메뉴 건너뛰기




Volumn 19, Issue 1, 2007, Pages 369-387

In vivo participation of red chlorophyll catabolite reductase in chlorophyll breakdown

Author keywords

[No Author keywords available]

Indexed keywords

BIOACCUMULATION; CELL DEATH; ENZYMES; MUTAGENESIS; OXYGEN;

EID: 34249788723     PISSN: 10404651     EISSN: 1532298X     Source Type: Journal    
DOI: 10.1105/tpc.106.044404     Document Type: Article
Times cited : (206)

References (77)
  • 2
    • 0027014897 scopus 로고
    • New plant binary vectors with selectable markers located proximal to the left T-DNA border
    • Becker, D., Kemper, E., Schell, J., and Masterson, R. (1992). New plant binary vectors with selectable markers located proximal to the left T-DNA border. Plant Mol. Biol. 20: 1195-1197.
    • (1992) Plant Mol. Biol , vol.20 , pp. 1195-1197
    • Becker, D.1    Kemper, E.2    Schell, J.3    Masterson, R.4
  • 3
    • 0036443535 scopus 로고    scopus 로고
    • Chlorophyll breakdown in spinach: On the structure of five nonfluorescent chlorophyll catabolites
    • Berghold, J., Breuker, K., Oberhuber, M., Hörtensteiner, S., and Kräutler, B. (2002). Chlorophyll breakdown in spinach: On the structure of five nonfluorescent chlorophyll catabolites. Photosynth. Res. 74: 109-119.
    • (2002) Photosynth. Res , vol.74 , pp. 109-119
    • Berghold, J.1    Breuker, K.2    Oberhuber, M.3    Hörtensteiner, S.4    Kräutler, B.5
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0030912124 scopus 로고    scopus 로고
    • New bile pigment excreted by a Chlamydomonas reinhardtii mutant: A possible breakdown catabolite of chlorophyll a
    • Doi, M., Shima, S., Egashira, T., Nakamura, K., and Okayama, S. (1997). New bile pigment excreted by a Chlamydomonas reinhardtii mutant: A possible breakdown catabolite of chlorophyll a. J. Plant Physiol. 150: 504-508.
    • (1997) J. Plant Physiol , vol.150 , pp. 504-508
    • Doi, M.1    Shima, S.2    Egashira, T.3    Nakamura, K.4    Okayama, S.5
  • 6
    • 12344310587 scopus 로고    scopus 로고
    • Recent edvences in chlorophyll biosynthesis and breakdown in higher plants
    • Eckhardt, U., Grimm, B., and Hörtensteiner, S. (2004). Recent edvences in chlorophyll biosynthesis and breakdown in higher plants. Plant Mol. Biol. 56: 1-14.
    • (2004) Plant Mol. Biol , vol.56 , pp. 1-14
    • Eckhardt, U.1    Grimm, B.2    Hörtensteiner, S.3
  • 7
    • 0032935861 scopus 로고    scopus 로고
    • ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites
    • Emanualsson, O., Nielsen, H., and Von Haljna, G. (1999). ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites. Protein Sci. 8: 978-984.
    • (1999) Protein Sci , vol.8 , pp. 978-984
    • Emanualsson, O.1    Nielsen, H.2    Von Haljna, G.3
  • 8
    • 0002371956 scopus 로고    scopus 로고
    • Chlorophyll catabolism in Chlorella protothecoides. VIII. Facts and artefacts
    • Engel, N., Curty, C., and Gossauer, A. (1996). Chlorophyll catabolism in Chlorella protothecoides. VIII. Facts and artefacts. Plant Physiol. Biochem. 34: 77-83.
    • (1996) Plant Physiol. Biochem , vol.34 , pp. 77-83
    • Engel, N.1    Curty, C.2    Gossauer, A.3
  • 9
    • 0025989308 scopus 로고
    • Chlorophyll catebolism in Chlorella protothecoides. Isolation and structure elucidation of a red bilin derivative
    • Engel, N., Jenny, T.A., Mooser, V., and Gossauer, A. (1991). Chlorophyll catebolism in Chlorella protothecoides. Isolation and structure elucidation of a red bilin derivative. FEBS Lett. 293: 131-133.
    • (1991) FEBS Lett , vol.293 , pp. 131-133
    • Engel, N.1    Jenny, T.A.2    Mooser, V.3    Gossauer, A.4
  • 10
    • 0037999874 scopus 로고    scopus 로고
    • Phycocyanobilin: Ferredoxin oxidoreductase of Anabaena sp. PCC 7120
    • Frankenberg, N., and Lagarias, J.C. (2003). Phycocyanobilin: ferredoxin oxidoreductase of Anabaena sp. PCC 7120. J. Biol. Chem. 278: 9219-9226.
