메뉴 건너뛰기




Volumn 26, Issue 3, 2014, Pages 894-914

Complete proteomic-based enzyme reaction and inhibition kinetics reveal how monolignol biosynthetic enzyme families affect metabolic flux and lignin in Populus trichocarpa

Author keywords

[No Author keywords available]

Indexed keywords

LIGNIN; PROTEOME; VEGETABLE PROTEIN;

EID: 84899150986     PISSN: 10404651     EISSN: 1532298X     Source Type: Journal    
DOI: 10.1105/tpc.113.120881     Document Type: Article
Times cited : (138)

References (96)
  • 1
    • 0041886402 scopus 로고    scopus 로고
    • Efficiency of lignin biosynthesis: A quantitative analysis
    • Amthor, J.S.B. (2003). Efficiency of lignin biosynthesis: A quantitative analysis. Ann. Bot. (Lond.) 91: 673-695.
    • (2003) Ann. Bot. (Lond.) , vol.91 , pp. 673-695
    • Amthor, J.S.B.1
  • 2
    • 0028018107 scopus 로고
    • Quantitative relationship between phenylalanine ammonia-lyase levels and phenylpropanoid accumulation in transgenic tobacco identifies a rate-determining step in natural product synthesis
    • Bate, N.J., Orr, J., Ni, W., Meromi, A., Nadler-Hassar, T., Doerner, P.W., Dixon, R.A., Lamb, C.J., and Elkind, Y. (1994). Quantitative relationship between phenylalanine ammonia-lyase levels and phenylpropanoid accumulation in transgenic tobacco identifies a rate-determining step in natural product synthesis. Proc. Natl. Acad. Sci. USA 91: 7608-7612.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7608-7612
    • Bate, N.J.1    Orr, J.2    Ni, W.3    Meromi, A.4    Nadler-Hassar, T.5    Doerner, P.W.6    Dixon, R.A.7    Lamb, C.J.8    Elkind, Y.9
  • 3
    • 77956536493 scopus 로고    scopus 로고
    • Ultrastructure and mechanical properties of populus wood with reduced lignin content caused by transgenic down-regulation of cinnamate 4-hydroxylase
    • Bjurhager, I., Olsson, A.M., Zhang, B., Gerber, L., Kumar, M., Berglund, L.A., Burgert, I., Sundberg, B., and Salmén, L. (2010). Ultrastructure and mechanical properties of populus wood with reduced lignin content caused by transgenic down-regulation of cinnamate 4-hydroxylase. Biomacromolecules 11: 2359-2365.
    • (2010) Biomacromolecules , vol.11 , pp. 2359-2365
    • Bjurhager, I.1    Olsson, A.M.2    Zhang, B.3    Gerber, L.4    Kumar, M.5    Berglund, L.A.6    Burgert, I.7    Sundberg, B.8    Salmén, L.9
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0038142482 scopus 로고
    • Chemistry of lignification: Biochemical research on lignins is yielding clues to the structure and formation of these complex polymers
    • Brown, S.A. (1961). Chemistry of lignification: Biochemical research on lignins is yielding clues to the structure and formation of these complex polymers. Science 134: 305-313.
    • (1961) Science , vol.134 , pp. 305-313
    • Brown, S.A.1
  • 8
    • 0035170102 scopus 로고    scopus 로고
    • Strong decrease in lignin content without significant alteration of plant development is induced by simultaneous down-regulation of cinnamoyl CoA reductase (CCR) and cinnamyl alcohol dehydrogenase (CAD) in tobacco plants
    • Chabannes, M., Barakate, A., Lapierre, C., Marita, J.M., Ralph, J., Pean, M., Danoun, S., Halpin, C., Grima-Pettenati, J., and Boudet, A.M. (2001). Strong decrease in lignin content without significant alteration of plant development is induced by simultaneous down-regulation of cinnamoyl CoA reductase (CCR) and cinnamyl alcohol dehydrogenase (CAD) in tobacco plants. Plant J. 28: 257-270.
    • (2001) Plant J. , vol.28 , pp. 257-270
    • Chabannes, M.1    Barakate, A.2    Lapierre, C.3    Marita, J.M.4    Ralph, J.5    Pean, M.6    Danoun, S.7    Halpin, C.8    Grima-Pettenati, J.9    Boudet, A.M.10
  • 9
    • 84874626790 scopus 로고    scopus 로고
    • Monolignol pathway 4-coumaric acid: Coenzyme A ligases in Populus trichocarpa: Novel specificity, metabolic regulation, and simulation of coenzyme A ligation fluxes
    • Chen, H.C., et al. (2013). Monolignol pathway 4-coumaric acid: coenzyme A ligases in Populus trichocarpa: Novel specificity, metabolic regulation, and simulation of coenzyme A ligation fluxes. Plant Physiol. 161: 1501-1516.
    • (2013) Plant Physiol. , vol.161 , pp. 1501-1516
    • Chen, H.C.1
  • 10
    • 84862908469 scopus 로고    scopus 로고
    • Membrane protein complexes catalyze both 4-and 3-hydroxylation of cinnamic acid derivatives in monolignol biosynthesis
    • Chen, H.C., Li, Q., Shuford, C.M., Liu, J., Muddiman, D.C., Sederoff, R.R., and Chiang, V.L. (2011). Membrane protein complexes catalyze both 4-and 3-hydroxylation of cinnamic acid derivatives in monolignol biosynthesis. Proc. Natl. Acad. Sci. USA 108: 21253-21258.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 21253-21258
    • Chen, H.C.1    Li, Q.2    Shuford, C.M.3    Liu, J.4    Muddiman, D.C.5    Sederoff, R.R.6    Chiang, V.L.7
  • 11
    • 34447319626 scopus 로고    scopus 로고
    • Lignin modification improves fermentable sugar yields for biofuel production
    • Chen, F., and Dixon, R.A. (2007). Lignin modification improves fermentable sugar yields for biofuel production. Nat. Biotechnol. 25: 759-761.
    • (2007) Nat. Biotechnol. , vol.25 , pp. 759-761
    • Chen, F.1    Dixon, R.A.2
  • 12
    • 84859344704 scopus 로고    scopus 로고
    • Insights into metabolic efficiency from flux analysis
    • Chen, X., and Shachar-Hill, Y. (2012). Insights into metabolic efficiency from flux analysis. J. Exp. Bot. 63: 2343-2351.
