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Volumn 65, Issue 3, 2007, Pages 311-328

Expression profiling of the lignin biosynthetic pathway in Norway spruce using EST sequencing and real-time RT-PCR

Author keywords

Compression wood; EST; Heterobasidion annosum; Lignin biosynthesis; Picea abies; Real time RT PCR

Indexed keywords

BIOSYNTHESIS; CARBON; ENZYMES; GENE EXPRESSION; PATHOGENS; POLYMERIZATION; TISSUE CULTURE; WOOD;

EID: 34548700817     PISSN: 01674412     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11103-007-9220-5     Document Type: Article
Times cited : (81)

References (90)
  • 2
    • 0036798592 scopus 로고    scopus 로고
    • Trends in lignin modification: A comprehensive analysis of the effects of genetic manipulations/mutations on lignification and vascular integrity
    • Anterola AM, Lewis NG (2002) Trends in lignin modification: a comprehensive analysis of the effects of genetic manipulations/mutations on lignification and vascular integrity. Phytochemistry 61:221-294
    • (2002) Phytochemistry , vol.61 , pp. 221-294
    • Anterola, A.M.1    Lewis, N.G.2
  • 3
    • 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 JH, Davin LB et al (2002) Transcriptional control of monolignol biosynthesis in Pinus taeda: factors affecting monolignol ratios and carbon allocation in phenylpropanoid metabolism. J Biol Chem 277:18272-18280
    • (2002) J Biol Chem , vol.277 , pp. 18272-18280
    • Anterola, A.M.1    Jeon, J.H.2    Davin, L.B.3
  • 4
    • 27644456718 scopus 로고    scopus 로고
    • Pathogen profile: Conifer root and butt rot caused by Heterobasidion annosum (Fr.) Bref. s.l
    • Asiegbu FO, Adomas A, Stenlid J (2005) Pathogen profile: conifer root and butt rot caused by Heterobasidion annosum (Fr.) Bref. s.l. Mol Plant Pathol 6:395-409
    • (2005) Mol Plant Pathol , vol.6 , pp. 395-409
    • Asiegbu, F.O.1    Adomas, A.2    Stenlid, J.3
  • 5
    • 0028796270 scopus 로고
    • Altered lignin composition in transgenic tobacco expressing O-methyltransferase sequences in sense and antisense orientation
    • Atanassova R, Favet N, Martz F et al (1995) Altered lignin composition in transgenic tobacco expressing O-methyltransferase sequences in sense and antisense orientation. Plant J 8:465-477
    • (1995) Plant J , vol.8 , pp. 465-477
    • Atanassova, R.1    Favet, N.2    Martz, F.3
  • 6
    • 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 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 91:7608-7612
    • (1994) Proc Natl Acad Sci , vol.91 , pp. 7608-7612
    • Bate, N.J.1    Orr, J.2    Ni, W.3
  • 7
    • 4043121180 scopus 로고    scopus 로고
    • Chemical composition of earlywood and latewood in Norway spruce heartwood, sapwood and transition zone wood
    • Bertaud F, Holmbom B (2004) Chemical composition of earlywood and latewood in Norway spruce heartwood, sapwood and transition zone wood. Wood Sci Technol 38:245-256
    • (2004) Wood Sci Technol , vol.38 , pp. 245-256
    • Bertaud, F.1    Holmbom, B.2
  • 8
    • 0042823502 scopus 로고    scopus 로고
    • A lignin-specific peroxidase in tobacco whose antisense suppression leads to vascular tissue modification
    • Blee KA, Choi JW, O'Connell AP et al (2003) A lignin-specific peroxidase in tobacco whose antisense suppression leads to vascular tissue modification. Phytochemistry 64:163-176
    • (2003) Phytochemistry , vol.64 , pp. 163-176
    • Blee, K.A.1    Choi, J.W.2    O'Connell, A.P.3
  • 10
    • 0343941811 scopus 로고
    • Lignins released from Picea abies suspension cultures - True native spruce lignins?
