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Volumn 12, Issue 1, 2007, Pages 29-36

Flavonoid oxidation in plants: from biochemical properties to physiological functions

Author keywords

[No Author keywords available]

Indexed keywords

FLAVONOID;

EID: 33846227093     PISSN: 13601385     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tplants.2006.11.006     Document Type: Review
Times cited : (758)

References (80)
  • 1
    • 33745934443 scopus 로고    scopus 로고
    • The genetics and biochemistry of floral pigments
    • Grotewold E. The genetics and biochemistry of floral pigments. Annu. Rev. Plant Biol. 57 (2006) 761-780
    • (2006) Annu. Rev. Plant Biol. , vol.57 , pp. 761-780
    • Grotewold, E.1
  • 2
    • 0036011081 scopus 로고    scopus 로고
    • Biosynthesis of flavonoids and effects of stress
    • Winkel-Shirley B. Biosynthesis of flavonoids and effects of stress. Curr. Opin. Plant Biol. 5 (2002) 218-223
    • (2002) Curr. Opin. Plant Biol. , vol.5 , pp. 218-223
    • Winkel-Shirley, B.1
  • 3
    • 33646895141 scopus 로고    scopus 로고
    • Genetics and biochemistry of seed flavonoids
    • Lepiniec L., et al. Genetics and biochemistry of seed flavonoids. Annu. Rev. Plant Biol. 57 (2006) 405-430
    • (2006) Annu. Rev. Plant Biol. , vol.57 , pp. 405-430
    • Lepiniec, L.1
  • 4
    • 11144274431 scopus 로고    scopus 로고
    • Proanthocyanidins - a final frontier in flavonoid research?
    • Dixon R.A., et al. Proanthocyanidins - a final frontier in flavonoid research?. New Phytol. 165 (2005) 9-28
    • (2005) New Phytol. , vol.165 , pp. 9-28
    • Dixon, R.A.1
  • 5
    • 84920093428 scopus 로고    scopus 로고
    • The biosynthesis of flavonoids
    • Grotewold E. (Ed), Springer
    • Winkel-Shirley B.S.J. The biosynthesis of flavonoids. In: Grotewold E. (Ed). The Science of Flavonoids (2006), Springer 71-95
    • (2006) The Science of Flavonoids , pp. 71-95
    • Winkel-Shirley, B.S.J.1
  • 6
    • 33744491283 scopus 로고    scopus 로고
    • Flavonoid diversity and biosynthesis in seed of Arabidopsis thaliana
    • Routaboul J.M., et al. Flavonoid diversity and biosynthesis in seed of Arabidopsis thaliana. Planta 224 (2006) 96-107
    • (2006) Planta , vol.224 , pp. 96-107
    • Routaboul, J.M.1
  • 8
    • 0037859527 scopus 로고    scopus 로고
    • New perspectives on proanthocyanidin biochemistry and molecular regulation
    • Marles M.A., et al. New perspectives on proanthocyanidin biochemistry and molecular regulation. Phytochemistry 64 (2003) 367-383
    • (2003) Phytochemistry , vol.64 , pp. 367-383
    • Marles, M.A.1
  • 9
    • 0025729397 scopus 로고
    • Alternatively spliced products of the maize P gene encode proteins with homology to the DNA-binding domain of myb-like transcription factors
    • Grotewold E., et al. Alternatively spliced products of the maize P gene encode proteins with homology to the DNA-binding domain of myb-like transcription factors. Proc. Natl. Acad. Sci. U. S. A. 88 (1991) 4587-4591
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 4587-4591
    • Grotewold, E.1
  • 10
    • 33746496150 scopus 로고    scopus 로고
    • Significance of flavonoids in plant resistance: a review
    • Treutter D. Significance of flavonoids in plant resistance: a review. Environ. Chem. Lett. 4 (2006) 147-157
    • (2006) Environ. Chem. Lett. , vol.4 , pp. 147-157
    • Treutter, D.1
  • 11
    • 31144447841 scopus 로고
    • Antimicrobial properties of tannins
    • Scalbert A. Antimicrobial properties of tannins. Phytochemistry 12 (1991) 3875-3883
    • (1991) Phytochemistry , vol.12 , pp. 3875-3883
    • Scalbert, A.1
  • 12
    • 0034657286 scopus 로고    scopus 로고
    • Proanthocyanidins and tannin-like compounds - nature, occurrence, dietary intake and effects on nutrition and health
    • Santos-Buelga C., and Scalbert A. Proanthocyanidins and tannin-like compounds - nature, occurrence, dietary intake and effects on nutrition and health. J. Sci. Food Agric. 80 (2000) 1094-1117
    • (2000) J. Sci. Food Agric. , vol.80 , pp. 1094-1117
    • Santos-Buelga, C.1    Scalbert, A.2
  • 13
    • 1542605222 scopus 로고    scopus 로고
    • Flavonoids: antioxidants or signalling molecules?