    • (2012) J. Exp. Bot. , vol.63 , pp. 2343-2351
    • Chen, X.1    Shachar-Hill, Y.2
  • 13
    • 0035984698 scopus 로고    scopus 로고
    • From rags to riches
    • Chiang, V.L. (2002). From rags to riches. Nat. Biotechnol. 20: 557-558.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 557-558
    • Chiang, V.L.1
  • 14
    • 41949114062 scopus 로고    scopus 로고
    • RNAi-mediated suppression of p-coumaroyl-CoA 39-hydroxylase in hybrid poplar impacts lignin deposition and soluble secondary metabolism
    • Coleman, H.D., Park, J.Y., Nair, R., Chapple, C., and Mansfield, S.D. (2008). RNAi-mediated suppression of p-coumaroyl-CoA 39-hydroxylase in hybrid poplar impacts lignin deposition and soluble secondary metabolism. Proc. Natl. Acad. Sci. USA 105: 4501-4506.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 4501-4506
    • Coleman, H.D.1    Park, J.Y.2    Nair, R.3    Chapple, C.4    Mansfield, S.D.5
  • 15
    • 34247147652 scopus 로고    scopus 로고
    • Presence of 5-hydroxyguaiacyl units as native lignin constituents in plants as seen by Py-GC/MS
    • del Rio, J.C., Martinez, A.T., and Gutierrez, A. (2006). Presence of 5-hydroxyguaiacyl units as native lignin constituents in plants as seen by Py-GC/MS. J. Anal. Appl. Pyrolysis 79: 33-38.
    • (2006) J. Anal. Appl. Pyrolysis , vol.79 , pp. 33-38
    • del Rio, J.C.1    Martinez, A.T.2    Gutierrez, A.3
  • 16
    • 34548539195 scopus 로고    scopus 로고
    • Both caffeoyl coenzyme A 3-O-methyltransferase 1 and caffeic acid O-methyltransferase 1 are involved in redundant functions for lignin, flavonoids and sinapoyl malate biosynthesis in Arabidopsis
    • Do, C.T., Pollet, B., Thévenin, J., Sibout, R., Denoue, D., Barrière, Y., Lapierre, C., and Jouanin, L. (2007). Both caffeoyl coenzyme A 3-O-methyltransferase 1 and caffeic acid O-methyltransferase 1 are involved in redundant functions for lignin, flavonoids and sinapoyl malate biosynthesis in Arabidopsis. Planta 226: 1117-1129.
    • (2007) Planta , vol.226 , pp. 1117-1129
    • Do, C.T.1    Pollet, B.2    Thévenin, J.3    Sibout, R.4    Denoue, D.5    Barrière, Y.6    Lapierre, C.7    Jouanin, L.8
  • 17
    • 0035832807 scopus 로고    scopus 로고
    • The biosynthesis of monolignols: A "metabolic grid", or independent pathways to guaiacyl and syringyl units?
    • Dixon, R.A., Chen, F., Guo, D., and Parvathi, K. (2001). The biosynthesis of monolignols: A "metabolic grid", or independent pathways to guaiacyl and syringyl units? Phytochemistry 57: 1069-1084.
    • (2001) Phytochemistry , vol.57 , pp. 1069-1084
    • Dixon, R.A.1    Chen, F.2    Guo, D.3    Parvathi, K.4
  • 18
    • 0028518712 scopus 로고
    • Modification of lignin biosynthesis in transgenic Nicotiana through expression of an antisense O-methyltransferase gene from Populus
    • Dwivedi, U.N., Campbell, W.H., Yu, J., Datla, R.S., Bugos, R.C., Chiang, V.L., and Podila, G.K. (1994). Modification of lignin biosynthesis in transgenic Nicotiana through expression of an antisense O-methyltransferase gene from Populus. Plant Mol. Biol. 26: 61-71.
    • (1994) Plant Mol. Biol. , vol.26 , pp. 61-71
    • Dwivedi, U.N.1    Campbell, W.H.2    Yu, J.3    Datla, R.S.4    Bugos, R.C.5    Chiang, V.L.6    Podila, G.K.7
  • 19
    • 0034031635 scopus 로고    scopus 로고
    • Modified lignin in tobacco and poplar plants over-expressing the Arabidopsis gene encoding ferulate 5-hydroxylase
    • Franke, R., McMichael, C.M., Meyer, K., Shirley, A.M., Cusumano, J.C., and Chapple, C. (2000). Modified lignin in tobacco and poplar plants over-expressing the Arabidopsis gene encoding ferulate 5-hydroxylase. Plant J. 22: 223-234.
    • (2000) Plant J. , vol.22 , pp. 223-234
    • Franke, R.1    McMichael, C.M.2    Meyer, K.3    Shirley, A.M.4    Cusumano, J.C.5    Chapple, C.6
  • 20
    • 84981756592 scopus 로고
    • The enzyme system participating in lignification
    • Freudenberg, K., Reznik, H., and Boesenberg, H. (1952). The enzyme system participating in lignification. Chem. Ber. 85: 641-647.
    • (1952) Chem. Ber. , vol.85 , pp. 641-647
    • Freudenberg, K.1    Reznik, H.2    Boesenberg, H.3
  • 21
  • 22
    • 79953839352 scopus 로고    scopus 로고
    • High-throughput SNP genotyping in the highly heterozygous genome of Eucalyptus: Assay success, polymorphism and transferability across species
    • Grattapaglia, D., Silva-Junior, O.B., Kirst, M., de Lima, B.M., Faria, D.A., and Pappas, G.J., Jr., (2011). High-throughput SNP genotyping in the highly heterozygous genome of Eucalyptus: Assay success, polymorphism and transferability across species. BMC Plant Biol. 11: 65.
    • (2011) BMC Plant Biol. , vol.11 , pp. 65
    • Grattapaglia, D.1    Silva-Junior, O.B.2    Kirst, M.3    de Lima, B.M.4    Faria, D.A.5    Pappas Jr., G.J.6
  • 23
    • 0035105233 scopus 로고    scopus 로고
    • Downregulation of caffeic acid 3-O-methyltransferase and caffeoyl CoA 3-O-methyltransferase in transgenic alfalfa. impacts on lignin structure and implications for the biosynthesis of G and S lignin
    • Guo, D., Chen, F., Inoue, K., Blount, J.W., and Dixon, R.A. (2001). Downregulation of caffeic acid 3-O-methyltransferase and caffeoyl CoA 3-O-methyltransferase in transgenic alfalfa. impacts on lignin structure and implications for the biosynthesis of G and S lignin. Plant Cell 13: 73-88.
