메뉴 건너뛰기




Volumn 54, Issue , 2003, Pages 519-546

Lignin Biosynthesis

Author keywords

Dehydrogenation; Nucleation; Polymerization; Structure; Topochemistry; Transgenic plants

Indexed keywords

LIGNIN;

EID: 0042100516     PISSN: 15435008     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.arplant.54.031902.134938     Document Type: Review
Times cited : (3808)

References (161)
  • 1
    • 0036006035 scopus 로고    scopus 로고
    • Simultaneous suppression of multiple genes by single transgenes. Down-regulation of three unrelated lignin biosynthetic genes in tobacco
    • Abbott JC, Barakate A, Pinçon G, Legrand M, Lapierre C, et al. 2002. Simultaneous suppression of multiple genes by single transgenes. Down-regulation of three unrelated lignin biosynthetic genes in tobacco. Plant Physiol. 128:844-53
    • (2002) Plant Physiol. , vol.128 , pp. 844-853
    • Abbott, J.C.1    Barakate, A.2    Pinçon, G.3    Legrand, M.4    Lapierre, C.5
  • 2
    • 4243064911 scopus 로고
    • Lignin chemistry - Past present and future
    • Adler E. 1977. Lignin chemistry - past present and future. Wood Sci. Technol. 11:169-218
    • (1977) Wood Sci. Technol. , vol.11 , pp. 169-218
    • Adler, E.1
  • 4
    • 0037166234 scopus 로고    scopus 로고
    • Transcriptional control of monolignol biosynthesis in Pinus taeda. Factors affecting monolignol ratios and carbon allocation in phenylpropanoid metabolism
    • Anterola AM, Jeon J-H, Davin LB, Lewis NG. 2002. Transcriptional control of monolignol biosynthesis in Pinus taeda. Factors affecting monolignol ratios and carbon allocation in phenylpropanoid metabolism. J. Biol. Chem. 277:18272-80
    • (2002) J. Biol. Chem. , vol.277 , pp. 18272-18280
    • Anterola, A.M.1    Jeon, J.-H.2    Davin, L.B.3    Lewis, N.G.4
  • 5
    • 33745962010 scopus 로고
    • Raman microprobe evidence for lignin orientation in the cell walls of native woody tissue
    • Atalla RH, Agarwal UP. 1985. Raman microprobe evidence for lignin orientation in the cell walls of native woody tissue. Science 227:636-38
    • (1985) Science , vol.227 , pp. 636-638
    • Atalla, R.H.1    Agarwal, U.P.2
  • 6
    • 0028796270 scopus 로고
    • Altered lignin composition in transgenic tobacco expressing O-methyltransferase sequences in sense and antisense orientation
    • Atanassova R, Favet N, Martz F, Chabbert B, Tollier MT, et al. 1995. Altered lignin composition in transgenic tobacco expressing O-methyltransferase sequences in sense and antisense orientation. Plant J. 8:465-77
    • (1995) Plant J. , vol.8 , pp. 465-477
    • Atanassova, R.1    Favet, N.2    Martz, F.3    Chabbert, B.4    Tollier, M.T.5
  • 7
    • 0027240897 scopus 로고
    • A laccase associated with lignification in loblolly pine xylem
    • Bao W, O'Malley DM, Whetten R, Sederoff RR. 1993. A laccase associated with lignification in loblolly pine xylem. Science 260:672-74
    • (1993) Science , vol.260 , pp. 672-674
    • Bao, W.1    O'Malley, D.M.2    Whetten, R.3    Sederoff, R.R.4
  • 8
    • 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 NJ, Orr J, Ni W, Meromi A, Nadler-Hassar T, et al. 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 91:7608-12
    • (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
  • 9
    • 0033082660 scopus 로고    scopus 로고
    • Down-regulation of cinnamyl alcohol dehydrogenase in transgenic alfalfa (Medicago sativa L.) and the impact on lignin composition and digestibility
    • Baucher M, Bernard-Vailhé MA, Chabbert B, Besle J-M, Opsomer C, et al. 1999. Down-regulation of cinnamyl alcohol dehydrogenase in transgenic alfalfa (Medicago sativa L.) and the impact on lignin composition and digestibility. Plant Mol. Biol. 39:437-47
    • (1999) Plant Mol. Biol. , vol.39 , pp. 437-447
    • Baucher, M.1    Bernard-Vailhé, M.A.2    Chabbert, B.3    Besle, J.-M.4    Opsomer, C.5
  • 10
    • 12644283533 scopus 로고    scopus 로고
    • Red xylem and higher lignin extractability by down-regulating a cinnamyl alcohol dehydrogenase in poplar (Populus tremula x P. alba)
    • Baucher M, Chabbert B, Pilate G, Van Doorsselaere J, Tollier M-T, et al. 1996. Red xylem and higher lignin extractability by down-regulating a cinnamyl alcohol dehydrogenase in poplar (Populus tremula x P. alba). Plant Physiol. 112: 1479-90
    • (1996) Plant Physiol. , vol.112 , pp. 1479-1490
    • Baucher, M.1    Chabbert, B.2    Pilate, G.3    Van Doorsselaere, J.4    Tollier, M.-T.5
  • 12
    • 0542407699 scopus 로고    scopus 로고
    • Effect of modification of the O-methyltransferase activity on cell wall composition, ultrastructure and degradability of transgenic tobacco
    • Bernard-Vailhé MA, Migné C, Cornu A, Maillot MP, Grenet E, et al. 1996. Effect of modification of the O-methyltransferase activity on cell wall composition, ultrastructure and degradability of transgenic tobacco. J. Sci. Food Agric. 72:385-91
    • (1996) J. Sci. Food Agric. , vol.72 , pp. 385-391
    • Bernard-Vailhé, M.A.1    Migné, C.2    Cornu, A.3    Maillot, M.P.4    Grenet, E.5
  • 13
    • 0033759391 scopus 로고    scopus 로고
    • Altering expression of cinnamic acid 4-hydroxylase in transgenic plants provides evidence for a feedback loop at the entry point into the phenylpropanoid pathway
    • Blount JW, Korth KL, Masoud SA, Rasmussen S, Lamb C, Dixon RA. 2000. Altering expression of cinnamic acid 4-hydroxylase in transgenic plants provides evidence for a feedback loop at the entry point into the phenylpropanoid pathway. Plant Physiol. 122:107-16
    • (2000) Plant Physiol. , vol.122 , pp. 107-116
    • Blount, J.W.1    Korth, K.L.2    Masoud, S.A.3    Rasmussen, S.4    Lamb, C.5    Dixon, R.A.6
  • 14
    • 0036927885 scopus 로고    scopus 로고
    • Over-expression of cinnamate 4-hydroxylase leads to increased accumulation of acetosyringone in elicited tobacco cell-suspension cultures
    • Blount JW, Masoud S, Sumner LW, Huhman D, Dixon RA. 2002. Over-expression of cinnamate 4-hydroxylase leads to increased accumulation of acetosyringone in elicited tobacco cell-suspension cultures. Planta 214:902-10
    • (2002) Planta , vol.214 , pp. 902-910
    • Blount, J.W.1    Masoud, S.2    Sumner, L.W.3    Huhman, D.4    Dixon, R.A.5
  • 16
    • 0002535074 scopus 로고
    • L-phenylalanine ammonia-lyase from Phaseolus vulgaris. Modulation of the levels of active enzyme by trans-cinnamic acid
    • Bolwell GP, Cramer CL, Lamb CJ, Schuch W, Dixon RA. 1986. L-Phenylalanine ammonia-lyase from Phaseolus vulgaris. Modulation of the levels of active enzyme by trans-cinnamic acid. Planta 169:97-107
    • (1986) Planta , vol.169 , pp. 97-107
    • Bolwell, G.P.1    Cramer, C.L.2    Lamb, C.J.3    Schuch, W.4    Dixon, R.A.5
  • 17
    • 0031595211 scopus 로고    scopus 로고
    • 2-generating oxalate oxidase gene expression during wheat embryo germination
    • 2-generating oxalate oxidase gene expression during wheat embryo germination. Plant J. 15:165-71
    • (1998) Plant J. , vol.15 , pp. 165-171
    • Caliskan, M.1    Cuming, A.C.2
  • 18
    • 0030021535 scopus 로고    scopus 로고
    • Variation in lignin content and composition. Mechanisms of control and implications for the genetic improvement of plants
    • Campbell MM, Sederoff RR. 1996. Variation in lignin content and composition. Mechanisms of control and implications for the genetic improvement of plants. Plant Physiol. 110:3-13
    • (1996) Plant Physiol. , vol.110 , pp. 3-13
    • Campbell, M.M.1    Sederoff, R.R.2
  • 20
    • 0345425797 scopus 로고    scopus 로고
    • Molecular cloning and tissue-specific expression of an anionic peroxidase in zucchini
    • Carpin S, Crèvecoeur M, Greppin H, Penel C. 1999. Molecular cloning and tissue-specific expression of an anionic peroxidase in zucchini. Plant Physiol 120:799-810
    • (1999) Plant Physiol , vol.120 , pp. 799-810
    • Carpin, S.1    Crèvecoeur, M.2    Greppin, H.3    Penel, C.4