    • Williams R.J., et al. Flavonoids: antioxidants or signalling molecules?. Free Radic. Biol. Med. 36 (2004) 838-849
    • (2004) Free Radic. Biol. Med. , vol.36 , pp. 838-849
    • Williams, R.J.1
  • 14
    • 0036774226 scopus 로고    scopus 로고
    • Flavonoid antioxidants: chemistry, metabolism and structure-activity relationships
    • Heim K.E., et al. Flavonoid antioxidants: chemistry, metabolism and structure-activity relationships. J. Nutr. Biochem. 13 (2002) 572-584
    • (2002) J. Nutr. Biochem. , vol.13 , pp. 572-584
    • Heim, K.E.1
  • 15
    • 26444576839 scopus 로고    scopus 로고
    • Active anthocyanin degradation in Brunfelsia calycina (yesterday-today-tomorrow) flowers
    • Vaknin H., et al. Active anthocyanin degradation in Brunfelsia calycina (yesterday-today-tomorrow) flowers. Planta 222 (2005) 19-26
    • (2005) Planta , vol.222 , pp. 19-26
    • Vaknin, H.1
  • 16
    • 33645101192 scopus 로고    scopus 로고
    • Are the biological properties of kaempferol determined by its oxidation products?
    • Pirker K.F., et al. Are the biological properties of kaempferol determined by its oxidation products?. Free Radic. Res. 40 (2006) 513-521
    • (2006) Free Radic. Res. , vol.40 , pp. 513-521
    • Pirker, K.F.1
  • 17
    • 33745602782 scopus 로고    scopus 로고
    • Enzymatic polymerization of phenolic compounds using laccase and tyrosinase from Ustilago maydis
    • Desentis-Mendoza R.M., et al. Enzymatic polymerization of phenolic compounds using laccase and tyrosinase from Ustilago maydis. Biomacromolecules 7 (2006) 1845-1854
    • (2006) Biomacromolecules , vol.7 , pp. 1845-1854
    • Desentis-Mendoza, R.M.1
  • 18
    • 0035211211 scopus 로고    scopus 로고
    • Chemical properties of catechols and their molecular modes of toxic action in cells, from microorganisms to mammals
    • Schweigert N., et al. Chemical properties of catechols and their molecular modes of toxic action in cells, from microorganisms to mammals. Environ. Microbiol. 3 (2001) 81-91
    • (2001) Environ. Microbiol. , vol.3 , pp. 81-91
    • Schweigert, N.1
  • 19
    • 44049116662 scopus 로고
    • Impact of oxidized plant phenolics on the nutritional quality of dietary protein to a noctuid herbivore, Spodoptera exigua
    • Felton G.W., et al. Impact of oxidized plant phenolics on the nutritional quality of dietary protein to a noctuid herbivore, Spodoptera exigua. J. Insect Physiol. 38 (1992) 277-285
    • (1992) J. Insect Physiol. , vol.38 , pp. 277-285
    • Felton, G.W.1
  • 20
    • 0031900371 scopus 로고    scopus 로고
    • Diphenol oxidases, enzyme-catalysed browning and plant disease resistance
    • Walker J.R., and Ferrar P.H. Diphenol oxidases, enzyme-catalysed browning and plant disease resistance. Biotechnol. Genet. Eng. Rev. 15 (1998) 457-498
    • (1998) Biotechnol. Genet. Eng. Rev. , vol.15 , pp. 457-498
    • Walker, J.R.1    Ferrar, P.H.2
  • 21
    • 0030186877 scopus 로고    scopus 로고
    • Structural determination of colourless and yellow dimers resulting from (+)-catechin coupling catalysed by grape polyphenoloxidase
    • Guyot S., et al. Structural determination of colourless and yellow dimers resulting from (+)-catechin coupling catalysed by grape polyphenoloxidase. Phytochemistry 42 (1996) 1279-1288
    • (1996) Phytochemistry , vol.42 , pp. 1279-1288
    • Guyot, S.1
  • 22
    • 0002108070 scopus 로고
    • Polyphenols and enzymatic browning
    • Scalbert A. (Ed), INRA Editions
    • Nicolas J., et al. Polyphenols and enzymatic browning. In: Scalbert A. (Ed). Polyphenolic Phenomena (1993), INRA Editions 165-175