    • (2001) Plant Cell , vol.13 , pp. 73-88
    • Guo, D.1    Chen, F.2    Inoue, K.3    Blount, J.W.4    Dixon, R.A.5
  • 26
    • 85047681876 scopus 로고    scopus 로고
    • Differential substrate inhibition couples kinetically distinct 4-coumarate: Coenzyme a ligases with spatially distinct metabolic roles in quaking aspen
    • Harding, S.A., Leshkevich, J., Chiang, V.L., and Tsai, C.J. (2002). Differential substrate inhibition couples kinetically distinct 4-coumarate: coenzyme a ligases with spatially distinct metabolic roles in quaking aspen. Plant Physiol. 128: 428-438.
    • (2002) Plant Physiol. , vol.128 , pp. 428-438
    • Harding, S.A.1    Leshkevich, J.2    Chiang, V.L.3    Tsai, C.J.4
  • 27
    • 79960900581 scopus 로고    scopus 로고
    • 13C metabolic flux analysis
    • 13C metabolic flux analysis. Plant J. 67: 513-525.
    • (2011) Plant J. , vol.67 , pp. 513-525
    • Hay, J.1    Schwender, J.2
  • 28
    • 0037804892 scopus 로고
    • Studies of lignin biosynthesis using isotopic carbon: XIII. The phenylpropanoid system in lignification
    • Higuchi, T., and Brown, S.A. (1963). Studies of lignin biosynthesis using isotopic carbon: XIII. The phenylpropanoid system in lignification. Can. J. Biochem. Physiol. 41: 621-628.
    • (1963) Can. J. Biochem. Physiol. , vol.41 , pp. 621-628
    • Higuchi, T.1    Brown, S.A.2
  • 30
    • 2942633712 scopus 로고    scopus 로고
    • Silencing of hydroxycinnamoyl-coenzyme A shikimate/quinate hydroxycinnamoyltransferase affects phenylpropanoid biosynthesis
    • Hoffmann, L., Besseau, S., Geoffroy, P., Ritzenthaler, C., Meyer, D., Lapierre, C., Pollet, B., and Legrand, M. (2004). Silencing of hydroxycinnamoyl-coenzyme A shikimate/quinate hydroxycinnamoyltransferase affects phenylpropanoid biosynthesis. Plant Cell 16: 1446-1465.
    • (2004) Plant Cell , vol.16 , pp. 1446-1465
    • Hoffmann, L.1    Besseau, S.2    Geoffroy, P.3    Ritzenthaler, C.4    Meyer, D.5    Lapierre, C.6    Pollet, B.7    Legrand, M.8
  • 31
    • 36248990302 scopus 로고    scopus 로고
    • Including metabolite concentrations into flux balance analysis: Thermodynamic realizability as a constraint on flux distributions in metabolic networks
    • Hoppe, A., Hoffmann, S., and Holzhütter, H.G. (2007). Including metabolite concentrations into flux balance analysis: Thermodynamic realizability as a constraint on flux distributions in metabolic networks. BMC Syst. Biol. 1: 23.
    • (2007) BMC Syst. Biol. , vol.1 , pp. 23
    • Hoppe, A.1    Hoffmann, S.2    Holzhütter, H.G.3
  • 33
    • 33847026853 scopus 로고    scopus 로고
    • Exploring the role of protein phosphorylation in plants: From signalling to metabolism
    • Huber, S.C. (2007). Exploring the role of protein phosphorylation in plants: From signalling to metabolism. Biochem. Soc. Trans. 35: 28-32.
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 28-32
    • Huber, S.C.1
  • 34
    • 0141706534 scopus 로고    scopus 로고
    • Significant increases in pulping efficiency in C4H-F5Htransformed poplars: Improved chemical savings and reduced environmental toxins
    • Huntley, S.K., Ellis, D., Gilbert, M., Chapple, C., and Mansfield, S.D. (2003). Significant increases in pulping efficiency in C4H-F5Htransformed poplars: improved chemical savings and reduced environmental toxins. J. Agric. Food Chem. 51: 6178-6183.
    • (2003) J. Agric. Food Chem. , vol.51 , pp. 6178-6183
    • Huntley, S.K.1    Ellis, D.2    Gilbert, M.3    Chapple, C.4    Mansfield, S.D.5
  • 35
    • 0001360385 scopus 로고
    • Stress responses in alfalfa (Medicago sativa L.): II. Purification, characterization, and induction of phenylalanine ammonia-lyase isoforms from elicitor-treated cell suspension cultures
    • Jorrin, J., and Dixon, R.A. (1990). Stress responses in alfalfa (Medicago sativa L.): II. Purification, characterization, and induction of phenylalanine ammonia-lyase isoforms from elicitor-treated cell suspension cultures. Plant Physiol. 92: 447-455.
    • (1990) Plant Physiol. , vol.92 , pp. 447-455
    • Jorrin, J.1    Dixon, R.A.2
  • 36
    • 0030267242 scopus 로고    scopus 로고
    • Alterations in the biosynthesis of lignin in transgenic plants with chimeric genes for 4-coumarate: Coenzyme A ligase
    • Kajita, S., Katayama, Y., and Omori, S. (1996). Alterations in the biosynthesis of lignin in transgenic plants with chimeric genes for 4-coumarate: coenzyme A ligase. Plant Cell Physiol. 37: 957-965.
    • (1996) Plant Cell Physiol. , vol.37 , pp. 957-965
    • Kajita, S.1    Katayama, Y.2    Omori, S.3
  • 37
    • 0029535737 scopus 로고
    • Particle swarm optimization
    • Kennedy, J., and Eberhart, R. (1995). Particle swarm optimization. Proc. IEEE 4: 1942-1948.