    • (2003) J. Biol. Chem , vol.278 , pp. 9219-9226
    • Frankenberg, N.1    Lagarias, J.C.2
  • 11
    • 0035032642 scopus 로고    scopus 로고
    • Functional genomic analysis of the HY2 femily of ferredoxin-dependent bilin reductases from oxygenic photosynthetic organisms
    • Frankenberg, N., Mukougawa, K., Kohchi, T., and Lagarias, J.C. (2001). Functional genomic analysis of the HY2 femily of ferredoxin-dependent bilin reductases from oxygenic photosynthetic organisms. Plant Cell 13: 965-978.
    • (2001) Plant Cell , vol.13 , pp. 965-978
    • Frankenberg, N.1    Mukougawa, K.2    Kohchi, T.3    Lagarias, J.C.4
  • 12
    • 0001362295 scopus 로고
    • Identification of catabolites of chlorophyll porphyrin in senescent rape cotyledons
    • Ginsburg, S., and Matile, P. (1993). Identification of catabolites of chlorophyll porphyrin in senescent rape cotyledons. Plant Physiol. 102: 521-527.
    • (1993) Plant Physiol , vol.102 , pp. 521-527
    • Ginsburg, S.1    Matile, P.2
  • 13
    • 0030891317 scopus 로고    scopus 로고
    • A novel suppressor of cell death in plants encoded by the Lls1 gene of maize
    • Gray, J., Close, P.S., Briggs, S.P., and Johal, G.S. (1997). A novel suppressor of cell death in plants encoded by the Lls1 gene of maize. Cell 89: 25-31.
    • (1997) Cell , vol.89 , pp. 25-31
    • Gray, J.1    Close, P.S.2    Briggs, S.P.3    Johal, G.S.4
  • 14
    • 3442885737 scopus 로고    scopus 로고
    • A small family of LLS1-related non-heme oxygenases in plants with an origin amongst oxygenic photosynthesizers
    • Gray, J., Wardzala, E., Yang, M., Reinbothe, S., Haller, S., and Pauli, F. (2004). A small family of LLS1-related non-heme oxygenases in plants with an origin amongst oxygenic photosynthesizers. Plant Mol. Biol. 54: 39-54.
    • (2004) Plant Mol. Biol , vol.54 , pp. 39-54
    • Gray, J.1    Wardzala, E.2    Yang, M.3    Reinbothe, S.4    Haller, S.5    Pauli, F.6
  • 15
    • 0027648727 scopus 로고
    • Arabidopsis mutants compromised for the control of cellular damage during pathogenesis and aging
    • Greenberg, J.T., and Ausubel, F.M. (1993). Arabidopsis mutants compromised for the control of cellular damage during pathogenesis and aging. Plant J. 4: 327-341.
    • (1993) Plant J , vol.4 , pp. 327-341
    • Greenberg, J.T.1    Ausubel, F.M.2
  • 16
    • 0028337519 scopus 로고
    • Programmed cell death in plants: A pathogen-triggered response activated coordinately with multiple defense functions
    • Greenberg, J.T., Guo, A., Klessig, D.F., and Ausubel, F.M. (1994). Programmed cell death in plants: A pathogen-triggered response activated coordinately with multiple defense functions. Cell 77: 551-563.
    • (1994) Cell , vol.77 , pp. 551-563
    • Greenberg, J.T.1    Guo, A.2    Klessig, D.F.3    Ausubel, F.M.4
  • 17
    • 0342803566 scopus 로고    scopus 로고
    • pGreen: A versatile and flexible binary Ti vector for Agrobacterium-mediated plant transformation
    • Hellens, R., Edwards, E.A., Leyland, N.R., Bean, S., and Mullineaux, P.M. (2000). pGreen: A versatile and flexible binary Ti vector for Agrobacterium-mediated plant transformation. Plant Mol. Biol. 42: 819-832.
    • (2000) Plant Mol. Biol , vol.42 , pp. 819-832
    • Hellens, R.1    Edwards, E.A.2    Leyland, N.R.3    Bean, S.4    Mullineaux, P.M.5
  • 18
    • 0345055799 scopus 로고    scopus 로고
    • Photoinhibition of photosynthesis in vivo results in singlet oxygen production detection via nitroxide-induced fluorescence quenching in broad bean leaves
    • Hideg, É., Kálai, T., Hideg, K., and Vass, I. (1998). Photoinhibition of photosynthesis in vivo results in singlet oxygen production detection via nitroxide-induced fluorescence quenching in broad bean leaves. Biochemistry 37: 11405-11411.
    • (1998) Biochemistry , vol.37 , pp. 11405-11411
    • Hideg, E.1    Kálai, T.2    Hideg, K.3    Vass, I.4
  • 19
    • 0029970870 scopus 로고    scopus 로고
    • How plants dispose of chlorophyll catabolites. Directly energized uptake of tetrapyrrolic breakdown products into isolated vacuoles
    • Hinder, B., Schellenberg, M., Rodoni, S., Ginsburg, S., Vogt, E., Martinola, E., Matile, P., and Hörtensteiner, S. (1996). How plants dispose of chlorophyll catabolites. Directly energized uptake of tetrapyrrolic breakdown products into isolated vacuoles. J. Biol. Chem. 271: 27233-27236.
