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Volumn 35, Issue C, 2001, Pages 297-312

Chapter Fourteen Models for vacuolar sequestration of anthocyanins

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EID: 77957097927     PISSN: 00799920     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0079-9920(01)80015-0     Document Type: Article
Times cited : (19)

References (59)
  • 3
    • 0028814339 scopus 로고
    • Genetics and biochemistry of anthocyanin biosynthesis
    • Holton T.A., and Cornish E.C. Genetics and biochemistry of anthocyanin biosynthesis. Plant Cell 7 (1995) 1071-1083
    • (1995) Plant Cell , vol.7 , pp. 1071-1083
    • Holton, T.A.1    Cornish, E.C.2
  • 4
    • 0028155769 scopus 로고
    • The flavonoid biosynthetic pathway in plants: Function and evolution
    • Koes R.E., Quattrocchio F., and Mol J.N.M. The flavonoid biosynthetic pathway in plants: Function and evolution. BioEssays 16 (1994) 123-132
    • (1994) BioEssays , vol.16 , pp. 123-132
    • Koes, R.E.1    Quattrocchio, F.2    Mol, J.N.M.3
  • 5
    • 0034706024 scopus 로고    scopus 로고
    • Cell wall sited flavonoids in Lisianthus flower petals
    • Markham K., Ryan K., Gould K., and Rickards G. Cell wall sited flavonoids in Lisianthus flower petals. Phytochemistry 54 (2000) 681-687
    • (2000) Phytochemistry , vol.54 , pp. 681-687
    • Markham, K.1    Ryan, K.2    Gould, K.3    Rickards, G.4
  • 6
    • 77957029181 scopus 로고
    • The localization of flavonoids and phenolic enzymes in barley plastids
    • Saunders J., and McClure J.W. The localization of flavonoids and phenolic enzymes in barley plastids. Am. J. Bot. 59 (1972) 673
    • (1972) Am. J. Bot. , vol.59 , pp. 673
    • Saunders, J.1    McClure, J.W.2
  • 7
    • 77957065661 scopus 로고
    • The subcellular localization of enzymes in the flavonoid biosynthetic pathway
    • Saunders J.A., McClure J.W., and Wallace J.W. The subcellular localization of enzymes in the flavonoid biosynthetic pathway. Am. J. Bot. 60 (1973) 29
    • (1973) Am. J. Bot. , vol.60 , pp. 29
    • Saunders, J.A.1    McClure, J.W.2    Wallace, J.W.3
  • 8
    • 0028119251 scopus 로고
    • Variations in the lipophilic and vacuolar flavonoids of the genus Vellozia
    • Harborne J.B., Williams C.A., Greenham J., and Eagles J. Variations in the lipophilic and vacuolar flavonoids of the genus Vellozia. Phytochemistry 35 (1994) 1475-1480
    • (1994) Phytochemistry , vol.35 , pp. 1475-1480
    • Harborne, J.B.1    Williams, C.A.2    Greenham, J.3    Eagles, J.4
  • 9
    • 0022417989 scopus 로고
    • Purification, properties and kinetic mechanisim of flavonol 8-O-methyltransferase from Lotus corniculatus L
    • Jay M., De Luca V., and Ibrahim R.K. Purification, properties and kinetic mechanisim of flavonol 8-O-methyltransferase from Lotus corniculatus L. Eur. J. Biochem. 153 (1985) 321-325
    • (1985) Eur. J. Biochem. , vol.153 , pp. 321-325
    • Jay, M.1    De Luca, V.2    Ibrahim, R.K.3
  • 10
    • 0026326053 scopus 로고
    • Genetic and developmental control of anthocyanin biosynthesis
    • Dooner H.K., Robbins T.P., and Jorgensen R.A. Genetic and developmental control of anthocyanin biosynthesis. Annu. Rev. Gen. 25 (1991) 173-199