    • (1995) Proc. IEEE , vol.4 , pp. 1942-1948
    • Kennedy, J.1    Eberhart, R.2
  • 38
    • 77957741379 scopus 로고    scopus 로고
    • Tyloses and phenolic deposits in xylem vessels impede water transport in low-lignin transgenic poplars: A study by cryo-fluorescence microscopy
    • Kitin, P., Voelker, S.L., Meinzer, F.C., Beeckman, H., Strauss, S.H., and Lachenbruch, B. (2010). Tyloses and phenolic deposits in xylem vessels impede water transport in low-lignin transgenic poplars: A study by cryo-fluorescence microscopy. Plant Physiol. 154: 887-898.
    • (2010) Plant Physiol. , vol.154 , pp. 887-898
    • Kitin, P.1    Voelker, S.L.2    Meinzer, F.C.3    Beeckman, H.4    Strauss, S.H.5    Lachenbruch, B.6
  • 39
    • 0043228616 scopus 로고
    • Purification and properties of O-methyltransferase involved in the biosynthesis of gymnosperm lignin
    • Kuroda, H., Shimada, M., and Higuchi, T. (1975). Purification and properties of O-methyltransferase involved in the biosynthesis of gymnosperm lignin. Phytochemistry 14: 1759-1763.
    • (1975) Phytochemistry , vol.14 , pp. 1759-1763
    • Kuroda, H.1    Shimada, M.2    Higuchi, T.3
  • 40
    • 84859351415 scopus 로고    scopus 로고
    • Fluxes in central carbohydrate metabolism of source leaves in a fructan-storing C3 grass: Rapid turnover and futile cycling of sucrose in continuous light under contrasted nitrogen nutrition status
    • Lattanzi, F.A., Ostler, U., Wild, M., Morvan-Bertrand, A., Decau, M.L., Lehmeier, C.A., Meuriot, F., Prud'homme, M.P., Schäufele, R., and Schnyder, H. (2012). Fluxes in central carbohydrate metabolism of source leaves in a fructan-storing C3 grass: Rapid turnover and futile cycling of sucrose in continuous light under contrasted nitrogen nutrition status. J. Exp. Bot. 63: 2363-2375.
    • (2012) J. Exp. Bot. , vol.63 , pp. 2363-2375
    • Lattanzi, F.A.1    Ostler, U.2    Wild, M.3    Morvan-Bertrand, A.4    Decau, M.L.5    Lehmeier, C.A.6    Meuriot, F.7    Prud'homme, M.P.8    Schäufele, R.9    Schnyder, H.10
  • 41
    • 0031277875 scopus 로고    scopus 로고
    • Antisense suppression of 4-coumarate:Coenzyme A ligase activity in Arabidopsis leads to altered lignin subunit composition
    • Lee, D., Meyer, K., Chapple, C., and Douglas, C.J. (1997). Antisense suppression of 4-coumarate:coenzyme A ligase activity in Arabidopsis leads to altered lignin subunit composition. Plant Cell 9: 1985-1998.
    • (1997) Plant Cell , vol.9 , pp. 1985-1998
    • Lee, D.1    Meyer, K.2    Chapple, C.3    Douglas, C.J.4
  • 42
    • 79958142451 scopus 로고    scopus 로고
    • Integrative analysis of transgenic alfalfa (Medicago sativa L.) suggests new metabolic control mechanisms for monolignol biosynthesis
    • Lee, Y., Chen, F., Gallego-Giraldo, L., Dixon, R.A., and Voit, E.O. (2011). Integrative analysis of transgenic alfalfa (Medicago sativa L.) suggests new metabolic control mechanisms for monolignol biosynthesis. PLOS Comput. Biol. 7: e1002047.
    • (2011) PLOS Comput. Biol. , vol.7
    • Lee, Y.1    Chen, F.2    Gallego-Giraldo, L.3    Dixon, R.A.4    Voit, E.O.5
  • 43
    • 84870722795 scopus 로고    scopus 로고
    • Functional analysis of metabolic channeling and regulation in lignin biosynthesis: A computational approach
    • Lee, Y., Escamilla-Treviño, L., Dixon, R.A., and Voit, E.O. (2012). Functional analysis of metabolic channeling and regulation in lignin biosynthesis: A computational approach. PLOS Comput. Biol. 8: e1002769.
    • (2012) PLOS Comput. Biol. , vol.8
    • Lee, Y.1    Escamilla-Treviño, L.2    Dixon, R.A.3    Voit, E.O.4
  • 44
    • 77957687260 scopus 로고    scopus 로고
    • Mathematical modeling of monolignol biosynthesis in Populus xylem
    • Lee, Y., and Voit, E.O. (2010). Mathematical modeling of monolignol biosynthesis in Populus xylem. Math. Biosci. 228: 78-89.
    • (2010) Math. Biosci. , vol.228 , pp. 78-89
    • Lee, Y.1    Voit, E.O.2
  • 45
    • 25444453719 scopus 로고    scopus 로고
    • Clarification of cinnamoyl co-enzyme A reductase catalysis in monolignol biosynthesis of aspen
    • Li, L., Cheng, X., Lu, S., Nakatsubo, T., Umezawa, T., and Chiang, V.L. (2005). Clarification of cinnamoyl co-enzyme A reductase catalysis in monolignol biosynthesis of aspen. Plant Cell Physiol. 46: 1073-1082.
    • (2005) Plant Cell Physiol. , vol.46 , pp. 1073-1082
    • Li, L.1    Cheng, X.2    Lu, S.3    Nakatsubo, T.4    Umezawa, T.5    Chiang, V.L.6
  • 46
    • 0037447081 scopus 로고    scopus 로고
    • Combinatorial modification of multiple lignin traits in trees through multigene cotransformation
    • Li, L., Zhou, Y., Cheng, X., Sun, J., Marita, J.M., Ralph, J., and Chiang, V.L. (2003). Combinatorial modification of multiple lignin traits in trees through multigene cotransformation. Proc. Natl. Acad. Sci. USA 100: 4939-4944.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 4939-4944
    • Li, L.1    Zhou, Y.2    Cheng, X.3    Sun, J.4    Marita, J.M.5    Ralph, J.6    Chiang, V.L.7
  • 47
    • 84891552533 scopus 로고    scopus 로고
    • SND1 transcription factor-directed quantitative functional hierarchical genetic regulatory network in wood formation in Populus trichocarpa
    • Lin, Y.-C., Li, W., Sun, Y.-H., Kumari, S., Wei, H., Li, Q., Tunlaya-Anukit, S., Sederoff, R.R., and Chiang, V.L. (2013). SND1 transcription factor-directed quantitative functional hierarchical genetic regulatory network in wood formation in Populus trichocarpa. Plant Cell 25: 4324-4341.
