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Volumn 72, Issue 18, 2011, Pages 2275-2287

Eggplant polyphenol oxidase multigene family: Cloning, phylogeny, expression analyses and immunolocalization in response to wounding

Author keywords

Eggplant; Immunolocalization; Multigene family; Phylogenetic analysis; Polyphenol oxidase gene; PPO; Solanaceae; Solanum melongena; Synteny; Wounding

Indexed keywords

CATECHOL OXIDASE; MESSENGER RNA; VEGETABLE PROTEIN;

EID: 80054915271     PISSN: 00319422     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.phytochem.2011.08.028     Document Type: Article
Times cited : (48)

References (66)
  • 1
    • 33745256005 scopus 로고    scopus 로고
    • Approximate likelihood-ratio test for branches: A fast, accurate, and powerful alternative
    • DOI 10.1080/10635150600755453, PII T8083888667361
    • M. Anisimova, and O. Gascuel Approximate likelihood-ratio test for branches: a fast, accurate, and powerful alternative Syst. Biol. 55 2006 539 552 (Pubitemid 43922340)
    • (2006) Systematic Biology , vol.55 , Issue.4 , pp. 539-552
    • Anisimova, M.1    Gascuel, O.2
  • 2
    • 57749210026 scopus 로고    scopus 로고
    • Research on catecholases, laccases and cresolases in plants. Recent progress and future needs
    • T. Aniszewski, R. Lieberei, and K. Gulewicz Research on catecholases, laccases and cresolases in plants. Recent progress and future needs Acta Biol. Cracov. Bot. 50 2008 7 18
    • (2008) Acta Biol. Cracov. Bot. , vol.50 , pp. 7-18
    • Aniszewski, T.1    Lieberei, R.2    Gulewicz, K.3
  • 4
    • 59549103093 scopus 로고    scopus 로고
    • Defensive role of tomato polyphenol oxidases against cotton bollworm (Helicoverpa armigera) and beet armyworm (Spodoptera exigua)
    • A. Bhonwong, M.J. Stout, J. Attajarusit, and P. Tantasawat Defensive role of tomato polyphenol oxidases against cotton bollworm (Helicoverpa armigera) and beet armyworm (Spodoptera exigua) J. Chem. Ecol. 35 2009 28 38
    • (2009) J. Chem. Ecol. , vol.35 , pp. 28-38
    • Bhonwong, A.1    Stout, M.J.2    Attajarusit, J.3    Tantasawat, P.4
  • 5
    • 0029159295 scopus 로고
    • An apple polyphenol oxidase cDNA is up-regulated in wounded tissues
    • P.K. Boss, R.C. Gardner, B.J. Janssen, and G.S. Ross An apple polyphenol oxidase cDNA is up-regulated in wounded tissues Plant Mol. Biol. 27 1995 429 433
    • (1995) Plant Mol. Biol. , vol.27 , pp. 429-433
    • Boss, P.K.1    Gardner, R.C.2    Janssen, B.J.3    Ross, G.S.4
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0026930134 scopus 로고
    • Cloning and characterization of cDNAs coding for Vicia faba polyphenol oxidase
    • J.W. Cary, A.R. Lax, and W.H. Flurkey Cloning and characterization of cDNAs coding for Vicia faba polyphenol oxidase Plant Mol. Biol. 20 1992 245 253
    • (1992) Plant Mol. Biol. , vol.20 , pp. 245-253
    • Cary, J.W.1    Lax, A.R.2    Flurkey, W.H.3
  • 8
    • 0034043778 scopus 로고    scopus 로고
    • Selection of conserved blocks from multiple alignments for their use in phylogenetic analysis
