메뉴 건너뛰기




Volumn 41, Issue 8, 2003, Pages 677-687

Genes involved in the biosynthesis of lignin precursors in Arabidopsis thaliana

Author keywords

Arabidopsis; Lignin; Monolignol biosynthesis; Mutant; Secondary cell wall

Indexed keywords

ARABIDOPSIS; ARABIDOPSIS THALIANA;

EID: 0038693626     PISSN: 09819428     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0981-9428(03)00095-0     Document Type: Review
Times cited : (106)

References (70)
  • 2
    • 0034649566 scopus 로고    scopus 로고
    • Arabidopsis genome initiative, analysis of the genome sequence of the flowering plant Arabidopsis thaliana
    • Arabidopsis genome initiative, Analysis of the genome sequence of the flowering plant Arabidopsis thaliana, Nature 208 (2000) 796-815.
    • (2000) Nature , vol.208 , pp. 796-815
  • 3
    • 0029205727 scopus 로고
    • Genomic nucleotide sequence of an Arabidopsis thaliana gene encoding a cinnamyl alcohol dehydrogenase
    • M. Baucher, J. Van Doorsselaere, J. Gielen, M. Van Montagu, D. Inzé, W. Boerjan, Genomic nucleotide sequence of an Arabidopsis thaliana gene encoding a cinnamyl alcohol dehydrogenase, Plant Physiol. 107 (1995) 285-286.
    • (1995) Plant Physiol. , vol.107 , pp. 285-286
    • Baucher, M.1    Van Doorsselaere, J.2    Gielen, J.3    Van Montagu, M.4    Inzé, D.5    Boerjan, W.6
  • 6
    • 0034028789 scopus 로고    scopus 로고
    • Lignins and lignification: Selected issues
    • A.M. Boudet, Lignins and lignification: selected issues, Plant Physiol. Biochem. 38 (2000) 81-96.
    • (2000) Plant Physiol. Biochem. , vol.38 , pp. 81-96
    • Boudet, A.M.1
  • 7
    • 0033197808 scopus 로고    scopus 로고
    • Molecular characterisation and expression of a wound-inducible cDNA encoding a novel cinnamyl-alcohol dehydrogenase enzyme in lucerne (Medicago sativa L.)
    • E.M. Brill, S. Abrahams, C.M. Hayes, C.L.D. Jenkin, J.M. Watson, Molecular characterisation and expression of a wound-inducible cDNA encoding a novel cinnamyl-alcohol dehydrogenase enzyme in lucerne (Medicago sativa L.), Plant Mol. Biol. 41 (1999) 279-291.
    • (1999) Plant Mol. Biol. , vol.41 , pp. 279-291
    • Brill, E.M.1    Abrahams, S.2    Hayes, C.M.3    Jenkin, C.L.D.4    Watson, J.M.5
  • 8
    • 0026409291 scopus 로고
    • cDNA cloning, sequence analysis and seasonal expression of lignin-bispecific caffeic acid/5-hydroxyferulic acid O-methyl transferase of aspen
    • R.C. Bugos, V.L.C. Chiang, W.H. Campell, cDNA cloning, sequence analysis and seasonal expression of lignin-bispecific caffeic acid/5-hydroxyferulic acid O-methyl transferase of aspen, Plant Mol. Biol. 17 (1991) 1203-1215.
    • (1991) Plant Mol. Biol. , vol.17 , pp. 1203-1215
    • Bugos, R.C.1    Chiang, V.L.C.2    Campell, W.H.3
  • 9
    • 0030021535 scopus 로고    scopus 로고
    • Variation in lignin content and composition. Mechanisms of control and implications for the genetic improvement of plants
    • M.M. Campbell, R.R. Sederoff, Variation in lignin content and composition. Mechanisms of control and implications for the genetic improvement of plants, Plant Physiol. 110 (1996) 3-13.
    • (1996) Plant Physiol. , vol.110 , pp. 3-13
    • Campbell, M.M.1    Sederoff, R.R.2
  • 10
    • 0026947812 scopus 로고
    • An Arabidopsis mutant defective in the general phenylpropanoid pathway
    • C.C.S. Chapple, T. Vogt, B.E. Ellis, C.S. Sommerville, An Arabidopsis mutant defective in the general phenylpropanoid pathway, Plant Cell 4 (1992) 1413-1424.