    • Brunow G, Ede RM, Simola LK et al (1990) Lignins released from Picea abies suspension cultures - true native spruce lignins? Phytochemistry 29:2535-2538
    • (1990) Phytochemistry , vol.29 , pp. 2535-2538
    • Brunow, G.1    Ede, R.M.2    Simola, L.K.3
  • 11
    • 0001218014 scopus 로고
    • The chemical structure of extracellular lignin released by cultures of Picea abies
    • Brunow G, Kilpeläinen I, Lapierre C et al (1993) The chemical structure of extracellular lignin released by cultures of Picea abies. Phytochemistry 32:845-850
    • (1993) Phytochemistry , vol.32 , pp. 845-850
    • Brunow, G.1    Kilpeläinen, I.2    Lapierre, C.3
  • 12
    • 0542420392 scopus 로고    scopus 로고
    • Oxidative coupling of phenols and the biosynthesis of lignin
    • Lewis NG, Sarkanen S (eds) Lignin and lignan biosynthesis, 1st edn. Oxford University Press
    • Brunow G, Kilpeläinen I, Sipilä J et al (1998) Oxidative coupling of phenols and the biosynthesis of lignin. In: Lewis NG, Sarkanen S (eds) Lignin and lignan biosynthesis, 1st edn. ACS symposium series 697, Oxford University Press
    • (1998) ACS Symposium Series 697
    • Brunow, G.1    Kilpeläinen, I.2    Sipilä, J.3
  • 13
    • 33747893836 scopus 로고    scopus 로고
    • Mutant identification and characterization of the laccase gene family in Arabidopsis
    • Cai X, Davis EJ, Ballif J et al (2006) Mutant identification and characterization of the laccase gene family in Arabidopsis. J Exp Bot 57:2563-2569
    • (2006) J Exp Bot , vol.57 , pp. 2563-2569
    • Cai, X.1    Davis, E.J.2    Ballif, J.3
  • 14
    • 51249169259 scopus 로고
    • A simple and efficient method for isolating RNA from pine trees
    • Chang S, Puryear J, Cairney J (1993) A simple and efficient method for isolating RNA from pine trees. Plant Mol Biol Rep 11:113-116
    • (1993) Plant Mol Biol Rep , vol.11 , pp. 113-116
    • Chang, S.1    Puryear, J.2    Cairney, J.3
  • 15
    • 0033064130 scopus 로고    scopus 로고
    • Evidence for a novel biosynthetic pathway that regulates the ration 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 ration 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
  • 16
    • 33748696780 scopus 로고    scopus 로고
    • Multi-site genetic modulation of monolignol biosynthesis suggests new routes for formation of syringyl lignin and wall-bound ferulic acid in alfalfa (Medicago sativa L.)
    • Chen F, Srinivasa Reddy MS, Temple S, Jackson L, Shadle G, Dixon RA (2006) Multi-site genetic modulation of monolignol biosynthesis suggests new routes for formation of syringyl lignin and wall-bound ferulic acid in alfalfa (Medicago sativa L.) Plant J 48:113-124
    • (2006) Plant J , vol.48 , pp. 113-124
    • Chen, F.1    Srinivasa Reddy, M.S.2    Temple, S.3    Jackson, L.4    Shadle, G.5    Dixon, R.A.6
  • 18
    • 0142058136 scopus 로고    scopus 로고
    • An in silico assessment of gene function and organization of the phenylpropanoid pathway metabolic networks in Arabidopsis thaliana and limitations thereof
    • Costa MA, Collins RE, Anterola AM et al (2003) An in silico assessment of gene function and organization of the phenylpropanoid pathway metabolic networks in Arabidopsis thaliana and limitations thereof. Phytochemistry 64:1097-1112
    • (2003) Phytochemistry , vol.64 , pp. 1097-1112
    • Costa, M.A.1    Collins, R.E.2    Anterola, A.M.3
  • 20
    • 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 107:331-339
    • (1995) Plant Physiol , vol.107 , pp. 331-339
    • Dharmawardhana, D.P.1    Ellis, B.E.2    Carlson, J.E.3
  • 21
    • 0029188326 scopus 로고
    • A novel lignin in poplar trees with a reduced caffeic acid/5-hydroxyferulic acid O-methyltransferase activity
    • von Doorsselaere J, Baucher M, Chognot E et al (1995) A novel lignin in poplar trees with a reduced caffeic acid/5-hydroxyferulic acid O-methyltransferase activity. Plant J 8:855-864
    • (1995) Plant J , vol.8 , pp. 855-864
    • Von Doorsselaere, J.1    Baucher, M.2    Chognot, E.3
  • 22
    • 0039552100 scopus 로고    scopus 로고
    • Three 4-coumarate:coenzyme a ligases in Arabidopsis thaliana represent two evolutionarily divergent classes in angiosperms
    • Ehlting J, Buttner D, Wang Q et al (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    Buttner, D.2    Wang, Q.3
  • 23
    • 20444484861 scopus 로고    scopus 로고
    • Global transcript profiling of primary stems from Arabidopsis thaliana identifies candidate genes for missing links in lignin biosynthesis and transcriptional regulators of fiber differentiation
    • Ehlting J, Mattheus N, Aeschliman DS et al (2005) Global transcript profiling of primary stems from Arabidopsis thaliana identifies candidate genes for missing links in lignin biosynthesis and transcriptional regulators of fiber differentiation. Plant J 42:618-640
    • (2005) Plant J , vol.42 , pp. 618-640
    • Ehlting, J.1    Mattheus, N.2    Aeschliman, D.S.3
  • 24
    • 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 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 87:9057-9061
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 9057-9061
    • Elkind, Y.1    Edwards, R.2    Mavandad, M.3
  • 25
    • 0001876240 scopus 로고    scopus 로고
    • Peroxidase activity, isoenzymes and histological localisation in sapwood and heartwood of Scots pine (Pinus sylvestris L.)