    • J. Castresana Selection of conserved blocks from multiple alignments for their use in phylogenetic analysis Mol. Biol. Evol. 17 2000 540 552 (Pubitemid 30210700)
    • (2000) Molecular Biology and Evolution , vol.17 , Issue.4 , pp. 540-552
    • Castresana, J.1
  • 11
    • 14644430471 scopus 로고    scopus 로고
    • ProbCons: Probabilistic consistency-based multiple sequence alignment
    • DOI 10.1101/gr.2821705
    • C.B. Do, M.S. Mahabhashyam, M. Brudno, and S. Batzoglou ProbCons: probabilistic consistency-based multiple sequence alignment Genome Res. 15 2005 330 340 (Pubitemid 40309398)
    • (2005) Genome Research , vol.15 , Issue.2 , pp. 330-340
    • Do, C.B.1    Mahabhashyam, M.S.P.2    Brudno, M.3    Batzoglou, S.4
  • 12
    • 0032935861 scopus 로고    scopus 로고
    • ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites
    • O. Emanuelsson, H. Nielsen, and G. von Heijne ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites Protein Sci. 8 1999 978 984 (Pubitemid 29211735)
    • (1999) Protein Science , vol.8 , Issue.5 , pp. 978-984
    • Emanuelsson, O.1    Nielsen, H.2    Von Heijne, G.3
  • 13
    • 0012432860 scopus 로고
    • Electrophoretic and molecular weight anomalies associated with broad bean polyphenoloxidase in SDS-PAGE electrophoresis
    • W.H. Flurkey Electrophoretic and molecular weight anomalies associated with broad bean polyphenoloxidase in SDS-PAGE electrophoresis Phytochemistry 29 1990 387 391
    • (1990) Phytochemistry , vol.29 , pp. 387-391
    • Flurkey, W.H.1
  • 14
    • 0001303619 scopus 로고
    • Microheterogeneity in purified broad bean polyphenol oxidase
    • C. Ganesa, M.T. Fox, and W.H. Flurkey Microheterogeneity in purified broad bean polyphenol oxidase Plant Physiol. 98 1992 472 479
    • (1992) Plant Physiol. , vol.98 , pp. 472-479
    • Ganesa, C.1    Fox, M.T.2    Flurkey, W.H.3
  • 15
    • 0034800754 scopus 로고    scopus 로고
    • Molecular cloning and characterisation of banana fruit polyphenol oxidase
    • DOI 10.1007/s004250100553
    • P.S. Gooding, C. Bird, and S.P. Robinson Molecular cloning and characterisation of banana fruit polyphenol oxidase Planta 213 2001 748 757 (Pubitemid 32908178)
    • (2001) Planta , vol.213 , Issue.5 , pp. 748-757
    • Gooding, P.S.1    Bird, C.2    Robinson, S.P.3
  • 16
    • 0242578620 scopus 로고    scopus 로고
    • A Simple, Fast, and Accurate Algorithm to Estimate Large Phylogenies by Maximum Likelihood
    • DOI 10.1080/10635150390235520
    • S. Guindon, and O. Gascuel A simple, fast, and accurate algorithm to estimate large phylogenies by maximum likelihood Syst. Biol. 52 2003 696 704 (Pubitemid 37365050)
    • (2003) Systematic Biology , vol.52 , Issue.5 , pp. 696-704
    • Guindon, S.1    Gascuel, O.2
  • 17
    • 80054925157 scopus 로고    scopus 로고
    • Clinico-immunological analysis of eggplant (Solanum melongena) allergy indicates preponderance of allergens in the peel
    • B.N. Harish Babu, and Y.P. Venkatesh Clinico-immunological analysis of eggplant (Solanum melongena) allergy indicates preponderance of allergens in the peel WAO J. 2 2009 192 200
    • (2009) WAO J. , vol.2 , pp. 192-200
    • Harish Babu, B.N.1    Venkatesh, Y.P.2
  • 18
