroids in light-dependent development of Arabidopsis
    • Li J, Nagpal P, Witart V, McMorris TC, Chory J. 1996. A role for brassinosteroids in light-dependent development of Arabidopsis. Science 272:398-401
    • (1996) Science , vol.272 , pp. 398-401
    • Li, J.1    Nagpal, P.2    Witart, V.3    McMorris, T.C.4    Chory, J.5
  • 81
    • 0030014654 scopus 로고    scopus 로고
    • Characterization of yeast methyl sterol oxidase (ERG25) and identification of a human homologue
    • Li L, Kaplan J. 1996. Characterization of yeast methyl sterol oxidase (ERG25) and identification of a human homologue. J. Biol. Chem. 271:16927-33
    • (1996) J. Biol. Chem. , vol.271 , pp. 16927-16933
    • Li, L.1    Kaplan, J.2
  • 82
    • 0026439784 scopus 로고
    • Cloning, sequencing and disruption of the encoding sterol C-14 reductase in Saccharomyces cerevisiae
    • Lorenz RT, Parks LW. 1992. Cloning, sequencing and disruption of the encoding sterol C-14 reductase in Saccharomyces cerevisiae. DNA Cell. Biol. 11:685-92
    • (1992) DNA Cell. Biol. , vol.11 , pp. 685-692
    • Lorenz, R.T.1    Parks, L.W.2
  • 83
    • 0034607844 scopus 로고    scopus 로고
    • Functional cloning of an Arabidopsis thaliana cDNA encoding cycloeucalenol cycloisomerase
    • Lovato MA, Hart EA, Segura MJR, Giner JL, Matsuda SPT. 2000. Functional cloning of an Arabidopsis thaliana cDNA encoding cycloeucalenol cycloisomerase. J. Biol. Chem. 275:13394-97
    • (2000) J. Biol. Chem. , vol.275 , pp. 13394-13397
    • Lovato, M.A.1    Hart, E.A.2    Segura, M.J.R.3    Giner, J.L.4    Matsuda, S.P.T.5
  • 84
    • 0035822096 scopus 로고    scopus 로고
    • Role of PHABULOSA and PHAVOLUTA in determining radial patterning in shoots
    • McConnell JR, Emery J, Eshed Y, Bao N, Bowman J, et al. 2001. Role of PHABULOSA and PHAVOLUTA in determining radial patterning in shoots. Nature 411:709-13
    • (2001) Nature , vol.411 , pp. 709-713
    • McConnell, J.R.1    Emery, J.2    Eshed, Y.3    Bao, N.4    Bowman, J.5
  • 87
  • 88
    • 9044254525 scopus 로고    scopus 로고
    • P450 superfamily: Update on new sequences, gene mapping, accession numbers and nomenclature
    • Nelson DR, Koymans L, Kamataki T, Stegeman JJ, Feyereisen R, et al. 1996. P450 superfamily: update on new sequences, gene mapping, accession numbers and nomenclature. Pharmacogenetics 6:1-42
    • (1996) Pharmacogenetics , vol.6 , pp. 1-42
    • Nelson, D.R.1    Koymans, L.2    Kamataki, T.3    Stegeman, J.J.4    Feyereisen, R.5
  • 89
    • 0034672702 scopus 로고    scopus 로고
    • Sterol methyl transferase: Enzymology and inhibition
    • Nes WD. 2000. Sterol methyl transferase: enzymology and inhibition. Biochim. Biophys. Acta. 1529:63-88
    • (2000) Biochim. Biophys. Acta , vol.1529 , pp. 63-88
    • Nes, W.D.1
  • 90
    • 0041821530 scopus 로고    scopus 로고
    • Enzyme mechanism for sterol C-methylations
    • Nes WD. 2003. Enzyme mechanism for sterol C-methylations. Phytochemistry 64:75-95
    • (2003) Phytochemistry , vol.64 , pp. 75-95
    • Nes, W.D.1
  • 91
    • 0002601660 scopus 로고
    • The biochemistry of plant sterols
    • Nes WR. 1977. The biochemistry of plant sterols. Adv. Lipid Res. 15:233-324
    • (1977) Adv. Lipid Res. , vol.15 , pp. 233-324
    • Nes, W.R.1
  • 92
    • 0033963681 scopus 로고    scopus 로고