    • (1992) Plant Cell , vol.4 , pp. 1413-1424
    • Chapple, C.C.S.1    Vogt, T.2    Ellis, B.E.3    Sommerville, C.S.4
  • 11
    • 0001247284 scopus 로고    scopus 로고
    • Phenylpropanoid metabolism: Biosynthesis of monolignols, lignans, lignins and suberins
    • H.A. Stafford, R.K. Ibrahim (Eds.), Plenum Press, New York
    • L.B. Davin, N.G. Lewis, Phenylpropanoid metabolism: biosynthesis of monolignols, lignans, lignins and suberins, in: H.A. Stafford, R.K. Ibrahim (Eds.), Recent Advances in Phytochemistry, vol. 26, Plenum Press, New York, pp. 325-375.
    • Recent Advances in Phytochemistry , vol.26 , pp. 325-375
    • Davin, L.B.1    Lewis, N.G.2
  • 12
    • 0000686529 scopus 로고
    • Characterization of vascular lignification in Arabidopsis thaliana
    • D.P. Dharmawardhana, B.E. Ellis, J.E. Carlson, Characterization of vascular lignification in Arabidopsis thaliana, Can. J. Bot. 70 (1992) 2238-2244.
    • (1992) Can. J. Bot. , vol.70 , pp. 2238-2244
    • Dharmawardhana, D.P.1    Ellis, B.E.2    Carlson, J.E.3
  • 13
    • 0035832807 scopus 로고    scopus 로고
    • The biosynthesis of monolignols: A "metabolic grid", or independant pathway to guaiacyl and syringyl units?
    • R.A. Dixon, F. Chen, D. Guo, K. Parvathi, The biosynthesis of monolignols: a "metabolic grid", or independant pathway to guaiacyl and syringyl units?, Phytochemistry 57 (2001) 1069-1084.
    • (2001) Phytochemistry , vol.57 , pp. 1069-1084
    • Dixon, R.A.1    Chen, F.2    Guo, D.3    Parvathi, K.4
  • 14
    • 0035800123 scopus 로고    scopus 로고
    • Lignification and lignin topochemistry - An ultrastructural view
    • D.A. Donaldson, Lignification and lignin topochemistry - an ultrastructural view, Phytochemistry 57 (2001) 859-873.
    • (2001) Phytochemistry , vol.57 , pp. 859-873
    • Donaldson, D.A.1
  • 15
    • 0001686898 scopus 로고
    • Structure and elicitor or U.V. light-stimulated expression of two 4-coumarate:CoA ligases in parsley
    • C. Douglas, H. Hoffmann, W. Schulz, K. Hahlbrock, Structure and elicitor or U.V. light-stimulated expression of two 4-coumarate:CoA ligases in parsley, EMBO J. 6 (1987) 1189-1195.
    • (1987) EMBO J. , vol.6 , pp. 1189-1195
    • Douglas, C.1    Hoffmann, H.2    Schulz, W.3    Hahlbrock, K.4
  • 17
    • 0039552100 scopus 로고    scopus 로고
    • Three 4-coumarate:coenzyme A ligases in Arabidopsis thaliana represent two evolutionarily divergent classes in angiosperms
    • J. Ehlting, D. Büttner, Q. Wang, C.J. Douglas, I.E. Somssich, E. Kombrink, Three 4-coumarate:coenzyme A ligases in Arabidopsis thaliana represent two evolutionarily divergent classes in angiosperms, Plant J. 19 (1999) 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
  • 18
    • 0034788886 scopus 로고    scopus 로고
    • Identification of 4-coumarate:coenzyme A ligase (4CL) substrate recognition domains
    • J. Ehlting, J.J. Shin, C.J. Douglas, Identification of 4-coumarate: coenzyme A ligase (4CL) substrate recognition domains, Plant J. 27 (2001) 455-465.