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory Press Cold Spring Harbor, New York
    • E. Harlow, and D. Lane Antibodies: A Laboratory Manual 1988 Cold Spring Harbor Laboratory Press Cold Spring Harbor, New York
    • (1988) Antibodies: A Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 19
    • 68949120961 scopus 로고    scopus 로고
    • The unique enzymatic function of field bean (Dolichos lablab) d-galactose specific lectin: A polyphenol oxidase
    • S.R. Kanade, D.H. Rao, R.N. Hegde, and L.R. Gowda The unique enzymatic function of field bean (Dolichos lablab) d-galactose specific lectin: a polyphenol oxidase Glycoconjugate J. 26 2009 535 545
    • (2009) Glycoconjugate J. , vol.26 , pp. 535-545
    • Kanade, S.R.1    Rao, D.H.2    Hegde, R.N.3    Gowda, L.R.4
  • 20
    • 0035661424 scopus 로고    scopus 로고
    • Two polyphenol oxidases are differentially expressed during vegetative and reproductive development and in response to wounding in the fuji apple
    • DOI 10.1016/S0168-9452(01)00522-2, PII S0168945201005222
    • J.Y. Kim, Y.S. Seo, J.E. Kim, S.K. Sung, K.J. Song, G. An, and W.T. Kim Two polyphenol oxidases are differentially expressed during vegetative and reproductive development and in response to wounding in the Fuji apple Plant Sci. 161 2001 1145 1152 (Pubitemid 34003150)
    • (2001) Plant Science , vol.161 , Issue.6 , pp. 1145-1152
    • Kim, J.Y.1    Seo, Y.S.2    Kim, J.E.3    Sung, S.-K.4    Song, K.J.5    An, G.6    Kim, W.T.7
  • 21
    • 0031760504 scopus 로고    scopus 로고
    • Crystal structure of a plant catechol oxidase containing a dicopper center
    • DOI 10.1038/4193
    • T. Klabunde, C. Eicken, J.C. Sacchettini, and B. Krebs Crystal structure of a plant catechol oxidase containing a dicopper center Nat. Struct. Biol. 5 1998 1084 1090 (Pubitemid 28546272)
    • (1998) Nature Structural Biology , vol.5 , Issue.12 , pp. 1084-1090
    • Klabunde, T.1    Eicken, C.2    Sacchettini, J.C.3    Krebs, B.4
  • 22
    • 0032538436 scopus 로고    scopus 로고
    • Purification and properties of a novel chloroplast stromal peptidase: Processing of polyphenol oxidase and other imported precursors
    • DOI 10.1074/jbc.273.42.27064
    • S. Koussevitzky, E. Ne'eman, A. Sommer, J.C. Steffens, and E. Harel Purification and properties of a novel chloroplast stromal peptidase. Processing of polyphenol oxidase and other imported precursors J. Biol. Chem. 273 1998 27064 27069 (Pubitemid 28500410)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.42 , pp. 27064-27069
    • Koussevitzky, S.1    Ne'Eman, E.2    Sommer, A.3    Steffens, J.C.4    Harel, E.5
  • 23
    • 0030492849 scopus 로고    scopus 로고
    • Purification of the glycosylated polyphenol oxidase from potato tuber
    • D.Y. Kwon, and W.Y. Kim Purification of the glycosylated polyphenol oxidase from potato tuber J. Biochem. Mol. Biol. 29 1996 163 168
    • (1996) J. Biochem. Mol. Biol. , vol.29 , pp. 163-168
    • Kwon, D.Y.1    Kim, W.Y.2
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 29344448672 scopus 로고    scopus 로고
    • Comparative analysis of polyphenol oxidase from plant and fungal species