    • Fagerstedt KV, Saranpää P, Piispanen R (1998) Peroxidase activity, isoenzymes and histological localisation in sapwood and heartwood of Scots pine (Pinus sylvestris L.). J For Res 3:43-47
    • (1998) J for Res , vol.3 , pp. 43-47
    • Fagerstedt, K.V.1    Saranpää, P.2    Piispanen, R.3
  • 26
    • 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 24:113-117
    • (1970) Holzforschung , vol.24 , pp. 113-117
    • Fergus, B.J.1    Goring, D.A.I.2
  • 27
    • 0034808429 scopus 로고    scopus 로고
    • Isolation of the first putative peroxidase cDNA from a conifer and the local and systemic accumulation of related proteins upon pathogen infection
    • Fossdal CG, Sharma P, Lönneborg A (2001) Isolation of the first putative peroxidase cDNA from a conifer and the local and systemic accumulation of related proteins upon pathogen infection. Plant Mol Biol 47:423-435
    • (2001) Plant Mol Biol , vol.47 , pp. 423-435
    • Fossdal, C.G.1    Sharma, P.2    Lönneborg, A.3
  • 28
    • 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 et al (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
  • 29
    • 0033102469 scopus 로고    scopus 로고
    • Regiochemical control of monolignol radical coupling: A new paradigm for lignin and lignan biosynthesis
    • Gang DR, Costa MA, Fujita M et al (1999) Regiochemical control of monolignol radical coupling: a new paradigm for lignin and lignan biosynthesis. Chem Biol 6:143-151
    • (1999) Chem Biol , vol.6 , pp. 143-151
    • Gang, D.R.1    Costa, M.A.2    Fujita, M.3
  • 30
    • 0027953261 scopus 로고
    • Purification and characterization of cinnamoyl-coenzyme A: NADP oxidoreductase in Eucalyptus gunnii
    • Goffner D, Campbell MM, Campargue C et al (1994) Purification and characterization of cinnamoyl-coenzyme A: NADP oxidoreductase in Eucalyptus gunnii. Plant Physiol 106:625-632
    • (1994) Plant Physiol , vol.106 , pp. 625-632
    • Goffner, D.1    Campbell, M.M.2    Campargue, C.3
  • 31
    • 0027954821 scopus 로고
    • Manipulation of lignin quality by downregulation of cinnamyl alcohol dehydrogenase
    • Halpin C, Knight ME, Foxon GA et al (1994) Manipulation of lignin quality by downregulation of cinnamyl alcohol dehydrogenase. Plant J 6:339-350
    • (1994) Plant J , vol.6 , pp. 339-350
    • Halpin, C.1    Knight, M.E.2    Foxon, G.A.3
  • 32
    • 37049232851 scopus 로고
    • Lignification in trees: Indication of exclusive peroxidase participation
    • Harkin JM, Obst TR (1973) Lignification in trees: indication of exclusive peroxidase participation. Science 180:296-297
    • (1973) Science , vol.180 , pp. 296-297
    • Harkin, J.M.1    Obst, T.R.2
  • 33
    • 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 126:1351-1357
    • (2001) Plant Physiol , vol.126 , pp. 1351-1357
    • Hatfield, R.1    Vermerris, W.2
  • 34
    • 0043031304 scopus 로고    scopus 로고
    • Multiplex real-time PCR for monitoring Heterobasidion annosum colonization in Norway spruce clones that differ in disease resistance
    • Hietala AM, Eikenes M, Kvaalen H et al (2003) Multiplex real-time PCR for monitoring Heterobasidion annosum colonization in Norway spruce clones that differ in disease resistance. Appl Environ Microbiol 69:4413-4420
    • (2003) Appl Environ Microbiol , vol.69 , pp. 4413-4420
    • Hietala, A.M.1    Eikenes, M.2    Kvaalen, H.3
  • 36
    • 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 et al (2003) Purification, cloning, and properties of an acyltransferase controlling shikimate and quinate ester intermediates in phenylpropanoid metabolism. J Biol Chem 278:95-103
    • (2003) J Biol Chem , vol.278 , pp. 95-103
    • Hoffmann, L.1    Maury, S.2    Martz, F.3