    • (2001) Plant J. , vol.27 , pp. 455-465
    • Ehlting, J.1    Shin, J.J.2    Douglas, C.J.3
  • 19
    • 0034031635 scopus 로고    scopus 로고
    • Modified lignin in tobacco and poplar plants overexpressing the Arabidopsis gene encoding ferulate 5-hydroxylase
    • R. Franke, C.M. McMichael, K. Meyer, A.M. Shirely, J.C. Cusumano, C. Chapple, Modified lignin in tobacco and poplar plants overexpressing the Arabidopsis gene encoding ferulate 5-hydroxylase, Plant J. 22 (2000) 223-234.
    • (2000) Plant J. , vol.22 , pp. 223-234
    • Franke, R.1    McMichael, C.M.2    Meyer, K.3    Shirely, A.M.4    Cusumano, J.C.5    Chapple, C.6
  • 20
    • 0036011028 scopus 로고    scopus 로고
    • Changes in secondary metabolism and deposition of an unusual lignin in the ref8 mutant of Arabidopsis
    • R. Franke, R.M. Hemm, J.W. Denault, M.O. Ruegger, J.M. Humpheys, C. Chapple, Changes in secondary metabolism and deposition of an unusual lignin in the ref8 mutant of Arabidopsis, Plant J. 30 (2002) 33-45.
    • (2002) Plant J. , vol.30 , pp. 33-45
    • Franke, R.1    Hemm, R.M.2    Denault, J.W.3    Ruegger, M.O.4    Humpheys, J.M.5    Chapple, C.6
  • 24
    • 0034869281 scopus 로고    scopus 로고
    • Lignin formation in plants. The dilemma of linkage specificity
    • R. Hatfield, W. Vermerris, Lignin formation in plants. The dilemma of linkage specificity, Plant Physiol. 126 (2001) 1351-1357.
    • (2001) Plant Physiol. , vol.126 , pp. 1351-1357
    • Hatfield, R.1    Vermerris, W.2
  • 25
    • 0004159313 scopus 로고
    • Lignin biochemistry: Biosynthesis and degradation
    • M. Higuchi, Lignin biochemistry: biosynthesis and degradation, Wood Sci. Technol. 24 (1990) 23-63.
    • (1990) Wood Sci. Technol. , vol.24 , pp. 23-63
    • Higuchi, M.1
  • 27
    • 0033621061 scopus 로고    scopus 로고
    • New routes for lignin biosynthesis defined by biochemical characterization of recombinant ferulate 5-hydroxylase, a multifunctional cytochrome P450-dependant monooxygenase
    • J.M. Humphreys, M.R. Hemm, C. Chapple, New routes for lignin biosynthesis defined by biochemical characterization of recombinant ferulate 5-hydroxylase, a multifunctional cytochrome P450-dependant monooxygenase, Proc. Natl. Acad. Sci. USA 96 (1999) 10045-10050.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10045-10050
    • Humphreys, J.M.1    Hemm, M.R.2    Chapple, C.3
  • 29
    • 0034967467 scopus 로고    scopus 로고
    • Cloning and characterization of irregular xylem 4 (irx4): A severely lignin deficient mutant of Arabidopsis
    • L. Jones, A.R. Ennos, S.R. Turner, Cloning and characterization of irregular xylem 4 (irx4): a severely lignin deficient mutant of Arabidopsis, Plant J. 26 (2001) 206-216.
    • (2001) Plant J. , vol.26 , pp. 206-216
    • Jones, L.1    Ennos, A.R.2    Turner, S.R.3
  • 32
    • 0030267242 scopus 로고    scopus 로고
    • Alterations in the biosynthesis of lignin in transgenic plants with chimeric genes for 4-coumarate:coenzyme A ligase
    • S. Kajita, Y. Katayama, S. Omori, Alterations in the biosynthesis of lignin in transgenic plants with chimeric genes for 4-coumarate:coenzyme A ligase, Plant Cell Physiol. 37 (1996) S957-S965.
    • (1996) Plant Cell Physiol. , vol.37
    • Kajita, S.1    Katayama, Y.2    Omori, S.3
  • 33
    • 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
    • S. Kajita, S. Hishiyama, Y. Tomimura, Y. Katayama, S. Omori, Structural characterization of modified lignin in transgenic tobacco plants in which the activity of 4-coumarate:coenzyme A ligase is depressed, Plant Physiol. 114 (1997) 871-879.