    • DOI 10.1016/j.jinorgbio.2005.10.008, PII S0162013405003053
    • C.M. Marusek, N.M. Trobaugh, W.H. Flurkey, and J.K. Inlow Comparative analysis of polyphenol oxidase from plant and fungal species J. Inorg. Biochem. 100 2006 108 123 (Pubitemid 43005023)
    • (2006) Journal of Inorganic Biochemistry , vol.100 , Issue.1 , pp. 108-123
    • Marusek, C.M.1    Trobaugh, N.M.2    Flurkey, W.H.3    Inlow, J.K.4
  • 26
    • 34247874476 scopus 로고    scopus 로고
    • Polyphenol oxidase (PPO) in wheat and wild relatives: Molecular evidence for a multigene family
    • DOI 10.1007/s00122-007-0514-4
    • A.N. Massa, B. Beecher, and C.F. Morris Polyphenol oxidase (PPO) in wheat and wild relatives: molecular evidence for a multigene family Theor. Appl. Genet. 114 2007 1239 1247 (Pubitemid 46697833)
    • (2007) Theoretical and Applied Genetics , vol.114 , Issue.7 , pp. 1239-1247
    • Massa, A.N.1    Beecher, B.2    Morris, C.F.3
  • 27
    • 33749517866 scopus 로고    scopus 로고
    • Polyphenol oxidases in plants and fungi: Going places? A review
    • DOI 10.1016/j.phytochem.2006.08.006, PII S0031942206004560
    • A.M. Mayer Polyphenol oxidases in plants and fungi: going places? A review Phytochemistry 67 2006 2318 2331 (Pubitemid 44527933)
    • (2006) Phytochemistry , vol.67 , Issue.21 , pp. 2318-2331
    • Mayer, A.M.1
  • 28
    • 49249153466 scopus 로고
    • Polyphenol oxidases in plants
    • A.M. Mayer, and E. Harel Polyphenol oxidases in plants Phytochemistry 18 1979 193 215
    • (1979) Phytochemistry , vol.18 , pp. 193-215
    • Mayer, A.M.1    Harel, E.2
  • 29
    • 22444432126 scopus 로고    scopus 로고
    • Gene structure and molecular analysis of the laccase-like multicopper oxidase (LMCO) gene family in Arabidopsis thaliana
    • DOI 10.1007/s00425-004-1472-6
    • B.C. McCaig, R.B. Meagher, and J.F. Dean Gene structure and molecular analysis of the laccase-like multicopper oxidase (LMCO) gene family in Arabidopsis thaliana Planta 221 2005 619 636 (Pubitemid 41003879)
    • (2005) Planta , vol.221 , Issue.5 , pp. 619-636
    • McCaig, B.C.1    Meagher, R.B.2    Dean, J.F.D.3
  • 30
    • 3242891684 scopus 로고    scopus 로고
    • DIALIGN: Multiple DNA and protein sequence alignment at BiBiServ
    • DOI 10.1093/nar/gkh373
    • Morgenstern, B.; 2004. DIALIGN: multiple DNA and protein sequence alignment at BiBiServ. Nucleic Acids Res. 32 (Web Server issue), W33-W36. (Pubitemid 38997294)
    • (2004) Nucleic Acids Research , vol.32
    • Morgenstern, B.1
  • 31
    • 0035132001 scopus 로고    scopus 로고
    • Analysis of genes preferentially expressed in early stage of pollinated and parthenocarpic fruit in eggplant
    • M. Nagasawa, A. Sugiyama, H. Mori, S.K. Katsuhiro, and S. Yamaki Analysis of genes preferentially expressed in early stage of pollinated and parthenocarpic fruit in eggplant J. Plant Physiol. 158 2001 235 240 (Pubitemid 32161067)
    • (2001) Journal of Plant Physiology , vol.158 , Issue.2 , pp. 235-240
    • Nagasawa, M.1    Sugiyama, A.2    Mori, H.3    Shiratake, K.4    Yamaki, S.5
  • 33
    • 0022507362 scopus 로고