  • 37
    • 2942633712 scopus 로고    scopus 로고
    • Silencing of hydroxycinnamoyl-coenzyme a shikimate/quinate hydroxycinnamoyltransferase affects phenylpropanoid biosynthesis
    • Hoffmann L, Besseau S, Geoffroy P et al (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
  • 38
    • 0032574720 scopus 로고    scopus 로고
    • Compartmentalized expression of two structurally and functionally distinct 4-coumarate:CoA ligase genes in aspen (Populus tremuloides)
    • Hu WJ, Kawaoka A, Tsai CJ 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 95:5407-5412
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 5407-5412
    • Hu, W.J.1    Kawaoka, A.2    Tsai, C.J.3
  • 39
    • 21344471138 scopus 로고    scopus 로고
    • Real-time RT-PCR normalisation; Strategies and considerations
    • Huggett J, Dheda K, Bustin S et al (2005) Real-time RT-PCR normalisation; strategies and considerations. Genes Immun 6:284
    • (2005) Genes Immun , vol.6 , pp. 284
    • Huggett, J.1    Dheda, K.2    Bustin, S.3
  • 40
    • 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 96:10045-10050
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 10045-10050
    • Humphreys, J.M.1    Hemm, M.R.2    Chapple, C.3
  • 41
    • 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 37:957-965
    • (1996) Plant Cell Physiol , vol.37 , pp. 957-965
    • Kajita, S.1    Katayama, Y.2    Omori, S.3
  • 42
    • 0036105306 scopus 로고    scopus 로고
    • Lignification related enzymes in Picea abies suspension cultures
    • Kärkönen A, Koutaniemi S, Mustonen M et al (2002) Lignification related enzymes in Picea abies suspension cultures. Physiol Plant 114:343-353
    • (2002) Physiol Plant , vol.114 , pp. 343-353
    • Kärkönen, A.1    Koutaniemi, S.2    Mustonen, M.3
  • 43
    • 1242274657 scopus 로고    scopus 로고
    • Functional reclassification of the putative cinnamyl alcohol dehydrogenase multigene family in Arabidopsis
    • Kim SJ, Kim MR, Bedgar DL et al (2004) Functional reclassification of the putative cinnamyl alcohol dehydrogenase multigene family in Arabidopsis. Proc Natl Acad Sci USA 101:1455-1460
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 1455-1460
    • Kim, S.J.1    Kim, M.R.2    Bedgar, D.L.3
  • 44
    • 23744484454 scopus 로고    scopus 로고
    • Characterization of basic p-coumaryl and coniferyl alcohol oxidizing peroxidases from a lignin-forming Picea abies suspension culture
    • Koutaniemi S, Toikka MM, Kärkönen A et al (2005) Characterization of basic p-coumaryl and coniferyl alcohol oxidizing peroxidases from a lignin-forming Picea abies suspension culture. Plant Mol Biol 58:141-157
    • (2005) Plant Mol Biol , vol.58 , pp. 141-157
    • Koutaniemi, S.1    Toikka, M.M.2    Kärkönen, A.3
  • 45
    • 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 et al (2001) Two cinnamoyl-CoA reductase (CCR) genes from Arabidopsis thaliana are differentially expressed during development and in response to infection with pathogenic bacteria. Phytochemistry 57:1187-1195
    • (2001) Phytochemistry , vol.57 , pp. 1187-1195
    • Lauvergeat, V.1    Lacomme, C.2    Lacombe, E.3
  • 46
    • 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 et al (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
  • 48
    • 0030973546 scopus 로고    scopus 로고
    • A novel multifunctional O-methyltransferase implicated in a dual methylation pathway associated with lignin biosynthesis in loblolly pine
    • Li L, Popko JL, Zhang XH et al (1997) A novel multifunctional O-methyltransferase implicated in a dual methylation pathway associated with lignin biosynthesis in loblolly pine. Proc Natl Acad Sci USA 94:5461-5466