    • (1991) Annu. Rev. Gen. , vol.25 , pp. 173-199
    • Dooner, H.K.1    Robbins, T.P.2    Jorgensen, R.A.3
  • 12
    • 0012005634 scopus 로고
    • Subcellular localization of flavonoid synthesizing enzymes in Pisum, Phaseolus, Brassica and Spinacia cultivars
    • Hrazdina G., Alscher-Herman R., and Kish V.M. Subcellular localization of flavonoid synthesizing enzymes in Pisum, Phaseolus, Brassica and Spinacia cultivars. Phytochemistry 19 (1980) 1355-1359
    • (1980) Phytochemistry , vol.19 , pp. 1355-1359
    • Hrazdina, G.1    Alscher-Herman, R.2    Kish, V.M.3
  • 13
    • 0000455261 scopus 로고
    • Biosynthesis of cyanidin in cell cultures of Haplopappus gracilis
    • Fritsch J.H., and Grisebach H. Biosynthesis of cyanidin in cell cultures of Haplopappus gracilis. Phytochemistry 14 (1975) 2437-2442
    • (1975) Phytochemistry , vol.14 , pp. 2437-2442
    • Fritsch, J.H.1    Grisebach, H.2
  • 14
    • 0022425458 scopus 로고
    • Metabolic pathways as enzyme complexes: Evidence for the synthesis of phenylpropanoids and flavonoids on membrane associated enzyme complexes
    • Hrazdina G., and Wagner G.J. Metabolic pathways as enzyme complexes: Evidence for the synthesis of phenylpropanoids and flavonoids on membrane associated enzyme complexes. Arch. Biochem. Biophys. 237 (1984) 88-100
    • (1984) Arch. Biochem. Biophys. , vol.237 , pp. 88-100
    • Hrazdina, G.1    Wagner, G.J.2
  • 15
    • 0033607282 scopus 로고    scopus 로고
    • Interactions among enzymes of the Arabidopsis flavonoid biosynthetic pathway
    • Burbulis I.E., and Winkel-Shirley B. Interactions among enzymes of the Arabidopsis flavonoid biosynthetic pathway. Proc. Natl. Acad. Sci. USA 96 (1999) 12929-12934
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 12929-12934
    • Burbulis, I.E.1    Winkel-Shirley, B.2
  • 16
    • 0028843439 scopus 로고
    • Detection and characterization of vacuolar protein (VP24) in anthocyanin-producing cells of sweet potato in suspension culture
    • Nozue M., Kubo H., Nishimura M., and Yasuda H. Detection and characterization of vacuolar protein (VP24) in anthocyanin-producing cells of sweet potato in suspension culture. Plant Cell Phys. 36 (1995) 883-889
    • (1995) Plant Cell Phys. , vol.36 , pp. 883-889
    • Nozue, M.1    Kubo, H.2    Nishimura, M.3    Yasuda, H.4
  • 17
    • 0031277453 scopus 로고    scopus 로고
    • Expression of a vacuolar protein (VP24) in anthocyanin-producing cells of sweet potato in suspension culture
    • Nozue M., Yamada K., Nakamura T., Kubo H., Kondo M., and Nishimura M. Expression of a vacuolar protein (VP24) in anthocyanin-producing cells of sweet potato in suspension culture. Plant Physiol. 115 (1997) 1065-1072
    • (1997) Plant Physiol. , vol.115 , pp. 1065-1072
    • Nozue, M.1    Yamada, K.2    Nakamura, T.3    Kubo, H.4    Kondo, M.5    Nishimura, M.6
  • 19
    • 0027210070 scopus 로고
    • ATP-dependent glutathione S-conjugate 'export' pump in the vacuolar membrane of plants
    • Martinoia E., Grill E., Tommasini R., Kreuz K., and Amrhein N. ATP-dependent glutathione S-conjugate 'export' pump in the vacuolar membrane of plants. Nature 364 (1993) 247-249