  • 21
    • 0027351945 scopus 로고
    • Structural models of primary cell walls in flowering plants: Consistency of molecular structure with the physical properties of the walls during growth
    • Carpita NC, Gibeaut DM. 1993. Structural models of primary cell walls in flowering plants: consistency of molecular structure with the physical properties of the walls during growth. Plant J. 3:1-30
    • (1993) Plant J. , vol.3 , pp. 1-30
    • Carpita, N.C.1    Gibeaut, D.M.2
  • 22
    • 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 JM, Ralph J, et al. 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. 28:257-70
    • (2001) Plant J. , vol.28 , pp. 257-270
    • Chabannes, M.1    Barakate, A.2    Lapierre, C.3    Marita, J.M.4    Ralph, J.5
  • 23
    • 0035162622 scopus 로고    scopus 로고
    • In situ analysis of lignins in transgenic tobacco reveals a differential impact of individual transformations on the spatial patterns of lignin deposition at the cellular and subcellular levels
    • Chabannes M, Ruel K, Yoshinaga A, Chabbert B, Jauneau A, et al. 2001. In situ analysis of lignins in transgenic tobacco reveals a differential impact of individual transformations on the spatial patterns of lignin deposition at the cellular and subcellular levels. Plant J. 28:271-82
    • (2001) Plant J. , vol.28 , pp. 271-282
    • Chabannes, M.1    Ruel, K.2    Yoshinaga, A.3    Chabbert, B.4    Jauneau, A.5
  • 24
    • 0028003226 scopus 로고
    • Biological variability in lignification of maize: Expression of the brown midrib bm2 mutation
    • Chabbert B, Tollier MT, Monties B, Barrière Y, Argillier O. 1994. Biological variability in lignification of maize: expression of the brown midrib bm2 mutation. J. Sci. Food Agric. 64:455-60
    • (1994) J. Sci. Food Agric. , vol.64 , pp. 455-460
    • Chabbert, B.1    Tollier, M.T.2    Monties, B.3    Barrière, Y.4    Argillier, O.5
  • 25
    • 0031766440 scopus 로고    scopus 로고
    • Molecular-genetic analysis of plant cytochrome P450-dependent monooxygenases
    • Chapple C. 1998. Molecular-genetic analysis of plant cytochrome P450-dependent monooxygenases. Annu. Rev. Plant Physiol. Plant Mol. Biol. 49:311-43
    • (1998) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.49 , pp. 311-343
    • Chapple, C.1
  • 26
    • 0026947812 scopus 로고
    • An Arabidopsis mutant defective in the general phenylpropanoid pathway
    • Chapple CCS, Vogt T, Ellis BE, Somerville CR. 1992. An Arabidopsis mutant defective in the general phenylpropanoid pathway. Plant Cell 4:1413-24
    • (1992) Plant Cell , vol.4 , pp. 1413-1424
    • Chapple, C.C.S.1    Vogt, T.2    Ellis, B.E.3    Somerville, C.R.4
  • 27
    • 18344410700 scopus 로고    scopus 로고
    • Cell-specific and conditional expression of caffeoyl-CoA O-methyltransferase in poplar
    • Chen C, Meyermans H, Burggraeve B, De Rycke RM, Inoue K, et al. 2000. Cell-specific and conditional expression of caffeoyl-CoA O-methyltransferase in poplar. Plant Physiol. 123:853-67
    • (2000) Plant Physiol. , vol.123 , pp. 853-867
    • Chen, C.1    Meyermans, H.2    Burggraeve, B.3    De Rycke, R.M.4    Inoue, K.5
  • 28
    • 0035818763 scopus 로고    scopus 로고
    • Chemical synthesis of caffeoyl and 5-OH coniferyl aldehydes and alcohols and determination of lignin O-methyltransferase activities in dicot and monocot species
    • Chen F, Kota P, Blount JW, Dixon RA. 2001. Chemical synthesis of caffeoyl and 5-OH coniferyl aldehydes and alcohols and determination of lignin O-methyltransferase activities in dicot and monocot species. Phytochemistry 58:1035-42
    • (2001) Phytochemistry , vol.58 , pp. 1035-1042
    • Chen, F.1    Kota, P.2    Blount, J.W.3    Dixon, R.A.4
  • 29
    • 0033064130 scopus 로고    scopus 로고
    • Evidence for a novel biosynthetic pathway that regulates the ratio of syringyl to guaiacyl residues in lignin in the differentiating xylem of Magnolia kobus DC
    • Chen F, Yasuda S, Fukushima K. 1999. Evidence for a novel biosynthetic pathway that regulates the ratio of syringyl to guaiacyl residues in lignin in the differentiating xylem of Magnolia kobus DC. Planta 207:597-603
    • (1999) Planta , vol.207 , pp. 597-603
    • Chen, F.1    Yasuda, S.2    Fukushima, K.3
  • 30
    • 0000830127 scopus 로고    scopus 로고
    • Control of lignin biosynthesis
    • Molecular Biology of Woody Plants, Volume 1, ed. SM Jain, SC Minocha, Dordrecht: Kluwer. 520 pp.
    • Christensen JH, Baucher M, O'Connell AP, Van Montagu M, Boerjan W. 2000. Control of lignin biosynthesis. In Molecular Biology of Woody Plants, Volume 1, ed. SM Jain, SC Minocha, For. Sci., 64:227-67. Dordrecht: Kluwer. 520 pp.
    • (2000) For. Sci. , vol.64 , pp. 227-267
    • Christensen, J.H.1    Baucher, M.2    O'Connell, A.P.3    Van Montagu, M.4    Boerjan, W.5
  • 31
    • 0035165908 scopus 로고    scopus 로고
    • The syringaldazine-oxidizing peroxidase PXP 3-4 from poplar xylem: CDNA isolation, characterization and expression
    • Christensen JH, Overney S, Rohde A, Ardiles Diaz W, Bauw G, et al. 2001. The syringaldazine-oxidizing peroxidase PXP 3-4 from poplar xylem: cDNA isolation, characterization and expression. Plant Mol. Biol 47:581-93
    • (2001) Plant Mol. Biol , vol.47 , pp. 581-593
    • Christensen, J.H.1    Overney, S.2    Rohde, A.3    Ardiles Diaz, W.4    Bauw, G.5
  • 32
    • 0034130986 scopus 로고    scopus 로고
    • Dirigent proteins and dirigent sites explain the mystery of specificity of radial precursor coupling in lignan and lignin biosynthesis
    • Davin LB, Lewis NG. 2000. Dirigent proteins and dirigent sites explain the mystery of specificity of radial precursor coupling in lignan and lignin biosynthesis. Plant Physiol. 123:453-61
    • (2000) Plant Physiol. , vol.123 , pp. 453-461
    • Davin, L.B.1    Lewis, N.G.2
  • 33
    • 0031031957 scopus 로고    scopus 로고
    • Stereo-selective bimolecular phenoxy radical coupling by an auxiliary (dirigent) protein without an active center
    • Davin LB, Wang H-B, Crowell AL, Bedgar DL, Martin DM, et al. 1997. Stereo-selective bimolecular phenoxy radical coupling by an auxiliary (dirigent) protein without an active center. Science 275:362-66
    • (1997) Science , vol.275 , pp. 362-366
    • Davin, L.B.1    Wang, H.-B.2    Crowell, A.L.3    Bedgar, D.L.4    Martin, D.M.5
  • 34
    • 0542444144 scopus 로고    scopus 로고
    • Laccases associate with lignifying vascular tissues
    • (ACS Symp. Series), ed. NG Lewis, S Sarkanen, Washington, DC: Am. Chem. Soc. 436 pp.
    • Dean JFD, LaFayette PR, Rugh C, Tristram AH, Hoopes JT, et al. 1998. Laccases associate with lignifying vascular tissues. In Lignin and Lignan Biosynthesis (ACS Symp. Series), ed. NG Lewis, S Sarkanen, 697:96-108. Washington, DC: Am. Chem. Soc. 436 pp.
    • (1998) Lignin and Lignan Biosynthesis , vol.697 , pp. 96-108
    • Dean, J.F.D.1    LaFayette, P.R.2    Rugh, C.3    Tristram, A.H.4    Hoopes, J.T.5
  • 35
    • 0029240490 scopus 로고
    • A β-glucosidase from lodgepole pine xylem specific for the lignin precursor coniferin
    • Dharmawardhana DP, Ellis BE, Carlson JE. 1995. A β-glucosidase from lodgepole pine xylem specific for the lignin precursor coniferin. Plant Physiol. 107: 331-39
    • (1995) Plant Physiol. , vol.107 , pp. 331-339
    • Dharmawardhana, D.P.1    Ellis, B.E.2    Carlson, J.E.3
  • 36
    • 0033137091 scopus 로고    scopus 로고
    • cDNA cloning and heterologous expression of coniferin β-glucosidase
    • Dharmawardhana DP, Ellis BE, Carlson JE. 1999. cDNA cloning and heterologous expression of coniferin β-glucosidase. Plant Mol. Biol. 40:365-72
    • (1999) Plant Mol. Biol. , vol.40 , pp. 365-372
    • Dharmawardhana, D.P.1    Ellis, B.E.2    Carlson, J.E.3
  • 37
    • 0035832807 scopus 로고    scopus 로고
    • The biosynthesis of monolignols: A "metabolic grid," or independant pathways to guaiacyl and syringyl units?