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 5461-5466
    • Li, L.1    Popko, J.L.2    Zhang, X.H.3
  • 49
    • 0033167045 scopus 로고    scopus 로고
    • Secondary xylem-specific expression of caffeoyl-coenzyme a 3-O-methyltransferase plays an important role in the methylation pathway associated with lignin biosynthesis in loblolly pine
    • Li L, Osakabe Y, Joshi CP et al (1999) Secondary xylem-specific expression of caffeoyl-coenzyme A 3-O-methyltransferase plays an important role in the methylation pathway associated with lignin biosynthesis in loblolly pine. Plant Mol Biol 40:555-565
    • (1999) Plant Mol Biol , vol.40 , pp. 555-565
    • Li, L.1    Osakabe, Y.2    Joshi, C.P.3
  • 50
    • 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 et al (2000) 5-Hydroxyconiferyl aldehyde modulates enzymatic methylation for syringyl monolignol formation, a new view of monolignol biosynthesis in angiosperms. J Biol Chem 275:6537-6545
    • (2000) J Biol Chem , vol.275 , pp. 6537-6545
    • Li, L.1    Popko, J.L.2    Umezawa, T.3
  • 51
    • 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 et al (2001) The last step of syringyl monolignol biosynthesis in angiosperms is regulated by a novel gene encoding sinapyl alcohol dehydrogenase. Plant Cell 13:1567-1586
    • (2001) Plant Cell , vol.13 , pp. 1567-1586
    • Li, L.1    Cheng, X.F.2    Leshkevich, J.3
  • 52
    • 33748944014 scopus 로고    scopus 로고
    • Involvement of AtLAC15 in lignin synthesis in seeds and in root elongation of Arabidopsis
    • Liang M, Davis E, Gardner D et al (2006) Involvement of AtLAC15 in lignin synthesis in seeds and in root elongation of Arabidopsis. Planta 224:1185-1196
    • (2006) Planta , vol.224 , pp. 1185-1196
    • Liang, M.1    Davis, E.2    Gardner, D.3
  • 53
    • 0030754872 scopus 로고    scopus 로고
    • A novel type of pathogen defense-related cinnamyl alcohol dehydrogenase
    • Logemann E, Reinold S, Somssich IE et al (1997) A novel type of pathogen defense-related cinnamyl alcohol dehydrogenase. Biol Chem 378:909-913
    • (1997) Biol Chem , vol.378 , pp. 909-913
    • Logemann, E.1    Reinold, S.2    Somssich, I.E.3
  • 54
    • 0029011039 scopus 로고
    • Genetic analysis of cinnamyl alcohol dehydrogenase in loblolly pine: Single gene inheritance, molecular characterization and evolution
    • MacKay JJ, Liu W, Whetten R et al (1995) Genetic analysis of cinnamyl alcohol dehydrogenase in loblolly pine: single gene inheritance, molecular characterization and evolution. Mol Gen Genet 247:537-545
    • (1995) Mol Gen Genet , vol.247 , pp. 537-545
    • MacKay, J.J.1    Liu, W.2    Whetten, R.3
  • 55
    • 33746762277 scopus 로고    scopus 로고
    • Cloning, characterization and localization of three novel class III peroxidases in lignifying xylem of Norway spruce (Picea abies)
    • Marjamaa K, Hildén K, Kukkola E et al (2006) Cloning, characterization and localization of three novel class III peroxidases in lignifying xylem of Norway spruce (Picea abies). Plant Mol Biol 61:719-732
    • (2006) Plant Mol Biol , vol.61 , pp. 719-732
    • Marjamaa, K.1    Hildén, K.2    Kukkola, E.3
  • 56
    • 27644584401 scopus 로고    scopus 로고
    • Callus cultures and bark from Norway spruce clones show similar cellular features and relative resistance to fungal pathogens
    • Nagy NE, Franceschi VR, Kvaalen H et al (2005) Callus cultures and bark from Norway spruce clones show similar cellular features and relative resistance to fungal pathogens. Trees 19:694-702
    • (2005) Trees , vol.19 , pp. 694-702
    • Nagy, N.E.1    Franceschi, V.R.2    Kvaalen, H.3
  • 57
    • 0033120033 scopus 로고    scopus 로고