    • (2013) Plant Cell , vol.25 , pp. 4324-4341
    • Lin, Y.-C.1    Li, W.2    Sun, Y.-H.3    Kumari, S.4    Wei, H.5    Li, Q.6    Tunlaya-Anukit, S.7    Sederoff, R.R.8    Chiang, V.L.9
  • 48
    • 81055148229 scopus 로고    scopus 로고
    • Identification and analysis of phosphorylation status of proteins in dormant terminal buds of poplar
    • Liu, C.C., Liu, C.F., Wang, H.X., Shen, Z.Y., Yang, C.P., and Wei, Z.G. (2011). Identification and analysis of phosphorylation status of proteins in dormant terminal buds of poplar. BMC Plant Biol. 11: 158.
    • (2011) BMC Plant Biol. , vol.11 , pp. 158
    • Liu, C.C.1    Liu, C.F.2    Wang, H.X.3    Shen, Z.Y.4    Yang, C.P.5    Wei, Z.G.6
  • 49
    • 84865590931 scopus 로고    scopus 로고
    • A standard reaction condition and a single HPLC separation system are sufficient for estimation of monolignol biosynthetic pathway enzyme activities
    • Liu, J., Shi, R., Li, Q., Sederoff, R.R., and Chiang, V.L. (2012). A standard reaction condition and a single HPLC separation system are sufficient for estimation of monolignol biosynthetic pathway enzyme activities. Planta 236: 879-885.
    • (2012) Planta , vol.236 , pp. 879-885
    • Liu, J.1    Shi, R.2    Li, Q.3    Sederoff, R.R.4    Chiang, V.L.5
  • 50
    • 84879518951 scopus 로고    scopus 로고
    • Ptr-miR397a is a negative regulator of laccase genes affecting lignin content in Populus trichocarpa
    • Lu, S., et al. (2013). Ptr-miR397a is a negative regulator of laccase genes affecting lignin content in Populus trichocarpa. Proc. Natl. Acad. Sci. USA 110: 10848-10853.
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 10848-10853
    • Lu, S.1
  • 51
    • 0003174033 scopus 로고    scopus 로고
    • Structural and compositional modifications in lignin of transgenic alfalfa down-regulated in caffeic acid 3-methyltransferase and caffeoyl coenzyme A 3-O-methyltransferase
    • Marita, J.M., Ralph, J., Hatfield, R.D., Guo, D., Chen, F., and Dixon, R.A. (2003). Structural and compositional modifications in lignin of transgenic alfalfa down-regulated in caffeic acid 3-methyltransferase and caffeoyl coenzyme A 3-O-methyltransferase. Phytochemistry 62: 53-65.
    • (2003) Phytochemistry , vol.62 , pp. 53-65
    • Marita, J.M.1    Ralph, J.2    Hatfield, R.D.3    Guo, D.4    Chen, F.5    Dixon, R.A.6
  • 52
    • 0032499766 scopus 로고    scopus 로고
    • Lignin monomer composition is determined by the expression of a cytochrome P450-dependent monooxygenase in Arabidopsis
    • Meyer, K., Shirley, A.M., Cusumano, J.C., Bell-Lelong, D.A., and Chapple, C. (1998). Lignin monomer composition is determined by the expression of a cytochrome P450-dependent monooxygenase in Arabidopsis. Proc. Natl. Acad. Sci. USA 95: 6619-6623.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6619-6623
    • Meyer, K.1    Shirley, A.M.2    Cusumano, J.C.3    Bell-Lelong, D.A.4    Chapple, C.5
  • 53
    • 0034711291 scopus 로고    scopus 로고
    • Modifications in lignin and accumulation of phenolic glucosides in poplar xylem upon down-regulation of caffeoyl-coenzyme A O-methyltransferase, an enzyme involved in lignin biosynthesis
    • Meyermans, H., et al. (2000). Modifications in lignin and accumulation of phenolic glucosides in poplar xylem upon down-regulation of caffeoyl-coenzyme A O-methyltransferase, an enzyme involved in lignin biosynthesis. J. Biol. Chem. 275: 36899-36909.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36899-36909
    • Meyermans, H.1
  • 54
    • 34248639844 scopus 로고    scopus 로고
    • Introduction of sense constructs of cinnamate 4-hydroxylase (CYP73A24) in transgenic tomato plants shows opposite effects on flux into stem lignin and fruit flavonoids
    • Millar, D.J., Long, M., Donovan, G., Fraser, P.D., Boudet, A.M., Danoun, S., Bramley, P.M., and Bolwell, G.P. (2007). Introduction of sense constructs of cinnamate 4-hydroxylase (CYP73A24) in transgenic tomato plants shows opposite effects on flux into stem lignin and fruit flavonoids. Phytochemistry 68: 1497-1509.
    • (2007) Phytochemistry , vol.68 , pp. 1497-1509
    • Millar, D.J.1    Long, M.2    Donovan, G.3    Fraser, P.D.4    Boudet, A.M.5    Danoun, S.6    Bramley, P.M.7    Bolwell, G.P.8
  • 55
    • 77957730551 scopus 로고    scopus 로고
    • Lignin and biomass: A negative correlation for wood formation and lignin content in trees
    • Novaes, E., Kirst, M., Chiang, V., Winter-Sederoff, H., and Sederoff, R.R. (2010). Lignin and biomass: A negative correlation for wood formation and lignin content in trees. Plant Physiol. 154: 555-561.
    • (2010) Plant Physiol. , vol.154 , pp. 555-561
    • Novaes, E.1    Kirst, M.2    Chiang, V.3    Winter-Sederoff, H.4    Sederoff, R.R.5
  • 57
    • 12244269747 scopus 로고    scopus 로고
    • Down-regulation of caffeic acid o-methyltransferase in maize revisited using a transgenic approach
    • Piquemal, J., et al. (2002). Down-regulation of caffeic acid o-methyltransferase in maize revisited using a transgenic approach. Plant Physiol. 130: 1675-1685.
