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Volumn , Issue , 2005, Pages 37-54

Chlorophyll biosynthesis - a review

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EID: 26444607511     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1201/9781420027877     Document Type: Chapter
Times cited : (17)

References (163)
  • 1
    • 0002450748 scopus 로고    scopus 로고
    • Chlorophyll biosynthesis
    • Pessarakli M, ed, New York: Marcel Dekker
    • Schoefs B, Bertrand M. Chlorophyll biosynthesis. In:Pessarakli M, ed. Handbook of Photosynthesis. New York: Marcel Dekker, 1997:49-69.
    • (1997) Handbook of Photosynthesis. , pp. 49-69
    • Schoefs, B.1    Bertrand, M.2
  • 2
    • 0032524680 scopus 로고    scopus 로고
    • Greening in the dark: Light-independent chlorophyll biosynthesis from anoxygenic bacteria to gymnosperms
    • Armstrong GA. Greening in the dark: light-independent chlorophyll biosynthesis from anoxygenic bacteria to gymnosperms. J. Photochem. Photobiol. B 1998; 43:87-100.
    • (1998) J. Photochem. Photobiol. B , vol.43 , pp. 87-100
    • Armstrong, G.A.1
  • 4
    • 0032817545 scopus 로고    scopus 로고
    • Enzymes of the chlorophyll biosynthesis
    • Beale SI. Enzymes of the chlorophyll biosynthesis. Photosynth. Res. 1999; 60:43-73.
    • (1999) Photosynth. Res. , vol.60 , pp. 43-73
    • Beale, S.I.1
  • 5
    • 0033384092 scopus 로고    scopus 로고
    • The light-dependent and the light-independent reduction of protochlorophyllide a to chlorophyllide a
    • Schoefs B. The light-dependent and the light-independent reduction of protochlorophyllide a to chlorophyllide a. Photosynthetica 1999; 36:481-496.
    • (1999) Photosynthetica , vol.36 , pp. 481-496
    • Schoefs, B.1
  • 6
    • 0034437934 scopus 로고    scopus 로고
    • 18O and mass spectrometry in chlorophyll research: Derivation and loss of oxygen atom at the periphery of the chlorophyll macrocycle during biosynthesis, degradation and adaptation
    • 18O and mass spectrometry in chlorophyll research: derivation and loss of oxygen atom at the periphery of the chlorophyll macrocycle during biosynthesis, degradation and adaptation. Photosynth. Res. 2000; 66:159-175.
    • (2000) Photosynth. Res. , vol.66 , pp. 159-175
    • Porra, R.J.1    Scheer, H.2
  • 7
    • 0034794448 scopus 로고    scopus 로고
    • Regulatory network of tetrapyrrole biosynthesis - studies of intracellular signalling involved in metabolic and developmental control of plastids
    • Papenbrock J, Grimm B. Regulatory network of tetrapyrrole biosynthesis - studies of intracellular signalling involved in metabolic and developmental control of plastids. Planta 2001; 213:667-681.
    • (2001) Planta , vol.213 , pp. 667-681
    • Papenbrock, J.1    Grimm, B.2
  • 8
    • 0008779316 scopus 로고    scopus 로고
    • The light-dependent protochlorophyllide reduction: From a photoprotecting mechanism to a metabolic reaction
    • Panadalai, ed, Trivandrum: Research Signpost
    • Schoefs B. The light-dependent protochlorophyllide reduction: from a photoprotecting mechanism to a metabolic reaction. In: Panadalai, ed. Recent Research in Photosynthesis. Vol. 2. Trivandrum: Research Signpost, 2001:241-258.
    • (2001) Recent Research in Photosynthesis. , vol.2 , pp. 241-258
    • Schoefs, B.1
  • 9
    • 0035731530 scopus 로고    scopus 로고
    • The protochlorophyllide-chlorophylide cycle
    • Schoefs B. The protochlorophyllide-chlorophylide cycle. Photosynth. Res. 2001; 70:257-271.
    • (2001) Photosynth. Res. , vol.70 , pp. 257-271
    • Schoefs, B.1
  • 10
    • 85055375003 scopus 로고    scopus 로고
    • Chlorophyll biosynthesis: Lightdependent and light-independent protochlorophyllide reduction
    • Schoefs B, Franck F. Chlorophyll biosynthesis: lightdependent and light-independent protochlorophyllide reduction. Bull. Cl. Sci. Acad. R. Belgique 2002; 13:113-157.
    • (2002) Bull. Cl. Sci. Acad. R. Belgique , vol.13 , pp. 113-157
    • Schoefs, B.1    Franck, F.2
  • 11
    • 0036278316 scopus 로고    scopus 로고
    • Tetrapyrrole regulation of nuclear gene expression
    • Brusslan JA, Peterson MP. Tetrapyrrole regulation of nuclear gene expression. Photosynth. Res. 2002; 71:185-194.
    • (2002) Photosynth. Res. , vol.71 , pp. 185-194
    • Brusslan, J.A.1    Peterson, M.P.2
  • 12
    • 0032750527 scopus 로고    scopus 로고
    • Predicted structure and fold recognition for the glutamyl-TRNA reductase family of protein
    • Brody SS, Gough SP, Kannangara CG. Predicted structure and fold recognition for the glutamyl-TRNA reductase family of protein. Proteins 1999; 37:483-493.
    • (1999) Proteins , vol.37 , pp. 483-493
    • Brody, S.S.1    Gough, S.P.2    Kannangara, C.G.3
  • 14
    • 0028821439 scopus 로고
    • Heme binds to a short sequence that serve as regulatory function in diverse proteins
    • Zhang L, Guarente L. Heme binds to a short sequence that serve as regulatory function in diverse proteins. EMBO J. 1995; 14:313-320.