    • Dixon RA, Chen F, Guo D, Parvathi K. 2001. The biosynthesis of monolignols: a "metabolic grid," or independant pathways to guaiacyl and syringyl units? Phytochemistry 57:1069-84
    • (2001) Phytochemistry , vol.57 , pp. 1069-1084
    • Dixon, R.A.1    Chen, F.2    Guo, D.3    Parvathi, K.4
  • 38
    • 0035800123 scopus 로고    scopus 로고
    • Lignification and lignin topochemistry - An ultrastructural view
    • Donaldson LA. 2001. Lignification and lignin topochemistry - an ultrastructural view. Phytochemistry 57:859-73
    • (2001) Phytochemistry , vol.57 , pp. 859-873
    • Donaldson, L.A.1
  • 39
    • 0002075691 scopus 로고
    • Characterization and localization of laccase forms in stem and cell cultures of sycomore
    • Driouich A, Lainé A-C, Vian B, Faye L. 1992. Characterization and localization of laccase forms in stem and cell cultures of sycomore. Plant J. 2:13-24
    • (1992) Plant J. , vol.2 , pp. 13-24
    • Driouich, A.1    Lainé, A.-C.2    Vian, B.3    Faye, L.4
  • 40
    • 0039552100 scopus 로고    scopus 로고
    • Three 4-coumarate:coenzyme A ligases in Arabidopsis thaliana represent two evolutionarily divergent classes in angiosperms
    • Ehlting J, Büttner D, Wang Q, Douglas CJ, Somssich IE, Kombrink E. 1999. Three 4-coumarate:coenzyme A ligases in Arabidopsis thaliana represent two evolutionarily divergent classes in angiosperms. Plant J. 19:9-20
    • (1999) Plant J. , vol.19 , pp. 9-20
    • Ehlting, J.1    Büttner, D.2    Wang, Q.3    Douglas, C.J.4    Somssich, I.E.5    Kombrink, E.6
  • 42
    • 0034772307 scopus 로고    scopus 로고
    • Overexpression of the endogenous peroxidase-like gene spi 2 in transgenic Norway spruce plants results in increased total peroxidase activity and reduced growth
    • Elfstrand M, Fossdal CG, Sitbon F, Olsson O, Lönneberg A, von Arnold S. 2001. Overexpression of the endogenous peroxidase-like gene spi 2 in transgenic Norway spruce plants results in increased total peroxidase activity and reduced growth. Plant Cell Rep. 20: 596-603
    • (2001) Plant Cell Rep. , vol.20 , pp. 596-603
    • Elfstrand, M.1    Fossdal, C.G.2    Sitbon, F.3    Olsson, O.4    Lönneberg, A.5    Von Arnold, S.6
  • 43
    • 0347997281 scopus 로고    scopus 로고
    • Altered lignin structure and resistance to pathogens in spi 2-expressing tobacco plants
    • Elfstrand M, Sitbon F, Lapierre C, Bottin A, von Arnold S. 2002. Altered lignin structure and resistance to pathogens in spi 2-expressing tobacco plants. Planta 214:708-16
    • (2002) Planta , vol.214 , pp. 708-716
    • Elfstrand, M.1    Sitbon, F.2    Lapierre, C.3    Bottin, A.4    Von Arnold, S.5
  • 44
    • 0025204325 scopus 로고
    • Abnormal plant development and down-regulation of phenylpropanoid biosynthesis in transgenic tobacco containing a heterologous phenylalanine ammonia-lyase gene
    • Elkind Y, Edwards R, Mavandad M, Hedrick SA, Ribak O, et al. 1990. Abnormal plant development and down-regulation of phenylpropanoid biosynthesis in transgenic tobacco containing a heterologous phenylalanine ammonia-lyase gene. Proc. Natl. Acad. Sci. USA 87:9057-61
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 9057-9061
    • Elkind, Y.1    Edwards, R.2    Mavandad, M.3    Hedrick, S.A.4    Ribak, O.5
  • 45
    • 84941843939 scopus 로고
    • The location of guaiacyl and syringyl lignins in birch xylem tissue
    • Fergus BJ, Goring DAI. 1970. The location of guaiacyl and syringyl lignins in birch xylem tissue. Holzforschung 24:113-17
    • (1970) Holzforschung , vol.24 , pp. 113-117
    • Fergus, B.J.1    Goring, D.A.I.2
  • 47
    • 0036011028 scopus 로고    scopus 로고
    • Changes in secondary metabolism and deposition of an unusual lignin in the ref8 mutant of Arabidopsis
    • Franke R, Hemm MR, Denault JW, Ruegger MO, Humphreys JM, Chapple C. 2002. Changes in secondary metabolism and deposition of an unusual lignin in the ref8 mutant of Arabidopsis. Plant J. 30:47-59
    • (2002) Plant J. , vol.30 , pp. 47-59
    • Franke, R.1    Hemm, M.R.2    Denault, J.W.3    Ruegger, M.O.4    Humphreys, J.M.5    Chapple, C.6
  • 48
    • 0036011027 scopus 로고    scopus 로고
    • The Arabidopsis REF8 gene encodes the 3-hydroxylase of phenylpropanoid metabolism
    • Franke R, Humphreys JM, Hemm MR, Denault JW, Ruegger MO, et al. 2002. The Arabidopsis REF8 gene encodes the 3-hydroxylase of phenylpropanoid metabolism. Plant J. 30:33-45
    • (2002) Plant J. , vol.30 , pp. 33-45
    • Franke, R.1    Humphreys, J.M.2    Hemm, M.R.3    Denault, J.W.4    Ruegger, M.O.5
  • 49
    • 0034031635 scopus 로고    scopus 로고
    • Modified lignin in tobacco and poplar plants over-expressing the Arabidopsis gene encoding ferulate 5-hydroxylase
    • Franke R, McMichael CM, Meyer K, Shirley AM, Cusumano JC, Chapple C. 2000. Modified lignin in tobacco and poplar plants over-expressing the Arabidopsis gene encoding ferulate 5-hydroxylase. Plant J. 22:223-34
    • (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
  • 50
    • 0000816896 scopus 로고
    • Beiträge zur Erforschung des Lignins
    • Freudenberg K. 1956. Beiträge zur Erforschung des Lignins. Angew. Chem. 68:508-12
    • (1956) Angew. Chem. , vol.68 , pp. 508-512
    • Freudenberg, K.1
  • 53
    • 0001493387 scopus 로고    scopus 로고
    • p-hydroxyphenyl, guaiacyl, and syringyl lignins have similar inhibitory effects on wall degradability
    • Grabber JH, Ralph J, Hatfield RD, Quideau S. 1997. p-hydroxyphenyl, guaiacyl, and syringyl lignins have similar inhibitory effects on wall degradability. J. Agric. Food Chem. 45:2530-32
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 2530-2532
    • Grabber, J.H.1    Ralph, J.2    Hatfield, R.D.3    Quideau, S.4
  • 54
    • 0030911080 scopus 로고    scopus 로고
    • Dehydrogenative polymerization of coniferyl alcohol on macromolecular lignin templates
    • Guan S-Y, Mlynár J, Sarkanen S. 1997. Dehydrogenative polymerization of coniferyl alcohol on macromolecular lignin templates. Phytochemistry 45: 911-18
    • (1997) Phytochemistry , vol.45 , pp. 911-918
    • Guan, S.-Y.1    Mlynár, J.2    Sarkanen, S.3
  • 55
    • 0036855457 scopus 로고    scopus 로고
    • Monolignol biosynthesis in microsomal preparations from lignifying stems of alfalfa (Medicago saliva L.)
    • Guo D, Chen F, Dixon RA. 2002. Monolignol biosynthesis in microsomal preparations from lignifying stems of alfalfa (Medicago saliva L.). Phytochemistry 61:657-67
    • (2002) Phytochemistry , vol.61 , pp. 657-667
    • Guo, D.1    Chen, F.2    Dixon, R.A.3
  • 56
    • 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 JW, Dixon RA. 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
  • 57
    • 0034779150 scopus 로고    scopus 로고
    • Improvement of in-rumen digestibility of alfalfa forage by genetic manipulation of lignin O-methyltransferases
    • Guo D, Chen F, Wheeler J, Winder J, Selman S, et al. 2001. Improvement of in-rumen digestibility of alfalfa forage by genetic manipulation of lignin O-methyltransferases. Transgenic Res. 10:457-64
    • (2001) Transgenic Res. , vol.10 , pp. 457-464
    • Guo, D.1    Chen, F.2    Wheeler, J.3    Winder, J.4    Selman, S.5
  • 58
    • 0032102476 scopus 로고    scopus 로고
    • Brown-midrib maize (bml) - A mutation affecting the cinnamyl alcohol dehydrogenase gene
    • Halpin C, Holt K, Chojecki J, Oliver D, Chabbert B, et al. 1998. Brown-midrib maize (bml) - a mutation affecting the cinnamyl alcohol dehydrogenase gene. Plant J. 14:545-53
    • (1998) Plant J. , vol.14 , pp. 545-553
    • Halpin, C.1    Holt, K.2    Chojecki, J.3    Oliver, D.4    Chabbert, B.5
  • 59
    • 0027954821 scopus 로고
    • Manipulation of lignin quality by down-regulation of cinnamyl alcohol dehydrogenase
    • Halpin C, Knight ME, Foxon GA, Campbell MM, Boudet AM, et al. 1994. Manipulation of lignin quality by down-regulation of cinnamyl alcohol dehydrogenase. Plant J. 6:339-50
    • (1994) Plant J. , vol.6 , pp. 339-350
    • Halpin, C.1    Knight, M.E.2    Foxon, G.A.3    Campbell, M.M.4    Boudet, A.M.5
  • 60
    • 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 SA, Leshkevich J, Chiang VL, 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. 128:428-38
    • (2002) Plant Physiol. , vol.128 , pp. 428-438
    • Harding, S.A.1    Leshkevich, J.2    Chiang, V.L.3    Tsai, C.-J.4
  • 61
    • 2942575667 scopus 로고    scopus 로고
    • A potential role of sinapyl p-coummarate in grass lignin formation
    • Abstr. #346
    • Hatfield RD, Grabber J, Ralph J. 1997. A potential role of sinapylp-coummarate in grass lignin formation. Plant Physiol. Suppl. 114:86 (Abstr. #346)
