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1
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0742307297
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On the origins of triterpenoid skeletal diversity
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This review categorizes nearly 200 triterpene skeletons identified from natural sources and provides the mechanisms by which they could be formed.
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Xu R., Fazio G.C., and Matsuda S.P.T. On the origins of triterpenoid skeletal diversity. Phytochemistry 65 (2004) 261-291. This review categorizes nearly 200 triterpene skeletons identified from natural sources and provides the mechanisms by which they could be formed.
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Phytochemistry
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Xu, R.1
Fazio, G.C.2
Matsuda, S.P.T.3
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0035111648
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Molecular cloning and expression in yeast of 2,3-oxidosqualene-triterpenoid cyclases from Arabidopsis thaliana
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Husselstein-Muller T., Schaller H., and Benveniste P. Molecular cloning and expression in yeast of 2,3-oxidosqualene-triterpenoid cyclases from Arabidopsis thaliana. Plant Mol Biol 45 (2001) 75-92
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Husselstein-Muller, T.1
Schaller, H.2
Benveniste, P.3
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3
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22144482368
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Structure and reactivity of the dammarenyl cation: configurational transmission in triterpene synthesis
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By studying the structure and reactivity of the dammarenyl cation, the authors grouped cyclases according to mechanistic and taxonomic criteria and determined which mechanistic changes were evolutionarily rare and which evolved readily.
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Xiong Q., Rocco F., Wilson W.K., Xu R., Ceruti M., and Matsuda S.P.T. Structure and reactivity of the dammarenyl cation: configurational transmission in triterpene synthesis. J Org Chem 70 (2005) 5362-5375. By studying the structure and reactivity of the dammarenyl cation, the authors grouped cyclases according to mechanistic and taxonomic criteria and determined which mechanistic changes were evolutionarily rare and which evolved readily.
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J Org Chem
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Xiong, Q.1
Rocco, F.2
Wilson, W.K.3
Xu, R.4
Ceruti, M.5
Matsuda, S.P.T.6
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4
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0027146637
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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
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Corey E.J., Matsuda S.P.T., and Bartel B. 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 (1993) 11628-11632
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Proc Natl Acad Sci USA
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Corey, E.J.1
Matsuda, S.P.T.2
Bartel, B.3
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5
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0002657871
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La biosynthèse des stérols dans les tissus de tabac cultivés in vitro - II. Particularités de la biosynthèse des phytostérols des tissus de tabac cultivés in vitro
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[Title translation: The biosynthesis of sterols in tobacco tissue cultivated in vitro - II. Characteristics of the biosynthesis of phytosterols in tobacco tissue cultured in vitro]
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Benveniste P., Hirth L., and Ourisson G. La biosynthèse des stérols dans les tissus de tabac cultivés in vitro - II. Particularités de la biosynthèse des phytostérols des tissus de tabac cultivés in vitro. Phytochemistry 5 (1966) 45-58 [Title translation: The biosynthesis of sterols in tobacco tissue cultivated in vitro - II. Characteristics of the biosynthesis of phytosterols in tobacco tissue cultured in vitro]
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Phytochemistry
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Benveniste, P.1
Hirth, L.2
Ourisson, G.3
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6
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0037703414
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Études sur les triterpènes précurseurs des phytostérols. Recherche du cycloarténol et du lanostérol dans diverses espèces végétales
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[Title translation: Studies on the triterpene precursors of the phytosterols. Research on cycloartenol and lanosterol in various plants.]
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Ehrhardt J.D., Hirth L., and Ourisson G. Études sur les triterpènes précurseurs des phytostérols. Recherche du cycloarténol et du lanostérol dans diverses espèces végétales. Phytochemistry 6 (1967) 815-821 [Title translation: Studies on the triterpene precursors of the phytosterols. Research on cycloartenol and lanosterol in various plants.]