    • (1993) Nature , vol.364 , pp. 247-249
    • Martinoia, E.1    Grill, E.2    Tommasini, R.3    Kreuz, K.4    Amrhein, N.5
  • 21
    • 0032004066 scopus 로고    scopus 로고
    • AtMRP2, an Arabidopsis ATP binding cassette transporter able to transport glutathione S-conjugates and chlorophyll catabolites: Functional comparisons with AtMRP1
    • Lu Y.-P., Li Z.-S., Dorzdowicz Y.M., Hörtensteiner S., Martinoia E., and Rea P.A. AtMRP2, an Arabidopsis ATP binding cassette transporter able to transport glutathione S-conjugates and chlorophyll catabolites: Functional comparisons with AtMRP1. Plant Cell 10 (1998) 267-282
    • (1998) Plant Cell , vol.10 , pp. 267-282
    • Lu, Y.-P.1    Li, Z.-S.2    Dorzdowicz, Y.M.3    Hörtensteiner, S.4    Martinoia, E.5    Rea, P.A.6
  • 22
    • 0029909552 scopus 로고    scopus 로고
    • Different energization mechanisms drive the vacuolar uptake of a flavonoid glucoside and a herbicide glucoside
    • Klein M., Weissenböck G., Dufaud A., Gaillard C., Kreuz K., and Martinoia E. Different energization mechanisms drive the vacuolar uptake of a flavonoid glucoside and a herbicide glucoside. J. Biol. Chem. 271 (1996) 29666-29671
    • (1996) J. Biol. Chem. , vol.271 , pp. 29666-29671
    • Klein, M.1    Weissenböck, G.2    Dufaud, A.3    Gaillard, C.4    Kreuz, K.5    Martinoia, E.6
  • 23
    • 0001791972 scopus 로고
    • The uptake of acylated anthocyanin into isolated vacuoles from a cell suspension culture of Daucus carota
    • Hopp W., and Seitz H.U. The uptake of acylated anthocyanin into isolated vacuoles from a cell suspension culture of Daucus carota. Planta 170 (1987) 74-85
    • (1987) Planta , vol.170 , pp. 74-85
    • Hopp, W.1    Seitz, H.U.2
  • 24
    • 0029009655 scopus 로고
    • A glutathione S-transferase involved in vacuolar transfer encoded by the maize gene Bronze-2
    • Marrs K.A., Alfenito M.R., Lloyd A.M., and Walbot V. A glutathione S-transferase involved in vacuolar transfer encoded by the maize gene Bronze-2. Nature 375 (1995) 397-400
    • (1995) Nature , vol.375 , pp. 397-400
    • Marrs, K.A.1    Alfenito, M.R.2    Lloyd, A.M.3    Walbot, V.4
  • 26
    • 0000677401 scopus 로고    scopus 로고
    • The functions and regulation of glutathione S-transferases in plants
    • Marrs K.A. The functions and regulation of glutathione S-transferases in plants. Annu. Rev. Plant Mol. Biol. 47 (1996) 127-158
    • (1996) Annu. Rev. Plant Mol. Biol. , vol.47 , pp. 127-158
    • Marrs, K.A.1
  • 27
    • 0031172678 scopus 로고    scopus 로고
    • Vacuolar uptake of the phytoalexin medicarpin by the glutathione conjugate pump
    • Li Z.-S., Alfenito M., Rea P.A., Walbot V., and Dixon R.A. Vacuolar uptake of the phytoalexin medicarpin by the glutathione conjugate pump. Phytochemistry 45 (1997) 689-693
    • (1997) Phytochemistry , vol.45 , pp. 689-693
    • Li, Z.-S.1    Alfenito, M.2    Rea, P.A.3    Walbot, V.4    Dixon, R.A.5
  • 28
    • 0000705071 scopus 로고
    • Efficient uptake of flavonoids into parsley (Petroselinum hortense) vacuoles requires acylated glycosides