    • (1996) J. Biol. Chem , vol.271 , pp. 27233-27236
    • Hinder, B.1    Schellenberg, M.2    Rodoni, S.3    Ginsburg, S.4    Vogt, E.5    Martinola, E.6    Matile, P.7    Hörtensteiner, S.8
  • 20
    • 0033569362 scopus 로고    scopus 로고
    • Chlorophyll breakdown in higher plants and algae
    • Hörtensteiner, S. (1999). Chlorophyll breakdown in higher plants and algae. Cell. Mol. Life Sci. 56: 330-347.
    • (1999) Cell. Mol. Life Sci , vol.56 , pp. 330-347
    • Hörtensteiner, S.1
  • 21
    • 4344566447 scopus 로고    scopus 로고
    • The loss of green color during chlorophyll degradation - A prerequisite to prevent cell death?
    • Hörtensteiner, S. (2004). The loss of green color during chlorophyll degradation - A prerequisite to prevent cell death? Planta 219: 191-194.
    • (2004) Planta , vol.219 , pp. 191-194
    • Hörtensteiner, S.1
  • 22
    • 33745940126 scopus 로고    scopus 로고
    • Chlorophyll degradation during senescence
    • Hörtensteiner, S. (2006). Chlorophyll degradation during senescence. Annu. Rev. Plant Biol. 57: 55-77.
    • (2006) Annu. Rev. Plant Biol , vol.57 , pp. 55-77
    • Hörtensteiner, S.1
  • 23
    • 0343618696 scopus 로고    scopus 로고
    • Chlorophyll breakdown in Chlorella protothecoides: Characterization of degreening and cloning of degreening-related genes
    • Hörtensteiner, S., Chinner, J., Matile, P., Thomas, H., and Donnison, I.S. (2000a). Chlorophyll breakdown in Chlorella protothecoides: Characterization of degreening and cloning of degreening-related genes. Plant Mol. Biol. 42: 439-450.
    • (2000) Plant Mol. Biol , vol.42 , pp. 439-450
    • Hörtensteiner, S.1    Chinner, J.2    Matile, P.3    Thomas, H.4    Donnison, I.S.5
  • 24
    • 0000628012 scopus 로고
    • Reappearance of hydrolytic activities and tonoplast proteins in the regenerated vacuole of evacuolated protoplasts
    • Hörtensteiner, S., Martinola, E., and Amrhein, N. (1992). Reappearance of hydrolytic activities and tonoplast proteins in the regenerated vacuole of evacuolated protoplasts. Planta 187: 113-121.
    • (1992) Planta , vol.187 , pp. 113-121
    • Hörtensteiner, S.1    Martinola, E.2    Amrhein, N.3
  • 25
    • 0027966571 scopus 로고
    • Factors affecting the re-formation of vacuoles in evacuolated protoplasts and the expression of the two vacuolar proton pumps
    • Hörtensteiner, S., Martinola, E., and Amrhein, N. (1994). Factors affecting the re-formation of vacuoles in evacuolated protoplasts and the expression of the two vacuolar proton pumps. Planta 192: 395-403.
    • (1994) Planta , vol.192 , pp. 395-403
    • Hörtensteiner, S.1    Martinola, E.2    Amrhein, N.3
  • 27
    • 0029107117 scopus 로고    scopus 로고
    • Hörtensteiner, S., Vicentini, F., and Matile, P. (1995). Chlorophyll breakdown in senescent cotyledons of rape, Brassica napus L.: Enzymatic cleavage of phaeophorbide a in vitro. New Phytol. 129: 237-246.
    • Hörtensteiner, S., Vicentini, F., and Matile, P. (1995). Chlorophyll breakdown in senescent cotyledons of rape, Brassica napus L.: Enzymatic cleavage of phaeophorbide a in vitro. New Phytol. 129: 237-246.
  • 28
    • 0032546794 scopus 로고    scopus 로고
    • The key step in chlorophyll breakdown in higher plants. Cleavage of pheophorbide a macrocycle by a monooxygenase
    • Hörtensteiner, S., Wüthrich, K.L., Matile, P., Onganla, K.-H., and Kräutler, B. (1998). The key step in chlorophyll breakdown in higher plants. Cleavage of pheophorbide a macrocycle by a monooxygenase. J. Biol. Chem. 273: 15335-15339.
    • (1998) J. Biol. Chem , vol.273 , pp. 15335-15339
    • Hörtensteiner, S.1    Wüthrich, K.L.2    Matile, P.3    Onganla, K.-H.4    Kräutler, B.5
  • 29
    • 0032124749 scopus 로고    scopus 로고
    • A porphyrin pathway impairment is responsible for the phenotype of a dominant disease lesion mimic mutant of maize
    • Hu, G., Yalpani, N., Briggs, S.P., and Johal, G.S. (1998). A porphyrin pathway impairment is responsible for the phenotype of a dominant disease lesion mimic mutant of maize. Plant Cell 10: 1095-1105.