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Phytochemistry
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Ehrhardt, J.D.1
Hirth, L.2
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7
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Phytosterol biosynthesis: the sterols of Latrix decidua leaves
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Goad L.J., and Goodwin T.W. Phytosterol biosynthesis: the sterols of Latrix decidua leaves. Eur J Biochem 1 (1967) 357-362
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Goad, L.J.1
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8
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0038717630
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Cloning and characterization of the Dictyostelium discoideum cycloartenol synthase cDNA
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Godzina S.M., Lovato M.A., Meyer M.M., Foster K.A., Wilson W.K., Gu W., de Hostos E.L., and Matsuda S.P.T. Cloning and characterization of the Dictyostelium discoideum cycloartenol synthase cDNA. Lipids 35 (2000) 249-255
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Godzina, S.M.1
Lovato, M.A.2
Meyer, M.M.3
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Wilson, W.K.5
Gu, W.6
de Hostos, E.L.7
Matsuda, S.P.T.8
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9
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0037238414
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Steroid biosynthesis in prokaryotes: identification of myxobacterial steroids and cloning of the first bacterial 2,3(S)-oxidosqualene cyclase from the myxobacterium Stigmatella aurantiaca
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Bode H.B., Zeggel B., Silakowski B., Wenzel S.C., Reichenbach H., and Muller R. Steroid biosynthesis in prokaryotes: identification of myxobacterial steroids and cloning of the first bacterial 2,3(S)-oxidosqualene cyclase from the myxobacterium Stigmatella aurantiaca. Mol Microbiol 47 (2003) 471-481
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Mol Microbiol
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Bode, H.B.1
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Muller, R.6
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0015239686
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Concerning the role of lanosterol and cycloartenol in steroid biosynthesis
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0033997360
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Giner J.L., Berkowitz J.D., and Andersson T. Nonpolar components of the latex of Euphorbia peplus. J Nat Prod 63 (2000) 267-269
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Berkowitz, J.D.2
Andersson, T.3
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12
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33644621499
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This paper presents the first cloned and characterized lanosterol synthase from plants. The authors also identify, using similarity and active-site residue conservation, other potential plant lanosterol synthases.
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Kolesnikova M.D., Xiong Q., Lodeiro S., Hua L., and Matsuda S.P.T. Lanosterol biosynthesis in plants. Arch Biochem Biophys 447 (2006) 87-95. This paper presents the first cloned and characterized lanosterol synthase from plants. The authors also identify, using similarity and active-site residue conservation, other potential plant lanosterol synthases.
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Arch Biochem Biophys
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Kolesnikova, M.D.1
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Lodeiro, S.3
Hua, L.4
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13
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0033610475
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Directed evolution to investigate steric control of enzymatic oxidosqualene cyclization. An isoleucine to valine mutation in cycloartenol synthase allows lanosterol and parkeol biosynthesis
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Hart E.A., Hua L., Darr L.B., Wilson W.K., Pang J., and Matsuda S.P.T. Directed evolution to investigate steric control of enzymatic oxidosqualene cyclization. An isoleucine to valine mutation in cycloartenol synthase allows lanosterol and parkeol biosynthesis. J Am Chem Soc 121 (1999) 9887-9888
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Hart, E.A.1
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14
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0034686761
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A tyrosine to threonine mutation converts cycloartenol synthase to an oxidosqualene cyclase that forms lanosterol as its major product
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Herrera J.B.R., Wilson W.K., and Matsuda S.P.T. A tyrosine to threonine mutation converts cycloartenol synthase to an oxidosqualene cyclase that forms lanosterol as its major product. J Am Chem Soc 122 (2000) 6765-6766
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Herrera, J.B.R.1
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15
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8844253028
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Oxidosqualene cyclase second-sphere residues profoundly influence the product profile
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Lodeiro S., Segura M.J., Stahl M., Schulz-Gasch T., and Matsuda S.P.T. Oxidosqualene cyclase second-sphere residues profoundly influence the product profile. ChemBioChem 5 (2004) 1581-1585
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Lodeiro, S.1
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16
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26844446540
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Enzyme redesign: two mutations cooperate to convert cycloartenol synthase into an accurate lanosterol synthase
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This paper identifies two pivotal mutational changes (H477N and I481V) that are sufficient to convert an accurate cycloartenol synthase into an accurate lanosterol synthase.
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Lodeiro S., Schulz-Gasch T., and Matsuda S.P.T. Enzyme redesign: two mutations cooperate to convert cycloartenol synthase into an accurate lanosterol synthase. J Am Chem Soc 127 (2005) 14132-14133. This paper identifies two pivotal mutational changes (H477N and I481V) that are sufficient to convert an accurate cycloartenol synthase into an accurate lanosterol synthase.
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J Am Chem Soc
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Lodeiro, S.1
Schulz-Gasch, T.2
Matsuda, S.P.T.3
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17
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3242741346
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Cucurbitadienol synthase, the first committed enzyme for cucurbitacin biosynthesis, is a distinct enzyme from cycloartenol synthase for phytosterol biosynthesis
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This paper describes the cloning and characterization of cucurbitadienol synthase, the first characterized plant enzyme that uses the protosteryl intermediate to make triterpene precursors of secondary metabolites.