    • (2002) Plant Physiol. , vol.130 , pp. 1675-1685
    • Piquemal, J.1
  • 58
    • 0142035247 scopus 로고    scopus 로고
    • Genome-wide characterization of the lignification toolbox in Arabidopsis
    • Raes, J., Rohde, A., Christensen, J.H., Van de Peer, Y., and Boerjan, W. (2003). Genome-wide characterization of the lignification toolbox in Arabidopsis. Plant Physiol. 133: 1051-1071.
    • (2003) Plant Physiol. , vol.133 , pp. 1051-1071
    • Raes, J.1    Rohde, A.2    Christensen, J.H.3    Van de Peer, Y.4    Boerjan, W.5
  • 59
    • 31544452808 scopus 로고    scopus 로고
    • The path forward for biofuels and biomaterials
    • Ragauskas, A.J., et al. (2006). The path forward for biofuels and biomaterials. Science 311: 484-489.
    • (2006) Science , vol.311 , pp. 484-489
    • Ragauskas, A.J.1
  • 60
    • 58149164536 scopus 로고    scopus 로고
    • Lignins
    • In F. Rose and K. Osborne, eds (Chichester, UK: John Wiley & Sons), doi/10.1002/9780470015902.a0020104
    • Ralph, J., Brunow, G., and Boerjan, W. (2007). Lignins. In Encyclopedia of Life Sciences, F. Rose and K. Osborne, eds (Chichester, UK: John Wiley & Sons), doi/10.1002/9780470015902.a0020104.
    • (2007) Encyclopedia of Life Sciences
    • Ralph, J.1    Brunow, G.2    Boerjan, W.3
  • 62
    • 33745037705 scopus 로고    scopus 로고
    • Down-regulation of lignin biosynthesis in transgenic Leucaena leucocephala harboring O-methyltransferase gene
    • Rastogi, S., and Dwivedi, U.N. (2006). Down-regulation of lignin biosynthesis in transgenic Leucaena leucocephala harboring O-methyltransferase gene. Biotechnol. Prog. 22: 609-616.
    • (2006) Biotechnol. Prog. , vol.22 , pp. 609-616
    • Rastogi, S.1    Dwivedi, U.N.2
  • 63
    • 28044451538 scopus 로고    scopus 로고
    • Targeted down-regulation of cytochrome P450 enzymes for forage quality improvement in alfalfa (Medicago sativa L.)
    • Reddy, M.S., Chen, F., Shadle, G., Jackson, L., Aljoe, H., and Dixon, R.A. (2005). Targeted down-regulation of cytochrome P450 enzymes for forage quality improvement in alfalfa (Medicago sativa L.). Proc. Natl. Acad. Sci. USA 102: 16573-16578.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 16573-16578
    • Reddy, M.S.1    Chen, F.2    Shadle, G.3    Jackson, L.4    Aljoe, H.5    Dixon, R.A.6
  • 64
    • 0032817823 scopus 로고    scopus 로고
    • Regulation of ferulate-5-hydroxylase expression in Arabidopsis in the context of sinapate ester biosynthesis
    • Ruegger, M., Meyer, K., Cusumano, J.C., and Chapple, C. (1999). Regulation of ferulate-5-hydroxylase expression in Arabidopsis in the context of sinapate ester biosynthesis. Plant Physiol. 119: 101-110.
    • (1999) Plant Physiol. , vol.119 , pp. 101-110
    • Ruegger, M.1    Meyer, K.2    Cusumano, J.C.3    Chapple, C.4
  • 65
    • 0001406705 scopus 로고
    • Inhibition of phenylalanine ammonia-lyase by cinnamic acid derivatives and related compounds
    • Sato, T., Kiuchi, F., and Sankawa, U. (1982). Inhibition of phenylalanine ammonia-lyase by cinnamic acid derivatives and related compounds. Phytochemistry 21: 845-850.
    • (1982) Phytochemistry , vol.21 , pp. 845-850
    • Sato, T.1    Kiuchi, F.2    Sankawa, U.3
  • 66
    • 11844257894 scopus 로고
    • Renewable resources for the production of fuels and chemicals
    • Sarkanen, K.V. (1976). Renewable resources for the production of fuels and chemicals. Science 191: 773-776.
    • (1976) Science , vol.191 , pp. 773-776
    • Sarkanen, K.V.1
  • 68
    • 77950536374 scopus 로고    scopus 로고
    • Simulating plant metabolic pathways with enzyme-kinetic models
    • Schallau, K., and Junker, B.H. (2010). Simulating plant metabolic pathways with enzyme-kinetic models. Plant Physiol. 152: 1763-1771.
    • (2010) Plant Physiol. , vol.152 , pp. 1763-1771
    • Schallau, K.1    Junker, B.H.2
  • 69
    • 71949117406 scopus 로고    scopus 로고
    • Mutations in the cinnamate 4-hydroxylase gene impact metabolism, growth and development in Arabidopsis
    • Schilmiller, A.L., Stout, J., Weng, J.K., Humphreys, J., Ruegger, M.O., and Chapple, C. (2009). Mutations in the cinnamate 4-hydroxylase gene impact metabolism, growth and development in Arabidopsis. Plant J. 60: 771-782.
    • (2009) Plant J. , vol.60 , pp. 771-782
    • Schilmiller, A.L.1    Stout, J.2    Weng, J.K.3    Humphreys, J.4    Ruegger, M.O.5    Chapple, C.6
  • 71
    • 0031397140 scopus 로고    scopus 로고
    • Reduced lignin content and altered lignin composition in transgenic tobacco down-regulated in expression of L-phenylalanine ammonia-lyase or cinnamate 4-hydroxylase
    • Sewalt, V., Ni, W., Blount, J.W., Jung, H.G., Masoud, S.A., Howles, P.A., Lamb, C., and Dixon, R.A. (1997). Reduced lignin content and altered lignin composition in transgenic tobacco down-regulated in expression of L-phenylalanine ammonia-lyase or cinnamate 4-hydroxylase. Plant Physiol. 115: 41-50.