    • (1993) Polyphenolic Phenomena , pp. 165-175
    • Nicolas, J.1
  • 23
    • 0037081807 scopus 로고    scopus 로고
    • Kinetic analysis and mechanistic aspects of autoxidation of catechins
    • Mochizuki M., et al. Kinetic analysis and mechanistic aspects of autoxidation of catechins. Biochim. Biophys. Acta. 1569 (2002) 35-44
    • (2002) Biochim. Biophys. Acta. , vol.1569 , pp. 35-44
    • Mochizuki, M.1
  • 24
    • 84988201446 scopus 로고
    • Anthocyanin degradation in oxidizing grape musts
    • Cheynier V., et al. Anthocyanin degradation in oxidizing grape musts. J. Sci. Food Agric. 66 (1994) 283-288
    • (1994) J. Sci. Food Agric. , vol.66 , pp. 283-288
    • Cheynier, V.1
  • 25
    • 0344083656 scopus 로고    scopus 로고
    • Proanthocyanidin-accumulating cells in Arabidopsis testa: regulation of differentiation and role in seed development
    • Debeaujon I., et al. Proanthocyanidin-accumulating cells in Arabidopsis testa: regulation of differentiation and role in seed development. Plant Cell 15 (2003) 2514-2531
    • (2003) Plant Cell , vol.15 , pp. 2514-2531
    • Debeaujon, I.1
  • 26
    • 33344460777 scopus 로고    scopus 로고
    • TRANSPARENT TESTA10 encodes a laccase-like enzyme involved in oxidative polymerization of flavonoids in Arabidopsis seed coat
    • Pourcel L., et al. 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
  • 27
    • 27144443662 scopus 로고    scopus 로고
    • Changes in polyphenols of the seed coat during the after-darkening process in pinto beans (Phaseolus vulgaris L.)
    • Beninger C.W., et al. Changes in polyphenols of the seed coat during the after-darkening process in pinto beans (Phaseolus vulgaris L.). J. Agric. Food Chem. 53 (2005) 7777-7782
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 7777-7782
    • Beninger, C.W.1
  • 28
    • 3242793283 scopus 로고    scopus 로고
    • Advances in understanding of enzymatic browning in harvested litchi fruit
    • Jiang Y.M., et al. Advances in understanding of enzymatic browning in harvested litchi fruit. Food Chem. 88 (2004) 443-446
    • (2004) Food Chem. , vol.88 , pp. 443-446
    • Jiang, Y.M.1
  • 29
    • 13844272546 scopus 로고    scopus 로고
    • Polyphenols in foods are more complex than often thought
    • Cheynier V. Polyphenols in foods are more complex than often thought. Am. J. Clin. Nutr. 81 (2005) 223S-229S
    • (2005) Am. J. Clin. Nutr. , vol.81
    • Cheynier, V.1
  • 31
    • 0035111563 scopus 로고    scopus 로고
    • Control of enzymatic browning in potato (Solanum tuberosum L.) by sense and antisense RNA from tomato polyphenol oxidase
    • Coetzer C., et al. Control of enzymatic browning in potato (Solanum tuberosum L.) by sense and antisense RNA from tomato polyphenol oxidase. J. Agric. Food Chem. 49 (2001) 652-657
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 652-657
    • Coetzer, C.1
  • 32
    • 0035983821 scopus 로고    scopus 로고
    • Laccase: new functions for an old enzyme
    • Mayer A.M., and Staples R.C. Laccase: new functions for an old enzyme. Phytochemistry 60 (2002) 551-565
    • (2002) Phytochemistry , vol.60 , pp. 551-565
    • Mayer, A.M.1    Staples, R.C.2
  • 33
    • 0033555267 scopus 로고    scopus 로고
    • Biochemical characterization, molecular cloning and expression of laccases - a divergent gene family - in poplar
    • Ranocha P., et al. Biochemical characterization, molecular cloning and expression of laccases - a divergent gene family - in poplar. Eur. J. Biochem. 259 (1999) 485-495