    • Matern U., Reichenbach C., and Heller W. Efficient uptake of flavonoids into parsley (Petroselinum hortense) vacuoles requires acylated glycosides. Planta 167 (1986) 183-189
    • (1986) Planta , vol.167 , pp. 183-189
    • Matern, U.1    Reichenbach, C.2    Heller, W.3
  • 29
    • 0001031834 scopus 로고
    • Malonated cyanidin 3-glucosides in Zea mays and other grasses
    • Harborne J.B., and Self R. Malonated cyanidin 3-glucosides in Zea mays and other grasses. Phytochemistry 26 (1986) 2417-2418
    • (1986) Phytochemistry , vol.26 , pp. 2417-2418
    • Harborne, J.B.1    Self, R.2
  • 31
    • 0033845760 scopus 로고    scopus 로고
    • An9, a glutathione S-transferase from petunia required for vacuolar localization of anthocyanins, is a flavonoid binding protein
    • Mueller L.A., Silady R.A., Goodman C.D., and Walbot V. An9, a glutathione S-transferase from petunia required for vacuolar localization of anthocyanins, is a flavonoid binding protein. Plant Physiol. 123 (2000) 1561-1570
    • (2000) Plant Physiol. , vol.123 , pp. 1561-1570
    • Mueller, L.A.1    Silady, R.A.2    Goodman, C.D.3    Walbot, V.4
  • 32
    • 0032125377 scopus 로고    scopus 로고
    • Functional complementation of anthocyanin sequestration in the vacuole by widely divergent glutathione S-transferases
    • Alfenito M., Souer E., Goodman C.D., Buell R., Mol J., Koes R., and Walbot V. Functional complementation of anthocyanin sequestration in the vacuole by widely divergent glutathione S-transferases. Plant Cell 10 (1998) 1135-1149
    • (1998) Plant Cell , vol.10 , pp. 1135-1149
    • Alfenito, M.1    Souer, E.2    Goodman, C.D.3    Buell, R.4    Mol, J.5    Koes, R.6    Walbot, V.7
  • 33
    • 0023464757 scopus 로고
    • Cloning of a mutable bz2 allele of maize by transposon tagging and differential hybridization
    • Mclaughlin M., and Walbot V. Cloning of a mutable bz2 allele of maize by transposon tagging and differential hybridization. Genetics 117 (1987) 771-776
    • (1987) Genetics , vol.117 , pp. 771-776
    • Mclaughlin, M.1    Walbot, V.2
  • 34
    • 0030292797 scopus 로고    scopus 로고
    • Structure and regulation of the maize Bronze2 promoter
    • Bodeau J.P., and Walbot V. Structure and regulation of the maize Bronze2 promoter. Plant Mol. Biol. 32 (1996) 599-609
    • (1996) Plant Mol. Biol. , vol.32 , pp. 599-609
    • Bodeau, J.P.1    Walbot, V.2
  • 35
    • 0025509304 scopus 로고
    • Bronze-2 gene of maize: Reconstruction of a wild-type allele and analysis of transcription and splicing
    • Nash J., Luehrsen K.R., and Walbot V. Bronze-2 gene of maize: Reconstruction of a wild-type allele and analysis of transcription and splicing. Plant Cell 2 (1990) 1039-1049
    • (1990) Plant Cell , vol.2 , pp. 1039-1049
    • Nash, J.1    Luehrsen, K.R.2    Walbot, V.3
  • 36
    • 0001301051 scopus 로고
    • Bronze-2 gene expression and intron splicing patterns in cells and tissues of Zea mays L
    • Nash J., and Walbot V. Bronze-2 gene expression and intron splicing patterns in cells and tissues of Zea mays L. Plant Physiol. 100 (1992) 464-471
    • (1992) Plant Physiol. , vol.100 , pp. 464-471
    • Nash, J.1    Walbot, V.2
  • 37
    • 0028042292 scopus 로고