    • (1998) Plant Cell , vol.10 , pp. 1095-1105
    • Hu, G.1    Yalpani, N.2    Briggs, S.P.3    Johal, G.S.4
  • 30
    • 0034884982 scopus 로고    scopus 로고
    • A deficiency of coproporphyrinogen III oxidase causes lesion formation in Arabidopsis
    • Ishikawa, A., Okamoto, H., Iwasaki, Y., and Asahi, T. (2001). A deficiency of coproporphyrinogen III oxidase causes lesion formation in Arabidopsis. Plant J. 27: 89-99.
    • (2001) Plant J , vol.27 , pp. 89-99
    • Ishikawa, A.1    Okamoto, H.2    Iwasaki, Y.3    Asahi, T.4
  • 31
    • 17844396639 scopus 로고    scopus 로고
    • Ancient haplotypes resulting from extensive molecular rearrangements in the wheat A genome have been maintained in species of three different ploidy levels
    • Isidore, E., Scherrer, B., Chalhoub, B., Feuillet, C., and Keller, B. (2005). Ancient haplotypes resulting from extensive molecular rearrangements in the wheat A genome have been maintained in species of three different ploidy levels. Genome Res. 15: 526-536.
    • (2005) Genome Res , vol.15 , pp. 526-536
    • Isidore, E.1    Scherrer, B.2    Chalhoub, B.3    Feuillet, C.4    Keller, B.5
  • 32
    • 0142007325 scopus 로고    scopus 로고
    • Double (fluorescent and spin) sensors for detection of reactive oxygen species in the thylakoid membrane
    • Kélel, T., Hideg, É., Vass, I., and Hideg, K. (1996). Double (fluorescent and spin) sensors for detection of reactive oxygen species in the thylakoid membrane. Free Radic. Biol. Med. 24: 649-652.
    • (1996) Free Radic. Biol. Med , vol.24 , pp. 649-652
    • Kélel, T.1    Hideg, E.2    Vass, I.3    Hideg, K.4
  • 34
    • 31844455820 scopus 로고    scopus 로고
    • The multidrug resistance-associated protein (MRP/ABCC) subfamily of ATP-binding cassette trensporters in plants
    • Klein, M., Burla, B., and Martinola, E. (2008). The multidrug resistance-associated protein (MRP/ABCC) subfamily of ATP-binding cassette trensporters in plants. FEBS Lett. 580: 1112-1122.
    • (2008) FEBS Lett , vol.580 , pp. 1112-1122
    • Klein, M.1    Burla, B.2    Martinola, E.3
  • 35
    • 0036671423 scopus 로고    scopus 로고
    • Unrevelling chlorophyll catabolism in higher plants
    • Kräutler, B. (2002). Unrevelling chlorophyll catabolism in higher plants. Biochem. Soc. Trens. 30: 625-630.
    • (2002) Biochem. Soc. Trens , vol.30 , pp. 625-630
    • Kräutler, B.1
  • 36
    • 7244237447 scopus 로고    scopus 로고
    • Chlorophyll breakdown and chlorophyll catabolites
    • In The, K.M. Kadish, K.M. Smith, and R. Guilard, eds Amsterdam: Elsevier Science, pp
    • Kräutler, B. (2003). Chlorophyll breakdown and chlorophyll catabolites. In The Porphyrin Handbook, K.M. Kadish, K.M. Smith, and R. Guilard, eds (Amsterdam: Elsevier Science), pp. 183-209.
    • (2003) Porphyrin Handbook , pp. 183-209
    • Kräutler, B.1
  • 37
    • 34249774431 scopus 로고    scopus 로고
    • Kräutler, B., and Hörtensteiner, S. (2008). Chlorophyll catabolites and the biochemistry of chlorophyll breakdown. In Chlorophylls and Bacteriochlorophylls: Biochemistry, Biophysics, Functions and Applications, B. Grimm, R. Porra, W. Rüdiger, and H. Schesr, eds (Dordracht, The Netherlands: Springer-Verlag), pp. 237-260.
    • Kräutler, B., and Hörtensteiner, S. (2008). Chlorophyll catabolites and the biochemistry of chlorophyll breakdown. In Chlorophylls and Bacteriochlorophylls: Biochemistry, Biophysics, Functions and Applications, B. Grimm, R. Porra, W. Rüdiger, and H. Schesr, eds (Dordracht, The Netherlands: Springer-Verlag), pp. 237-260.
  • 38
    • 33748598147 scopus 로고
    • On the enigma of chlorophyll degradation: The constitution of a secoporphinoid catabolite
    • Kräutler, B., Jaun, B., Bortlik, K.-H., Schellenberg, M., and Matile, P. (1991). On the enigma of chlorophyll degradation: The constitution of a secoporphinoid catabolite. Angew. Chem. Int. Ed. Engl. 30: 1315-1318.