    • (1999) Eur. J. Biochem. , vol.259 , pp. 485-495
    • Ranocha, P.1
  • 34
    • 29344448672 scopus 로고    scopus 로고
    • Comparative analysis of polyphenol oxidase from plant and fungal species
    • Marusek C.M., et al. Comparative analysis of polyphenol oxidase from plant and fungal species. J. Inorg. Biochem. 100 (2006) 108-123
    • (2006) J. Inorg. Biochem. , vol.100 , pp. 108-123
    • Marusek, C.M.1
  • 35
    • 33749517866 scopus 로고    scopus 로고
    • Polyphenol oxidases in plants and fungi: going places? A review
    • Mayer A.M. Polyphenol oxidases in plants and fungi: going places? A review. Phytochemistry 67 (2006) 2318-2331
    • (2006) Phytochemistry , vol.67 , pp. 2318-2331
    • Mayer, A.M.1
  • 36
    • 1242322589 scopus 로고    scopus 로고
    • Laccases: structure, reactions, distribution
    • Claus H. Laccases: structure, reactions, distribution. Micron 35 (2004) 93-96
    • (2004) Micron , vol.35 , pp. 93-96
    • Claus, H.1
  • 37
    • 33646154205 scopus 로고    scopus 로고
    • Laccases: blue enzymes for green chemistry
    • Riva S. Laccases: blue enzymes for green chemistry. Trends Biotechnol. 24 (2006) 219-226
    • (2006) Trends Biotechnol. , vol.24 , pp. 219-226
    • Riva, S.1
  • 38
    • 6944232502 scopus 로고    scopus 로고
    • Performing the paradoxical: how plant peroxidases modify the cell wall
    • Passardi F., et al. Performing the paradoxical: how plant peroxidases modify the cell wall. Trends Plant Sci. 9 (2004) 534-540
    • (2004) Trends Plant Sci. , vol.9 , pp. 534-540
    • Passardi, F.1
  • 39
    • 0035165908 scopus 로고    scopus 로고
    • The syringaldazine-oxidizing peroxidase PXP 3-4 from poplar xylem: cDNA isolation, characterization and expression
    • Christensen J.H., et al. The syringaldazine-oxidizing peroxidase PXP 3-4 from poplar xylem: cDNA isolation, characterization and expression. Plant Mol. Biol. 47 (2001) 581-593
    • (2001) Plant Mol. Biol. , vol.47 , pp. 581-593
    • Christensen, J.H.1
  • 40
    • 22444432126 scopus 로고    scopus 로고
    • Gene structure and molecular analysis of the laccase-like multicopper oxidase (LMCO) gene family in Arabidopsis thaliana
    • McCaig B.C., et al. Gene structure and molecular analysis of the laccase-like multicopper oxidase (LMCO) gene family in Arabidopsis thaliana. Planta 221 (2005) 619-636
    • (2005) Planta , vol.221 , pp. 619-636
    • McCaig, B.C.1
  • 41
    • 3042513609 scopus 로고    scopus 로고
    • Expression analysis of the Arabidopsis peroxidase multigenic family
    • Valerio L., et al. Expression analysis of the Arabidopsis peroxidase multigenic family. Phytochemistry 65 (2004) 1331-1342
    • (2004) Phytochemistry , vol.65 , pp. 1331-1342
    • Valerio, L.1
  • 42
    • 3242752669 scopus 로고    scopus 로고
    • The class III peroxidase multigenic family in rice and its evolution in land plants
    • Passardi F., et al. The class III peroxidase multigenic family in rice and its evolution in land plants. Phytochemistry 65 (2004) 1879-1893
    • (2004) Phytochemistry , vol.65 , pp. 1879-1893
    • Passardi, F.1
  • 43
    • 3543054123 scopus 로고    scopus 로고
    • Suppression of polyphenol oxidases increases stress tolerance in tomato
    • Thipyapong P., et al. Suppression of polyphenol oxidases increases stress tolerance in tomato. Plant Sci. 167 (2004) 693-703
    • (2004) Plant Sci. , vol.167 , pp. 693-703
    • Thipyapong, P.1
  • 44
    • 0033117525 scopus 로고    scopus 로고
    • Molecular cloning and characterization of apricot fruit polyphenol oxidase