    • Abscisic acid induces pink pigmentation in maize aleurone tissue in the absence of Bronze-2
    • Walbot V., Benito M.-I., Bodeau J., and Nash J. Abscisic acid induces pink pigmentation in maize aleurone tissue in the absence of Bronze-2. Maydica 39 (1994) 19-28
    • (1994) Maydica , vol.39 , pp. 19-28
    • Walbot, V.1    Benito, M.-I.2    Bodeau, J.3    Nash, J.4
  • 38
    • 0024269217 scopus 로고
    • Glutathione Transferases - Structure and catalytic activity
    • Mannervik B., and Danielson U.H. Glutathione Transferases - Structure and catalytic activity. CRC Crit. Rev. Biochem. 23 (1988) 283-337
    • (1988) CRC Crit. Rev. Biochem. , vol.23 , pp. 283-337
    • Mannervik, B.1    Danielson, U.H.2
  • 39
    • 0031565823 scopus 로고    scopus 로고
    • Crystal-structure of herbicide-detoxifying maize glutathione S-transferase-I in complex with lactoylglutathione: evidence for an induced-fit mecha
    • Neuefeind T., Huber R., Dasenbrock H., Prade L., and Bieseler B. Crystal-structure of herbicide-detoxifying maize glutathione S-transferase-I in complex with lactoylglutathione: evidence for an induced-fit mecha. J. Mol. Biol. 274 (1997) 446-453
    • (1997) J. Mol. Biol. , vol.274 , pp. 446-453
    • Neuefeind, T.1    Huber, R.2    Dasenbrock, H.3    Prade, L.4    Bieseler, B.5
  • 40
    • 0027240567 scopus 로고
    • Identification of the hydrophobic ligand-binding region in recombinant glutathione S-transferase P and its binding effect on the conformational state of the enzyme
    • Nishihira J., Ishibashi T., Sakai M., Tsuda S., and Hikichi K. Identification of the hydrophobic ligand-binding region in recombinant glutathione S-transferase P and its binding effect on the conformational state of the enzyme. Arch. Biochem. Biophys. 302 (1993) 128-133
    • (1993) Arch. Biochem. Biophys. , vol.302 , pp. 128-133
    • Nishihira, J.1    Ishibashi, T.2    Sakai, M.3    Tsuda, S.4    Hikichi, K.5
  • 41
    • 0029914965 scopus 로고    scopus 로고
    • Three-dimensional structure of glutathione S-transferase from Arabidopsis thaliana at 2.2A resolution: Structural characterization of herbicide-conjugating plant glutathione S-transferases and a novel active site architecture
    • Reinemer P., Prade L., Hof P., Neuefeind T., Huber R., Zettl R., Schell J., Koelln I., Bartunik H.D., and Bieseler B. Three-dimensional structure of glutathione S-transferase from Arabidopsis thaliana at 2.2A resolution: Structural characterization of herbicide-conjugating plant glutathione S-transferases and a novel active site architecture. J. Mol. Biol. 255 (1996) 289-309
    • (1996) J. Mol. Biol. , vol.255 , pp. 289-309
    • Reinemer, P.1    Prade, L.2    Hof, P.3    Neuefeind, T.4    Huber, R.5    Zettl, R.6    Schell, J.7    Koelln, I.8    Bartunik, H.D.9    Bieseler, B.10
  • 42
    • 0022237942 scopus 로고
    • Isolation and characterization of the multiple glutathione S-transferases from human liver
    • Vander Jagt D.L., Hunsaker L.A., Garcia K.B., and Royer R.E. Isolation and characterization of the multiple glutathione S-transferases from human liver. J. Biol. Chem. 260 (1985) 11603-11610
    • (1985) J. Biol. Chem. , vol.260 , pp. 11603-11610