    • (1995) EMBO J. , vol.14 , pp. 313-320
    • Zhang, L.1    Guarente, L.2
  • 15
    • 0033042748 scopus 로고    scopus 로고
    • Light-regulated expression of the GSA gene encoding the chlorophyll biosynthetic enzyme glutamate 1-semialdehyde aminotransferase in carotenoid-deficient Chlamydomonas reinhardtii cells
    • Hermann CA, Im CS, Beale SI. Light-regulated expression of the GSA gene encoding the chlorophyll biosynthetic enzyme glutamate 1-semialdehyde aminotransferase in carotenoid-deficient Chlamydomonas reinhardtii cells. Plant Mol. Biol. 1999; 30:289-297.
    • (1999) Plant Mol. Biol. , vol.30 , pp. 289-297
    • Hermann, C.A.1    Im, C.S.2    Beale, S.I.3
  • 16
    • 85055382971 scopus 로고    scopus 로고
    • Novel inhibitors of glutamyl-tRNA(Glu) reductase activity by benzyladenine in greening cucumber cotyledons
    • Loida PJ, Thompson RL, Walker DM, Jacob CA. Novel inhibitors of glutamyl-tRNA(Glu) reductase activity by benzyladenine in greening cucumber cotyledons. Plant Cell Physiol. 1999; 36:1237-1243.
    • (1999) Plant Cell Physiol. , vol.36 , pp. 1237-1243
    • Loida, P.J.1    Thompson, R.L.2    Walker, D.M.3    Jacob, C.A.4
  • 18
    • 19244372505 scopus 로고    scopus 로고
    • Photodynamic action of uroporphyrin and protochlorophyllide in greening barley leaves treated with cesium chloride
    • Shalygo NV, Mock HP, Averina NG, Grimm B. Photodynamic action of uroporphyrin and protochlorophyllide in greening barley leaves treated with cesium chloride. J. Photochem. Photobiol. B 1998; 42:151-158.
    • (1998) J. Photochem. Photobiol. B , vol.42 , pp. 151-158
    • Shalygo, N.V.1    Mock, H.P.2    Averina, N.G.3    Grimm, B.4
  • 21
    • 0000125103 scopus 로고
    • Biosynthesis of the pigments of life - Mechanistic studies on the conversion of porphobilinogen to uroporphyrinogen III
    • Battersby AR, Leeper FJ. Biosynthesis of the pigments of life - Mechanistic studies on the conversion of porphobilinogen to uroporphyrinogen III. Chem. Rev. 1990; 90:1261-1267.
    • (1990) Chem. Rev. , vol.90 , pp. 1261-1267
    • Battersby, A.R.1    Leeper, F.J.2
  • 22
    • 0035760901 scopus 로고    scopus 로고
    • Functional consequences of naturally occurring mutations in human uroporphyrinogen decarboxylase
    • Phillips JD, Parker TL, Schubert HL, Whitby FG, Kushner JP. Functional consequences of naturally occurring mutations in human uroporphyrinogen decarboxylase. Blood 2001; 98:3179-3185.
    • (2001) Blood , vol.98 , pp. 3179-3185
    • Phillips, J.D.1    Parker, T.L.2    Schubert, H.L.3    Whitby, F.G.4    Kushner, J.P.5
  • 24
    • 0037077688 scopus 로고    scopus 로고
    • Mutagenesis identifies a conserved tyrosine residue important for the activity of uroporphyrinogen III synthase from Anacystis nidulans
    • Roessner CA, Ponnamperuma K, Scott AI. Mutagenesis identifies a conserved tyrosine residue important for the activity of uroporphyrinogen III synthase from Anacystis nidulans. FEBS Lett. 2002; 525:25-28.
    • (2002) FEBS Lett. , vol.525 , pp. 25-28
    • Roessner, C.A.1    Ponnamperuma, K.2    Scott, A.I.3
  • 25
    • 0031008511 scopus 로고    scopus 로고
    • Characterization and crystallization of human uroporphyrinogen decarboxylase; X-ray diffraction
    • Phillips JD, Whitby FG, Kushner JP, Hill CP. Characterization and crystallization of human uroporphyrinogen decarboxylase; X-ray diffraction. Protein Sci. 1997; 6:1343-1346.
    • (1997) Protein Sci. , vol.6 , pp. 1343-1346
    • Phillips, J.D.1    Whitby, F.G.2    Kushner, J.P.3    Hill, C.P.4
  • 26
    • 0008615417 scopus 로고    scopus 로고
    • Molecular characterisation of coproporphyrinogen oxidase from soybean (Glycine max) and Arabidopsis thaliana
    • Santana MA, Tan F-C, Smith AG. Molecular characterisation of coproporphyrinogen oxidase from soybean (Glycine max) and Arabidopsis thaliana. Plant Physiol. Biochem. 2002; 40:289-298.
    • (2002) Plant Physiol. Biochem. , vol.40 , pp. 289-298
    • Santana, M.A.1    Tan, F.-C.2    Smith, A.G.3
  • 27
    • 0030738530 scopus 로고    scopus 로고
    • Cloning and characterization of plastidial and mitochondrial isoform of tobacco protoporphyrinogen IX oxidase
    • Lermontova I, Kruse E, Mock HP, Grimm B. Cloning and characterization of plastidial and mitochondrial isoform of tobacco protoporphyrinogen IX oxidase. Proc. Natl. Acad. Sci. USA 1997; 94:8895-8900.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 8895-8900
    • Lermontova, I.1    Kruse, E.2    Mock, H.P.3    Grimm, B.4
  • 28
    • 0343114321 scopus 로고    scopus 로고
    • Cloning, sequence and characterization of protoporphyrinogen IX oxidase from chicory
    • Adomat C, Böger P. Cloning, sequence and characterization of protoporphyrinogen IX oxidase from chicory. Pestic. Biochem. Physiol. 1999; 66:49-62.