    • Chevalier T., et al. Molecular cloning and characterization of apricot fruit polyphenol oxidase. Plant Physiol. 119 (1999) 1261-1269
    • (1999) Plant Physiol. , vol.119 , pp. 1261-1269
    • Chevalier, T.1
  • 45
    • 33745698762 scopus 로고    scopus 로고
    • Molecular and biochemical characterisation of polyphenol oxidases in developing kernels and senescing leaves of wheat (Triticum aestivum)
    • Jukanti A.K., et al. Molecular and biochemical characterisation of polyphenol oxidases in developing kernels and senescing leaves of wheat (Triticum aestivum). Funct. Plant Biol. 33 (2006) 685-696
    • (2006) Funct. Plant Biol. , vol.33 , pp. 685-696
    • Jukanti, A.K.1
  • 46
    • 0028002197 scopus 로고
    • Purification of an apple polyphenoloxidase isoform resistant to SDS-proteinase K digestion
    • Marques L., et al. Purification of an apple polyphenoloxidase isoform resistant to SDS-proteinase K digestion. Phytochemistry 36 (1994) 1117-1121
    • (1994) Phytochemistry , vol.36 , pp. 1117-1121
    • Marques, L.1
  • 47
    • 24344457565 scopus 로고    scopus 로고
    • Differential activation of a latent polyphenol oxidase mediated by sodium dodecyl sulfate
    • Gandia-Herrero F., et al. Differential activation of a latent polyphenol oxidase mediated by sodium dodecyl sulfate. J. Agric. Food Chem. 53 (2005) 6825-6830
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 6825-6830
    • Gandia-Herrero, F.1
  • 48
    • 0042415543 scopus 로고    scopus 로고
    • Physicochemical properties and function of plant polyphenol oxidase: a review
    • Yoruk R., and Marshall M.R. Physicochemical properties and function of plant polyphenol oxidase: a review. J. Food Biochem. 27 (2003) 361-422
    • (2003) J. Food Biochem. , vol.27 , pp. 361-422
    • Yoruk, R.1    Marshall, M.R.2
  • 49
    • 0034931568 scopus 로고    scopus 로고
    • Differential compartmentation of o-diphenols and peroxidase activity in the inner sapwood of the Juglans nigra tree
    • Dehon L., et al. Differential compartmentation of o-diphenols and peroxidase activity in the inner sapwood of the Juglans nigra tree. Plant Physiol. Biochem. 39 (2001) 473-477
    • (2001) Plant Physiol. Biochem. , vol.39 , pp. 473-477
    • Dehon, L.1
  • 50
    • 4644298103 scopus 로고    scopus 로고
    • The challenges of moving chemicals within and out of cells: insights into the transport of plant natural products
    • Grotewold E. The challenges of moving chemicals within and out of cells: insights into the transport of plant natural products. Planta 219 (2004) 906-909
    • (2004) Planta , vol.219 , pp. 906-909
    • Grotewold, E.1
  • 51
    • 0345874786 scopus 로고    scopus 로고
    • TRANSPARENT TESTA 19 is involved in the accumulation of both anthocyanins and proanthocyanidins in Arabidopsis
    • Kitamura S., et al. TRANSPARENT TESTA 19 is involved in the accumulation of both anthocyanins and proanthocyanidins in Arabidopsis. Plant J. 37 (2004) 104-114
    • (2004) Plant J. , vol.37 , pp. 104-114
    • Kitamura, S.1
  • 52
    • 33644886572 scopus 로고    scopus 로고
    • Localization of a flavonoid biosynthetic polyphenol oxidase in vacuoles
    • Ono E., et al. Localization of a flavonoid biosynthetic polyphenol oxidase in vacuoles. Plant J. 45 (2006) 133-143
    • (2006) Plant J. , vol.45 , pp. 133-143
    • Ono, E.1
  • 53
    • 19944390883 scopus 로고    scopus 로고
    • Oxidation of vacuolar and apoplastic phenolic substrates by peroxidase: physiological significance of the oxidation reactions