    • cDNA cloning of the mammalian sterol C5-desaturase and the expression in yeast mutant
    • Nishi S, Nishino H, Ishibashi T. 2000. cDNA cloning of the mammalian sterol C5-desaturase and the expression in yeast mutant. Biochim. Biophys. Acta. 1490:106-8
    • (2000) Biochim. Biophys. Acta , vol.1490 , pp. 106-108
    • Nishi, S.1    Nishino, H.2    Ishibashi, T.3
  • 94
    • 0025155656 scopus 로고
    • Oxidative C4-demethylation of 24-methylene cycloartanol by a cyanide-sensitive enzymatic system from higher plant microsomes
    • Pascal S, Taton M, Rahier A. 1990. Oxidative C4-demethylation of 24-methylene cycloartanol by a cyanide-sensitive enzymatic system from higher plant microsomes. Biochem. Biophys. Res. Commun. 172:98-106
    • (1990) Biochem. Biophys. Res. Commun. , vol.172 , pp. 98-106
    • Pascal, S.1    Taton, M.2    Rahier, A.3
  • 95
    • 0027323003 scopus 로고
    • Plant sterol biosynthesis: Identification and characterization of two distinct microsomal oxidative enzymatic systems involved in sterol C4-demethylation
    • Pascal S, Taton M, Rahier A. 1993. Plant sterol biosynthesis: identification and characterization of two distinct microsomal oxidative enzymatic systems involved in sterol C4-demethylation. J. Biol. Chem. 268:11639-54
    • (1993) J. Biol. Chem. , vol.268 , pp. 11639-11654
    • Pascal, S.1    Taton, M.2    Rahier, A.3
  • 96
    • 0028093435 scopus 로고
    • Plant sterol biosynthesis: Identification of a NADPH dependent plant sterone reductase involved in the sterol-4-demethylation
    • Pascal S, Taton M, Rahier A. 1994. Plant sterol biosynthesis: identification of a NADPH dependent plant sterone reductase involved in the sterol-4-demethylation. Arch. Biochem. Biophys. 312:260-71
    • (1994) Arch. Biochem. Biophys. , vol.312 , pp. 260-271
    • Pascal, S.1    Taton, M.2    Rahier, A.3
  • 97
    • 0032972399 scopus 로고    scopus 로고
    • Characterization of functional residues in the interfacial recognition domain of lecithin cholesterol acyltransferase (LCAT)
    • Peelman F, Vanloo B, Perez-Mendez O, Decout A, Verscheide JL, et al. 1999. Characterization of functional residues in the interfacial recognition domain of lecithin cholesterol acyltransferase (LCAT). Protein Engineering 12:71-78
    • (1999) Protein Engineering , vol.12 , pp. 71-78
    • Peelman, F.1    Vanloo, B.2    Perez-Mendez, O.3    Decout, A.4    Verscheide, J.L.5
  • 98
    • 0037016399 scopus 로고    scopus 로고
    • Sitosterol-β-glucoside as primer for cellulose synthesis in plants
    • Peng L, Kawagoe Y, Hogan P, Delmer D. 2002. Sitosterol-β-glucoside as primer for cellulose synthesis in plants. Science 295:147-50
    • (2002) Science , vol.295 , pp. 147-150
    • Peng, L.1    Kawagoe, Y.2    Hogan, P.3    Delmer, D.4
  • 99
    • 0035853108 scopus 로고    scopus 로고
    • Crystal structure of cytochrome P450 14α-sterol demethylase (CYP51) from Mycobacterium tuberculosis in complex with azole inhibitors
    • Podust LM, Poulos TL, Waterman MR. 2001. Crystal structure of cytochrome P450 14α-sterol demethylase (CYP51) from Mycobacterium tuberculosis in complex with azole inhibitors. Proc. Natl. Acad. Sci. USA 98:3068-73
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 3068-3073
    • Podust, L.M.1    Poulos, T.L.2    Waterman, M.R.3
  • 100