    • Novel characteristics and regulation of a divergent cinnamate 4-hydroxylase (CYP73A15) from French bean: Engineering expression in yeast
    • Nedelkina S, Jupe SC, Blee KA et al (1999) Novel characteristics and regulation of a divergent cinnamate 4-hydroxylase (CYP73A15) from French bean: engineering expression in yeast. Plant Mol Biol 39:1079-1090
    • (1999) Plant Mol Biol , vol.39 , pp. 1079-1090
    • Nedelkina, S.1    Jupe, S.C.2    Blee, K.A.3
  • 58
    • 13044258871 scopus 로고    scopus 로고
    • Coniferyl aldehyde 5-hydroxylation and methylation direct syringyl lignin biosynthesis in angiosperms
    • Osakabe K, Tsao CC, Li L et al (1999) Coniferyl aldehyde 5-hydroxylation and methylation direct syringyl lignin biosynthesis in angiosperms. Proc Natl Acad Sci 96:8955-8960
    • (1999) Proc Natl Acad Sci , vol.96 , pp. 8955-8960
    • Osakabe, K.1    Tsao, C.C.2    Li, L.3
  • 59
    • 3242752669 scopus 로고    scopus 로고
    • The class III peroxidase multigenic family in rice and its evolution in land plants
    • Passardi F, Longet D, Penel C et al (2004) The class III peroxidase multigenic family in rice and its evolution in land plants. Phytochemistry 65:1879-1893
    • (2004) Phytochemistry , vol.65 , pp. 1879-1893
    • Passardi, F.1    Longet, D.2    Penel, C.3
  • 60
    • 23644437138 scopus 로고    scopus 로고
    • Peroxidases have more functions than a Swiss army knife
    • Passardi F, Cosio C, Penel C et al (2005) Peroxidases have more functions than a Swiss army knife. Plant Cell Rep 24:255-265
    • (2005) Plant Cell Rep , vol.24 , pp. 255-265
    • Passardi, F.1    Cosio, C.2    Penel, C.3
  • 61
    • 23444458190 scopus 로고    scopus 로고
    • Reassessment of effects on lignification and vascular development in the irx4 Arabidopsis mutant
    • Patten AM, Cardenas CL, Cochrane FC et al (2005) Reassessment of effects on lignification and vascular development in the irx4 Arabidopsis mutant. Phytochemistry 66:2092-2107
    • (2005) Phytochemistry , vol.66 , pp. 2092-2107
    • Patten, A.M.1    Cardenas, C.L.2    Cochrane, F.C.3
  • 62
    • 27744527781 scopus 로고    scopus 로고
    • Generation, annotation, analysis and database integration of 16,500 white spruce EST clusters
    • Pavy N, Paule C, Parsons L et al (2005) Generation, annotation, analysis and database integration of 16,500 white spruce EST clusters. BMC Genomics 6:144
    • (2005) BMC Genomics , vol.6 , pp. 144
    • Pavy, N.1    Paule, C.2    Parsons, L.3
  • 63
    • 0031909507 scopus 로고    scopus 로고
    • Down-regulation of cinnamoyl-CoA reductase induces significant changes of lignin profiles in transgenic tobacco plants
    • Piquemal J, Lepierre C, Myton K et al (1998) Down-regulation of 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    Lepierre, C.2    Myton, K.3
  • 64
    • 33344460777 scopus 로고    scopus 로고
    • TRANSPARENT TESTA10 encodes a laccase-like enzyme involved in oxidative polymerization of flavonoids in Arabidopsis seed coat
    • Pourcel L, Routaboul J, Kerhoas L et al (2005) TRANSPARENT TESTA10 encodes a laccase-like enzyme involved in oxidative polymerization of flavonoids in Arabidopsis seed coat. Plant Cell 17:2966-2980
    • (2005) Plant Cell , vol.17 , pp. 2966-2980
    • Pourcel, L.1    Routaboul, J.2    Kerhoas, L.3
  • 65
    • 0142035247 scopus 로고    scopus 로고
    • Genome-wide characterization of the lignification toolbox in Arabidopsis
    • Raes J, Rohde A, Christensen JH et al (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
  • 66
    • 32044466069 scopus 로고    scopus 로고
    • Dirigent proteins in conifer defense: Gene discovery, phylogeny, and differential wound- and insect-induced expression of a family of DIR and DIR-like genes in spruce (Picea spp.)