    • (1991) Angew. Chem. Int. Ed. Engl , vol.30 , pp. 1315-1318
    • Kräutler, B.1    Jaun, B.2    Bortlik, K.-H.3    Schellenberg, M.4    Matile, P.5
  • 39
    • 0038039557 scopus 로고    scopus 로고
    • Solving the riddle of chlorophyll breakdown
    • Kräutler, B., and Matile, P. (1999). Solving the riddle of chlorophyll breakdown. Acc. Chem. Res. 32: 35-43.
    • (1999) Acc. Chem. Res , vol.32 , pp. 35-43
    • Kräutler, B.1    Matile, P.2
  • 40
    • 0030788963 scopus 로고    scopus 로고
    • Breakdown of chlorophyll: Partial synthesis of a putative intermediary catabolite
    • Kräutler, B., Mühlecker, W., Anderi, M., and Gerlach, B. (1997). Breakdown of chlorophyll: Partial synthesis of a putative intermediary catabolite. Helv. Chim. Acta 80: 1355-1362.
    • (1997) Helv. Chim. Acta , vol.80 , pp. 1355-1362
    • Kräutler, B.1    Mühlecker, W.2    Anderi, M.3    Gerlach, B.4
  • 41
    • 0033391482 scopus 로고    scopus 로고
    • T-DNA as an insertional mutagen in Arabidopsis
    • Krysan, P.J., Young, J.C., and Sussman, M.R. (1999). T-DNA as an insertional mutagen in Arabidopsis. Plant Cell 11: 2283-2290.
    • (1999) Plant Cell , vol.11 , pp. 2283-2290
    • Krysan, P.J.1    Young, J.C.2    Sussman, M.R.3
  • 42
    • 3242810318 scopus 로고    scopus 로고
    • MEGA3: Integrated software for molecular evolutionary genetics analysis and sequence alignment
    • Kumar, S., Tamura, K., and Nel, M. (2004). MEGA3: Integrated software for molecular evolutionary genetics analysis and sequence alignment. Brief. Bioinform. 5: 150-163.
    • (2004) Brief. Bioinform , vol.5 , pp. 150-163
    • Kumar, S.1    Tamura, K.2    Nel, M.3
  • 43
    • 0037593489 scopus 로고    scopus 로고
    • Lesion mimic mutants: Keys for deciphering cell death and defense pathways in plants?
    • Lorrain, S., Vallisau, F., Belaqué, C., and Roby, D. (2003). Lesion mimic mutants: Keys for deciphering cell death and defense pathways in plants? Trends Plant Sci. 8: 263-271.
    • (2003) Trends Plant Sci , vol.8 , pp. 263-271
    • Lorrain, S.1    Vallisau, F.2    Belaqué, C.3    Roby, D.4
  • 44
    • 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., Drozdowicz, Y.-M., Hörtensteiner, S., Martinoia, E., and Rea, P.A. (1998). AtMRP2, an Arabidopsis ATP binding cassette transporter able to transport glutathione S-conjugates and chlorophyll catabolites: Functional comparisons with AtMRP1. Plant Cell 10: 287-262.
    • (1998) Plant Cell , vol.10 , pp. 287-262
    • Lu, Y.-P.1    Li, Z.-S.2    Drozdowicz, Y.-M.3    Hörtensteiner, S.4    Martinoia, E.5    Rea, P.A.6
  • 45
    • 0035895231 scopus 로고    scopus 로고
    • The Arabidopsis accelerated cell death gene ACD2 encodes red chlorophyll catabolite reductase and suppresses the spread of disease symptoms
    • Mach, J.M., Castillo, A.R., Hoogstraten, R., and Greenberg, J.T. (2001). The Arabidopsis accelerated cell death gene ACD2 encodes red chlorophyll catabolite reductase and suppresses the spread of disease symptoms. Proc. Natl. Acad. Sci. USA 98: 771-776.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 771-776
    • Mach, J.M.1    Castillo, A.R.2    Hoogstraten, R.3    Greenberg, J.T.4
  • 46
    • 0000571968 scopus 로고    scopus 로고
    • Vacuolar transport of secondary metabolites and xenobiotics
    • Vacuolar Compartments, D.G. Robinson and J.C. Rogers, eds Sheffield, UK: Sheffield Academic Press, pp
    • Martinoia, E., Klein, M., Geisler, M., Sánchez- Fernández, R., and Rea, P.A. (2000). Vacuolar transport of secondary metabolites and xenobiotics. In Vacuolar Compartments. Annual Plant Reviews, D.G. Robinson and J.C. Rogers, eds (Sheffield, UK: Sheffield Academic Press), pp. 221-253.