    • 0022378733 scopus 로고
    • Sterol biosynthesis de nova via cycloartenol by the soil amoeba Acanthamoeba
    • Raederstorff D, Rohmer M. 1985. Sterol biosynthesis de nova via cycloartenol by the soil amoeba Acanthamoeba. Biochem. J. 231:609-15
    • (1985) Biochem. J. , vol.231 , pp. 609-615
    • Raederstorff, D.1    Rohmer, M.2
  • 101
    • 0035830418 scopus 로고    scopus 로고
    • 7-sterol-C5(6)-desaturase
    • 7-sterol-C5(6)- desaturase. Biochemistry 40:256-67
    • (2001) Biochemistry , vol.40 , pp. 256-267
    • Rahier, A.1
  • 102
    • 0021717940 scopus 로고
    • Inhibition of (S)-adenosyl-L-methionine sterol-C-24-methyltransferase by analogues of a car-bocationic ion high energy intermediatestructure activity relationships for C-25 heteroatoms (N,As,S) substituted triterpenoid derivatives
    • Rahier A, Génot JC, Schuber F, Benveniste P, Narula AS. 1984. Inhibition of (S)-adenosyl-L-methionine sterol-C-24-methyltransferase by analogues of a car-bocationic ion high energy intermediatestructure activity relationships for C-25 heteroatoms (N,As,S) substituted triterpenoid derivatives. J. Biol. Chem. 259:15215-23
    • (1984) J. Biol. Chem. , vol.259 , pp. 15215-15223
    • Rahier, A.1    Génot, J.C.2    Schuber, F.3    Benveniste, P.4    Narula, A.S.5
  • 103
    • 0031577221 scopus 로고    scopus 로고
    • The role of cytochrome b5 in 4α-methyloxidation and C5(6)-desaturation of plant sterol precursors
    • Rahier A, Smith M, Taton M. 1997. The role of cytochrome b5 in 4α-methyloxidation and C5(6)-desaturation of plant sterol precursors. Biochem. Biophys. Res. Commun. 236:434-37
    • (1997) Biochem. Biophys. Res. Commun. , vol.236 , pp. 434-437
    • Rahier, A.1    Smith, M.2    Taton, M.3
  • 104
    • 0029939653 scopus 로고    scopus 로고
    • 7-reductase by novel 6-aza-B-homosteroids and other analogs of a presumptive carbocationic intermediate of the reduction reaction
    • 7-reductase by novel 6-aza-B-homosteroids and other analogs of a presumptive carbocationic intermediate of the reduction reaction. Biochemistry 35:7069
    • (1996) Biochemistry , vol.35 , pp. 7069
    • Rahier, A.1    Taton, M.2
  • 105
    • 0024374583 scopus 로고
    • Cycloeucalenol-obtusifoliol isomerase. Structural requirements for substrates and inhibitors binding or transformation
    • Rahier A, Taton M, Benveniste P. 1989. Cycloeucalenol-obtusifoliol isomerase. Structural requirements for substrates and inhibitors binding or transformation. Eur. J. Biochem. 181:615-26
    • (1989) Eur. J. Biochem. , vol.181 , pp. 615-626
    • Rahier, A.1    Taton, M.2    Benveniste, P.3
  • 106
    • 51249171001 scopus 로고
    • Design of high energy intermediate analogues to study sterol biosynthesis in higher plants
    • Rahier A, Taton M, Bouvier-Navé P, Schmitt P, Benveniste P, et al. 1986. Design of high energy intermediate analogues to study sterol biosynthesis in higher plants. Lipids 21:52-62
    • (1986) Lipids , vol.21 , pp. 52-62
    • Rahier, A.1    Taton, M.2    Bouvier-Navé, P.3    Schmitt, P.4    Benveniste, P.5
  • 107
    • 0015927620 scopus 로고
    • Sterols and their precursors in Astasia longa Pringsheim
    • Rohmer M, Brandt RD. 1973. Sterols and their precursors in Astasia longa Pringsheim. Eur. J. Biochem. 36:446-54
    • (1973) Eur. J. Biochem. , vol.36 , pp. 446-454