    • (1999) Pestic. Biochem. Physiol. , vol.66 , pp. 49-62
    • Adomat, C.1    Böger, P.2
  • 29
    • 85055381295 scopus 로고
    • Expression of a clones protoporphyrinogen oxidase
    • Dailey HA, Meisner P, Dailey HA. Expression of a clones protoporphyrinogen oxidase. J. Biol. Chem. 1994; 271:8714-8718.
    • (1994) J. Biol. Chem. , vol.271 , pp. 8714-8718
    • Dailey, H.A.1    Meisner, P.2    Dailey, H.A.3
  • 30
    • 85009631734 scopus 로고    scopus 로고
    • Generation of resistance to the diphenyl herbicide, oxyfluorfen, via expression of Bacillus subtilis protoporphyrinogen oxidase gene in transgenic tobacco plants
    • Choi KW, Han O, Lee HJ, Yun YC, Moon YM, Kim M, Kuk YI, Han SU, Guh JO. Generation of resistance to the diphenyl herbicide, oxyfluorfen, via expression of Bacillus subtilis protoporphyrinogen oxidase gene in transgenic tobacco plants. Biosci. Biotechnol. Biochem. 1998; 62:558-560.
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , pp. 558-560
    • Choi, K.W.1    Han, O.2    Lee, H.J.3    Yun, Y.C.4    Moon, Y.M.5    Kim, M.6    Kuk, Y.I.7    Han, S.U.8    Guh, J.O.9
  • 31
    • 0033923452 scopus 로고    scopus 로고
    • Transgenic rice plants expressing a Bacillus subtilis protoporphyrinogen oxidase gene are resistant to diphenyl ether herbicide oxyfluorfen
    • Lee HJ, Lee SB, Chung JS, Han SU, Han O, Guh JO, Jeon J, An G, Back K. Transgenic rice plants expressing a Bacillus subtilis protoporphyrinogen oxidase gene are resistant to diphenyl ether herbicide oxyfluorfen. Plant Cell Physiol. 2000; 41:743-749.
    • (2000) Plant Cell Physiol. , vol.41 , pp. 743-749
    • Lee, H.J.1    Lee, S.B.2    Chung, J.S.3    Han, S.U.4    Han, O.5    Guh, J.O.6    Jeon, J.7    An, G.8    Back, K.9
  • 32
    • 0021456162 scopus 로고
    • Genetic-physical mapping of a photosynthetic gene cluster in R. capsulatus
    • Zsebo KM, Hearst, JE. Genetic-physical mapping of a photosynthetic gene cluster in R. capsulatus. Cell 1984; 37:937-947.
    • (1984) Cell , vol.37 , pp. 937-947
    • Zsebo, K.M.1    Hearst, J.E.2
  • 34
    • 0031444348 scopus 로고    scopus 로고
    • Isolation and characterisation of tobacco (Nicotiana tabacum) cDNA clones encoding proteins involved in magnesium chelation into protoporphyrin IX
    • Kruse E, Mock HP, Grimm B. Isolation and characterisation of tobacco (Nicotiana tabacum) cDNA clones encoding proteins involved in magnesium chelation into protoporphyrin IX. Plant Mol. Biol. 1997; 35:1053-1056.
    • (1997) Plant Mol. Biol. , vol.35 , pp. 1053-1056
    • Kruse, E.1    Mock, H.P.2    Grimm, B.3
  • 35
    • 0031279340 scopus 로고    scopus 로고
    • Mg-chelatase of tobacco: Identification of a ChlD cDNA sequence encoding a third subunit, analysis of the interaction of the three subunits with the east two-hybrid system and reconstitution of the enzyme activity by co-expression of recombinant ChlD, ChlH and ChlI
    • Papenbrock J, Gräfe S, Kruse E, Hänel F, Grimm B. Mg-chelatase of tobacco: identification of a ChlD cDNA sequence encoding a third subunit, analysis of the interaction of the three subunits with the east two-hybrid system and reconstitution of the enzyme activity by co-expression of recombinant ChlD, ChlH and ChlI. Plant J. 1997; 12:981-990.
    • (1997) Plant J. , vol.12 , pp. 981-990
    • Papenbrock, J.1    Gräfe, S.2    Kruse, E.3    Hänel, F.4    Grimm, B.5
  • 36
    • 0030662568 scopus 로고    scopus 로고
    • Mechanism and regulation of Mg-chelatase
    • Walker CJ, Willows RD. Mechanism and regulation of Mg-chelatase. Biochem. J. 1997; 327:321-333.
    • (1997) Biochem. J. , vol.327 , pp. 321-333
    • Walker, C.J.1    Willows, R.D.2
  • 38
    • 0030903547 scopus 로고    scopus 로고
    • Magnesium chelatase association with ribosomes and mutant complementation studies identify barley subunit Xantha-G as a functional counterpart of Rhodobacter subunit BchD
    • Kannangara CG, Vothknecht UC, Hansson M, von Wettstein D. Magnesium chelatase association with ribosomes and mutant complementation studies identify barley subunit Xantha-G as a functional counterpart of Rhodobacter subunit BchD. Mol. Gen. Genet. 1997; 254:85-92.