    • (1997) Plant Physiol. Suppl. , vol.114 , pp. 86
    • Hatfield, R.D.1    Grabber, J.2    Ralph, J.3
  • 62
    • 0034869281 scopus 로고    scopus 로고
    • Lignin formation in plants. The dilemma of linkage specificity
    • Hatfield R, Vermerris W. 2001. Lignin formation in plants. The dilemma of linkage specificity. Plant Physiol. 126:1351-57
    • (2001) Plant Physiol. , vol.126 , pp. 1351-1357
    • Hatfield, R.1    Vermerris, W.2
  • 63
    • 0000402528 scopus 로고
    • Formation and structure of lignin in monocotyledons. IV. Deposition process and structural diversity of the lignin in the cell wall of sugarcane and rice plant studied by ultraviolet microscopic spectroscopy
    • He L, Terashima N. 1991. Formation and structure of lignin in monocotyledons. IV. Deposition process and structural diversity of the lignin in the cell wall of sugarcane and rice plant studied by ultraviolet microscopic spectroscopy. Holzforschung 45:191-98
    • (1991) Holzforschung , vol.45 , pp. 191-198
    • He, L.1    Terashima, N.2
  • 64
    • 85007845296 scopus 로고
    • Increase of cinnamaldehyde groups in lignin of transgenic tobacco plants carrying an antisense gene for cinnamyl alcohol dehydrogenase
    • Hibino T, Takabe K, Kawazu T, Shibata D, Higuchi T. 1995. Increase of cinnamaldehyde groups in lignin of transgenic tobacco plants carrying an antisense gene for cinnamyl alcohol dehydrogenase. Biosci. Biotech. Biochem. 59:929-31
    • (1995) Biosci. Biotech. Biochem. , vol.59 , pp. 929-931
    • Hibino, T.1    Takabe, K.2    Kawazu, T.3    Shibata, D.4    Higuchi, T.5
  • 65
    • 0028500726 scopus 로고
    • Red-brown coloration of lignified tissues of transgenic plants with antisense CAD gene: Wine-red lignin from coniferaldehyde
    • Higuchi T, Ito T, Umezawa T, Hibino T, Shibata D. 1994. Red-brown coloration of lignified tissues of transgenic plants with antisense CAD gene: wine-red lignin from coniferaldehyde. J. Biotechnol. 37:151-58
    • (1994) J. Biotechnol. , vol.37 , pp. 151-158
    • Higuchi, T.1    Ito, T.2    Umezawa, T.3    Hibino, T.4    Shibata, D.5
  • 66
    • 0037414824 scopus 로고    scopus 로고
    • Purification, cloning and properties of an acyltransferase controlling shikimate and quinate ester intermediates in phenylpropanoid metabolism
    • Hoffmann L, Maury S, Martz F, Geoffrey P, Legrand M. 2002. Purification, cloning and properties of an acyltransferase controlling shikimate and quinate ester intermediates in phenylpropanoid metabolism. J. Biol. Chem. 278:95-103
    • (2002) J. Biol. Chem. , vol.278 , pp. 95-103
    • Hoffmann, L.1    Maury, S.2    Martz, F.3    Geoffrey, P.4    Legrand, M.5
  • 67
    • 0034789027 scopus 로고    scopus 로고
    • Progress of lignification mediated by intercellular transportation of monolignols during tracheary element differentiation of isolated Zinnia mesophyll cells
    • Hosokawa M, Suzuki S, Umezawa T, Sato Y. 2001. Progress of lignification mediated by intercellular transportation of monolignols during tracheary element differentiation of isolated Zinnia mesophyll cells. Plant Cell Physiol 42:959-68
    • (2001) Plant Cell Physiol , vol.42 , pp. 959-968
    • Hosokawa, M.1    Suzuki, S.2    Umezawa, T.3    Sato, Y.4
  • 68
    • 0030468571 scopus 로고    scopus 로고
    • Overexpression of L-phenylalanine ammonialyase in transgenic tobacco plants reveals control points for flux into phenylpropanoid biosynthesis
    • Howles PA, Sewalt VJH, Paiva NL, Elkind Y, Bate NJ, et al. 1996. Overexpression of L-phenylalanine ammonialyase in transgenic tobacco plants reveals control points for flux into phenylpropanoid biosynthesis. Plant Physiol. 112:1617-24
    • (1996) Plant Physiol. , vol.112 , pp. 1617-1624
    • Howles, P.A.1    Sewalt, V.J.H.2    Paiva, N.L.3    Elkind, Y.4    Bate, N.J.5
  • 69
    • 0032868744 scopus 로고    scopus 로고
    • Repression of lignin biosynthesis promotes cellulose accumulation and growth in transgenic trees
    • Hu W-J, Harding SA, Lung J, Popko JL, Ralph J, et al. 1999. Repression of lignin biosynthesis promotes cellulose accumulation and growth in transgenic trees. Nat. Biotechnol. 17:808-12
    • (1999) Nat. Biotechnol. , vol.17 , pp. 808-812
    • Hu, W.-J.1    Harding, S.A.2    Lung, J.3    Popko, J.L.4    Ralph, J.5
  • 70
    • 0032574720 scopus 로고    scopus 로고
    • Compartmentalized expression of two structurally and functionally distinct 4-coumarate: CoA ligase genes in aspen Populus tremuloides
    • Hu W-J, Kawaoka A, Tsai C-J, Lung J, Osakabe K, et al. 1998. Compartmentalized expression of two structurally and functionally distinct 4-coumarate: CoA ligase genes in aspen Populus tremuloides. Proc. Natl. Acad. Sci. USA 95:5407-12
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5407-5412
    • Hu, W.-J.1    Kawaoka, A.2    Tsai, C.-J.3    Lung, J.4    Osakabe, K.5
  • 72
    • 0033621061 scopus 로고    scopus 로고
    • New routes for lignin biosynthesis defined by biochemical characterization of recombinant ferulate 5-hydroxylase, a multifunctional cytochrome P450-dependent monooxygenase
    • Humphreys JM, Hemm MR, Chapple C. 1999. New routes for lignin biosynthesis defined by biochemical characterization of recombinant ferulate 5-hydroxylase, a multifunctional cytochrome P450-dependent monooxygenase. Proc. Natl. Acad. Sci. USA 96:10045-50
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10045-10050
    • Humphreys, J.M.1    Hemm, M.R.2    Chapple, C.3
  • 73
    • 0030793569 scopus 로고    scopus 로고
    • Structure and functions of feruloylated polysaccharides
    • Ishii T. 1997. Structure and functions of feruloylated polysaccharides. Plant Sci. 127:111-27
    • (1997) Plant Sci. , vol.127 , pp. 111-127
    • Ishii, T.1
  • 74
    • 0034669209 scopus 로고    scopus 로고
    • Transcriptional repression by AtMYB4 controls production of UV-protecting sunscreens in Arabidopsis
    • Jin H, Cominelli E, Bailey P, Parr A, Mehrtens F, et al. 2000. Transcriptional repression by AtMYB4 controls production of UV-protecting sunscreens in Arabidopsis. EMBO J. 19:6150-61
    • (2000) EMBO J. , vol.19 , pp. 6150-6161
    • Jin, H.1    Cominelli, E.2    Bailey, P.3    Parr, A.4    Mehrtens, F.5
  • 75
    • 0034967467 scopus 로고    scopus 로고
    • Cloning and characterization of irregular xylem4 (irx4): A severely lignin-deficient mutant of Arabidopsis
    • Jones L, Ennos AR, Turner SR. 2001. Cloning and characterization of irregular xylem4 (irx4): a severely lignin-deficient mutant of Arabidopsis. Plant J. 26:205-16
    • (2001) Plant J. , vol.26 , pp. 205-216
    • Jones, L.1    Ennos, A.R.2    Turner, S.R.3
  • 76
    • 0031177709 scopus 로고    scopus 로고
    • 13C-nuclear magnetic resonance spectroscopy and immunocytochemical transmission electron microscopy
    • 13C-nuclear magnetic resonance spectroscopy and immunocytochemical transmission electron microscopy. Plant Physiol. 114:1123-33
    • (1997) Plant Physiol. , vol.114 , pp. 1123-1133
    • Joseleau, J.-P.1    Ruel, K.2
  • 77
    • 0033844861 scopus 로고    scopus 로고
    • Lignification in transgenic poplars with extremely reduced caffeic acid O-methyltransferase activity
    • Jouanin L, Goujon T, de Nadaï V, Martin M-T, Mila I, et al. 2000. Lignification in transgenic poplars with extremely reduced caffeic acid O-methyltransferase activity. Plant Physiol. 123:1363-73
    • (2000) Plant Physiol. , vol.123 , pp. 1363-1373
    • Jouanin, L.1    Goujon, T.2    De Nadaï, V.3    Martin, M.-T.4    Mila, I.5
  • 78
    • 0031397319 scopus 로고    scopus 로고
    • Structural characterization of modified lignin in transgenic tobacco plants in which the activity of 4-coumarate: Coenzyme A ligase is depressed
    • Kajita S, Hishiyama S, Tomimura Y, Katayama Y, Omori S. 1997. Structural characterization of modified lignin in transgenic tobacco plants in which the activity of 4-coumarate: coenzyme A ligase is depressed. Plant Physiol. 114:871-79
    • (1997) Plant Physiol. , vol.114 , pp. 871-879
    • Kajita, S.1    Hishiyama, S.2    Tomimura, Y.3    Katayama, Y.4    Omori, S.5
  • 79
    • 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, Omori S. 1996. Alterations in the biosynthesis of lignin in transgenic plants with chimeric genes for 4-coumarate:coenzyme A ligase. Plant Cell Physiol. 37:957-65
    • (1996) Plant Cell Physiol. , vol.37 , pp. 957-965
    • Kajita, S.1    Katayama, Y.2    Omori, S.3
  • 80
    • 0000108442 scopus 로고
    • Specific localization of a plant cell wall glycine-rich protein in protoxylem cells of the vascular system