    • Takahama U. Oxidation of vacuolar and apoplastic phenolic substrates by peroxidase: physiological significance of the oxidation reactions. Phytochem. Rev. 3 (2004) 207-219
    • (2004) Phytochem. Rev. , vol.3 , pp. 207-219
    • Takahama, U.1
  • 54
    • 3543119626 scopus 로고    scopus 로고
    • Import of polyphenol oxidase by chloroplasts is enhanced by methyl jasmonate
    • Koussevitzky S., et al. Import of polyphenol oxidase by chloroplasts is enhanced by methyl jasmonate. Planta 219 (2004) 412-419
    • (2004) Planta , vol.219 , pp. 412-419
    • Koussevitzky, S.1
  • 55
    • 0036007895 scopus 로고    scopus 로고
    • Involvement of peroxidases in the formation of the brown coloration of heartwood in Juglans nigra
    • Dehon L., et al. Involvement of peroxidases in the formation of the brown coloration of heartwood in Juglans nigra. J. Exp. Bot. 53 (2002) 303-311
    • (2002) J. Exp. Bot. , vol.53 , pp. 303-311
    • Dehon, L.1
  • 56
    • 0037181104 scopus 로고    scopus 로고
    • Comparative study of the products of the peroxidase-catalyzed and the polyphenoloxidase-catalyzed (+)-catechin oxidation. Their possible implications in strawberry (Fragaria × ananassa) browning reactions
    • Lopez-Serrano M., and Barcelo A.R. Comparative study of the products of the peroxidase-catalyzed and the polyphenoloxidase-catalyzed (+)-catechin oxidation. Their possible implications in strawberry (Fragaria × ananassa) browning reactions. J. Agric. Food Chem. 50 (2002) 1218-1224
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 1218-1224
    • Lopez-Serrano, M.1    Barcelo, A.R.2
  • 57
    • 0020711295 scopus 로고
    • Excretion of laccase by sycamore (Acer pseudoplatanus L.) cells. Purification and properties of the enzyme
    • Bligny R., and Douce R. Excretion of laccase by sycamore (Acer pseudoplatanus L.) cells. Purification and properties of the enzyme. Biochem. J. 209 (1983) 489-496
    • (1983) Biochem. J. , vol.209 , pp. 489-496
    • Bligny, R.1    Douce, R.2
  • 58
    • 13744258114 scopus 로고    scopus 로고
    • Senescence and cell death in Brassica napus and Arabidopsis
    • Garland J.M. (Ed), BIOS Scientific Publishers
    • Buchanan-Wollaston V., and Morris K. Senescence and cell death in Brassica napus and Arabidopsis. In: Garland J.M. (Ed). Programmed Cell Death in Animals and Plants (2000), BIOS Scientific Publishers 163-174
    • (2000) Programmed Cell Death in Animals and Plants , pp. 163-174
    • Buchanan-Wollaston, V.1    Morris, K.2
  • 59
    • 2342475831 scopus 로고    scopus 로고
    • Die and let live: leaf senescence contributes to plant survival under drought stress
    • Munné-Bosch S., and Alegre L. Die and let live: leaf senescence contributes to plant survival under drought stress. Funct. Plant Biol. 31 (2004) 203-216
    • (2004) Funct. Plant Biol. , vol.31 , pp. 203-216
    • Munné-Bosch, S.1    Alegre, L.2
  • 60
    • 0000018917 scopus 로고
    • Relation between the anatomy of the testa, water permeability and the presence of phenolics in the genus Pisum
    • Werker E., et al. Relation between the anatomy of the testa, water permeability and the presence of phenolics in the genus Pisum. Ann. Bot. (Lond.) 43 (1979) 765-771
    • (1979) Ann. Bot. (Lond.) , vol.43 , pp. 765-771
    • Werker, E.1
  • 61
    • 84982646830 scopus 로고
    • Localization and changes in catechin and tannins during development and ripening of cottonseed
    • Halloin J.M. Localization and changes in catechin and tannins during development and ripening of cottonseed. New Phytol. 90 (1982) 651-657