    • (1997) Mol. Gen. Genet. , vol.254 , pp. 85-92
    • Kannangara, C.G.1    Vothknecht, U.C.2    Hansson, M.3    von Wettstein, D.4
  • 39
    • 0032168182 scopus 로고    scopus 로고
    • Determinants of catalytic activity with the use of purified I, D and H subunits of the magnesium protoporphyrin IX chelatase from Synechocystis PCC6803
    • Jensen PE, Gibson LCD, Hunter CN. Determinants of catalytic activity with the use of purified I, D and H subunits of the magnesium protoporphyrin IX chelatase from Synechocystis PCC6803. Biochem. J. 1998; 334:335-344.
    • (1998) Biochem. J. , vol.334 , pp. 335-344
    • Jensen, P.E.1    Gibson, L.C.D.2    Hunter, C.N.3
  • 42
    • 0033573997 scopus 로고    scopus 로고
    • Molecular basis for semidominance of missense mutations in the XANTHA-H (42 kDa) subunit of magnesium chelatase
    • Hansson M, Kannangara CG, von Wettstein D, Hansson M. Molecular basis for semidominance of missense mutations in the XANTHA-H (42 kDa) subunit of magnesium chelatase. Proc. Natl. Acad. Sci. USA 1999; 96:1744-1749.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1744-1749
    • Hansson, M.1    Kannangara, C.G.2    von Wettstein, D.3    Hansson, M.4
  • 43
    • 0030695453 scopus 로고    scopus 로고
    • ATPases and phosphate exchange activities in magnesium chelatase subunits of Rhodobacter sphaeroides
    • Hansson M, Kannangara CG. ATPases and phosphate exchange activities in magnesium chelatase subunits of Rhodobacter sphaeroides. Proc. Natl. Acad. Sci. USA 1997; 94:13351-13356.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13351-13356
    • Hansson, M.1    Kannangara, C.G.2
  • 44
    • 0035822662 scopus 로고    scopus 로고
    • Characterization of the binding of deuteroporphyrin IX to the magnesium chelatase H subunit and spectroscopic properties of the complex
    • Karger GA, Reid JD, Hunter CN. Characterization of the binding of deuteroporphyrin IX to the magnesium chelatase H subunit and spectroscopic properties of the complex. Biochemistry 2001; 40:9291-9299.
    • (2001) Biochemistry , vol.40 , pp. 9291-9299
    • Karger, G.A.1    Reid, J.D.2    Hunter, C.N.3
  • 45
    • 0034885052 scopus 로고    scopus 로고
    • + superfamily ATPases: Common structures - diverse function
    • + superfamily ATPases:common structures - diverse function. Genes Cells 2001; 6:575-587.
    • (2001) Genes Cells , vol.6 , pp. 575-587
    • Ogura, T.1    Wilkinson, A.T.2
  • 47
  • 48
    • 0034533228 scopus 로고    scopus 로고
    • Modification of cysteine residues in the CHLI and CHLL subunits of magnesium chelatase results in enzyme inactivation
    • Jensen PE, Reid JD, Hunter CN. Modification of cysteine residues in the CHLI and CHLL subunits of magnesium chelatase results in enzyme inactivation. Biochem. J. 2000; 352:435-441.
    • (2000) Biochem. J. , vol.352 , pp. 435-441
    • Jensen, P.E.1    Reid, J.D.2    Hunter, C.N.3
  • 49
    • 0035190234 scopus 로고    scopus 로고
    • A plastidic ABC protein involved in intercompartmental communication of light signaling
    • Moller SG, Kunkel T, Chua N-H. A plastidic ABC protein involved in intercompartmental communication of light signaling. Genes Dev. 2001; 15:90-103.
    • (2001) Genes Dev. , vol.15 , pp. 90-103
    • Moller, S.G.1    Kunkel, T.2    Chua, N.-H.3
  • 50
    • 0001951550 scopus 로고    scopus 로고
    • Introduction to marine phytoplankton and their pigment signatures
    • Jeffrey SW, Mantoura RFC, Vesk M, eds, Paris: UNESCO
    • Jeffrey SW, Vesk M. Introduction to marine phytoplankton and their pigment signatures. In: Jeffrey SW, Mantoura RFC, Vesk M, eds. Phytoplankton Pigments in Oceanography. Paris: UNESCO, 1997:37-84.
    • (1997) Phytoplankton Pigments in Oceanography. , pp. 37-84
    • Jeffrey, S.W.1    Vesk, M.2
  • 51
    • 0030492071 scopus 로고    scopus 로고
    • Origin of the chlorophyll a biosynthetic heterogeneity in higher plants
    • Kim JS, Rebeiz CA. Origin of the chlorophyll a biosynthetic heterogeneity in higher plants. J. Biochem. Mol. Biol. 1996; 29:327-334.
    • (1996) J. Biochem. Mol. Biol. , vol.29 , pp. 327-334
    • Kim, J.S.1    Rebeiz, C.A.2
  • 52
    • 0002533621 scopus 로고
    • Chloroplast biogenesis 60. Conversion of divinyl protochlorophyllide to monovinyl protochlorophylide in green(ing) barley, a dark monovinyl/light divinyl plant species
    • Tripathy BC, Rebeiz CA. Chloroplast biogenesis 60. Conversion of divinyl protochlorophyllide to monovinyl protochlorophylide in green(ing) barley, a dark monovinyl/light divinyl plant species. Plant Physiol. 1988; 87:89-94.