    • Rohmer, M.1    Brandt, R.D.2
  • 108
    • 0033563873 scopus 로고    scopus 로고
    • Identification, characterization, and partial purification of 4α-carboxysterol-C3-dehydrogenase/C4-decarboxylase from Zea mays
    • Rondet S, Taton M, Rahier A. 1999. Identification, characterization, and partial purification of 4α-carboxysterol-C3-dehydrogenase/C4-decarboxylase from Zea mays. Arch. Biochem. Biophys. 366:249-60
    • (1999) Arch. Biochem. Biophys. , vol.366 , pp. 249-60
    • Rondet, S.1    Taton, M.2    Rahier, A.3
  • 109
    • 0026758283 scopus 로고
    • Plant sterol biosynthesis: Novel potent and selective inhibitors of cytochrome P-450 dependent obtusifoliol 1α-methyl demethylase
    • Salmon F, Taton M, Benveniste P, Rahier A. 1992. Plant sterol biosynthesis: novel potent and selective inhibitors of cytochrome P-450 dependent obtusifoliol 1α-methyl demethylase. Arch. Biochem. Biophys. 297:123-31
    • (1992) Arch. Biochem. Biophys. , vol.297 , pp. 123-131
    • Salmon, F.1    Taton, M.2    Benveniste, P.3    Rahier, A.4
  • 110
    • 0034077650 scopus 로고    scopus 로고
    • Plant sterol-C24-methyl transferases: Different profiles of tobacco transformed with SMT1 or SMT2
    • Schaeffer A, Bouvier-Navé P, Benveniste P, Schaller H. 2000. Plant sterol-C24-methyl transferases: different profiles of tobacco transformed with SMT1 or SMT2. Lipids 35:263-69
    • (2000) Lipids , vol.35 , pp. 263-269
    • Schaeffer, A.1    Bouvier-Navé, P.2    Benveniste, P.3    Schaller, H.4
  • 111
    • 0035049995 scopus 로고    scopus 로고
    • The ratio of campesterol to sitosterol which modulates growth in Arabidopsis is controlled by Sterol Methyltransferase 2-1
    • Schaeffer A, Bronner R, Benveniste P, Schaller H. 2001. The ratio of campesterol to sitosterol which modulates growth in Arabidopsis is controlled by STEROL METHYLTRANSFERASE 2-1. Plant J. 25:605-15
    • (2001) Plant J. , vol.25 , pp. 605-615
    • Schaeffer, A.1    Bronner, R.2    Benveniste, P.3    Schaller, H.4
  • 112
    • 0037402336 scopus 로고    scopus 로고
    • The role of sterol in plant growth and development
    • Schaller H. 2003. The role of sterol in plant growth and development. Progr. Lipid Res. 422:163-75
    • (2003) Progr. Lipid Res. , vol.422 , pp. 163-175
    • Schaller, H.1
  • 113
    • 0032188021 scopus 로고    scopus 로고
    • 1-methyltransferase in Nicotiana tabacum L. modifies the ratio of 24-methyl cholesterol to sitosterol and is associated with growth reduction
    • 1-methyltransferase in Nicotiana tabacum L. modifies the ratio of 24-methyl cholesterol to sitosterol and is associated with growth reduction. Plant Physiol. 118:461-69
    • (1998) Plant Physiol. , vol.118 , pp. 461-469
    • Schaller, H.1    Bouvier-Navé, P.2    Benveniste, P.3
  • 114
    • 0028119083 scopus 로고
    • Sterol overproduction is the biochemical basis of resistance to a triazole in calli from a tobacco mutant
    • Schaller H, Gondet L, Maillot-Vernier P, Benveniste P. 1994. Sterol overproduction is the biochemical basis of resistance to a triazole in calli from a tobacco mutant. Planta 194:295-305
    • (1994) Planta , vol.194 , pp. 295-305
    • Schaller, H.1    Gondet, L.2    Maillot-Vernier, P.3    Benveniste, P.4
  • 116
    • 0034659406 scopus 로고    scopus 로고