    • (1982) New Phytol. , vol.90 , pp. 651-657
    • Halloin, J.M.1
  • 62
    • 0000931998 scopus 로고
    • Role of peroxidase in the development of water-impermeable seed coats in Sida spinosa L
    • Egley G.H., et al. Role of peroxidase in the development of water-impermeable seed coats in Sida spinosa L. Planta 157 (1983) 224-232
    • (1983) Planta , vol.157 , pp. 224-232
    • Egley, G.H.1
  • 63
    • 0035920998 scopus 로고    scopus 로고
    • Interactions between apple cell walls and native apple polyphenols: quantification and some consequences
    • Renard C.M., et al. Interactions between apple cell walls and native apple polyphenols: quantification and some consequences. Int. J. Biol. Macromol. 29 (2001) 115-125
    • (2001) Int. J. Biol. Macromol. , vol.29 , pp. 115-125
    • Renard, C.M.1
  • 64
    • 0000905094 scopus 로고
    • Barley (Hordeum vulgare) seed dormancy as related to glumella characteristics
    • Lenoir C., et al. Barley (Hordeum vulgare) seed dormancy as related to glumella characteristics. Physiol. Plant. 68 (1986) 301-307
    • (1986) Physiol. Plant. , vol.68 , pp. 301-307
    • Lenoir, C.1
  • 65
    • 17544394802 scopus 로고    scopus 로고
    • Influence of the testa on seed dormancy, germination, and longevity in Arabidopsis
    • Debeaujon I., et al. Influence of the testa on seed dormancy, germination, and longevity in Arabidopsis. Plant Physiol. 122 (2000) 403-414
    • (2000) Plant Physiol. , vol.122 , pp. 403-414
    • Debeaujon, I.1
  • 66
    • 33846232704 scopus 로고
    • The role of the oxygen permeability of the seed coat in the dormancy of seeds of Xanthium pennsylvanicum Wallr
    • Porter N.G., and Wareing P.F. The role of the oxygen permeability of the seed coat in the dormancy of seeds of Xanthium pennsylvanicum Wallr. J. Exp. Bot. 25 (1974) 583-594
    • (1974) J. Exp. Bot. , vol.25 , pp. 583-594
    • Porter, N.G.1    Wareing, P.F.2
  • 67
    • 33645746791 scopus 로고    scopus 로고
    • Hypoxia interferes with ABA metabolism and increases ABA sensitivity in embryos of dormant barley grains
    • Benech-Arnold R.L., et al. Hypoxia interferes with ABA metabolism and increases ABA sensitivity in embryos of dormant barley grains. J. Exp. Bot. 57 (2006) 1423-1430
    • (2006) J. Exp. Bot. , vol.57 , pp. 1423-1430
    • Benech-Arnold, R.L.1
  • 68
    • 3042850902 scopus 로고    scopus 로고
    • Active oxygen species and antioxidants in seed biology
    • Bailly C. Active oxygen species and antioxidants in seed biology. Seed Sci. Res. 14 (2004) 93-107
    • (2004) Seed Sci. Res. , vol.14 , pp. 93-107
    • Bailly, C.1
  • 69
    • 0033776330 scopus 로고    scopus 로고
    • Deglucosidation of quercetin glucosides to the aglycone and formation of antifungal agents by peroxidase-dependent oxidation of quercetin on browning of onion scales
    • Takahama U., and Hirota S. Deglucosidation of quercetin glucosides to the aglycone and formation of antifungal agents by peroxidase-dependent oxidation of quercetin on browning of onion scales. Plant Cell Physiol. 41 (2000) 1021-1029
    • (2000) Plant Cell Physiol. , vol.41 , pp. 1021-1029
    • Takahama, U.1    Hirota, S.2
  • 70
    • 3042825330 scopus 로고    scopus 로고
    • Ex planta phytoremediation of trichlorophenol and phenolic allelochemicals via an engineered secretory laccase
    • Wang G.D., et al. Ex planta phytoremediation of trichlorophenol and phenolic allelochemicals via an engineered secretory laccase. Nat. Biotechnol. 22 (2004) 893-897