    • Simple methods for estimating the numbers of synonymous and nonsynonymous nucleotide substitutions
    • M. Nei, and T. Gojobori Simple methods for estimating the numbers of synonymous and nonsynonymous nucleotide substitutions Mol. Biol. Evol. 3 1986 418 426 (Pubitemid 16010523)
    • (1986) Molecular Biology and Evolution , vol.3 , Issue.5 , pp. 418-426
    • Nei, M.1    Gojobori, T.2
  • 35
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • H. Nielsen, J. Engelbrecht, S. Brunak, and G. von Heijne Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites Protein Eng. 10 1997 1 6
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 38
    • 33744901041 scopus 로고    scopus 로고
    • Purification of IgG using caprylic acid
    • J.M. Walker, 2nd ed. Humana Press Totowa, New Jersey
    • M. Page, and R. Thorpe Purification of IgG using caprylic acid J.M. Walker, The Protein Protocols Handbook 2nd ed. 2002 Humana Press Totowa, New Jersey 985
    • (2002) The Protein Protocols Handbook , pp. 985
    • Page, M.1    Thorpe, R.2
  • 39
    • 0343570017 scopus 로고    scopus 로고
    • Characterization of catecholase and cresolase activities of eggplant polyphenol oxidase
    • DOI 10.1021/jf990292r
    • M. Pérez-Gilabert, and F. García Carmona Characterization of catecholase and cresolase activities of eggplant polyphenol oxidase J. Agric. Food Chem. 48 2000 695 700 (Pubitemid 30193991)
    • (2000) Journal of Agricultural and Food Chemistry , vol.48 , Issue.3 , pp. 695-700
    • Perez-Gilabert, M.1    Garcia Carmona, F.A.2
  • 40
    • 33344460777 scopus 로고    scopus 로고
    • TRANSPARENT TESTA10 encodes a laccase-like enzyme involved in oxidative polymerization of flavonoids in Arabidopsis seed coat
    • L. Pourcel, J.M. Routaboul, L. Kerhoas, M. Caboche, L. Lepiniec, and I. Debeaujon TRANSPARENT TESTA10 encodes a laccase-like enzyme involved in oxidative polymerization of flavonoids in Arabidopsis seed coat Plant Cell 17 2005 2966 2980
    • (2005) Plant Cell , vol.17 , pp. 2966-2980
    • Pourcel, L.1    Routaboul, J.M.2    Kerhoas, L.3    Caboche, M.4    Lepiniec, L.5    Debeaujon, I.6
  • 41
    • 0029141813 scopus 로고
    • Carbohydrate associated with broad bean polyphenol oxidase is resistant to enzymatic and chemical deglycosylation
    • G. Raffert, and W.H. Flurkey Carbohydrate associated with broad bean polyphenol oxidase is resistant to enzymatic and chemical deglycosylation Phytochemistry 38 1995 1355 1360
    • (1995) Phytochemistry , vol.38 , pp. 1355-1360
    • Raffert, G.1    Flurkey, W.H.2
  • 43
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • A. Shevchenko, H. Tomas, J. Havlis, J.V. Olsen, and M. Mann In-gel digestion for mass spectrometric characterization of proteins and proteomes Nat. Protoc. 1 2006 2856 2860
    • (2006) Nat. Protoc. , vol.1 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4    Mann, M.5
  • 48
    • 43649103954 scopus 로고    scopus 로고
    • Immunoaffinity chromatography
    • John Wiley and Sons, New York. Unit 8.2.1-8.2.9
    • Springer, T. A.; 2001. Immunoaffinity chromatography. In: Current Protocols in Immunology. John Wiley and Sons, New York. Unit 8.2.1-8.2.9.