    • (1997) Plant Physiol. , vol.114 , pp. 871-879
    • Kajita, S.1    Hishiyama, S.2    Tomimura, Y.3    Katayama, Y.4    Omori, S.5
  • 34
    • 0027086425 scopus 로고
    • Rapid activation of a novel plant defense gene is strictly dependent on the Arabidopsis RPM1 disease resistance locus
    • S. Kiedrowski, P. Kwalleck, K. Hahlbrock, I.E. Somssich, J.L. Dangl, Rapid activation of a novel plant defense gene is strictly dependent on the Arabidopsis RPM1 disease resistance locus, EMBO J. 11 (1992) 4677-4684.
    • (1992) EMBO J. , vol.11 , pp. 4677-4684
    • Kiedrowski, S.1    Kwalleck, P.2    Hahlbrock, K.3    Somssich, I.E.4    Dangl, J.L.5
  • 35
    • 0026901226 scopus 로고
    • Identification and characterization of cDNA clones encoding cinnamyl alcohol dehydrogenase from tobacco
    • R.E. Knight, C. Halpin, W. Schuch, Identification and characterization of cDNA clones encoding cinnamyl alcohol dehydrogenase from tobacco, Plant Mol. Biol. 19 (1992) 793-801.
    • (1992) Plant Mol. Biol. , vol.19 , pp. 793-801
    • Knight, R.E.1    Halpin, C.2    Schuch, W.3
  • 36
    • 0031105944 scopus 로고    scopus 로고
    • Cinnamoyl CoA reductase, the first committed enzyme of the lignin branch biosynthetic pathway: Cloning, expression and phylogenetic relationships
    • E. Lacombe, S.W. Hawkins, J. van Doorsselaere, J. Piquemal, D. Goffner, O. Poeydomenge, A.M. Boudet, J. Grima-Pettenati, Cinnamoyl CoA reductase, the first committed enzyme of the lignin branch biosynthetic pathway: cloning, expression and phylogenetic relationships, Plant J. 11 (1997) 429-441.
    • (1997) Plant J. , vol.11 , pp. 429-441
    • Lacombe, E.1    Hawkins, S.W.2    Van Doorsselaere, J.3    Piquemal, J.4    Goffner, D.5    Poeydomenge, O.6    Boudet, A.M.7    Grima-Pettenati, J.8
  • 37
    • 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
    • V. Lauvergeat, C. Lacomme, E. Lacombe, E. Lasserre, D. Roby, J. Grima-Pettenati, Two cinnamoyl-CoA reductase (CCR) genes from Arabidopsis thaliana are differentially expressed during development and in response to infection with pathogenic bacteria, Phytochemistry 57 (2001) 1187-1195.
    • (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
  • 38
    • 0029346985 scopus 로고
    • The Arabidopsis thaliana 4-coumarate:CoA ligase gene: Stress and developmentally regulated expression and nucleotide sequence of its cDNA
    • D. Lee, M. Ellard, L.A. Wanner, K.R. Davis, C.J. Douglas, The Arabidopsis thaliana 4-coumarate:CoA ligase gene: stress and developmentally regulated expression and nucleotide sequence of its cDNA, Plant Mol. Biol. 28 (1995) 871-884.
    • (1995) Plant Mol. Biol. , vol.28 , pp. 871-884
    • Lee, D.1    Ellard, M.2    Wanner, L.A.3    Davis, K.R.4    Douglas, C.J.5
  • 39
    • 0031277875 scopus 로고    scopus 로고
    • Antisense suppression of 4-coumarate:coenzyme A ligase activity in Arabidopsis leads to altered lignin subunit composition
    • D. Lee, K. Meyer, C. Chapple, C.J. Douglas, Antisense suppression of 4-coumarate:coenzyme A ligase activity in Arabidopsis leads to altered lignin subunit composition, Plant Cell 9 (1997) 1985-1998.