    • (1997) Plant Physiol. , vol.115 , pp. 41-50
    • Sewalt, V.1    Ni, W.2    Blount, J.W.3    Jung, H.G.4    Masoud, S.A.5    Howles, P.A.6    Lamb, C.7    Dixon, R.A.8
  • 72
    • 34248541296 scopus 로고    scopus 로고
    • Down-regulation of hydroxycinnamoyl CoA:Shikimate hydroxycinnamoyl transferase in transgenic alfalfa affects lignification, development and forage quality
    • Shadle, G., Chen, F., Srinivasa Reddy, M.S., Jackson, L., Nakashima, J., and Dixon, R.A. (2007). Down-regulation of hydroxycinnamoyl CoA:shikimate hydroxycinnamoyl transferase in transgenic alfalfa affects lignification, development and forage quality. Phytochemistry 68: 1521-1529.
    • (2007) Phytochemistry , vol.68 , pp. 1521-1529
    • Shadle, G.1    Chen, F.2    Srinivasa Reddy, M.S.3    Jackson, L.4    Nakashima, J.5    Dixon, R.A.6
  • 75
    • 74549176584 scopus 로고    scopus 로고
    • Towards a systems approach for lignin biosynthesis in Populus trichocarpa: Transcript abundance and specificity of the monolignol biosynthetic genes
    • Shi, R., Sun, Y.H., Li, Q., Heber, S., Sederoff, R.R., and Chiang, V.L. (2010). Towards a systems approach for lignin biosynthesis in Populus trichocarpa: Transcript abundance and specificity of the monolignol biosynthetic genes. Plant Cell Physiol. 51: 144-163.
    • (2010) Plant Cell Physiol. , vol.51 , pp. 144-163
    • Shi, R.1    Sun, Y.H.2    Li, Q.3    Heber, S.4    Sederoff, R.R.5    Chiang, V.L.6
  • 76
    • 84861831985 scopus 로고    scopus 로고
    • Comprehensive quantification of monolignol-pathway enzymes in Populus trichocarpa by protein cleavage isotope dilution mass spectrometry
    • Shuford, C.M., Li, Q., Sun, Y.H., Chen, H.C., Wang, J., Shi, R., Sederoff, R.R., Chiang, V.L., and Muddiman, D.C. (2012). Comprehensive quantification of monolignol-pathway enzymes in Populus trichocarpa by protein cleavage isotope dilution mass spectrometry. J. Proteome Res. 11: 3390-3404.
    • (2012) J. Proteome Res. , vol.11 , pp. 3390-3404
    • Shuford, C.M.1    Li, Q.2    Sun, Y.H.3    Chen, H.C.4    Wang, J.5    Shi, R.6    Sederoff, R.R.7    Chiang, V.L.8    Muddiman, D.C.9
  • 77
    • 0038120007 scopus 로고    scopus 로고
    • Expression pattern of two paralogs encoding cinnamyl alcohol dehydrogenases in Arabidopsis. Isolation and characterization of the corresponding mutants
    • Sibout, R., Eudes, A., Pollet, B., Goujon, T., Mila, I., Granier, F., Séguin, A., Lapierre, C., and Jouanin, L. (2003). Expression pattern of two paralogs encoding cinnamyl alcohol dehydrogenases in Arabidopsis. Isolation and characterization of the corresponding mutants. Plant Physiol. 132: 848-860.
    • (2003) Plant Physiol. , vol.132 , pp. 848-860
    • Sibout, R.1    Eudes, A.2    Pollet, B.3    Goujon, T.4    Mila, I.5    Granier, F.6    Séguin, A.7    Lapierre, C.8    Jouanin, L.9
  • 78
    • 78650519832 scopus 로고    scopus 로고
    • RNAi-mediated suppression of the phenylalanine ammonia-lyase gene in Salvia miltiorrhiza causes abnormal phenotypes and a reduction in rosmarinic acid biosynthesis
    • Song, J., and Wang, Z. (2011). RNAi-mediated suppression of the phenylalanine ammonia-lyase gene in Salvia miltiorrhiza causes abnormal phenotypes and a reduction in rosmarinic acid biosynthesis. J. Plant Res. 124: 183-192.
    • (2011) J. Plant Res. , vol.124 , pp. 183-192
    • Song, J.1    Wang, Z.2
  • 79
    • 85011933711 scopus 로고
    • Possible multienzyme complexes regulating the formation of C6-C3 phenolic compounds and lignins in higher plants
    • Stafford, H.A. (1974). Possible multienzyme complexes regulating the formation of C6-C3 phenolic compounds and lignins in higher plants. Recent Adv. Phytochem. 8: 53-79.
    • (1974) Recent Adv. Phytochem. , vol.8 , pp. 53-79
    • Stafford, H.A.1
  • 80
    • 0030832622 scopus 로고    scopus 로고
    • 5-Hydroxyguaiacyl nuclei as aromatic constituents of native lignin
    • Suzuki, S., Lam, T.B.T., and Bunkyo-ku, Y. (1997). 5-Hydroxyguaiacyl nuclei as aromatic constituents of native lignin. Phytochemistry 46: 695-700.
    • (1997) Phytochemistry , vol.46 , pp. 695-700
    • Suzuki, S.1    Lam, T.B.T.2    Bunkyo-ku, Y.3
  • 81
    • 79960515921 scopus 로고    scopus 로고
    • Characterization of a cinnamoyl-CoA reductase 1 (CCR1) mutant in maize: Effects on lignification, fibre development, and global gene expression
    • Tamasloukht, B., et al. (2011). Characterization of a cinnamoyl-CoA reductase 1 (CCR1) mutant in maize: Effects on lignification, fibre development, and global gene expression. J. Exp. Bot. 62: 3837-3848.
    • (2011) J. Exp. Bot. , vol.62 , pp. 3837-3848
    • Tamasloukht, B.1
  • 82
    • 72449126528 scopus 로고    scopus 로고
    • Nanostructural assembly of cellulose, hemicellulose, and lignin in the middle layer of secondary wall of ginkgo tracheid
    • Terashima, N., Kitano, K., Kojima, M., Yamamoto, H., and Westermark, U. (2009). Nanostructural assembly of cellulose, hemicellulose, and lignin in the middle layer of secondary wall of ginkgo tracheid. J. Wood Sci. 55: 409-416.