    • (2001) Current Protocols in Immunology
    • Springer, T.A.1
  • 49
    • 0024348923 scopus 로고
    • Immobilization of proteins on oxidized crosslinked sepharose preparations by reductive amination
    • N.L. Stults, L.M. Asta, and Y.C. Lee Immobilization of proteins on oxidized crosslinked sepharose preparations by reductive amination Anal. Biochem. 180 1989 114 119 (Pubitemid 19200571)
    • (1989) Analytical Biochemistry , vol.180 , Issue.1 , pp. 114-119
    • Stults, N.L.1    Asta, L.M.2    Lee, Y.C.3
  • 50
    • 16544395540 scopus 로고    scopus 로고
    • Cloning and characterization of red clover polyphenol oxidase cDNAs and expression of active protein in Escherichia coli and transgenic alfalfa
    • M.L. Sullivan, R.D. Hatfield, S.L. Thoma, and D.A. Samac Cloning and characterization of red clover polyphenol oxidase cDNAs and expression of active protein in Escherichia coli and transgenic alfalfa Plant Physiol. 136 2004 3234 3244
    • (2004) Plant Physiol. , vol.136 , pp. 3234-3244
    • Sullivan, M.L.1    Hatfield, R.D.2    Thoma, S.L.3    Samac, D.A.4
  • 51
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0
    • DOI 10.1093/molbev/msm092
    • K. Tamura, J. Dudley, M. Nei, and S. Kumar MEGA4: molecular evolutionary genetics analysis (MEGA) software version 4.0 Mol. Biol. Evol. 24 2007 1596 1599 (Pubitemid 47236692)
    • (2007) Molecular Biology and Evolution , vol.24 , Issue.8 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 52
    • 0001778168 scopus 로고
    • Immunocytolocalization of polygalacturonase in ripening tomato fruit
    • D.M. Tieman, and A.K. Handa Immunocytolocalization of polygalacturonase in ripening tomato fruit Plant Physiol. 90 1989 17 20
    • (1989) Plant Physiol. , vol.90 , pp. 17-20
    • Tieman, D.M.1    Handa, A.K.2
  • 53
    • 79960422847 scopus 로고    scopus 로고
    • Genome sequence and analysis of the tuber crop potato
    • The Potato Genome Sequencing Consortium
    • The Potato Genome Sequencing Consortium, 2011. Genome sequence and analysis of the tuber crop potato. Nature 475, 189-195.
    • (2011) Nature , vol.475 , pp. 189-195
  • 54
    • 0031401382 scopus 로고    scopus 로고
    • Tomato polyphenol oxidase. Differential response of the polyphenol oxidase F promoter to injuries and wound signals
    • P. Thipyapong, and J.C. Steffens Tomato polyphenol oxidase: differential response of the polyphenol oxidase F promoter to injuries and wound signals Plant Physiol. 115 1997 409 418 (Pubitemid 28395288)
    • (1997) Plant Physiology , vol.115 , Issue.2 , pp. 409-418
    • Thipyapong, P.1    Steffens, J.C.2
  • 55
    • 0028896298 scopus 로고
    • Systemic wound induction of potato (Solanum tuberosum) polyphenol oxidase
    • P. Thipyapong, M.D. Hunt, and J.C. Steffens Systemic wound induction of potato (Solanum tuberosum) polyphenol oxidase Phytochemistry 40 1995 673 676
    • (1995) Phytochemistry , vol.40 , pp. 673-676
    • Thipyapong, P.1    Hunt, M.D.2    Steffens, J.C.3
  • 56
    • 0030975250 scopus 로고    scopus 로고
    • Differential expression and turnover of the tomato polyphenol oxidase gene family during vegetative and reproductive development
    • P. Thipyapong, D.M. Joel, and J.C. Steffens Differential expression and turnover of the tomato polyphenol oxidase gene family during vegetative and reproductive development Plant Physiol. 113 1997 707 718 (Pubitemid 27169986)
    • (1997) Plant Physiology , vol.113 , Issue.3 , pp. 707-718
    • Thipyapong, P.1    Joel, D.M.2    Steffens, J.C.3
  • 57
    • 34548433005 scopus 로고    scopus 로고
    • Functional analysis of polyphenol oxidases by antisense/sense technology
    • P. Thipyapong, M.J. Stout, and J. Attajarusit Functional analysis of polyphenol oxidases by antisense/sense technology Molecules 12 2007 1569 1595
    • (2007) Molecules , vol.12 , pp. 1569-1595