    • FACKEL is a sterol C-14 reductase required for organized cell division and expansion in Arabidopsis embryogenesis
    • Schrick K, Mayer U, Horrichs A, Kuhnt C, Bellini C, et al. 2000. FACKEL is a sterol C-14 reductase required for organized cell division and expansion in Arabidopsis embryogenesis. Genes Dev. 14:1471-84
    • (2000) Genes Dev. , vol.14 , pp. 1471-1484
    • Schrick, K.1    Mayer, U.2    Horrichs, A.3    Kuhnt, C.4    Bellini, C.5
  • 117
    • 0035984148 scopus 로고    scopus 로고
    • Interactions between sterol biosynthesis genes in embryonic development of Arabidopsis
    • Schrick K, Mayer U, Martin G, Bellini C, Kuhnt C, et al. 2002. Interactions between sterol biosynthesis genes in embryonic development of Arabidopsis. Plant J. 31:61-73
    • (2002) Plant J. , vol.31 , pp. 61-73
    • Schrick, K.1    Mayer, U.2    Martin, G.3    Bellini, C.4    Kuhnt, C.5
  • 118
    • 0025835715 scopus 로고
    • Differential effects of plant sterols on water permeability and on acyl chain ordering of soybean phosphatidylcholine bilayers
    • Schuler I, Milon A, Nakatani Y, Ourisson G, Albrecht AM, et al. 1991. Differential effects of plant sterols on water permeability and on acyl chain ordering of soybean phosphatidylcholine bilayers. Proc. Natl. Acad. Sci. USA 88:6926-30
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 6926-6930
    • Schuler, I.1    Milon, A.2    Nakatani, Y.3    Ourisson, G.4    Albrecht, A.M.5
  • 119
    • 0037069721 scopus 로고    scopus 로고
    • Directed evolution experiments reveal mutations at cycloartenol synthase residue His477 that dramatically alter catalysis
    • Segura MJR, Lodeiro S, Meyer MM, Patel AJ, Matsuda SPT. 2002. Directed evolution experiments reveal mutations at cycloartenol synthase residue His477 that dramatically alter catalysis. Org. Lett. 4:4459-62
    • (2002) Org. Lett. , vol.4 , pp. 4459-4462
    • Segura, M.J.R.1    Lodeiro, S.2    Meyer, M.M.3    Patel, A.J.4    Matsuda, S.P.T.5
  • 120
    • 0028089687 scopus 로고
    • Eight histidine residues are catalytically essential in a membrane-associated iron enzyme stearoyl-CoA desaturase, and are conserved in alkane hydroxylase and xylene monooxygenase
    • Shanklin J, Whittle E, Fox BG. 1994. Eight histidine residues are catalytically essential in a membrane-associated iron enzyme stearoyl-CoA desaturase, and are conserved in alkane hydroxylase and xylene monooxygenase. Biochemistry 33:12787-94
    • (1994) Biochemistry , vol.33 , pp. 12787-12794
    • Shanklin, J.1    Whittle, E.2    Fox, B.G.3
  • 121
    • 0029079397 scopus 로고
    • Identification of cDNA clones encoding valosin-containing protein and other plant plasma membrane-associated proteins by a general immunoscreening strategy
    • Shi J, Dixon RA, Gonzales RA, Kjellborn P, Bhattacharyya MK. 1995. Identification of cDNA clones encoding valosin-containing protein and other plant plasma membrane-associated proteins by a general immunoscreening strategy. Proc. Natl. Acad. Sci. USA 92:4457-61
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4457-4461
    • Shi, J.1    Dixon, R.A.2    Gonzales, R.A.3    Kjellborn, P.4    Bhattacharyya, M.K.5
  • 122
    • 0029919176 scopus 로고    scopus 로고
    • Identification and characterization of an S-adenosyl-L-methionine: Δ24-sterol-C-methyltransferase cDNA from soybean