    • (2004) Nat. Biotechnol. , vol.22 , pp. 893-897
    • Wang, G.D.1
  • 71
    • 0041470136 scopus 로고    scopus 로고
    • Allelopathy and exotic plant invasion: from molecules and genes to species interactions
    • Bais H.P., et al. Allelopathy and exotic plant invasion: from molecules and genes to species interactions. Science 301 (2003) 1377-1380
    • (2003) Science , vol.301 , pp. 1377-1380
    • Bais, H.P.1
  • 72
    • 0034920595 scopus 로고    scopus 로고
    • Phenol-oxidizing peroxidases contribute to the protection of plants from ultraviolet radiation stress
    • Jansen M.A.K., et al. Phenol-oxidizing peroxidases contribute to the protection of plants from ultraviolet radiation stress. Plant Physiol. 126 (2001) 1012-1023
    • (2001) Plant Physiol. , vol.126 , pp. 1012-1023
    • Jansen, M.A.K.1
  • 74
    • 49249153466 scopus 로고
    • Polyphenol oxidases in plants
    • Mayer H.A., and Harel E. Polyphenol oxidases in plants. Phytochemistry 18 (1979) 193-215
    • (1979) Phytochemistry , vol.18 , pp. 193-215
    • Mayer, H.A.1    Harel, E.2
  • 75
    • 0036095164 scopus 로고    scopus 로고
    • Differences in the activity and distribution of peroxidases from three different portions of germinating Brassica oleracea seeds
    • Bellani L.M., et al. Differences in the activity and distribution of peroxidases from three different portions of germinating Brassica oleracea seeds. Physiol. Plant. 114 (2002) 102-108
    • (2002) Physiol. Plant. , vol.114 , pp. 102-108
    • Bellani, L.M.1
  • 76
    • 32644443456 scopus 로고    scopus 로고
    • Biochemistry of ginseng root tissues affected by rusty root symptoms
    • Rahman M., and Punja Z.K. Biochemistry of ginseng root tissues affected by rusty root symptoms. Plant Physiol. Biochem. 43 (2005) 1103-1114
    • (2005) Plant Physiol. Biochem. , vol.43 , pp. 1103-1114
    • Rahman, M.1    Punja, Z.K.2
  • 77
    • 33744524259 scopus 로고    scopus 로고
    • Enhanced oxidation of flavan-3-ols and proanthocyanidin accumulation in water-stressed tea plants
    • Hernandez I., et al. Enhanced oxidation of flavan-3-ols and proanthocyanidin accumulation in water-stressed tea plants. Phytochemistry 67 (2006) 1120-1126
    • (2006) Phytochemistry , vol.67 , pp. 1120-1126
    • Hernandez, I.1
  • 78
    • 0033829764 scopus 로고    scopus 로고
    • Polyphenol oxidase from hybrid poplar. Cloning and expression in response to wounding and herbivory
    • Constabel C.P., et al. Polyphenol oxidase from hybrid poplar. Cloning and expression in response to wounding and herbivory. Plant Physiol. 124 (2000) 285-295
    • (2000) Plant Physiol. , vol.124 , pp. 285-295
    • Constabel, C.P.1
  • 79
    • 11144325647 scopus 로고    scopus 로고
    • Antisense downregulation of polyphenol oxidase results in enhanced disease susceptibility
    • Thipyapong P., et al. Antisense downregulation of polyphenol oxidase results in enhanced disease susceptibility. Planta 220 (2004) 105-117
    • (2004) Planta , vol.220 , pp. 105-117
    • Thipyapong, P.1
  • 80
    • 0036939059 scopus 로고    scopus 로고
    • Overexpression of polyphenol oxidase in transgenic tomato plants results in enhanced bacterial disease resistance
    • Li L., and Steffens J.C. Overexpression of polyphenol oxidase in transgenic tomato plants results in enhanced bacterial disease resistance. Planta 215 (2002) 239-247
    • (2002) Planta , vol.215 , pp. 239-247
    • Li, L.1    Steffens, J.C.2


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