    • Vander Jagt, D.L.1    Hunsaker, L.A.2    Garcia, K.B.3    Royer, R.E.4
  • 43
    • 0027618889 scopus 로고
    • An Arabidopsis gene with homology to glutathione S-transferases is regulated by ethylene
    • Zhou J., and Goldsbrough P.B. An Arabidopsis gene with homology to glutathione S-transferases is regulated by ethylene. Plant Mol. Biol. 22 (1993) 517-523
    • (1993) Plant Mol. Biol. , vol.22 , pp. 517-523
    • Zhou, J.1    Goldsbrough, P.B.2
  • 44
    • 0029561598 scopus 로고
    • * and the contribution of the isoenzymes to cancer chemoprotection and drug resistance
    • * and the contribution of the isoenzymes to cancer chemoprotection and drug resistance. Crit. Rev. Biochem. Mol. Biol. 30 (1995) 445-600
    • (1995) Crit. Rev. Biochem. Mol. Biol. , vol.30 , pp. 445-600
    • Hayes, J.D.1    Pulford, D.J.2
  • 45
    • 0034192572 scopus 로고    scopus 로고
    • Plant glutathione S-transferases: enzymes with multiple functions in sickness and health
    • Edwards R., Dixon D.P., and Walbot V. Plant glutathione S-transferases: enzymes with multiple functions in sickness and health. Trends Plant Sci. 5 (2000) 193-198
    • (2000) Trends Plant Sci. , vol.5 , pp. 193-198
    • Edwards, R.1    Dixon, D.P.2    Walbot, V.3
  • 46
    • 0026601084 scopus 로고
    • Plant metabolism of xenobiotics
    • Sandermann H. Plant metabolism of xenobiotics. Trends Biol. Sci. 17 (1992) 82-84
    • (1992) Trends Biol. Sci. , vol.17 , pp. 82-84
    • Sandermann, H.1
  • 47
    • 0031003743 scopus 로고    scopus 로고
    • Detoxification of xenobiotics in plant cells by glutathione conjugation and vacuolar compartmentalization: a fluorescent assay using monochlorobimane
    • Coleman J.O.D., Randall R., and Blake-Kalff M.M.A. Detoxification of xenobiotics in plant cells by glutathione conjugation and vacuolar compartmentalization: a fluorescent assay using monochlorobimane. Plant Cell Environ. 20 (1997) 449-460
    • (1997) Plant Cell Environ. , vol.20 , pp. 449-460
    • Coleman, J.O.D.1    Randall, R.2    Blake-Kalff, M.M.A.3
  • 48
    • 0031127932 scopus 로고    scopus 로고
    • Detoxification of xenobiotics by plants: chemical modification and vacuolar compartmentation
    • Coleman J.O.D. Detoxification of xenobiotics by plants: chemical modification and vacuolar compartmentation. Trends Plant Sci. 2 (1997) 144-151
    • (1997) Trends Plant Sci. , vol.2 , pp. 144-151
    • Coleman, J.O.D.1
  • 49
    • 0026459859 scopus 로고
    • The ATP-dependent glutathione S-conjugate export pump
    • Ishikawa T. The ATP-dependent glutathione S-conjugate export pump. Trends Biol. Sci. 17 (1992) 463-468
    • (1992) Trends Biol. Sci. , vol.17 , pp. 463-468
    • Ishikawa, T.1
  • 50
    • 0030943564 scopus 로고    scopus 로고
    • Biochemistry and molecular biology of plant sulfotransferases
    • Varin L., Marsolais F., Richard M., and Rouleau M. Biochemistry and molecular biology of plant sulfotransferases. FASEB J. 11 (1997) 517-525
    • (1997) FASEB J. , vol.11 , pp. 517-525
    • Varin, L.1    Marsolais, F.2    Richard, M.3    Rouleau, M.4
  • 51
    • 0026705291 scopus 로고
    • Contribution of Tyrosine 6 to the catalytic mechanism of isoenzyme 3-3 of glutathione S-transferase