    • Keller B, Templeton MD, Lamb CJ. 1989. Specific localization of a plant cell wall glycine-rich protein in protoxylem cells of the vascular system. Proc. Natl. Acad. Sci. USA 86:1529-33
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 1529-1533
    • Keller, B.1    Templeton, M.D.2    Lamb, C.J.3
  • 81
    • 0037033009 scopus 로고    scopus 로고
    • Identification of the structure and origin of thioacidolysis marker compounds for cinnamyl alcohol dehydrogenase deficiency in angiosperms
    • Kim H, Ralph J, Lu F, Pilate G, Leplé JC, et al. 2002. Identification of the structure and origin of thioacidolysis marker compounds for cinnamyl alcohol dehydrogenase deficiency in angiosperms. J. Biol. Chem. 277:47412-19
    • (2002) J. Biol. Chem. , vol.277 , pp. 47412-47419
    • Kim, H.1    Ralph, J.2    Lu, F.3    Pilate, G.4    Leplé, J.C.5
  • 82
    • 0017349585 scopus 로고
    • trans-cinnamic acid as a mediator of the light-stimulated increase in hydroxycinnamoyl-CoA: Quinate hydroxycinnamoyl transferase
    • Lamb CJ. 1977. trans-cinnamic acid as a mediator of the light-stimulated increase in hydroxycinnamoyl-CoA: quinate hydroxycinnamoyl transferase. FEBS Lett. 75:37-40
    • (1977) FEBS Lett. , vol.75 , pp. 37-40
    • Lamb, C.J.1
  • 83
    • 0032840888 scopus 로고    scopus 로고
    • Structural alterations of lignins in transgenic poplars with depressed cinnamyl alcohol dehydrogenase or caffeic acid O-methyltransferase activity have opposite impact on the efficiency of industrial Kraft pulping
    • Lapierre C, Pollet B, Petit-Conil M, Toval G, Romero J, et al. 1999. Structural alterations of lignins in transgenic poplars with depressed cinnamyl alcohol dehydrogenase or caffeic acid O-methyltransferase activity have opposite impact on the efficiency of industrial Kraft pulping. Plant Physiol. 119:153-63
    • (1999) Plant Physiol. , vol.119 , pp. 153-163
    • Lapierre, C.1    Pollet, B.2    Petit-Conil, M.3    Toval, G.4    Romero, J.5
  • 84
    • 0035832861 scopus 로고    scopus 로고
    • Two cinnamoyl-CoA reductase (CCR) genes from Arabidopsis thaliana are differentially expressed during development and in response to infection with pathogenic bacteria
    • Lauvergeat V, Lacomme C, Lacombe E, Lasserre E, Roby D, Grima-Pettenati J. 2001. Two cinnamoyl-CoA reductase (CCR) genes from Arabidopsis thaliana are differentially expressed during development and in response to infection with pathogenic bacteria. Phytochemistry 57:1187-95
    • (2001) Phytochemistry , vol.57 , pp. 1187-1195
    • Lauvergeat, V.1    Lacomme, C.2    Lacombe, E.3    Lasserre, E.4    Roby, D.5    Grima-Pettenati, J.6
  • 85
    • 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, Douglas CJ. 1997. Antisense suppression of 4-coumarate: coenzyme A ligase activity in Arabidopsis leads to altered lignin subunit composition. Plant Cell 9:1985-98
    • (1997) Plant Cell , vol.9 , pp. 1985-1998
    • Lee, D.1    Meyer, K.2    Chapple, C.3    Douglas, C.J.4
  • 86
    • 0032588250 scopus 로고    scopus 로고
    • th century roller coaster ride: A short account of lignification
    • th century roller coaster ride: a short account of lignification. Curr. Opin. Plant Biol. 2:153-62
    • (1999) Curr. Opin. Plant Biol. , vol.2 , pp. 153-162
    • Lewis, N.G.1
  • 87
    • 0034927211 scopus 로고    scopus 로고
    • The last step of syringyl monolignol biosynthesis in angiosperms is regulated by a novel gene encoding sinapyl alcohol dehydrogenase
    • Li L, Cheng XF, Leshkevich J, Umezawa T, Hording SA, Chiang VL. 2001. The last step of syringyl monolignol biosynthesis in angiosperms is regulated by a novel gene encoding sinapyl alcohol dehydrogenase. Plant Cell 13:1567-85
    • (2001) Plant Cell , vol.13 , pp. 1567-1585
    • Li, L.1    Cheng, X.F.2    Leshkevich, J.3    Umezawa, T.4    Hording, S.A.5    Chiang, V.L.6
  • 88
    • 0034054073 scopus 로고    scopus 로고
    • 5-Hydroxyconiferyl aldehyde modulates enzymatic methylation for syringyl monolignol formation, a new view of monolignol biosynthesis in angiosperms
    • Li L, Popko JL, Umezawa T, Chiang VL. 2000. 5-Hydroxyconiferyl aldehyde modulates enzymatic methylation for syringyl monolignol formation, a new view of monolignol biosynthesis in angiosperms. J. Biol. Chem. 275:6537-45
    • (2000) J. Biol. Chem. , vol.275 , pp. 6537-6545
    • Li, L.1    Popko, J.L.2    Umezawa, T.3    Chiang, V.L.4
  • 89
    • 0035830864 scopus 로고    scopus 로고
    • Identification of glucosyltransferase genes involved in sinapate metabolism and lignin synthesis in Arabidopsis
    • Lim E-K, Li Y, Parr A, Jackson R, Ashford DA, Bowles DJ. 2001. Identification of glucosyltransferase genes involved in sinapate metabolism and lignin synthesis in Arabidopsis. J. Biol. Chem. 276:4344-49
    • (2001) J. Biol. Chem. , vol.276 , pp. 4344-4349
    • Lim, E.-K.1    Li, Y.2    Parr, A.3    Jackson, R.4    Ashford, D.A.5    Bowles, D.J.6
  • 90
    • 0036179613 scopus 로고    scopus 로고
    • Divergent members of a soybean (Glycine max L.) 4-coumarate:coenzyme A ligase gene family
    • Lindermayr C, Möllers B, Fliegmann J, Uhlmann A, Lottspeich F, et al. 2002. Divergent members of a soybean (Glycine max L.) 4-coumarate:coenzyme A ligase gene family. Eur. J. Biochem. 269:1304-15
    • (2002) Eur. J. Biochem. , vol.269 , pp. 1304-1315
    • Lindermayr, C.1    Möllers, B.2    Fliegmann, J.3    Uhlmann, A.4    Lottspeich, F.5
  • 91
    • 0032845294 scopus 로고    scopus 로고
    • Detection and determination of p-coumaroylated units in lignins
    • Lu F, Ralph J. 1999. Detection and determination of p-coumaroylated units in lignins. J. Agric. Food Chem. 47:1988-92
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 1988-1992
    • Lu, F.1    Ralph, J.2
  • 92
    • 0037033447 scopus 로고    scopus 로고
    • Preliminary evidence for sinapyl acetate as a lignin monomer in kenaf
    • Lu F, Ralph J. 2002. Preliminary evidence for sinapyl acetate as a lignin monomer in kenaf. Chem. Commun. (1):90-91
    • (2002) Chem. Commun. , Issue.1 , pp. 90-91
    • Lu, F.1    Ralph, J.2
  • 93
    • 0030759413 scopus 로고    scopus 로고
    • Inheritance, gene expression, and lignin characterization in a mutant pine deficient in cinnamyl alcohol dehydrogenase
    • MacKay JJ, O'Malley DM, Presnell T, Booker FL, Campbell MM, et al. 1997. Inheritance, gene expression, and lignin characterization in a mutant pine deficient in cinnamyl alcohol dehydrogenase. Proc. Natl. Acad Sci. USA 94:8255-60
    • (1997) Proc. Natl. Acad Sci. USA , vol.94 , pp. 8255-8260
    • MacKay, J.J.1    O'Malley, D.M.2    Presnell, T.3    Booker, F.L.4    Campbell, M.M.5
  • 94
    • 0033607210 scopus 로고    scopus 로고
    • NMR characterization of lignins in Arabidopsis altered in the activity of ferulate 5-hydroxylase
    • Marita JM, Ralph J, Hatfield RD, Chapple C. 1999. NMR characterization of lignins in Arabidopsis altered in the activity of ferulate 5-hydroxylase. Proc. Natl. Acad. Sci. USA 96:12328-32
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 12328-12332
    • Marita, J.M.1    Ralph, J.2    Hatfield, R.D.3    Chapple, C.4
  • 95
    • 0034015731 scopus 로고    scopus 로고
    • Conversion of guaiacyl to syringyl moieties on the cinnamyl alcohol pathway during the biosynthesis of lignin in angiosperms
    • Matsui N, Chen F, Yasuda S, Fukushima K. 2000. Conversion of guaiacyl to syringyl moieties on the cinnamyl alcohol pathway during the biosynthesis of lignin in angiosperms. Planta 210:831-35
    • (2000) Planta , vol.210 , pp. 831-835
    • Matsui, N.1    Chen, F.2    Yasuda, S.3    Fukushima, K.4
  • 96
    • 84942960316 scopus 로고
    • 3H at the hydroxymethyl group of side chain, and incorporation of the label into magnolia and ginkgo lignin
    • 3H at the hydroxymethyl group of side chain, and incorporation of the label into magnolia and ginkgo lignin. Holzforschung 48:375-80
    • (1994) Holzforschung , vol.48 , pp. 375-380
    • Matsui, N.1    Fukushima, K.2    Yasuda, S.3    Terashima, N.4
  • 97
    • 0001233460 scopus 로고
    • Effects of trans-cinnamic acid on expression of the bean phenylalanine ammonia-lyase gene family
    • Mavandad M, Edwards R, Liang X, Lamb CJ, Dixon RA. 1990. Effects of trans-cinnamic acid on expression of the bean phenylalanine ammonia-lyase gene family. Plant Physiol. 94:671-80
    • (1990) Plant Physiol. , vol.94 , pp. 671-680
    • Mavandad, M.1    Edwards, R.2    Liang, X.3    Lamb, C.J.4    Dixon, R.A.5
  • 98
    • 0032499766 scopus 로고    scopus 로고
    • Lignin monomer composition is determined by the expression of a cytochrome P450-dependent monooxygenase in Arabidopsis