    • (2000) Annual Plant Reviews , pp. 221-253
    • Martinoia, E.1    Klein, M.2    Geisler, M.3    Sánchez- Fernández, R.4    Rea, P.A.5
  • 48
    • 0001546658 scopus 로고
    • Production and release of a chlorophyll catabolite in isolated senescent chloroplasts
    • Matile, P., Schellenberg, M., and Pelsker, C. (1992). Production and release of a chlorophyll catabolite in isolated senescent chloroplasts. Planta 187: 230-235.
    • (1992) Planta , vol.187 , pp. 230-235
    • Matile, P.1    Schellenberg, M.2    Pelsker, C.3
  • 49
    • 0035940502 scopus 로고    scopus 로고
    • Meskauskiene, R., Nater, M., Goslings, D., Kessler, F., op den Camp, R., and Apel, K. (2001). FLU: A negative regulator of chlorophyll biosynthesis in Arabidopsis thaliana. Proc. Natl. Acad. Sci. USA 98: 12826-12831.
    • Meskauskiene, R., Nater, M., Goslings, D., Kessler, F., op den Camp, R., and Apel, K. (2001). FLU: A negative regulator of chlorophyll biosynthesis in Arabidopsis thaliana. Proc. Natl. Acad. Sci. USA 98: 12826-12831.
  • 50
    • 3242891684 scopus 로고    scopus 로고
    • DIALIGN: Multiple DNA and protein sequence alignment at BlBiServ
    • Morgenstern, B. (2004). DIALIGN: Multiple DNA and protein sequence alignment at BlBiServ. Nucleic Acids Res. 32: W33-W36.
    • (2004) Nucleic Acids Res , vol.32
    • Morgenstern, B.1
  • 51
    • 0003106633 scopus 로고    scopus 로고
    • Breakdown of chlorophyll: Constitution of nonfluorescing chlorophyll catabolites from senescent cotyledons of the dicot repe
    • Mühlecker, W., and Kräutler, B. (1996). Breakdown of chlorophyll: Constitution of nonfluorescing chlorophyll catabolites from senescent cotyledons of the dicot repe. Plant Physiol. Biochem. 34: 61-75.
    • (1996) Plant Physiol. Biochem , vol.34 , pp. 61-75
    • Mühlecker, W.1    Kräutler, B.2
  • 52
    • 0038524155 scopus 로고    scopus 로고
    • Breakdown of chlorophyll: A fluorescent chlorophyll catabolite from sweet pepper (Capsicum annuum)
    • Mühlecker, W., Kräutler, B., Mosar, D., Matile, P., and Hörtensteiner, S. (2000). Breakdown of chlorophyll: A fluorescent chlorophyll catabolite from sweet pepper (Capsicum annuum). Helv. Chim. Acta 83: 278-288.
    • (2000) Helv. Chim. Acta , vol.83 , pp. 278-288
    • Mühlecker, W.1    Kräutler, B.2    Mosar, D.3    Matile, P.4    Hörtensteiner, S.5
  • 53
    • 0030989742 scopus 로고    scopus 로고
    • Tracking down chlorophyll breakdown in plants: Elucidation of the constitution of a 'fluorescent' chlorophyll catabolite
    • Mühlecker, W., Ongania, K.-H., Kräutler, B., Matile, P., and Hörtensteiner, S. (1997). Tracking down chlorophyll breakdown in plants: Elucidation of the constitution of a 'fluorescent' chlorophyll catabolite. Angew. Chem. Int. Ed. Engl. 36: 401-404.
    • (1997) Angew. Chem. Int. Ed. Engl , vol.36 , pp. 401-404
    • Mühlecker, W.1    Ongania, K.-H.2    Kräutler, B.3    Matile, P.4    Hörtensteiner, S.5
  • 55
    • 0037795756 scopus 로고    scopus 로고
    • Breakdown of chlorophyll: A nonenzymatic reaction accounts for the formation of the colorless "nonfluorescent" chlorophyll catabolites
    • Oberhuber, M., Berghold, J., Breuker, K., Hörtensteiner, S., and Kräutler, B. (2003). Breakdown of chlorophyll: A nonenzymatic reaction accounts for the formation of the colorless "nonfluorescent" chlorophyll catabolites. Proc. Natl. Acad. Sci. USA 100: 6910-6915.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6910-6915
    • Oberhuber, M.1    Berghold, J.2    Breuker, K.3    Hörtensteiner, S.4    Kräutler, B.5
  • 57
    • 0037016636 scopus 로고    scopus 로고
    • Breakdown of chlorophyll: Electrochemical bilin reduction provides synthetic access to fluorescent chlorophyll catabolites
    • Oberhuber, M., and Kräutler, B. (2002). Breakdown of chlorophyll: Electrochemical bilin reduction provides synthetic access to fluorescent chlorophyll catabolites. ChemBioChem 3: 104-107.