    • Thipyapong, P.1    Stout, M.J.2    Attajarusit, J.3
  • 58
    • 0029379574 scopus 로고
    • Polyphenol oxidase in potato. A multigene family that exhibits differential expression patterns
    • P.W. Thygesen, I.B. Dry, and S.P. Robinson Polyphenol oxidase in potato. A multigene family that exhibits differential expression patterns Plant Physiol. 109 1995 525 531
    • (1995) Plant Physiol. , vol.109 , pp. 525-531
    • Thygesen, P.W.1    Dry, I.B.2    Robinson, S.P.3
  • 59
    • 0019741905 scopus 로고
    • Polyphenol oxidase and peroxidase in fruits and vegetables
    • L. Vámos-Vigyázó Polyphenol oxidase and peroxidase in fruits and vegetables Crit. Rev. Food Sci. Nutr. 15 1981 49 127
    • (1981) Crit. Rev. Food Sci. Nutr. , vol.15 , pp. 49-127
    • Vámos-Vigyázó, L.1
  • 60
    • 7044238819 scopus 로고    scopus 로고
    • Polyphenol oxidase overexpression in transgenic Populus enhances resistance to herbivory by forest tent caterpillar (Malacosoma disstria)
    • DOI 10.1007/s00425-004-1327-1
    • J. Wang, and C.P. Constabel Polyphenol oxidase overexpression in transgenic Populus enhances resistance to herbivory by forest tent caterpillar (Malacosoma disstria) Planta 220 2004 87 96 (Pubitemid 40033003)
    • (2004) Planta , vol.220 , Issue.1 , pp. 87-96
    • Wang, J.1    Constabel, C.P.2
  • 61
    • 7444261436 scopus 로고    scopus 로고
    • Three polyphenol oxidases from hybrid poplar are differentially expressed during development and after wounding and elicitor treatment
    • DOI 10.1111/j.1399-3054.2004.00403.x
    • J. Wang, and C.P. Constabel Three polyphenol oxidases from hybrid poplar are differentially expressed during development and after wounding and elicitor treatment Physiol. Plant. 122 2004 344 353 (Pubitemid 39437917)
    • (2004) Physiologia Plantarum , vol.122 , Issue.3 , pp. 344-353
    • Wang, J.1    Constabel, C.P.2
  • 62
    • 0038284941 scopus 로고    scopus 로고
    • Distribution of hydroxycinnamic acid conjugates in fruit of commercial eggplant (Solanum melongena L.) cultivars
    • B.D. Whitaker, and J.R. Stommel Distribution of hydroxycinnamic acid conjugates in fruit of commercial eggplant (Solanum melongena L.) cultivars J. Agric. Food Chem. 51 2003 3448 3454
    • (2003) J. Agric. Food Chem. , vol.51 , pp. 3448-3454
    • Whitaker, B.D.1    Stommel, J.R.2
  • 63
    • 68949173463 scopus 로고    scopus 로고
    • Identification of an extensive gene cluster among a family of PPOs in Trifolium pratense L. (red clover) using a large insert BAC library
    • doi: 10.1186/1471-2229-9-94
    • A. Winters, S. Heywood, K. Farrar, I. Donnison, A. Thomas, and K.J. Webb Identification of an extensive gene cluster among a family of PPOs in Trifolium pratense L. (red clover) using a large insert BAC library BMC Plant Biol. 9 2009 94 doi: 10.1186/1471-2229-9-94
    • (2009) BMC Plant Biol. , vol.9 , pp. 94
    • Winters, A.1    Heywood, S.2    Farrar, K.3    Donnison, I.4    Thomas, A.5    Webb, K.J.6
  • 64
    • 61649114190 scopus 로고    scopus 로고
    • A detailed synteny map of the eggplant genome based on conserved ortholog set II (COSII) markers
    • F. Wu, N.T. Eannetta, Y. Xu, and S.D. Tanksley A detailed synteny map of the eggplant genome based on conserved ortholog set II (COSII) markers Theor. Appl. Genet. 118 2009 927 935
    • (2009) Theor. Appl. Genet. , vol.118 , pp. 927-935
    • Wu, F.1    Eannetta, N.T.2    Xu, Y.3    Tanksley, S.D.4
  • 65
    • 0042415543 scopus 로고    scopus 로고
    • Physicochemical properties and function of plant polyphenol oxidase: A review
    • R. Yoruk, and M.R. Marshall Physicochemical properties and function of plant polyphenol oxidase: a review J. Food Biochem. 27 2003 361 422 (Pubitemid 38034245)
    • (2003) Journal of Food Biochemistry , vol.27 , Issue.5 , pp. 361-422
    • Yoruk, R.1    Marshall, M.R.2


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