    • Meyer K, Shirley AM, Cusumano JC, Bell-Lelong DA, Chapple C. 1998. Lignin monomer composition is determined by the expression of a cytochrome P450-dependent monooxygenase in Arabidopsis. Proc. Natl. Acad. Sci. USA 95:6619-23
    • (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
  • 99
    • 0034711291 scopus 로고    scopus 로고
    • Modification 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, Morreel K, Lapierre C, Pollet B, De Bruyn A, et al. 2000. Modification 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. 275:36899-909
    • (2000) J. Biol. Chem. , vol.275 , pp. 36899-36909
    • Meyermans, H.1    Morreel, K.2    Lapierre, C.3    Pollet, B.4    De Bruyn, A.5
  • 101
    • 0001017547 scopus 로고
    • Ester linkage of p-coumaric acid in bamboo lignin. II. Syntheses of coniferyl p-hydroxybenzoate and coniferyl p-coumarate as possible precursors of aromatic acid esters in lignin
    • Nakamura Y, Higuchi T. 1978. Ester linkage of p-coumaric acid in bamboo lignin. II. Syntheses of coniferyl p-hydroxybenzoate and coniferyl p-coumarate as possible precursors of aromatic acid esters in lignin. Cell. Chem. Technol. 12:199-208
    • (1978) Cell. Chem. Technol. , vol.12 , pp. 199-208
    • Nakamura, Y.1    Higuchi, T.2
  • 102
    • 0036742670 scopus 로고    scopus 로고
    • Arabidopsis CYP98A3 mediating aromatic 3-hydroxylation. Developmental regulation of the gene, and expression in yeast
    • Nair RB, Xia Q, Kartha CJ, Kurylo E, Hirji RN, Datla R, Selvaraj G. 2002. Arabidopsis CYP98A3 mediating aromatic 3-hydroxylation. Developmental regulation of the gene, and expression in yeast. Plant Physiol. 130:210-20
    • (2002) Plant Physiol. , vol.130 , pp. 210-220
    • Nair, R.B.1    Xia, Q.2    Kartha, C.J.3    Kurylo, E.4    Hirji, R.N.5    Datla, R.6    Selvaraj, G.7
  • 103
    • 6444244816 scopus 로고    scopus 로고
    • Improved paper pulp from plants with suppressed cinnamoyl-CoA reductase or cinnamyl alcohol dehydrogenase
    • O'Connell A, Holt K, Piquemal J, Grima-Pettenati J, Boudet A, et al. 2002. Improved paper pulp from plants with suppressed cinnamoyl-CoA reductase or cinnamyl alcohol dehydrogenase. Transgenic Res. 11:495-503
    • (2002) Transgenic Res. , vol.11 , pp. 495-503
    • O'Connell, A.1    Holt, K.2    Piquemal, J.3    Grima-Pettenati, J.4    Boudet, A.5
  • 104
    • 0031258492 scopus 로고    scopus 로고
    • Generation of superoxide anion and localization of CuZn-superoxide dismutase in the vascular tissue of spinach hypocotyls: Their association with lignification
    • Ogawa K, Kanematsu S, Asada K. 1997. Generation of superoxide anion and localization of CuZn-superoxide dismutase in the vascular tissue of spinach hypocotyls: their association with lignification. Plant Cell Physiol. 38:1118-26
    • (1997) Plant Cell Physiol. , vol.38 , pp. 1118-1126
    • Ogawa, K.1    Kanematsu, S.2    Asada, K.3
  • 105
    • 0036671747 scopus 로고    scopus 로고
    • Polymerization of monolignols by redox shuttle-mediated enzymatic oxidation: A new model in lignin biosynthesis. I
    • Önnerud H, Zhang L, Gellerstedt G, Henriksson G. 2002. Polymerization of monolignols by redox shuttle-mediated enzymatic oxidation: a new model in lignin biosynthesis. I. Plant Cell 14:1953-62
    • (2002) Plant Cell , vol.14 , pp. 1953-1962
    • Önnerud, H.1    Zhang, L.2    Gellerstedt, G.3    Henriksson, G.4
  • 106
    • 13044258871 scopus 로고    scopus 로고
    • Coniferyl aldehyde 5-hydroxylation and methylation direct syringyl lignin biosynthesis in angiosperms
    • Osakabe K, Tsao CC, Li L, Popko JL, Umezawa T, et al. 1999. Coniferyl aldehyde 5-hydroxylation and methylation direct syringyl lignin biosynthesis in angiosperms. Proc. Natl. Acad. Sci. USA 96:8955-60
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 8955-8960
    • Osakabe, K.1    Tsao, C.C.2    Li, L.3    Popko, J.L.4    Umezawa, T.5
  • 107
    • 0033671519 scopus 로고    scopus 로고
    • Arabidopsis ATP A2 peroxidase. Expression and high-resolution structure of a plant peroxidase with implications for lignification
    • Østergaard L, Teilum K, Mirza O, Mattsson O, Petersen M, et al. 2000. Arabidopsis ATP A2 peroxidase. Expression and high-resolution structure of a plant peroxidase with implications for lignification. Plant Mol. Biol. 44:231-43
    • (2000) Plant Mol. Biol. , vol.44 , pp. 231-243
    • Østergaard, L.1    Teilum, K.2    Mirza, O.3    Mattsson, O.4    Petersen, M.5
  • 108
    • 0035143813 scopus 로고    scopus 로고
    • Substrate preferences of O-methyltransferases in alfalfa suggest new pathways for 3-O-methylation of monolignols
    • Parvathi K, Chen F, Guo D, Blount JW, Dixon RA. 2001. Substrate preferences of O-methyltransferases in alfalfa suggest new pathways for 3-O-methylation of monolignols. Plant J. 25:193-202
    • (2001) Plant J. , vol.25 , pp. 193-202
    • Parvathi, K.1    Chen, F.2    Guo, D.3    Blount, J.W.4    Dixon, R.A.5
  • 109
    • 0029761728 scopus 로고    scopus 로고
    • Pectin binding proteins: Characterization of the binding and comparison with heparin
    • Penel C, Greppin H. 1996. Pectin binding proteins: characterization of the binding and comparison with heparin. Plant Physiol. Biochem. 34:479-88
    • (1996) Plant Physiol. Biochem. , vol.34 , pp. 479-488
    • Penel, C.1    Greppin, H.2
  • 110
    • 0000458713 scopus 로고
    • Xylem wall deposition. Radioautographic investigations using lignin precursors
    • Pickett-Heaps JD. 1968. Xylem wall deposition. Radioautographic investigations using lignin precursors. Protoplasma 65:181-205
    • (1968) Protoplasma , vol.65 , pp. 181-205
    • Pickett-Heaps, J.D.1
  • 111
    • 0035984719 scopus 로고    scopus 로고
    • Field and pulping performances of transgenic trees with altered lignification
    • Pilate G, Guiney E, Holt K, Petit-Conil M, Lapierre C, et al. 2002. Field and pulping performances of transgenic trees with altered lignification. Nat. Biotechnol. 20:607-12
    • (2002) Nat. Biotechnol. , vol.20 , pp. 607-612
    • Pilate, G.1    Guiney, E.2    Holt, K.3    Petit-Conil, M.4    Lapierre, C.5
  • 112
    • 0034978181 scopus 로고    scopus 로고
    • Simultaneous down-regulation of caffeic/5-hydroxy ferulic acid-O-methyltransferase I and cinnamoyl-coenzyme A reductase in the progeny from a cross between tobacco lines homozygous for each transgene. Consequences for plant development and lignin synthesis
    • Pinçon G, Chabannes M, Lapierre C, Pollet B, Ruel K, et al. 2001. Simultaneous down-regulation of caffeic/ 5-hydroxy ferulic acid-O- methyltransferase I and cinnamoyl-coenzyme A reductase in the progeny from a cross between tobacco lines homozygous for each transgene. Consequences for plant development and lignin synthesis. Plant Physiol. 126:145-55
    • (2001) Plant Physiol. , vol.126 , pp. 145-155
    • Pinçon, G.1    Chabannes, M.2    Lapierre, C.3    Pollet, B.4    Ruel, K.5
  • 113
    • 0035832880 scopus 로고    scopus 로고
    • Repression of O-methyltransferase genes in transgenic tobacco affects lignin synthesis and plant growth
    • Pinçon G, Maury S, Hoffmann L, Geoffroy P, Lapierre C, et al. 2001. Repression of O-methyltransferase genes in transgenic tobacco affects lignin synthesis and plant growth. Phytochemistry 57:1167-76
    • (2001) Phytochemistry , vol.57 , pp. 1167-1176
    • Pinçon, G.1    Maury, S.2    Hoffmann, L.3    Geoffroy, P.4    Lapierre, C.5
  • 114
    • 0031909507 scopus 로고    scopus 로고
    • Down-regulation in cinnamoyl-CoA reductase induces significant changes of lignin profiles in transgenic tobacco plants
    • Piquemal J, Lapierre C, Myton K, O'Connell A, Schuch W, et al. 1998. Down-regulation in cinnamoyl-CoA reductase induces significant changes of lignin profiles in transgenic tobacco plants. Plant J. 13:71-83
    • (1998) Plant J. , vol.13 , pp. 71-83
    • Piquemal, J.1    Lapierre, C.2    Myton, K.3    O'Connell, A.4    Schuch, W.5
  • 115
    • 12244269747 scopus 로고    scopus 로고
    • Down-regulation of caffeic acid O-methyltransferase in maize revisited using a transgenic approach
    • Piquemal J, Chamayou S, Nadaud I, Beckert M, Barrière Y, et al. 2002. Down-regulation of caffeic acid O-methyltransferase in maize revisited using a transgenic approach. Plant Physiol. 130:1675-85
    • (2002) Plant Physiol. , vol.130 , pp. 1675-1685
    • Piquemal, J.1    Chamayou, S.2    Nadaud, I.3    Beckert, M.4    Barrière, Y.5
  • 116
    • 0030897421 scopus 로고    scopus 로고
    • Characterisation of lignin from CAD and OMT deficient bm mutants of maize
    • Provan GJ, Scobbie L, Chesson A. 1997. Characterisation of lignin from CAD and OMT deficient bm mutants of maize. J. Sci. Food Agric. 73:133-42