    • Ralph S, Park JY, Bohlmann J et al (2006) Dirigent proteins in conifer defense: gene discovery, phylogeny, and differential wound- and insect-induced expression of a family of DIR and DIR-like genes in spruce (Picea spp.). Plant Mol Biol 60:21-40
    • (2006) Plant Mol Biol , vol.60 , pp. 21-40
    • Ralph, S.1    Park, J.Y.2    Bohlmann, J.3
  • 67
    • 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 et al (2002) Laccase down-regulation causes alterations in phenolic metabolism and cell wall structure in poplar. Plant Physiol 129:145-155
    • (2002) Plant Physiol , vol.129 , pp. 145-155
    • Ranocha, P.1    Chabannes, M.2    Chamayou, S.3
  • 68
    • 0033215860 scopus 로고    scopus 로고
    • Improvement of acetyl bromide method for lignin determination within large scale screening programmes
    • Rodrigues J, Faix O, Pereira H (1999) Improvement of acetyl bromide method for lignin determination within large scale screening programmes. Holz Roh Werkst 57:341-345
    • (1999) Holz Roh Werkst , vol.57 , pp. 341-345
    • Rodrigues, J.1    Faix, O.2    Pereira, H.3
  • 69
    • 20044362741 scopus 로고    scopus 로고
    • Light, the circadian clock, and sugar perception in the control of lignin biosynthesis
    • Rogers LA, Dubos C, Cullis IF et al (2005) Light, the circadian clock, and sugar perception in the control of lignin biosynthesis. J Exp Bot 56:1651-1663
    • (2005) J Exp Bot , vol.56 , pp. 1651-1663
    • Rogers, L.A.1    Dubos, C.2    Cullis, I.F.3
  • 70
    • 0037245987 scopus 로고    scopus 로고
    • Sputnik: A database platform for comparative plant genomics
    • Rudd S, Mewes HW, Mayer KFX (2003) Sputnik: a database platform for comparative plant genomics. Nucleic Acids Res 31:128-132
    • (2003) Nucleic Acids Res , vol.31 , pp. 128-132
    • Rudd, S.1    Mewes, H.W.2    Mayer, K.F.X.3
  • 71
    • 0036834965 scopus 로고    scopus 로고
    • Cellular machinery of wood production: Differentiation of secondary xylem in Pinus contorta var. latifolia
    • Samuels AL, Rensing KH, Douglas CJ et al (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.H.2    Douglas, C.J.3
  • 73
    • 1642377866 scopus 로고    scopus 로고
    • Lignin dehydrogenative polymerization mechanism: A poplar cell wall peroxidase directly oxidizes polymer lignin and produces in vitro dehydrogenative polymer rich in β-O-4 linkage
    • Sasaki S, Nishida T, Tsutsumi Y et al (2004) Lignin dehydrogenative polymerization mechanism: a poplar cell wall peroxidase directly oxidizes polymer lignin and produces in vitro dehydrogenative polymer rich in β-O-4 linkage. FEBS Lett 562:197-201
    • (2004) FEBS Lett , vol.562 , pp. 197-201
    • Sasaki, S.1    Nishida, T.2    Tsutsumi, Y.3
  • 74
    • 0000493035 scopus 로고
    • Cell wall-bound coniferyl alcohol oxidase associated with lignification in conifers
    • Savidge RA, Udagama-Randeniya PV (1992) Cell wall-bound coniferyl alcohol oxidase associated with lignification in conifers. Phytochemistry 31:2959-2966
    • (1992) Phytochemistry , vol.31 , pp. 2959-2966
    • Savidge, R.A.1    Udagama-Randeniya, P.V.2
  • 75
    • 0000980210 scopus 로고
    • Temporal and spatial patterns of gene expression around sites of attempted fungal infection in parsley leaves
    • Schmelzer E, Krüger-Lebus S, Hahlbrock K (1989) Temporal and spatial patterns of gene expression around sites of attempted fungal infection in parsley leaves. Plant Cell 1:993-1001
    • (1989) Plant Cell , vol.1 , pp. 993-1001
    • Schmelzer, E.1    Krüger-Lebus, S.2    Hahlbrock, K.3
  • 76
    • 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 et al (2001) CYP98A3 from Arabidopsis thaliana is a 3′-hydroxylase of phenolic esters, a missing link in the phenylpropanoid pathway. J Biol Chem 276:36566-36574
    • (2001) J Biol Chem , vol.276 , pp. 36566-36574
    • Schoch, G.1    Goepfert, S.2    Morant, M.3
  • 77
    • 0031714444 scopus 로고    scopus 로고
    • The cinnamyl alcohol dehydrogenase gene structure in Picea abies (L.) Karst.: Genomic sequences, southern hybridization, genetic analysis and phylogenetic relationships
    • Schubert R, Sperisen C, Müller-Starck G et al (1998) The cinnamyl alcohol dehydrogenase gene structure in Picea abies (L.) Karst.: genomic sequences, southern hybridization, genetic analysis and phylogenetic relationships. Trees 12:453-463