    • (1988) Plant Physiol. , vol.87 , pp. 89-94
    • Tripathy, B.C.1    Rebeiz, C.A.2
  • 53
    • 0028832211 scopus 로고
    • Chloroplast biogenesis 72: A [4-vinyl]chlorophyllide a reductase assay using divinyl chlorophyllide a as an exogenous substrate
    • Parham R, Rebeiz CA. Chloroplast biogenesis 72:a [4-vinyl]chlorophyllide a reductase assay using divinyl chlorophyllide a as an exogenous substrate. Anal. Biochem. 1995; 231:164-169.
    • (1995) Anal. Biochem. , vol.231 , pp. 164-169
    • Parham, R.1    Rebeiz, C.A.2
  • 54
    • 0001410067 scopus 로고    scopus 로고
    • Chloroplast biogenesis 81: Transient formation of divinyl chlorophyll a following a 2.5 ms light flash treatment of etiolated cucumber cotyledons
    • Andra AN, Rebeiz CA. Chloroplast biogenesis 81:transient formation of divinyl chlorophyll a following a 2.5 ms light flash treatment of etiolated cucumber cotyledons. Photochem. Photobiol. 1998; 68:852-856.
    • (1998) Photochem. Photobiol. , vol.68 , pp. 852-856
    • Andra, A.N.1    Rebeiz, C.A.2
  • 55
    • 0031291201 scopus 로고    scopus 로고
    • Chloroplast biogenesis 76: Regulation of 4-vinyl reduction during conversion of divinyl-Mg-protophorphyrin IX to monovinyl protochlorophyllide a is controlled by plastid membranes and stromal factors
    • Kim JS, Klossov V, Rebeiz CA. Chloroplast biogenesis 76: regulation of 4-vinyl reduction during conversion of divinyl-Mg-protophorphyrin IX to monovinyl protochlorophyllide a is controlled by plastid membranes and stromal factors. Photosynthetica 1997; 34:569-581.
    • (1997) Photosynthetica , vol.34 , pp. 569-581
    • Kim, J.S.1    Klossov, V.2    Rebeiz, C.A.3
  • 56
    • 0035881777 scopus 로고    scopus 로고
    • Chloroplast biogenesis 84: Solubilization and partial purification of membranebound [4-vinyl] chlorophyllide a reductase from etiolated barley leaves
    • Kolossov VL, Rebeiz CA. Chloroplast biogenesis 84:solubilization and partial purification of membranebound [4-vinyl] chlorophyllide a reductase from etiolated barley leaves. Anal. Biochem. 2001; 295:214-219.
    • (2001) Anal. Biochem. , vol.295 , pp. 214-219
    • Kolossov, V.L.1    Rebeiz, C.A.2
  • 57
  • 59
    • 0033621182 scopus 로고    scopus 로고
    • The AtCAO gene, encoding chlorophyll a oxygenase, is required for chlorophyll b synthesis in Arabidopsis thaliana
    • Espineda CE, Lindford AS, Devine D, Brusslan JA. The AtCAO gene, encoding chlorophyll a oxygenase, is required for chlorophyll b synthesis in Arabidopsis thaliana. Proc. Natl. Acad. Sci. USA 1999; 76:10507-10511.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 10507-10511
    • Espineda, C.E.1    Lindford, A.S.2    Devine, D.3    Brusslan, J.A.4
  • 60
    • 0033536171 scopus 로고    scopus 로고
    • Chlorophyll b and phycobilins in the common ancestor of cyanobacteria and chloroplasts
    • Tomitani A, Okada K, Miyashita H, Matthijs HC, Ohno T, Tanaka A. Chlorophyll b and phycobilins in the common ancestor of cyanobacteria and chloroplasts. Nature 1999; 400:159-162.
    • (1999) Nature , vol.400 , pp. 159-162
    • Tomitani, A.1    Okada, K.2    Miyashita, H.3    Matthijs, H.C.4    Ohno, T.5    Tanaka, A.6
  • 61
    • 0034058987 scopus 로고    scopus 로고
    • Cloning and functional expression of the gene encoding the key enzyme for chlorophyll b biosynthesis (CAO) from Arabidopsis thaliana
    • Oster U, Tanaka R, Tanaka A, Rüdiger W. Cloning and functional expression of the gene encoding the key enzyme for chlorophyll b biosynthesis (CAO) from Arabidopsis thaliana. Plant J. 2000; 21:301-305.
    • (2000) Plant J. , vol.21 , pp. 301-305
    • Oster, U.1    Tanaka, R.2    Tanaka, A.3    Rüdiger, W.4
  • 62
    • 0031796097 scopus 로고    scopus 로고
    • Changes in the photosynthetic pigments in bean leaves during the first photoperiod of greening and the subsequent darkphase. Comparison between old (10-d-old) leaves and young (2-d-old) leaves
    • Schoefs B, Bertrand M, Lemoine Y. Changes in the photosynthetic pigments in bean leaves during the first photoperiod of greening and the subsequent darkphase. Comparison between old (10-d-old) leaves and young (2-d-old) leaves. Photosynth. Res. 1998; 57:203-213.
    • (1998) Photosynth. Res. , vol.57 , pp. 203-213
    • Schoefs, B.1    Bertrand, M.2    Lemoine, Y.3
  • 63
    • 0029151252 scopus 로고
    • Reduction of coproporphyrinogen oxidase level by antisense RNA synthesis leads to deregulated gene expression of plastid proteins and affects the oxidation defense systems
    • Kruse E, Mock HP, Grimm B. Reduction of coproporphyrinogen oxidase level by antisense RNA synthesis leads to deregulated gene expression of plastid proteins and affects the oxidation defense systems. EMBO J. 1995; 14:3710-3720.