    • (1997) J. Sci. Food Agric. , vol.73 , pp. 133-142
    • Provan, G.J.1    Scobbie, L.2    Chesson, A.3
  • 117
  • 118
    • 0029117332 scopus 로고
    • Lignin-ferulate crosslinks in grasses: Active incorporation of ferulate polysaccharide esters into ryegrass lignins
    • Ralph J, Grabber JH, Hatfield RD. 1995. Lignin-ferulate crosslinks in grasses: active incorporation of ferulate polysaccharide esters into ryegrass lignins. Carbohydr. Res. 275:167-78
    • (1995) Carbohydr. Res. , vol.275 , pp. 167-178
    • Ralph, J.1    Grabber, J.H.2    Hatfield, R.D.3
  • 119
    • 0032573185 scopus 로고    scopus 로고
    • NMR characterization of altered lignins extracted from tobacco plants down-regulated for lignification enzymes cinnamyl-alcohol dehydrogenase and cinnamoyl-CoA reductase
    • Ralph J, Hatfield RD, Piquemal J, Yahiaoui N, Pean M, et al. 1998. NMR characterization of altered lignins extracted from tobacco plants down-regulated for lignification enzymes cinnamyl-alcohol dehydrogenase and cinnamoyl-CoA reductase. Proc. Natl. Acad. Sci. USA 95:12803-8
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12803-12808
    • Ralph, J.1    Hatfield, R.D.2    Piquemal, J.3    Yahiaoui, N.4    Pean, M.5
  • 120
    • 0033614870 scopus 로고    scopus 로고
    • Arylpropane-1,3-diols in lignins from normal and CAD-deficient pines
    • Ralph J, Kim H, Peng J, Lu F. 1999. Arylpropane-1,3-diols in lignins from normal and CAD-deficient pines. Org. Lett. 1:323-26
    • (1999) Org. Lett. , vol.1 , pp. 323-326
    • Ralph, J.1    Kim, H.2    Peng, J.3    Lu, F.4
  • 121
    • 0035132582 scopus 로고    scopus 로고
    • NMR evidence for benzodioxane structures resulting from incorporation of 5-hydroxyconiferyl alcohol into lignins of O-methyltransferase-deficient plants
    • Ralph J, Lapierre C, Lu F, Marita JM, Pilate G, et al. 2001. NMR evidence for benzodioxane structures resulting from incorporation of 5-hydroxyconiferyl alcohol into lignins of O-methyltransferase-deficient plants. J. Agric. Food Chem. 49:86-91
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 86-91
    • Ralph, J.1    Lapierre, C.2    Lu, F.3    Marita, J.M.4    Pilate, G.5
  • 122
    • 0035800125 scopus 로고    scopus 로고
    • Elucidation of new structures in lignins of CAD- and COMT-deficient plants by NMR
    • Ralph J, Lapierre C, Marita JM, Kim H, Lu F, et al. 2001. Elucidation of new structures in lignins of CAD-and COMT-deficient plants by NMR. Phytochemistry 57:993-1003
    • (2001) Phytochemistry , vol.57 , pp. 993-1003
    • Ralph, J.1    Lapierre, C.2    Marita, J.M.3    Kim, H.4    Lu, F.5
  • 125
    • 0036000026 scopus 로고    scopus 로고
    • Laccase down-regulation causes alterations in phenolic metabolism and cell wall structure in poplar
    • Ranocha P, Chabannes M, Chamayou S, Danoun S, Jauneau A, et al. 2002. Laccase down-regulation causes alterations in phenolic metabolism and cell wall structure in poplar. Plant Physiol. 129:145-55
    • (2002) Plant Physiol. , vol.129 , pp. 145-155
    • Ranocha, P.1    Chabannes, M.2    Chamayou, S.3    Danoun, S.4    Jauneau, A.5
  • 126
    • 0033555267 scopus 로고    scopus 로고
    • Biochemical characterization, molecular cloning and expression of laccases - A divergent gene family - In poplar
    • Ranocha P, McDougall G, Hawkins S, Sterjiades R, Borderies G, et al. 1999. Biochemical characterization, molecular cloning and expression of laccases - a divergent gene family - in poplar. Eur. J. Biochem. 259:485-95
    • (1999) Eur. J. Biochem. , vol.259 , pp. 485-495
    • Ranocha, P.1    McDougall, G.2    Hawkins, S.3    Sterjiades, R.4    Borderies, G.5
  • 127
    • 0032725627 scopus 로고    scopus 로고
    • Transgene-mediated and elicitor-induced perturbation of metabolic channeling at the entry point into the phenylpropanoid pathway
    • Rasmussen S, Dixon RA. 1999. Transgene-mediated and elicitor-induced perturbation of metabolic channeling at the entry point into the phenylpropanoid pathway. Plant Cell 11:1537-51
    • (1999) Plant Cell , vol.11 , pp. 1537-1551
    • Rasmussen, S.1    Dixon, R.A.2
  • 128
    • 0034965835 scopus 로고    scopus 로고
    • Functional characterization and subcellular localization of poplar (Populus trichocarpa x Populus deltoides) cinnamate 4-hydroxylase
    • Ro DK, Mah N, Ellis BE, Douglas CJ. 2001. Functional characterization and subcellular localization of poplar (Populus trichocarpa x Populus deltoides) cinnamate 4-hydroxylase. Plant Physiol. 126:317-29
    • (2001) Plant Physiol. , vol.126 , pp. 317-329
    • Ro, D.K.1    Mah, N.2    Ellis, B.E.3    Douglas, C.J.4
  • 131
    • 4243240529 scopus 로고    scopus 로고
    • Only facts will end the lignin war
    • Rouhi AM. 2001. Only facts will end the lignin war. Chem. Eng. News 79:52-56
    • (2001) Chem. Eng. News , vol.79 , pp. 52-56
    • Rouhi, A.M.1
  • 132
    • 0029632188 scopus 로고
    • Dynamic-model of lignin growing in restricted spaces
    • Roussel MR, Lim C. 1995. Dynamic-model of lignin growing in restricted spaces. Macromolecules 28:370-76
    • (1995) Macromolecules , vol.28 , pp. 370-376
    • Roussel, M.R.1    Lim, C.2
  • 133
    • 0001869093 scopus 로고
    • Localization of lignins in wood cell walls
    • ed. T Higuchi, Orlando: Academic. 679 pp.
    • Saka S, Goring DAI. 1985. Localization of lignins in wood cell walls. In Biosynthesis and Biodegradation of Wood Components, ed. T Higuchi, pp. 51-62. Orlando: Academic. 679 pp.
    • (1985) Biosynthesis and Biodegradation of Wood Components , pp. 51-62
    • Saka, S.1    Goring, D.A.I.2
  • 134
    • 0036834965 scopus 로고    scopus 로고
    • Cellular machinery of wood production: Differentiation of secondary xylem in Pinus contorta var. latifolia
    • Samuels AL, Rensing K, Douglas CJ, Mansfield S, Dharmawardhana P, Ellis B. 2002. Cellular machinery of wood production: differentiation of secondary xylem in Pinus contorta var. latifolia. Planta 216:72-82
    • (2002) Planta , vol.216 , pp. 72-82
    • Samuels, A.L.1    Rensing, K.2    Douglas, C.J.3    Mansfield, S.4    Dharmawardhana, P.5    Ellis, B.6
  • 136
    • 0035965253 scopus 로고    scopus 로고
    • CYP98A3 from Arabidopsis thaliana is a 3′-hydroxylase of phenolic esters, a missing link in the phenylpropanoid pathway
    • Schoch G, Goepfert S, Morant M, Hehn A, Meyer D, et al. 2001. CYP98A3 from Arabidopsis thaliana is a 3′-hydroxylase of phenolic esters, a missing link in the phenylpropanoid pathway. J. Biol. Chem. 276:36566-74
    • (2001) J. Biol. Chem. , vol.276 , pp. 36566-36574
    • Schoch, G.1    Goepfert, S.2    Morant, M.3    Hehn, A.4    Meyer, D.5
  • 138
    • 0242518089 scopus 로고    scopus 로고
    • A novel type of spiro compound formed by oxidative cross-coupling of methyl sinapate with a syringyl lignin model compound. A model system for the β-1 pathway in lignin biosynthesis
    • Setälä H, Pajunen A, Rummakko P, Sipilä J, Brunow G. 1999. A novel type of spiro compound formed by oxidative cross-coupling of methyl sinapate with a syringyl lignin model compound. A model system for the β-1 pathway in lignin biosynthesis. J. Chem. Soc. Perkin Trans. I 1999:461-64
    • (1999) J. Chem. Soc. Perkin Trans. I , vol.1999 , pp. 461-464
    • Setälä, H.1    Pajunen, A.2    Rummakko, P.3    Sipilä, J.4    Brunow, G.5
  • 139
    • 0031397140 scopus 로고    scopus 로고
    • Reduced lignin content and altered lignin composition in transgenic tobacco down-regulated in expression of L-phenylalanine ammonialyase or cinnamate 4-hydroxylase
    • Sewalt VJH, Ni W, Blount JW, Jung HG, Masoud SA, et al. 1997. Reduced lignin content and altered lignin composition in transgenic tobacco down-regulated in expression of L-phenylalanine ammonialyase or cinnamate 4-hydroxylase. Plant Physiol. 115:41-50
    • (1997) Plant Physiol. , vol.115 , pp. 41-50
    • Sewalt, V.J.H.1    Ni, W.2    Blount, J.W.3    Jung, H.G.4    Masoud, S.A.5
  • 140
    • 0001259496 scopus 로고    scopus 로고
    • Lignin impact on fiber degradation: Increased enzymatic digestibility of genetically engineered tobacco (Nicotiana tabacum) stems reduced in lignin content
    • Sewalt VJH, Ni W, Jung H, Dixon RA. 1997. Lignin impact on fiber degradation: increased enzymatic digestibility of genetically engineered tobacco (Nicotiana tabacum) stems reduced in lignin content. J. Agric. Food Chem. 45:1977-83
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 1977-1983
    • Sewalt, V.J.H.1    Ni, W.2    Jung, H.3    Dixon, R.A.4
  • 141
    • 0035832879 scopus 로고    scopus 로고
    • Coniferyl alcohol metabolism in conifers. I. Glucosidic turnover of cinnamyl aldehydes by UDPG: Coniferyl alcohol glucosyltransferase from pine cambium