    • Shi J, Gonzales RA, Bhattacharyya MK. 1996. Identification and characterization of an S-adenosyl-L-methionine: Δ24-sterol-C- methyltransferase cDNA from soybean. J. Biol. Chem. 271:9384-89
    • (1996) J. Biol. Chem. , vol.271 , pp. 9384-9389
    • Shi, J.1    Gonzales, R.A.2    Bhattacharyya, M.K.3
  • 123
    • 0028283156 scopus 로고
    • Isolation and characterization of the gene encoding 2.3-oxidosqualene- lanosterol cyclase from Saccharomyces cerevisiae
    • Shi Z, Buntel CJ, Griffin JH. 1994. Isolation and characterization of the gene encoding 2.3-oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 91:7370-24
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7370-7424
    • Shi, Z.1    Buntel, C.J.2    Griffin, J.H.3
  • 124
    • 0031838013 scopus 로고    scopus 로고
    • Human lamin B receptor exhibits sterol C14-reductase activity in Saccharomyces cerevisiae
    • Silve S, Dupuy PH, Ferrara P, Loison G. 1998. Human lamin B receptor exhibits sterol C14-reductase activity in Saccharomyces cerevisiae. Biochim. Biophys. Acta. 1392:233-44
    • (1998) Biochim. Biophys. Acta , vol.1392 , pp. 233-244
    • Silve, S.1    Dupuy, P.H.2    Ferrara, P.3    Loison, G.4
  • 126
    • 0036016435 scopus 로고    scopus 로고
    • Hydra mutants of Arabidopsis are defective in sterol profiles and auxin and ethylene signaling
    • Souter M, Topping J, Pullen M, Friml J, Palme K, et al. 2002. Hydra mutants of Arabidopsis are defective in sterol profiles and auxin and ethylene signaling. Plant Cell. 14:1017-31
    • (2002) Plant Cell. , vol.14 , pp. 1017-1031
    • Souter, M.1    Topping, J.2    Pullen, M.3    Friml, J.4    Palme, K.5
  • 127
    • 0028906888 scopus 로고
    • Sterol metabolism in the tobacco hornworm, Manduca sexta
    • Svoboda JA, Weirich GF. 1995. Sterol metabolism in the tobacco hornworm, Manduca sexta. Lipids. 30:263-67
    • (1995) Lipids , vol.30 , pp. 263-267
    • Svoboda, J.A.1    Weirich, G.F.2
  • 128
    • 0040845545 scopus 로고
    • Comparative study of the inhibition of sterol biosynthesis in Rubus fruticosus suspension cultures and Zea mays seedlings by N-(1,5,9- trimethyldecyl)-4α, 10-dimethyl-8-aza-trans-decal-3 β-ol and derivatives
    • Taton M, Benveniste P, Rahier A. 1987. Comparative study of the inhibition of sterol biosynthesis in Rubus fruticosus suspension cultures and Zea mays seedlings by (N-(1,5,9-trimethyldecyl)-4α, 10-dimethyl-8-aza- trans-decal-3 β-ol and derivatives. Phytochemistry 26:385-92
    • (1987) Phytochemistry , vol.26 , pp. 385-392
    • Taton, M.1    Benveniste, P.2    Rahier, A.3
  • 129
    • 0024388295 scopus 로고
    • 14-reductase in higher plants. Characterization and inhibition by analogues of a presumptive carbocationic intermediate of the reduction reaction
    • 14-reductase in higher plants. Characterization and inhibition by analogues of a presumptive carbocationic intermediate of the reduction reaction. Eur. J. Biochem. 185:605-14
    • (1989) Eur. J. Biochem. , vol.185 , pp. 605-614
    • Taton, M.1    Benveniste, P.2    Rahier, A.3
  • 131
    • 0025816145 scopus 로고
    • Properties and structural requirements for substrate specificity of cytochrome P450-dependent obtusifoliol 14α-demethylase from maize (Zea mays) seedlings