    • (1997) Plant Cell , vol.9 , pp. 1985-1998
    • Lee, D.1    Meyer, K.2    Chapple, C.3    Douglas, C.J.4
  • 40
    • 0034054073 scopus 로고    scopus 로고
    • 5-Hydroxyconiferyl aldehyde modulates enzymatic methylation for syringyl monolignol formation, a new view of monolignol biosynthesis in Angiosperms
    • L. Li, J.L. Popko, T. Umezawa, V.L. Chiang, 5-Hydroxyconiferyl aldehyde modulates enzymatic methylation for syringyl monolignol formation, a new view of monolignol biosynthesis in Angiosperms, J. Biol. Chem. 275 (2000) 6537-6545.
    • (2000) J. Biol. Chem. , vol.275 , pp. 6537-6545
    • Li, L.1    Popko, J.L.2    Umezawa, T.3    Chiang, V.L.4
  • 41
    • 0034927211 scopus 로고    scopus 로고
    • The last step of syringyl monolignol biosynthesis in Angiosperms is regulated by a novel gene encoding sinapyl alcohol dehydrogenase
    • L. Li, X.F. Cheng, J. Leshkevich, T. Umezawa, S.A. Hardling, V.L. Chiang, The last step of syringyl monolignol biosynthesis in Angiosperms is regulated by a novel gene encoding sinapyl alcohol dehydrogenase, Plant Cell 13 (2001) 1567-1585.
    • (2001) Plant Cell , vol.13 , pp. 1567-1585
    • Li, L.1    Cheng, X.F.2    Leshkevich, J.3    Umezawa, T.4    Hardling, S.A.5    Chiang, V.L.6
  • 42
    • 0033607210 scopus 로고    scopus 로고
    • NMR characterization of lignins in Arabidopsis altered in the activity of ferulate 5-hydroxylase
    • J.M. Marita, J. Ralph, R.D. Hatfield, C. Chapple, NMR characterization of lignins in Arabidopsis altered in the activity of ferulate 5-hydroxylase, Proc. Natl. Acad. Sci. USA 96 (1999) 12328-12332.
    • (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
  • 44
    • 0030006715 scopus 로고    scopus 로고
    • Ferulate-5-hydroxylase from Arabidopsis thaliana defines a new family of cytochrome P450-dependant monooxygenases
    • K. Meyer, J.C. Cusumano, C. Somerville, C.C.S. Chapple, Ferulate-5-hydroxylase from Arabidopsis thaliana defines a new family of cytochrome P450-dependant monooxygenases, Proc. Natl. Acad. Sci. USA 93 (1996) 6869-6874.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6869-6874
    • Meyer, K.1    Cusumano, J.C.2    Somerville, C.3    Chapple, C.C.S.4
  • 45
    • 0032499766 scopus 로고    scopus 로고
    • Lignin monomer composition is determined by the expression of a cytochrome P450-dependent monooxygenase in Arabidopsis
    • K. Meyer, A.M. Shirley, J.C. Cusumano, D.A. Bell-Lelong, C. Chapple, Lignin monomer composition is determined by the expression of a cytochrome P450-dependent monooxygenase in Arabidopsis, Proc. Natl. Acad. Sci. USA 95 (1998) 6619-6623.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6619-6623
    • Meyer, K.1    Shirley, A.M.2    Cusumano, J.C.3    Bell-Lelong, D.A.4    Chapple, C.5
  • 46
    • 0000890343 scopus 로고
    • Purification and characterization of a cytochrome P450 (trans-cinnamic acid 4-hydroxylase) from etiolated mung bean seedlings
    • M. Mizutani, D. Ohta, R. Sato, Purification and characterization of a cytochrome P450 (trans-cinnamic acid 4-hydroxylase) from etiolated mung bean seedlings, Plant Cell Physiol. 34 (1993) 481-488.
    • (1993) Plant Cell Physiol. , vol.34 , pp. 481-488
    • Mizutani, M.1    Ohta, D.2    Sato, R.3
  • 47
    • 0031105483 scopus 로고    scopus 로고
    • Isolation of a cDNA and a genomic clone encoding cinnamate 4-hydroxylase from Arabidopsis and its expression manner in planta
    • M. Mizutani, S. Ohta, R. Sato, Isolation of a cDNA and a genomic clone encoding cinnamate 4-hydroxylase from Arabidopsis and its expression manner in planta, Plant Physiol. 113 (1997) 755-763.