    • (1998) Trees , vol.12 , pp. 453-463
    • Schubert, R.1    Sperisen, C.2    Müller-Starck, G.3
  • 78
    • 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 VJH, Ni W, Blount JW et al (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.J.H.1    Ni, W.2    Blount, J.W.3
  • 79
    • 33644813108 scopus 로고    scopus 로고
    • CINNAMYL ALCOHOL DEHYDROGENASE-C and -D are the primary genes involved in lignin biosynthesis in the floral stem of Arabidopsis
    • Sibout R, Eudes A, Mouille G et al (2005) CINNAMYL ALCOHOL DEHYDROGENASE-C and -D are the primary genes involved in lignin biosynthesis in the floral stem of Arabidopsis. Plant Cell 17:2059-2076
    • (2005) Plant Cell , vol.17 , pp. 2059-2076
    • Sibout, R.1    Eudes, A.2    Mouille, G.3
  • 80
    • 84989751794 scopus 로고
    • Lignin release and photomixotrophism in suspension cultures of Picea abies
    • Simola LK, Lemmetyinen J, Santanen A (1992) Lignin release and photomixotrophism in suspension cultures of Picea abies. Physiol Plant 84:374-379
    • (1992) Physiol Plant , vol.84 , pp. 374-379
    • Simola, L.K.1    Lemmetyinen, J.2    Santanen, A.3
  • 81
    • 13144302845 scopus 로고    scopus 로고
    • Gene discovery in the wood-forming tissues of poplar: Analysis of 5,692 expressed sequence tags
    • Sterky F, Regan S, Karlsson J et al (1998) Gene discovery in the wood-forming tissues of poplar: analysis of 5,692 expressed sequence tags. Proc Natl Acad Sci USA 95:13330-13335
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 13330-13335
    • Sterky, F.1    Regan, S.2    Karlsson, J.3
  • 83
    • 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 et al (2002) Analysis and expression of the class III peroxidase large gene family in Arabidopsis thaliana. Gene 288:129-138
    • (2002) Gene , vol.288 , pp. 129-138
    • Tognolli, M.1    Penel, C.2    Greppin, H.3
  • 84
    • 33748760611 scopus 로고    scopus 로고
    • The genome of black cottonwood, Populus trichocarpa (Torr. & Gray)
    • Tuskan GA, DiFazio S, Jansson S et al (2006) The genome of black cottonwood, Populus trichocarpa (Torr. & Gray). Science 313:1596-1604
    • (2006) Science , vol.313 , pp. 1596-1604
    • Tuskan, G.A.1    Difazio, S.2    Jansson, S.3
  • 86
    • 0034876167 scopus 로고    scopus 로고
    • Functional genomics and cell wall biosynthesis in loblolly pine
    • Whetten R, Sun YH, Zhang Y et al (2001) Functional genomics and cell wall biosynthesis in loblolly pine. Plant Mol Biol 47:275-291
    • (2001) Plant Mol Biol , vol.47 , pp. 275-291
    • Whetten, R.1    Sun, Y.H.2    Zhang, Y.3
  • 87
    • 33746873661 scopus 로고    scopus 로고
    • Analysis of gene expression during bud burst initiation in Norway spruce via ESTs from subtracted cDNA libraries
    • Yakolev IA, Fossdal C, Johnsen Ø et al (2006) Analysis of gene expression during bud burst initiation in Norway spruce via ESTs from subtracted cDNA libraries. Tree Genet Genom 2:39-52
    • (2006) Tree Genet Genom , vol.2 , pp. 39-52
    • Yakolev, I.A.1    Fossdal, C.2    Johnsen, Ø.3
  • 88
    • 0028520357 scopus 로고
    • An alternative methylation pathway in lignin biosynthesis in Zinnia
    • Ye ZH, Kneusel RE, Matern U et al (1994) An alternative methylation pathway in lignin biosynthesis in Zinnia. Plant Cell 6:1427-1439
    • (1994) Plant Cell , vol.6 , pp. 1427-1439
    • Ye, Z.H.1    Kneusel, R.E.2    Matern, U.3
  • 89
    • 0031040101 scopus 로고    scopus 로고
    • Molecular cloning of 4-coumarate:coenzyme a ligase in loblolly pine and the roles of this enzyme in the biosynthesis of lignin in compression wood
    • Zhang XH, Chiang VL (1997) Molecular cloning of 4-coumarate:coenzyme A ligase in loblolly pine and the roles of this enzyme in the biosynthesis of lignin in compression wood. Plant Physiol 113:65-74
    • (1997) Plant Physiol , vol.113 , pp. 65-74
    • Zhang, X.H.1    Chiang, V.L.2
  • 90
    • 0032287625 scopus 로고    scopus 로고
    • Dual methylation pathways in lignin biosynthesis
    • Zhong R, Morrison WH III, Negrel J et al (1998) Dual methylation pathways in lignin biosynthesis. Plant Cell 10:2033-2045
    • (1998) Plant Cell , vol.10 , pp. 2033-2045
    • Zhong, R.1    Morrison III, W.H.2    Negrel, J.3


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