    • Taton M, Rahier A. 1991. Properties and structural requirements for substrate specificity of cytochrome P450-dependent obtusifoliol 14α-demethylase from maize (Zea mays) seedlings. Biochem. J. 277:483
    • (1991) Biochem. J. , vol.277 , pp. 483
    • Taton, M.1    Rahier, A.2
  • 132
    • 0030068701 scopus 로고    scopus 로고
    • Plant sterol biosynthesis: Identification and characterization of higher plant Δ7-sterol-C5(6)-desaturase
    • Taton M, Rahier A. 1996. Plant sterol biosynthesis: identification and characterization of higher plant Δ7-sterol-C5(6)-desaturase. Arch. Biochem. Biophys. 325:279-88
    • (1996) Arch. Biochem. Biophys. , vol.325 , pp. 279-288
    • Taton, M.1    Rahier, A.2
  • 133
    • 0027366574 scopus 로고
    • UDP-glucose sterol-β-D-glucosyltransferase, a plasma membrane-bound enzyme of plants: Enzymatic, properties and lipid dependence
    • Ullmann P, Ury A, Rimmele D, Benveniste P, Bouvier-Navé P. 1993. UDP-glucose sterol-β-D-glucosyltransferase, a plasma membrane-bound enzyme of plants: enzymatic, properties and lipid dependence. Biochimie 75:713-23
    • (1993) Biochimie , vol.75 , pp. 713-723
    • Ullmann, P.1    Ury, A.2    Rimmele, D.3    Benveniste, P.4    Bouvier-Navé, P.5
  • 134
    • 3242664614 scopus 로고
    • Target sites of sterol biosynthesis inhibitors: Secondary activities on cytochrome P-450-dependent reactions
    • ed. W Köllers, London: CRC Press
    • Vanden Bossche H, Janssen PAJ. 1992. Target sites of sterol biosynthesis inhibitors: secondary activities on cytochrome P-450-dependent reactions. In Target Sites of Fungicide Action, ed. W Köllers, pp. 227-54. London: CRC Press
    • (1992) Target Sites of Fungicide Action , pp. 227-254
    • Vanden Bossche, H.1    Janssen, P.A.J.2
  • 135
    • 0029975946 scopus 로고    scopus 로고
    • Sterol specificity of the Saccharomyces cerevisiae ERG6 gene product expressed in Escherichia coli
    • Venkatramesh M, Guo DA, Harman JG, Nes WD. 1996. Sterol specificity of the Saccharomyces cerevisiae ERG6 gene product expressed in Escherichia coli. Lipids 31:373-77
    • (1996) Lipids , vol.31 , pp. 373-377
    • Venkatramesh, M.1    Guo, D.A.2    Harman, J.G.3    Nes, W.D.4
  • 136
    • 0033532058 scopus 로고    scopus 로고
    • Cloning and functional expression of UGT genes encoding sterol glucosyl-transferases from Saccharomyces cerevisiae, Candida albicans, Pichia pastoris and Dictyostellum discoideum
    • Warnecke D, Erdmann R, Fahl A, Hube B, Müller F, et al. 1999. Cloning and functional expression of UGT genes encoding sterol glucosyl-transferases from Saccharomyces cerevisiae, Candida albicans, Pichia pastoris and Dictyostellum discoideum. J. Biol. Chem. 274:13048-59
    • (1999) J. Biol. Chem. , vol.274 , pp. 13048-13059
    • Warnecke, D.1    Erdmann, R.2    Fahl, A.3    Hube, B.4    Müller, F.5
  • 137
    • 0031282642 scopus 로고    scopus 로고
    • UDP-glucose sterol glucosyltransferase: Cloning and functional expression in Escherichia coli
    • Warnecke DC, Baltrusch M, Buck F, Wolter FP, Heinz E. 1997. UDP-glucose sterol glucosyltransferase: cloning and functional expression in Escherichia coli. Plant Mol. Biol. 35:597-603
    • (1997) Plant Mol. Biol. , vol.35 , pp. 597-603
    • Warnecke, D.C.1    Baltrusch, M.2    Buck, F.3    Wolter, F.P.4    Heinz, E.5
  • 138
    • 0028849110 scopus 로고