    • (1995) EMBO J. , vol.14 , pp. 3710-3720
    • Kruse, E.1    Mock, H.P.2    Grimm, B.3
  • 64
    • 0000868948 scopus 로고    scopus 로고
    • Photosynthetic pigment metabolism in plants during stress
    • Pessarakli M, ed, New York: Marcel Dekker
    • Bertrand M, Schoefs B. Photosynthetic pigment metabolism in plants during stress. In: Pessarakli M, ed. Handbook of Plant and Crop Stress. New York: Marcel Dekker, 1999:527-543.
    • (1999) Handbook of Plant and Crop Stress. , pp. 527-543
    • Bertrand, M.1    Schoefs, B.2
  • 65
    • 0033753278 scopus 로고    scopus 로고
    • Rice plants with a high protochlorophyllide accumulation show oxidative stress in low light that mimics water stress
    • Boo YC, Lee KP, Jung J. Rice plants with a high protochlorophyllide accumulation show oxidative stress in low light that mimics water stress. J. Plant Physiol. 2000; 157:405-411.
    • (2000) J. Plant Physiol. , vol.157 , pp. 405-411
    • Boo, Y.C.1    Lee, K.P.2    Jung, J.3
  • 66
    • 0034469261 scopus 로고    scopus 로고
    • Comparative analysis of the low molecular weight and enzymatic antioxidants in response to the phototoxicity of accumulating uroporphyrin and protochlorophyllide in barley leaves treated with cesium chloride
    • Shalygo NV, Mock HP, Averina NG, Grimm B. Comparative analysis of the low molecular weight and enzymatic antioxidants in response to the phototoxicity of accumulating uroporphyrin and protochlorophyllide in barley leaves treated with cesium chloride. Photosynth. Res. 2000; 64:267-276.
    • (2000) Photosynth. Res. , vol.64 , pp. 267-276
    • Shalygo, N.V.1    Mock, H.P.2    Averina, N.G.3    Grimm, B.4
  • 67
    • 0030988808 scopus 로고    scopus 로고
    • Developmental and circadian control of the capacity for d-aminolevulinic acid synthesis in green barley
    • Kruse E, Grimm B, Beator J, Kloppstech K. Developmental and circadian control of the capacity for d-aminolevulinic acid synthesis in green barley. Planta 1997; 202:235-241.
    • (1997) Planta , vol.202 , pp. 235-241
    • Kruse, E.1    Grimm, B.2    Beator, J.3    Kloppstech, K.4
  • 68
    • 0028369994 scopus 로고
    • Light regulation of chlorophyll biosynthesis at the level of 5-aminolevulinic formation in Arabidopsis
    • Ilag LL, Kumar AM, Söll D. Light regulation of chlorophyll biosynthesis at the level of 5-aminolevulinic formation in Arabidopsis. Plant Cell 1994; 6:265-275.
    • (1994) Plant Cell , vol.6 , pp. 265-275
    • Ilag, L.L.1    Kumar, A.M.2    Söll, D.3
  • 70
    • 0033181037 scopus 로고    scopus 로고
    • Selective inhibition of HEMA gene expression by photooxidation in Arabidopsis thaliana
    • Kumar AM, Chaturvedi S, Söll D. Selective inhibition of HEMA gene expression by photooxidation in Arabidopsis thaliana. Phytochemistry 1999; 51:847-850.
    • (1999) Phytochemistry , vol.51 , pp. 847-850
    • Kumar, A.M.1    Chaturvedi, S.2    Söll, D.3
  • 71
    • 0035034119 scopus 로고    scopus 로고
    • Regulation of HEMA1 expression by phytochrome and a plastid signal during de-etiolation in Arabidopsis thaliana
    • McCormac AC, Fischer A, Kumar AM, Söll D, Terry MJ. Regulation of HEMA1 expression by phytochrome and a plastid signal during de-etiolation in Arabidopsis thaliana. Plant J. 2001; 25:549-561.
    • (2001) Plant J. , vol.25 , pp. 549-561
    • McCormac, A.C.1    Fischer, A.2    Kumar, A.M.3    Söll, D.4    Terry, M.J.5
  • 72
    • 0037772260 scopus 로고    scopus 로고
    • Light-signalling pathways leading to the co-ordinated expression of HEMA1 and Lhcb during chloroplast development in Arabidopsis thaliana
    • McCormac AC, Terry MJ. Light-signalling pathways leading to the co-ordinated expression of HEMA1 and Lhcb during chloroplast development in Arabidopsis thaliana. Plant J. 2002; 32:549-559.
    • (2002) Plant J. , vol.32 , pp. 549-559
    • McCormac, A.C.1    Terry, M.J.2
  • 73
    • 0036742783 scopus 로고    scopus 로고
    • Loss of nuclear gene expression during the phytochrome A-mediated far-red block of greening response
    • McCormac AC, Terry MJ. Loss of nuclear gene expression during the phytochrome A-mediated far-red block of greening response. Plant Physiol. 2002; 130:402-414.
    • (2002) Plant Physiol. , vol.130 , pp. 402-414
    • McCormac, A.C.1    Terry, M.J.2
  • 74
    • 0032004065 scopus 로고    scopus 로고
    • Etioplast differentiation in Arabidopsis: Both PORA and PORB restore the prolamellar body and photoactive Pchlide-F655 to the cop1 photomorphogenic mutant
    • Sperling U, Franck F, van Cleve B, Frick G, Apel K, Armstrong G. Etioplast differentiation in Arabidopsis:both PORA and PORB restore the prolamellar body and photoactive Pchlide-F655 to the cop1 photomorphogenic mutant. Plant Cell 1998; 10:283-296.