    • (1997) Plant Physiol. , vol.113 , pp. 755-763
    • Mizutani, M.1    Ohta, S.2    Sato, R.3
  • 48
    • 0025478576 scopus 로고
    • Functional properties of a phenylalanine ammonia-lyase promoter from Arabidopsis
    • S. Ohl, S.A. Hebrick, J. Chory, C.J. Lamb, Functional properties of a phenylalanine ammonia-lyase promoter from Arabidopsis, Plant Cell 2 (1990) 837-848.
    • (1990) Plant Cell , vol.2 , pp. 837-848
    • Ohl, S.1    Hebrick, S.A.2    Chory, J.3    Lamb, C.J.4
  • 50
    • 0024688821 scopus 로고
    • S-Adenosyl-L-methionine: Trans-caffeoyl-coenzymeA 3- O-methyltransferase from elicitortreated parsley cell suspension cultures
    • A.E. Pakusch, R.E. Kneusel, U. Matern, S-Adenosyl-L-methionine: trans-caffeoyl-coenzymeA 3- O-methyltransferase from elicitortreated parsley cell suspension cultures, Arch. Biochem. Biophys. 271 (1989) 488-494.
    • (1989) Arch. Biochem. Biophys. , vol.271 , pp. 488-494
    • Pakusch, A.E.1    Kneusel, R.E.2    Matern, U.3
  • 51
    • 0031909507 scopus 로고    scopus 로고
    • Down-regulation of cinnamoyl-CoA reductase induces significant changes of lignin profiles in transgenic tobacco plants
    • J. Piquemal, C. Lapierre, K. Myton, A. O'Connell, W. Schuch, J. Grima-Pettenati, A.M. Boudet, Down-regulation of cinnamoyl-CoA reductase induces significant changes of lignin profiles in transgenic tobacco plants, Plant J. 13 (1998) 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    Grima-Pettenati, J.6    Boudet, A.M.7
  • 52
    • 0035132582 scopus 로고    scopus 로고
    • NMR evidence for benzodioxane structure resulting from incorporation of 5-hydroxyconiferyl alcohol in lignins of O-methyltransferase-deficient plants
    • J. Ralph, C. Lapierre, F. Lu, J.M. Marita, J. Van Doorseleare, W. Boerjan, L. Jouanin, NMR evidence for benzodioxane structure resulting from incorporation of 5-hydroxyconiferyl alcohol in lignins of O-methyltransferase-deficient plants, J. Agri. Food Sci. 49 (2001) 86-91.
    • (2001) J. Agri. Food Sci. , vol.49 , pp. 86-91
    • Ralph, J.1    Lapierre, C.2    Lu, F.3    Marita, J.M.4    Van Doorseleare, J.5    Boerjan, W.6    Jouanin, L.7
  • 53
    • 0032817823 scopus 로고    scopus 로고
    • Regulation of ferulate-5-hydroxylase expression in Arabidopsis in the context of sinapate ester biosynthesis
    • M. Ruegger, K. Meyer, J. Cusumano, C. Chapple, Regulation of ferulate-5-hydroxylase expression in Arabidopsis in the context of sinapate ester biosynthesis, Plant Physiol. 119 (1999) 101-110.
    • (1999) Plant Physiol. , vol.119 , pp. 101-110
    • Ruegger, M.1    Meyer, K.2    Cusumano, J.3    Chapple, C.4
  • 54
    • 0035692238 scopus 로고    scopus 로고
    • Mutations that reduce sinapoylmalate accumulation in Arabidopsis thaliana define loci with diverse roles in phenylpropanoid metabolism
    • M. Ruegger, C. Chapple, Mutations that reduce sinapoylmalate accumulation in Arabidopsis thaliana define loci with diverse roles in phenylpropanoid metabolism, Genetics 159 (2001) 1741-1749.
    • (2001) Genetics , vol.159 , pp. 1741-1749
    • Ruegger, M.1    Chapple, C.2
  • 55
    • 0035965253 scopus 로고    scopus 로고
    • CYP98A3 from Arabidopsis thaliana is a 3′-hydroxylase of phenolic esters, a missing link in the phenylpropanoid pathway
    • G. Schoch, S. Goepfert, M. Morant, A. Hehn, D. Meyer, P. Ullmann, D. Werck-Reichhart, CYP98A3 from Arabidopsis thaliana is a 3′-hydroxylase of phenolic esters, a missing link in the phenylpropanoid pathway, J. Biol. Chem. 276 (2001) 36566-36574.