    • (2002) ChemBioChem , vol.3 , pp. 104-107
    • Oberhuber, M.1    Kräutler, B.2
  • 58
    • 85115040224 scopus 로고    scopus 로고
    • op den Camp, R.G., Przybyla, D., Ochsenbein, C., Laloi, C., Kim, C., Danon, A., Wagner, D., Hideg, E., Gobel, C., Feussner, I., Nater, M., and Apel, K. (2003). Rapid induction of distinct stress responses after release of singlet oxygen in Arabidopsis. Plant Cell 15: 2320-2332.
    • op den Camp, R.G., Przybyla, D., Ochsenbein, C., Laloi, C., Kim, C., Danon, A., Wagner, D., Hideg, E., Gobel, C., Feussner, I., Nater, M., and Apel, K. (2003). Rapid induction of distinct stress responses after release of singlet oxygen in Arabidopsis. Plant Cell 15: 2320-2332.
  • 59
    • 0344735844 scopus 로고    scopus 로고
    • Chlorophyll breakdown: Pheophorbide a oxygenase is a Rieske-type iron-sulfur protein, encoded by the accelerated cell death 1 gene
    • Pružinskȧ, A., Anders, I., Tanner, G., Roca, M., and Hörtensteiner, S. (2003). Chlorophyll breakdown: Pheophorbide a oxygenase is a Rieske-type iron-sulfur protein, encoded by the accelerated cell death 1 gene. Proc. Natl. Acad. Sci. USA 100: 15259-15264.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 15259-15264
    • Pružinskȧ, A.1    Anders, I.2    Tanner, G.3    Roca, M.4    Hörtensteiner, S.5
  • 62
    • 20244377471 scopus 로고    scopus 로고
    • Functional annotation of a full-length Arabidopsis cDNA collection
    • Seki, M., et al. (2002). Functional annotation of a full-length Arabidopsis cDNA collection. Science 296: 141-145.
    • (2002) Science , vol.296 , pp. 141-145
    • Seki, M.1
  • 63
    • 0030425666 scopus 로고    scopus 로고
    • Enzymatic conversion of pheophorbide a to a precursor of pyrophsophorbide a in leaves of Chenopodium album
    • Shloi, Y., Watanabe, K., and Takamiya, K. (1998). Enzymatic conversion of pheophorbide a to a precursor of pyrophsophorbide a in leaves of Chenopodium album. Plant Cell Physiol. 37: 1143-1149.
    • (1998) Plant Cell Physiol , vol.37 , pp. 1143-1149
    • Shloi, Y.1    Watanabe, K.2    Takamiya, K.3
  • 64
    • 0031742765 scopus 로고    scopus 로고
    • Involvement of an ABC transporter in a developmental pathway regulating hypocotyl cell elongation in the light
    • Sidler, M., Hasse, P., Hasan, S., Ringil, C., and Dudler, R. (1998). Involvement of an ABC transporter in a developmental pathway regulating hypocotyl cell elongation in the light. Plant Cell 10: 1623-1638.
    • (1998) Plant Cell , vol.10 , pp. 1623-1638
    • Sidler, M.1    Hasse, P.2    Hasan, S.3    Ringil, C.4    Dudler, R.5
  • 65
    • 77956990141 scopus 로고
    • Analytical procedures for the isolation, identification, estimation and investigation of the chlorophylls
    • Strain, H.H., Cope, B.T., and Svec, W.A. (1971). Analytical procedures for the isolation, identification, estimation and investigation of the chlorophylls. Methods Enzymol. 23: 452-478.
    • (1971) Methods Enzymol , vol.23 , pp. 452-478
    • Strain, H.H.1    Cope, B.T.2    Svec, W.A.3
  • 66
    • 33646848806 scopus 로고    scopus 로고
    • Characterization and cloning of the chlorophyll-degrading enzyme pheophorbidase from cotyledons of radish
    • Suzuki, Y., Amano, T., and Shloi, Y. (2006). Characterization and cloning of the chlorophyll-degrading enzyme pheophorbidase from cotyledons of radish. Plant Physiol. 140: 716-725.
    • (2006) Plant Physiol , vol.140 , pp. 716-725
    • Suzuki, Y.1    Amano, T.2    Shloi, Y.3
  • 67
    • 0036443539 scopus 로고    scopus 로고
    • Re-examination of Mg-dechelation reaction in the degradation of chlorophylls using chlorophyllin a as substrate
    • Suzuki, T., and Shloi, Y. (2002). Re-examination of Mg-dechelation reaction in the degradation of chlorophylls using chlorophyllin a as substrate. Photosynth. Res. 74: 217-223.
    • (2002) Photosynth. Res , vol.74 , pp. 217-223
    • Suzuki, T.1    Shloi, Y.2
  • 68
    • 0033775653 scopus 로고    scopus 로고
    • Degradation pathway(s) of chlorophyll: What has gene cloning revealed?
    • Takamiya, K., Tsuchiya, T., and Ohta, H. (2000). Degradation pathway(s) of chlorophyll: What has gene cloning revealed? Trends Plant Sci. 5: 426-431.