    • (1998) Plant Cell , vol.10 , pp. 283-296
    • Sperling, U.1    Franck, F.2    van Cleve, B.3    Frick, G.4    Apel, K.5    Armstrong, G.6
  • 75
    • 0030162258 scopus 로고    scopus 로고
    • Members of low-copy number of gene family glutamyl-tRNA reductase are differentially expressed in barley
    • Bougi O, Grimm B. Members of low-copy number of gene family glutamyl-tRNA reductase are differentially expressed in barley. Plant J. 1996; 9:867-878.
    • (1996) Plant J. , vol.9 , pp. 867-878
    • Bougi, O.1    Grimm, B.2
  • 76
    • 0030292241 scopus 로고    scopus 로고
    • Glutamyltransfer RNA: At the crossroad between chlorophyll and protein synthesis
    • Kumar AM, Schaub U, Söll D, Ujwal ML. Glutamyltransfer RNA: at the crossroad between chlorophyll and protein synthesis. Trends Plant Sci. 1996; 1:371-376.4
    • (1996) Trends Plant Sci. , vol.1 , pp. 371-376
    • Kumar, A.M.1    Schaub, U.2    Söll, D.3    Ujwal, M.L.4
  • 77
    • 0030112935 scopus 로고    scopus 로고
    • Differential expression of two hemA mRNAs encoding glutamyl-tRNA reductase proteins in greening cucumber seedlings
    • Tanaka R, Yoshida K, Nakayashiki T, Masuda T, Tsuji H, Inokuchi H, Tanaka A. Differential expression of two hemA mRNAs encoding glutamyl-tRNA reductase proteins in greening cucumber seedlings. Plant Physiol. 1996; 110:1223-1230.
    • (1996) Plant Physiol. , vol.110 , pp. 1223-1230
    • Tanaka, R.1    Yoshida, K.2    Nakayashiki, T.3    Masuda, T.4    Tsuji, H.5    Inokuchi, H.6    Tanaka, A.7
  • 78
    • 0030780145 scopus 로고    scopus 로고
    • The third member of the hemA gene family encoding glutamyl-tRNA reductase is primarily expressed in roots of Hordeum vulgare
    • Tanaka R, Yoshida K, Nakayashiki T, Tsuji H, Inokuchi H, Okada K, Tanaka A. The third member of the hemA gene family encoding glutamyl-tRNA reductase is primarily expressed in roots of Hordeum vulgare. Photosynth. Res. 1997; 53:161-171.
    • (1997) Photosynth. Res. , vol.53 , pp. 161-171
    • Tanaka, R.1    Yoshida, K.2    Nakayashiki, T.3    Tsuji, H.4    Inokuchi, H.5    Okada, K.6    Tanaka, A.7
  • 79
    • 0020200155 scopus 로고
    • Protoporphyrinogen oxidation in chloroplast and plant mitochondria, a step in heme and chlorophyll biosynthesis
    • Jacobs JM, Jacobs NJ, DeMaggio AE. Protoporphyrinogen oxidation in chloroplast and plant mitochondria, a step in heme and chlorophyll biosynthesis. Arch. Biochem. Biophys. 1982; 218:233-239.
    • (1982) Arch. Biochem. Biophys. , vol.218 , pp. 233-239
    • Jacobs, J.M.1    Jacobs, N.J.2    DeMaggio, A.E.3
  • 80
    • 0030786269 scopus 로고    scopus 로고
    • A single precursor protein for ferrochelatase-I form from Arabidopsis is imported in vitro into both chloroplast and mitochondria
    • Chow K-S, Singh DP, Roper JM, Smith AG. A single precursor protein for ferrochelatase-I form from Arabidopsis is imported in vitro into both chloroplast and mitochondria J. Biol. Chem. 1997; 272:27565-27571.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27565-27571
    • Chow, K.-S.1    Singh, D.P.2    Roper, J.M.3    Smith, A.G.4
  • 81
    • 0032901677 scopus 로고    scopus 로고
    • Expression studies in tetrapyrrole biosynthetic: Inverse maxima of magnesium chelatase and ferrochelatase activity during cyclic photoperiods
    • Papenbrock J, Mock HP, Kruse E, Grimm B. Expression studies in tetrapyrrole biosynthetic: inverse maxima of magnesium chelatase and ferrochelatase activity during cyclic photoperiods. Planta 1999; 208:264-273.
    • (1999) Planta , vol.208 , pp. 264-273
    • Papenbrock, J.1    Mock, H.P.2    Kruse, E.3    Grimm, B.4
  • 82
    • 0036499460 scopus 로고    scopus 로고
    • Measurement of ferrochelatase activity using a novel assay suggests that plastids are the major site of haem biosynthesis in both photosynthetic and non-photosynthetic cells of pea (Pisum sativum L.)
    • Cornah JE, Roper JM, Pal Singh D, Smith AG. Measurement of ferrochelatase activity using a novel assay suggests that plastids are the major site of haem biosynthesis in both photosynthetic and non-photosynthetic cells of pea (Pisum sativum L.). Biochem. J. 2002; 362:423-432.