    • (2001) J. Biol. Chem. , vol.276 , pp. 36566-36574
    • Schoch, G.1    Goepfert, S.2    Morant, M.3    Hehn, A.4    Meyer, D.5    Ullmann, P.6    Werck-Reichhart, D.7
  • 56
    • 0025948396 scopus 로고
    • Molecular cloning, induction, and taxonomic distribution of caffeoyl-CoA-3-O-methyltransferase, an enzyme involved in disease resistance
    • D. Schmitt, A.E. Pakusch, U. Matern, Molecular cloning, induction, and taxonomic distribution of caffeoyl-CoA-3-O-methyltransferase, an enzyme involved in disease resistance, J. Biol. Chem. 266 (1991) 17416-17423.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17416-17423
    • Schmitt, D.1    Pakusch, A.E.2    Matern, U.3
  • 58
    • 0038120007 scopus 로고    scopus 로고
    • Expression pattern of two paralogs encoding cinnamyl alcohol dehydrogenases in Arabidopsis. Isolation and characterization of the corresponding mutants
    • in press
    • R. Sibout, A. Eudes, B. Pollet, T. Goujon, I. Mila, F. Granier, A. Séguin, C. Lapierre, L. Jouanin, Expression pattern of two paralogs encoding cinnamyl alcohol dehydrogenases in Arabidopsis. Isolation and characterization of the corresponding mutants, Plant Physiol. 132 (2003) in press.
    • (2003) Plant Physiol. , vol.132
    • Sibout, R.1    Eudes, A.2    Pollet, B.3    Goujon, T.4    Mila, I.5    Granier, F.6    Séguin, A.7    Lapierre, C.8    Jouanin, L.9
  • 59
    • 0029340683 scopus 로고
    • A gene encoding a cinnamyl alcohol dehydrogenase homolog in Arabidopsis thaliana
    • D.A. Somers, J.P. Nourse, J.M. Manners, S. Abrahms, J.M. Watson, A gene encoding a cinnamyl alcohol dehydrogenase homolog in Arabidopsis thaliana, Plant Physiol. 108 (1995) 1309-1310.
    • (1995) Plant Physiol. , vol.108 , pp. 1309-1310
    • Somers, D.A.1    Nourse, J.P.2    Manners, J.M.3    Abrahms, S.4    Watson, J.M.5
  • 60
    • 0030475230 scopus 로고    scopus 로고
    • Arabidopsis thaliana defense-related protein ELI3 is an aromatic alcohol:NADP+ oxidoreductase
    • I.E. Somssich, P. Wernert, S. Kiedrowski, K. Hahlbrock, Arabidopsis thaliana defense-related protein ELI3 is an aromatic alcohol:NADP+ oxidoreductase, Proc. Natl. Acad. Sci. USA 93 (1996) 14199-14203.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14199-14203
    • Somssich, I.E.1    Wernert, P.2    Kiedrowski, S.3    Hahlbrock, K.4
  • 61
    • 0032964297 scopus 로고    scopus 로고
    • BLAST sequences, a new tool for comparing protein and nucleotide sequences
    • T.A. Tatusova, T.L. Madden, BLAST sequences, a new tool for comparing protein and nucleotide sequences, FEMS Microbiol. Lett. 174 (1999) 247-250.
    • (1999) FEMS Microbiol. Lett. , vol.174 , pp. 247-250
    • Tatusova, T.A.1    Madden, T.L.2
  • 62
    • 0034017734 scopus 로고    scopus 로고
    • Organization and structural evolution of four multigene families in Arabidopsis thaliana: AtLCAD, AtLGT, AtMYST and AtHD-GL2
    • R. Tavares, S. Aubourg, A. Lecharny, M. Kreis, Organization and structural evolution of four multigene families in Arabidopsis thaliana: AtLCAD, AtLGT, AtMYST and AtHD-GL2, Plant Mol. Biol. 42 (2000) 703-717.