    • Effects of plant sterols on the hydration and phase behavior of DOPE/DOPC mixtures
    • Webb MS, Irving TC, Steponkus PL. 1995. Effects of plant sterols on the hydration and phase behavior of DOPE/DOPC mixtures. Biochim. Biophys. Acta. 1239:226-38
    • (1995) Biochim. Biophys. Acta , vol.1239 , pp. 226-238
    • Webb, M.S.1    Irving, T.C.2    Steponkus, P.L.3
  • 139
    • 0030769202 scopus 로고    scopus 로고
    • Structure and function of a squalene cyclase
    • Wendt KU, Poralla K, Schulz GE. 1997. Structure and function of a squalene cyclase. Science 277:1811-14
    • (1997) Science , vol.277 , pp. 1811-1814
    • Wendt, K.U.1    Poralla, K.2    Schulz, G.E.3
  • 140
    • 0015911544 scopus 로고
    • S-adenosyl-L-methionine-cycloartenol methyltransferase activity in cell-free systems from Trebouxia sp. and Scenedesmus obliquus
    • Wojciechoswki ZA, Goad LJ, Goodwin TW. 1973. S-adenosyl-L-methionine- cycloartenol methyltransferase activity in cell-free systems from Trebouxia sp. and Scenedesmus obliquus. Biochem. J. 136:405-12
    • (1973) Biochem. J. , vol.136 , pp. 405-412
    • Wojciechoswki, Z.A.1    Goad, L.J.2    Goodwin, T.W.3
  • 141
    • 0002965819 scopus 로고
    • Biochemistry of phytosterol conjugates
    • American Oil Chemists' Society, ed. GW Patterson, WD Nes, Champaign: American Oil Chemist's Society
    • Wojciechowski ZA. 1991. Biochemistry of phytosterol conjugates, In Physiology and Biochemistry of Sterols. American Oil Chemists' Society, ed. GW Patterson, WD Nes, pp. 361-95. Champaign: American Oil Chemist's Society
    • (1991) Physiology and Biochemistry of Sterols , pp. 361-395
    • Wojciechowski, Z.A.1
  • 142
    • 0033019671 scopus 로고    scopus 로고
    • Steryl esters in the elaioplasts of the tapetum in developing Brassica anthers and their recovery on the pollen surface
    • Wu SSH, Moreau RA, Whitaker BD, Huang AHC. 1999. Steryl esters in the elaioplasts of the tapetum in developing Brassica anthers and their recovery on the pollen surface. Lipids 34:517-23
    • (1999) Lipids , vol.34 , pp. 517-523
    • Wu, S.S.H.1    Moreau, R.A.2    Whitaker, B.D.3    Huang, A.H.C.4
  • 143
    • 0018416992 scopus 로고
    • 7-sterol isomerization and methyl transfer of sterols in ergosterol biosynthesis of yeast
    • 7-sterol isomerization and methyl transfer of sterols in ergosterol biosynthesis of yeast. J. Biochem. 85:1531-44
    • (1979) J. Biochem. , vol.85 , pp. 1531-1544
    • Yabuzaki, Y.1    Niohino, T.2    Ariga, N.3    Katsuki, H.4
  • 144
    • 0018096668 scopus 로고
    • Characterization of the microsomal steroid-8-en isomerase of cholesterol biosynthesis
    • Yamaga N, Gaylor JL. 1978. Characterization of the microsomal steroid-8-en isomerase of cholesterol biosynthesis. J. Lipid Res. 19:375-82
    • (1978) J. Lipid Res. , vol.19 , pp. 375-382
    • Yamaga, N.1    Gaylor, J.L.2
  • 146
    • 0037492686 scopus 로고
    • Partial purification and specificity of triacylglycerol sterol acyltransferase from Sinapsis alba
    • Zimowski J, Wojciechowski ZA. 1981. Partial purification and specificity of triacylglycerol sterol acyltransferase from Sinapsis alba. Phytochemistry 20:1799-803
    • (1981) Phytochemistry , vol.20 , pp. 1799-1803
    • Zimowski, J.1    Wojciechowski, Z.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.