    • Steeves C, Förster H, Pommer U, Savidge R. 2001. Coniferyl alcohol metabolism in conifers. I. Glucosidic turnover of cinnamyl aldehydes by UDPG: coniferyl alcohol glucosyltransferase from pine cambium. Phytochemistry 51:1085-93
    • (2001) Phytochemistry , vol.51 , pp. 1085-1093
    • Steeves, C.1    Förster, H.2    Pommer, U.3    Savidge, R.4
  • 142
    • 0000232190 scopus 로고
    • Laccase from sycamore maple (Acer pseudoplatanus) polymerizes monolignols
    • Sterjiades R, Dean JFD, Eriksson K-EL. 1992. Laccase from sycamore maple (Acer pseudoplatanus) polymerizes monolignols. Plant Physiol. 99:1162-68
    • (1992) Plant Physiol. , vol.99 , pp. 1162-1168
    • Sterjiades, R.1    Dean, J.F.D.2    Eriksson, K.-E.L.3
  • 143
    • 0030903905 scopus 로고    scopus 로고
    • Fourier-transform infrared and Raman spectroscopic evidence for the incorporation of cinnamaldehydes into the lignin of transgenic tobacco (Nicotiana tabacum L.) plants with reduced expression of cinnamyl alcohol dehydrogenase
    • Stewart D, Yahiaoui N, McDougall GJ, Myton K, Marque C, et al. 1997. Fourier-transform infrared and Raman spectroscopic evidence for the incorporation of cinnamaldehydes into the lignin of transgenic tobacco (Nicotiana tabacum L.) plants with reduced expression of cinnamyl alcohol dehydrogenase. Planta 201:311-18
    • (1997) Planta , vol.201 , pp. 311-318
    • Stewart, D.1    Yahiaoui, N.2    McDougall, G.J.3    Myton, K.4    Marque, C.5
  • 144
    • 0034695715 scopus 로고    scopus 로고
    • Regio-selectivity in lignin biosynthesis. The influence of dimerization and cross-coupling
    • Syrjanen K, Brunow G. 2000. Regio-selectivity in lignin biosynthesis. The influence of dimerization and cross-coupling. J. Chem. Soc. Perkin Trans. 1:183-87
    • (2000) J. Chem. Soc. Perkin Trans. , vol.1 , pp. 183-187
    • Syrjanen, K.1    Brunow, G.2
  • 145
    • 0028055613 scopus 로고
    • Effects of ascorbate on the oxidation of derivatives of hydroxycinnamic acid and the mechanism of oxidation of sinapic acid by cell wall-bound peroxidases
    • Takahama U, Oniki T. 1994. Effects of ascorbate on the oxidation of derivatives of hydroxycinnamic acid and the mechanism of oxidation of sinapic acid by cell wall-bound peroxidases. Plant Cell Physiol. 35:593-600
    • (1994) Plant Cell Physiol. , vol.35 , pp. 593-600
    • Takahama, U.1    Oniki, T.2
  • 146
    • 0000700532 scopus 로고
    • Effect of the hydrophobic regions of hemicelluloses on dehydrogenative polymerization of sinapyl alcohol
    • Tanahashi M, Higuchi T. 1990. Effect of the hydrophobic regions of hemicelluloses on dehydrogenative polymerization of sinapyl alcohol. Mokuzai Gakkaishi 36:424-28
    • (1990) Mokuzai Gakkaishi , vol.36 , pp. 424-428
    • Tanahashi, M.1    Higuchi, T.2
  • 147
    • 0029424152 scopus 로고
    • New preparation of lignin polymer models under conditions that approximate cell wall lignification. Part 1
    • Terashima N, Atalla RH, Ralph SA, Landucci LL, Lapierre C, Monties B. 1995. New preparation of lignin polymer models under conditions that approximate cell wall lignification. Part 1. Holzforschung 49:521-27
    • (1995) Holzforschung , vol.49 , pp. 521-527
    • Terashima, N.1    Atalla, R.H.2    Ralph, S.A.3    Landucci, L.L.4    Lapierre, C.5    Monties, B.6
  • 148
    • 85102331755 scopus 로고
    • Comprehensive model of the lignified plant cell wall
    • ed. HG Jung, DR Buxton, RD Hatfield, J Ralph, Madison: ASA-CSSA-SSSA. 794 pp.
    • Terashima N, Fukushima K, He LF, Takabe K. 1993. Comprehensive model of the lignified plant cell wall. In Forage Cell Wall Structure and Digestibility, ed. HG Jung, DR Buxton, RD Hatfield, J Ralph, pp. 247-70. Madison: ASA-CSSA-SSSA. 794 pp.
    • (1993) Forage Cell Wall Structure and Digestibility , pp. 247-270
    • Terashima, N.1    Fukushima, K.2    He, L.F.3    Takabe, K.4
  • 149
    • 0007659335 scopus 로고
    • Heterogeneity in formation of lignin. IX. Factors influencing the formation of condensed structures in lignins
    • Terashima N, Seguchi Y. 1988. Heterogeneity in formation of lignin. IX. Factors influencing the formation of condensed structures in lignins. Cellulose Chem. Technol. 22:147-54
    • (1988) Cellulose Chem. Technol. , vol.22 , pp. 147-154
    • Terashima, N.1    Seguchi, Y.2
  • 151
    • 0037123359 scopus 로고    scopus 로고
    • Analysis and expression of the class III peroxidase large gene family in Arabidopsis thaliana
    • Tognolli M, Penel C, Greppin H, Simon P. 2002. Analysis and expression of the class III peroxidase large gene family in Arabidopsis thaliana. Gene 288:129-38
    • (2002) Gene , vol.288 , pp. 129-138
    • Tognolli, M.1    Penel, C.2    Greppin, H.3    Simon, P.4
  • 153
    • 0001388669 scopus 로고
    • Partial purification and properties of para-hydroxycinnamoyl-CoA- shikimate-para-hydroxycinnamoyl transferase from higher plants
    • Ulbrich B, Zenk MH. 1980. Partial purification and properties of para-hydroxycinnamoyl-CoA-shikimate-para-hydroxycinnamoyl transferase from higher plants. Phytochemistry 19:1625-29
    • (1980) Phytochemistry , vol.19 , pp. 1625-1629
    • Ulbrich, B.1    Zenk, M.H.2
  • 154
    • 0029188326 scopus 로고
    • A novel lignin in poplar trees with a reduced caffeic acid/5-hydroxyferulic acid O-methyltransferase activity
    • Van Doorsselaere J, Baucher M, Chognot E, Chabbert B, Tollier M-T, et al. 1995. A novel lignin in poplar trees with a reduced caffeic acid/5-hydroxyferulic acid O-methyltransferase activity. Plant J. 8:855-64
    • (1995) Plant J. , vol.8 , pp. 855-864
    • Van Doorsselaere, J.1    Baucher, M.2    Chognot, E.3    Chabbert, B.4    Tollier, M.-T.5
  • 155
    • 0029278933 scopus 로고
    • The brown midrib3 (bm3) mutation in maize occurs in the gene encoding caffeic acid O-methyltransferase
    • Vignols F, Rigau J, Torres MA, Capellades M, Puigdomènech P. 1995. The brown midrib3 (bm3) mutation in maize occurs in the gene encoding caffeic acid O-methyltransferase. Plant Cell 7:407-16
    • (1995) Plant Cell , vol.7 , pp. 407-416
    • Vignols, F.1    Rigau, J.2    Torres, M.A.3    Capellades, M.4    Puigdomènech, P.5
  • 156
    • 0035113745 scopus 로고    scopus 로고
    • Genetic modification of herbaceous plants for feed and fuel
    • Vogel KP, Jung HJG. 2001. Genetic modification of herbaceous plants for feed and fuel. Crit. Rev. Plant Sci. 20:15-49
    • (2001) Crit. Rev. Plant Sci. , vol.20 , pp. 15-49
    • Vogel, K.P.1    Jung, H.J.G.2
  • 157
    • 0037157054 scopus 로고    scopus 로고
    • Evidence for the biosynthetic pathway from sinapic acid to syringyl lignin using labeled sinapic acid with stable isotope at both methoxy groups in Robinia pseudoacacia and Nerium indicum
    • Yamauchi K, Yasuda S, Fukushima K. 2002. Evidence for the biosynthetic pathway from sinapic acid to syringyl lignin using labeled sinapic acid with stable isotope at both methoxy groups in Robinia pseudoacacia and Nerium indicum. J. Agric. Food Chem. 22:3222-27
    • (2002) J. Agric. Food Chem. , vol.22 , pp. 3222-3227
    • Yamauchi, K.1    Yasuda, S.2    Fukushima, K.3
  • 158
    • 0028520357 scopus 로고
    • An alternative methylation pathway in lignin biosynthesis in Zinnia
    • Ye Z-H, Kneusel RE, Matern U, Varner JE. 1994. An alternative methylation pathway in lignin biosynthesis in Zinnia. Plant Cell 6:1427-39
    • (1994) Plant Cell , vol.6 , pp. 1427-1439
    • Ye, Z.-H.1    Kneusel, R.E.2    Matern, U.3    Varner, J.E.4
  • 159
    • 0033783438 scopus 로고    scopus 로고
    • Essential role of caffeoyl coenzyme A O-methyltransferase in lignin biosynthesis in woody poplar plants
    • Zhong R, Morrison WH III, Himmelsbach DS, Poole FL II, Ye Z-H 2000. Essential role of caffeoyl coenzyme A O-methyltransferase in lignin biosynthesis in woody poplar plants. Plant Physiol. 124:563-77
    • (2000) Plant Physiol. , vol.124 , pp. 563-577
    • Zhong, R.1    Morrison III, W.H.2    Himmelsbach, D.S.3    Poole II, F.L.4    Ye, Z.-H.5
  • 161
    • 0035983842 scopus 로고    scopus 로고
    • Structural basis for the modulation of lignin monomer methylation by caffeic acid/5-hydroxyferulic acid 3/5-O-methyltransferase
    • Zubieta C, Kota P, Ferrer J-L, Dixon RA, Noel JP. 2002. Structural basis for the modulation of lignin monomer methylation by caffeic acid/5- hydroxyferulic acid 3/5-O-methyltransferase. Plant Cell 14:1265-77
    • (2002) Plant Cell , vol.14 , pp. 1265-1277
    • Zubieta, C.1    Kota, P.2    Ferrer, J.-L.3    Dixon, R.A.4    Noel, J.P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.