    • (2000) Plant Mol. Biol. , vol.42 , pp. 703-717
    • Tavares, R.1    Aubourg, S.2    Lecharny, A.3    Kreis, M.4
  • 63
    • 0031131608 scopus 로고    scopus 로고
    • Collapsed xylem phenotype of Arabidopsis thaliana identifies mutants deficient in cellulose deposition in the secondary cell wall
    • S. Turner, C.R. Sommerville, Collapsed xylem phenotype of Arabidopsis thaliana identifies mutants deficient in cellulose deposition in the secondary cell wall, Plant Cell 9 (1997) 689-701.
    • (1997) Plant Cell , vol.9 , pp. 689-701
    • Turner, S.1    Sommerville, C.R.2
  • 64
  • 65
    • 0029140785 scopus 로고
    • The phenylalanine ammonia-lyase gene family in Arabidopsis thaliana
    • L.A. Wanner, G. Li, D. Ware, I.E. Somssich, K.R. Davis, The phenylalanine ammonia-lyase gene family in Arabidopsis thaliana, Plant Mol. Biol. 27 (1995) 327-338.
    • (1995) Plant Mol. Biol. , vol.27 , pp. 327-338
    • Wanner, L.A.1    Li, G.2    Ware, D.3    Somssich, I.E.4    Davis, K.R.5
  • 66
    • 0028520357 scopus 로고
    • An alternative methylation pathway in lignin biosynthesis in Zinnia
    • Z.-H. Ye, R.E. Kneusel, U. Matern, J.E. Varner, An alternative methylation pathway in lignin biosynthesis in Zinnia, Plant Cell 6 (1994) 1427-1439.
    • (1994) Plant Cell , vol.6 , pp. 1427-1439
    • Ye, Z.-H.1    Kneusel, R.E.2    Matern, U.3    Varner, J.E.4
  • 67
    • 0029310479 scopus 로고
    • Differential expression of two O-methyltransferases in lignin biosynthesis in Zinnia elegans
    • Z.-H. Ye, R.E. Kneusel, U. Matern, J.E. Varner, Differential expression of two O-methyltransferases in lignin biosynthesis in Zinnia elegans, Plant Physiol. 108 (1995) 459-467.
    • (1995) Plant Physiol. , vol.108 , pp. 459-467
    • Ye, Z.-H.1    Kneusel, R.E.2    Matern, U.3    Varner, J.E.4
  • 68
    • 0036999751 scopus 로고    scopus 로고
    • Vascular tissue differentiation and pattern formation in plants
    • Z.-H. Ye, Vascular tissue differentiation and pattern formation in plants, Annu. Rev. Plant Biol. 53 (2002) 183-202.
    • (2002) Annu. Rev. Plant Biol. , vol.53 , pp. 183-202
    • Ye, Z.-H.1
  • 69
    • 0030869476 scopus 로고    scopus 로고
    • An Arabidopsis gene encoding a putative 14-3-3-interacting protein, caffeic acid/5-hydroxyferulic acid O-methyltransferase
    • H. Zhang, J. Wang, H.M. Goodman, An Arabidopsis gene encoding a putative 14-3-3-interacting protein, caffeic acid/5-hydroxyferulic acid O-methyltransferase, Biochem. Biophys. Acta 1353 (1997) 199-202.
    • (1997) Biochem. Biophys. Acta , vol.1353 , pp. 199-202
    • Zhang, H.1    Wang, J.2    Goodman, H.M.3
  • 70
    • 0028066303 scopus 로고
    • Isolation of an Arabidopsis thaliana cDNA homologous to parsley (Petroselinum crispum) S-adenosyl-L-methionine: Trans-caffeyol-Coenzyme A 3- O-methyltransferase, an enzyme involved in disease resistance
    • J. Zou, D.C. Taylor, Isolation of an Arabidopsis thaliana cDNA homologous to parsley (Petroselinum crispum) S-adenosyl-L-methionine: trans-caffeyol-Coenzyme A 3- O-methyltransferase, an enzyme involved in disease resistance, Plant Physiol. Biochem. 32 (1994) 423-427.
    • (1994) Plant Physiol. Biochem. , vol.32 , pp. 423-427
    • Zou, J.1    Taylor, D.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.