    • (2009) J. Wood Sci. , vol.55 , pp. 409-416
    • Terashima, N.1    Kitano, K.2    Kojima, M.3    Yamamoto, H.4    Westermark, U.5
  • 83
    • 0000433683 scopus 로고    scopus 로고
    • Suppression of O-methyltransferase gene by homologous sense transgene in quaking aspen causes red-brown wood phenotypes
    • Tsai, C.J., Popko, J.L., Mielke, M.R., Hu, W.J., Podila, G.K., and Chiang, V.L. (1998). Suppression of O-methyltransferase gene by homologous sense transgene in quaking aspen causes red-brown wood phenotypes. Plant Physiol. 117: 101-112.
    • (1998) Plant Physiol. , vol.117 , pp. 101-112
    • Tsai, C.J.1    Popko, J.L.2    Mielke, M.R.3    Hu, W.J.4    Podila, G.K.5    Chiang, V.L.6
  • 85
    • 77954248061 scopus 로고    scopus 로고
    • Modeling lignin polymerization. I. Simulation model of dehydrogenation polymers
    • van Parijs, F.R., Morreel, K., Ralph, J., Boerjan, W., and Merks, R.M.H. (2010). Modeling lignin polymerization. I. Simulation model of dehydrogenation polymers. Plant Physiol. 153: 1332-1344.
    • (2010) Plant Physiol. , vol.153 , pp. 1332-1344
    • van Parijs, F.R.1    Morreel, K.2    Ralph, J.3    Boerjan, W.4    Merks, R.M.H.5
  • 86
    • 84883489184 scopus 로고    scopus 로고
    • Caffeoyl shikimate esterase (CSE) is an enzyme in the lignin biosynthetic pathway in Arabidopsis
    • Vanholme, R., et al. (2013). Caffeoyl shikimate esterase (CSE) is an enzyme in the lignin biosynthetic pathway in Arabidopsis. Science 341: 1103-1106.
    • (2013) Science , vol.341 , pp. 1103-1106
    • Vanholme, R.1
  • 87
    • 77957728522 scopus 로고    scopus 로고
    • Antisense down-regulation of 4CL expression alters lignification, tree growth, and saccharification potential of field-grown poplar
    • Voelker, S.L., et al. (2010). Antisense down-regulation of 4CL expression alters lignification, tree growth, and saccharification potential of field-grown poplar. Plant Physiol. 154: 874-886.
    • (2010) Plant Physiol. , vol.154 , pp. 874-886
    • Voelker, S.L.1
  • 90
    • 84865584315 scopus 로고    scopus 로고
    • Functional redundancy of the two 5-hydroxylases in monolignol biosynthesis of Populus trichocarpa: LC-MS/MS based protein quantification and metabolic flux analysis
    • Wang, J.P., Shuford, C.M., Li, Q., Song, J., Lin, Y.C., Sun, Y.H., Chen, H.C., Williams, C.M., Muddiman, D.C., Sederoff, R.R., andChiang, V.L. (2012). Functional redundancy of the two 5-hydroxylases in monolignol biosynthesis of Populus trichocarpa: LC-MS/MS based protein quantification and metabolic flux analysis. Planta 236: 795-808.
    • (2012) Planta , vol.236 , pp. 795-808
    • Wang, J.P.1    Shuford, C.M.2    Li, Q.3    Song, J.4    Lin, Y.C.5    Sun, Y.H.6    Chen, H.C.7    Williams, C.M.8    Muddiman, D.C.9    Sederoff, R.R.10    Chiang, V.L.11
  • 92
    • 0032695916 scopus 로고    scopus 로고
    • Evidence for enzyme complexes in the phenylpropanoid and flavonoid pathways
    • Winkel-Shirley, B. (1999). Evidence for enzyme complexes in the phenylpropanoid and flavonoid pathways. Physiol. Plant. 107: 142-149.
    • (1999) Physiol. Plant. , vol.107 , pp. 142-149
    • Winkel-Shirley, B.1
  • 93
    • 70449216418 scopus 로고
    • Studies of lignin biosynthesis using isotopic carbon. VI. Formation of the side chain of the phenylpropane monomer
    • Wright, D., Brown, S.A., and Neish, A.C. (1958). Studies of lignin biosynthesis using isotopic carbon. VI. Formation of the side chain of the phenylpropane monomer. Can. J. Biochem. Physiol. 36: 1037-1045.
    • (1958) Can. J. Biochem. Physiol. , vol.36 , pp. 1037-1045
    • Wright, D.1    Brown, S.A.2    Neish, A.C.3
  • 94
    • 80054835879 scopus 로고    scopus 로고
    • Silencing of 4-coumarate:Coenzyme A ligase in switchgrass leads to reduced lignin content and improved fermentable sugar yields for biofuel production
    • Xu, B., Escamilla-Treviño, L.L., Sathitsuksanoh, N., Shen, Z., Shen, H., Zhang, Y.H., Dixon, R.A., and Zhao, B. (2011). Silencing of 4-coumarate:coenzyme A ligase in switchgrass leads to reduced lignin content and improved fermentable sugar yields for biofuel production. New Phytol. 192: 611-625.
    • (2011) New Phytol. , vol.192 , pp. 611-625
    • Xu, B.1    Escamilla-Treviño, L.L.2    Sathitsuksanoh, N.3    Shen, Z.4    Shen, H.5    Zhang, Y.H.6    Dixon, R.A.7    Zhao, B.8
  • 95
    • 0032287625 scopus 로고    scopus 로고
    • Dual methylation pathways in lignin biosynthesis
    • Zhong, R., Iii, W.H., Negrel, J., and Ye, Z.H. (1998). Dual methylation pathways in lignin biosynthesis. Plant Cell 10: 2033-2046.
    • (1998) Plant Cell , vol.10 , pp. 2033-2046
    • Zhong, R.1    Iii, W.H.2    Negrel, J.3    Ye, Z.H.4
  • 96
    • 0033783438 scopus 로고    scopus 로고
    • Essential role of caffeoyl coenzyme A O-methyltransferase in lignin biosynthesis in woody poplar plants
    • Zhong, R., Morrison, W.H., III., Himmelsbach, D.S., Poole, F.L., II., and Ye, Z.H. (2000). Essential role of caffeoyl coenzyme A O-methyltransferase in lignin biosynthesis in woody poplar plants. Plant Physiol. 124: 563-578.
    • (2000) Plant Physiol. , vol.124 , pp. 563-578
    • Zhong, R.1    Morrison III, W.H.2    Himmelsbach, D.S.3    Poole II, F.L.4    Ye, Z.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.