    • (2000) Trends Plant Sci , vol.5 , pp. 426-431
    • Takamiya, K.1    Tsuchiya, T.2    Ohta, H.3
  • 70
    • 0032033674 scopus 로고    scopus 로고
    • An ABC transporter of Arabidopsis thaliana has both glutathione-conjugate and chlorophyll catabolite transport activity
    • Tommasini, R., Vogt, E., Fromenteau, M., Hörtensteiner, S., Matile, P., Amrhein, N., and Martinola, E. (1998). An ABC transporter of Arabidopsis thaliana has both glutathione-conjugate and chlorophyll catabolite transport activity. Plant J. 13: 773-780.
    • (1998) Plant J , vol.13 , pp. 773-780
    • Tommasini, R.1    Vogt, E.2    Fromenteau, M.3    Hörtensteiner, S.4    Matile, P.5    Amrhein, N.6    Martinola, E.7
  • 71
    • 3242698569 scopus 로고    scopus 로고
    • Biliverdin reduction by cyanobacterial phycocyanobilin: Ferredoxin oxidoreductase (PcyA) proceeds via linear tetrapyrrole radical intermediates
    • Tu, S.L., Gunn, A., Toney, M.D., Britt, R.D., and Lagarias, J.C. (2004). Biliverdin reduction by cyanobacterial phycocyanobilin: ferredoxin oxidoreductase (PcyA) proceeds via linear tetrapyrrole radical intermediates. J. Am. Chem. Soc. 126: 8682-8693.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 8682-8693
    • Tu, S.L.1    Gunn, A.2    Toney, M.D.3    Britt, R.D.4    Lagarias, J.C.5
  • 72
    • 8444221224 scopus 로고    scopus 로고
    • Wagner, D., Przybyla, D., op den Camp, R., Kim, C., Landgraf, F., Lee, K.P., Würsch, M., Laloi, C., Nater, M., Hideg, E., and Apel, K. (2004). The genetic basis of singlet oxygen-induced stress responses of Arabidopsis thaliana. Science 306: 1163-1185.
    • Wagner, D., Przybyla, D., op den Camp, R., Kim, C., Landgraf, F., Lee, K.P., Würsch, M., Laloi, C., Nater, M., Hideg, E., and Apel, K. (2004). The genetic basis of singlet oxygen-induced stress responses of Arabidopsis thaliana. Science 306: 1163-1185.
  • 73
    • 0034800385 scopus 로고    scopus 로고
    • Construct design for efficient, effective and high-throughput gene silencing in plants
    • Wsaley, S.V., et al. (2001). Construct design for efficient, effective and high-throughput gene silencing in plants. Plant J. 27: 581-590.
    • (2001) Plant J , vol.27 , pp. 581-590
    • Wsaley, S.V.1
  • 74
    • 0037650660 scopus 로고    scopus 로고
    • Molecular cloning, functional expression and characterisation of RCC reductase involved in chlorophyll catabolism
    • Wüthrich, K.L., Bovet, L., Hunzikar, P.E., Donnison, I.S., and Hörtensteiner, S. (2000). Molecular cloning, functional expression and characterisation of RCC reductase involved in chlorophyll catabolism. Plant J. 21: 189-198.
    • (2000) Plant J , vol.21 , pp. 189-198
    • Wüthrich, K.L.1    Bovet, L.2    Hunzikar, P.E.3    Donnison, I.S.4    Hörtensteiner, S.5
  • 75
    • 8444244951 scopus 로고    scopus 로고
    • The mitochondrion - An organelle commonly involved in programmed cell death in Arabidopsis thaliana
    • Yao, N., Eisfelder, B.J., Marvin, J., and Greenberg, J.T. (2004). The mitochondrion - An organelle commonly involved in programmed cell death in Arabidopsis thaliana. Plant J. 40: 596-610.
    • (2004) Plant J , vol.40 , pp. 596-610
    • Yao, N.1    Eisfelder, B.J.2    Marvin, J.3    Greenberg, J.T.4
  • 76
    • 33745449719 scopus 로고    scopus 로고
    • Arabidopsis ACCELERATED CELL DEATH2 modulates programmed cell death
    • Yeo, N., and Greenberg, J.T. (2006). Arabidopsis ACCELERATED CELL DEATH2 modulates programmed cell death. Plant Cell 18: 397-411.
    • (2006) Plant Cell , vol.18 , pp. 397-411
    • Yeo, N.1    Greenberg, J.T.2
  • 77
    • 0034493939 scopus 로고    scopus 로고
    • Photosensitized formation of singlet oxygen by phycobiliproteins in neutral aqueous solutions
    • Zhang, S.P., Zhao, J.Q., and Jiang, L.J. (2000). Photosensitized formation of singlet oxygen by phycobiliproteins in neutral aqueous solutions. Free Radic. Res. 33: 489-496.
    • (2000) Free Radic. Res , vol.33 , pp. 489-496
    • Zhang, S.P.1    Zhao, J.Q.2    Jiang, L.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.