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Shibuya M., Adachi S., and Ebizuka Y. Cucurbitadienol synthase, the first committed enzyme for cucurbitacin biosynthesis, is a distinct enzyme from cycloartenol synthase for phytosterol biosynthesis. Tetrahedron 60 (2004) 6995-7003. This paper describes the cloning and characterization of cucurbitadienol synthase, the first characterized plant enzyme that uses the protosteryl intermediate to make triterpene precursors of secondary metabolites.
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Tetrahedron
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Shibuya, M.1
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Chen J.C., Chiu M.H., Nie R.L., Cordell G.A., and Qiu S.X. Cucurbitacins and cucurbitane glycosides: structures and biological activities. Nat Prod Rep 22 (2005) 386-399
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Chen, J.C.1
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19
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0035818591
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Haralampidis K., Bryan G., Qi X., Papadopoulou K., Bakht S., Melton R., and Osbourn A. A new class of oxidosqualene cyclases directs synthesis of antimicrobial phytoprotectants in monocots. Proc Natl Acad Sci USA 98 (2001) 13431-13436
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2542634233
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A gene cluster for secondary metabolism in oat: implications for the evolution of metabolic diversity in plants
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The authors identify a functional gene cluster in a chromosomal region that is unique to Avena that encodes four distinct steps in avenacin biosynthesis. This is only the second example in plants of a gene cluster that encodes enzymes acting in a single secondary metabolic pathway.
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Qi X., Bakht S., Leggett M., Maxwell C., Melton R., and Osbourn A. A gene cluster for secondary metabolism in oat: implications for the evolution of metabolic diversity in plants. Proc Natl Acad Sci USA 101 (2004) 8233-8238. The authors identify a functional gene cluster in a chromosomal region that is unique to Avena that encodes four distinct steps in avenacin biosynthesis. This is only the second example in plants of a gene cluster that encodes enzymes acting in a single secondary metabolic pathway.
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Proc Natl Acad Sci USA
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Qi, X.1
Bakht, S.2
Leggett, M.3
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Osbourn, A.6
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22
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The authors quantify 31 different saponins in five Medicago truncatula tissues. Through this analysis, the authors observe the differential accumulation of triterpene saponins in various organs, implying that these saponins have tissue-specific biosynthesis and functions.
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Huhman D.V., Berhow M.A., and Sumner L.W. Quantification of saponins in aerial and subterranean tissues of Medicago truncatula. J Agric Food Chem 53 (2005) 1914-1920. The authors quantify 31 different saponins in five Medicago truncatula tissues. Through this analysis, the authors observe the differential accumulation of triterpene saponins in various organs, implying that these saponins have tissue-specific biosynthesis and functions.
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A genomics approach to the early stages of triterpene saponin biosynthesis in Medicago truncatula
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Suzuki H., Achnine L., Xu R., Matsuda S.P.T., and Dixon R.A. A genomics approach to the early stages of triterpene saponin biosynthesis in Medicago truncatula. Plant J 32 (2002) 1033-1048
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Suzuki, H.1
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24
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Molecular cloning and characterization of triterpene synthases from Medicago truncatula and Lotus japonicus
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Iturbe-Ormaetxe I., Haralampidis K., Papadopoulou K., and Osbourn A.E. Molecular cloning and characterization of triterpene synthases from Medicago truncatula and Lotus japonicus. Plant Mol Biol 51 (2003) 731-743
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Cloning of a cDNA probably encoding oxidosqualene cyclase associated with asiaticoside biosynthesis from Centella asiatica (L.) Urban
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Kim O.T., Kim M.Y., Huh S.M., Bai D.G., Ahn J.C., and Hwang B. Cloning of a cDNA probably encoding oxidosqualene cyclase associated with asiaticoside biosynthesis from Centella asiatica (L.) Urban. Plant Cell Rep 24 (2005) 304-311
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The authors compare mRNA levels of cycloartenol, lupeol, and β-amyrin synthases through seasonal variations, in different tissue types, with and without MeJA treatment, and during germination. Additionally, they follow the accumulation of lupeol and β-amyrin derivatives (i.e. betulinic acid and oleanane-type triterpene saponins) in some of these conditions.
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Hayashi H., Huang P., Takada S., Obinata M., Inoue K., Shibuya M., and Ebizuka Y. Differential expression of three oxidosqualene cyclase mRNAs in Glycyrrhiza glabra. Biol Pharm Bull 27 (2004) 1086-1092. The authors compare mRNA levels of cycloartenol, lupeol, and β-amyrin synthases through seasonal variations, in different tissue types, with and without MeJA treatment, and during germination. Additionally, they follow the accumulation of lupeol and β-amyrin derivatives (i.e. betulinic acid and oleanane-type triterpene saponins) in some of these conditions.
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