    • Liu S., Pinghui Z., Ji X., Johnson W.W., Gilliland G.L., and Armstrong R.N. Contribution of Tyrosine 6 to the catalytic mechanism of isoenzyme 3-3 of glutathione S-transferase. J. Biol. Chem. 267 (1992) 4296-4299
    • (1992) J. Biol. Chem. , vol.267 , pp. 4296-4299
    • Liu, S.1    Pinghui, Z.2    Ji, X.3    Johnson, W.W.4    Gilliland, G.L.5    Armstrong, R.N.6
  • 52
    • 0029101750 scopus 로고
    • Evidence for an essential serine residue in the active site of the theta class glutathione transferases
    • Board P.G., Coggan M., Wilce M.C.J., and Parker M.W. Evidence for an essential serine residue in the active site of the theta class glutathione transferases. Biochem. J. 311 (1995) 247-250
    • (1995) Biochem. J. , vol.311 , pp. 247-250
    • Board, P.G.1    Coggan, M.2    Wilce, M.C.J.3    Parker, M.W.4
  • 53
    • 0015238924 scopus 로고
    • Ligandin: A hepatic protein which binds steroids, bilirubin, carcinogens and a number of exogenous organic anions
    • Litwack G., Ketterer B., and Arias I.M. Ligandin: A hepatic protein which binds steroids, bilirubin, carcinogens and a number of exogenous organic anions. Nature 234 (1971) 466-467
    • (1971) Nature , vol.234 , pp. 466-467
    • Litwack, G.1    Ketterer, B.2    Arias, I.M.3
  • 56
    • 0027588574 scopus 로고
    • A soluble auxin-binding protein from Hyoscyamus muticus is a glutathione S-transferase
    • Bilang J., Macdonald H., King P.J., and Sturm A. A soluble auxin-binding protein from Hyoscyamus muticus is a glutathione S-transferase. Plant Physiol. 102 (1993) 29-34
    • (1993) Plant Physiol. , vol.102 , pp. 29-34
    • Bilang, J.1    Macdonald, H.2    King, P.J.3    Sturm, A.4
  • 57
    • 0029360715 scopus 로고
    • Cloning and characterization of a glutathione S-transferase that can be photolabeled with 5-azido-indole-3-acetic acid
    • Bilang J., and Sturm A. Cloning and characterization of a glutathione S-transferase that can be photolabeled with 5-azido-indole-3-acetic acid. Plant Physiol. 109 (1995) 253-260
    • (1995) Plant Physiol. , vol.109 , pp. 253-260
    • Bilang, J.1    Sturm, A.2
  • 58
    • 0028144380 scopus 로고
    • Photoaffinity labeling of Arabidopsis thaliana plasma membrane vesicles by 5-azido-[7-3H]indole-3-acetic acid: Identification of a glutathione S-transferase
    • Zettl R., Schell J., and Palme K. Photoaffinity labeling of Arabidopsis thaliana plasma membrane vesicles by 5-azido-[7-3H]indole-3-acetic acid: Identification of a glutathione S-transferase. Proc. Natl. Acad. Sci. USa 91 (1994) 689-693
    • (1994) Proc. Natl. Acad. Sci. USa , vol.91 , pp. 689-693
    • Zettl, R.1    Schell, J.2    Palme, K.3
  • 59
    • 0031853047 scopus 로고    scopus 로고
    • A Nicotiana plumbaginifolia protein labeled with an azido cytokinin agonist is a glutathione S-transferase
    • Gonneau J., Mornet R., and Laloue M. A Nicotiana plumbaginifolia protein labeled with an azido cytokinin agonist is a glutathione S-transferase. Physiol. Plant. 103 (1998) 114-124
    • (1998) Physiol. Plant. , vol.103 , pp. 114-124
    • Gonneau, J.1    Mornet, R.2    Laloue, M.3


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