    • (2002) Biochem. J. , vol.362 , pp. 423-432
    • Cornah, J.E.1    Roper, J.M.2    Pal Singh, D.3    Smith, A.G.4
  • 85
    • 0034003620 scopus 로고    scopus 로고
    • Role of magnesium chelatase activity in the early steps of the tetrapyrrole biosynthetic pathway
    • Papenbrock J, Mock HP, Tanaka R, Kruse E, Grimm B. Role of magnesium chelatase activity in the early steps of the tetrapyrrole biosynthetic pathway. Plant Physiol. 2000; 122:1161-1169.
    • (2000) Plant Physiol. , vol.122 , pp. 1161-1169
    • Papenbrock, J.1    Mock, H.P.2    Tanaka, R.3    Kruse, E.4    Grimm, B.5
  • 86
    • 0037021449 scopus 로고    scopus 로고
    • Interaction of FLU, a negative regulator of tetrapyrrole synthesis, with the glutamyl-tRNA reductase requires the tetratricopeptide repeat domain of FLU
    • Meskauskiene R, Apel K. Interaction of FLU, a negative regulator of tetrapyrrole synthesis, with the glutamyl-tRNA reductase requires the tetratricopeptide repeat domain of FLU. FEBS Lett. 2002; 532:27-30.
    • (2002) FEBS Lett. , vol.532 , pp. 27-30
    • Meskauskiene, R.1    Apel, K.2
  • 87
    • 0030271515 scopus 로고    scopus 로고
    • Coils coils: New structures and new functions
    • Lupas A. Coils coils: new structures and new functions. Trends Biochem. Sci. 1996; 21:375-382.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 375-382
    • Lupas, A.1
  • 88
    • 0344496513 scopus 로고    scopus 로고
    • The tetratricopeptide repeat: A structural motif mediating protein-protein interactions
    • Blatch GL, Lässle M. The tetratricopeptide repeat:a structural motif mediating protein-protein interactions. BioEssays 1999; 21:932-939.
    • (1999) BioEssays , vol.21 , pp. 932-939
    • Blatch, G.L.1    Lässle, M.2
  • 89
    • 0000811472 scopus 로고
    • Genetic control of light inhibited hypocotyl elongation in Arabidopsis thaliana (L.) Heynh
    • Korneef M, Roff E, Spruit CJP. Genetic control of light inhibited hypocotyl elongation in Arabidopsis thaliana (L.) Heynh. Z. Pflanzenphyiol. 1980; 100:147-160.
    • (1980) Z. Pflanzenphyiol. , vol.100 , pp. 147-160
    • Korneef, M.1    Roff, E.2    Spruit, C.J.P.3
  • 91
    • 0024965016 scopus 로고
    • Arabidopsis thaliana mutant that develops as a lightgrown plant in the absence of light
    • Chory J, Peto C, Feinbaum R, Pratt L, Ausubel F. Arabidopsis thaliana mutant that develops as a lightgrown plant in the absence of light. Cell 1989; 58:991-999.
    • (1989) Cell , vol.58 , pp. 991-999
    • Chory, J.1    Peto, C.2    Feinbaum, R.3    Pratt, L.4    Ausubel, F.5
  • 92
    • 0032991822 scopus 로고    scopus 로고
    • The Arabidopsis thaliana HY1 locus required for phytochrome-chromophore biosynthesis, encodes a protein related to heme oxygenases
    • Davis SJ, Kurepa J, Vierstra RDC. The Arabidopsis thaliana HY1 locus required for phytochrome-chromophore biosynthesis, encodes a protein related to heme oxygenases. Proc. Natl. Acad. Sci. USA 1999; 96:6541-6546.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6541-6546
    • Davis, S.J.1    Kurepa, J.2    Vierstra, R.D.C.3
  • 93
    • 0033101492 scopus 로고    scopus 로고
    • The Arabidopsis photomorphogenic mutant hy1 is deficient in phytochrome chromophore biosynthesis as a result of a mutation in a plastid heme oxygenase
    • Muramoto T, Kohchi T, Yokota A, Hwang I, Goodman HM. The Arabidopsis photomorphogenic mutant hy1 is deficient in phytochrome chromophore biosynthesis as a result of a mutation in a plastid heme oxygenase. Plant Cell 1999; 11:335-348.
    • (1999) Plant Cell , vol.11 , pp. 335-348
    • Muramoto, T.1    Kohchi, T.2    Yokota, A.3    Hwang, I.4    Goodman, H.M.5
  • 94
    • 0342803696 scopus 로고    scopus 로고
    • Microinjection of heme oxygenase genes rescues phytochrome-deficient mutants of the moss Ceratodon purpureus
    • Brücker G, Zeidler M, Kohdi T, Hartmann E, Lamparter T. Microinjection of heme oxygenase genes rescues phytochrome-deficient mutants of the moss Ceratodon purpureus. Planta 2000; 210:520-535.
    • (2000) Planta , vol.210 , pp. 520-535
    • Brücker, G.1    Zeidler, M.2    Kohdi, T.3    Hartmann, E.4    Lamparter, T.5
  • 95
    • 0033905732 scopus 로고    scopus 로고
    • Phytobilin synthesis: The Synechocystis sp. PCC 6803 heme oxygenase-encoding ho1 gene complements a phytochrome-deficient Arabidopsis thaliana hy1 mutant
    • Willows RD, Mayer SM, Falk MS, DeLong A, Hansson K, Chory J, Beale SI. Phytobilin synthesis: the Synechocystis sp. PCC 6803 heme oxygenase-encoding ho1 gene complements a phytochrome-deficient Arabidopsis thaliana hy1 mutant. Plant Mol. Biol. 2000; 43:113-120.
    • (2000) Plant Mol. Biol. , vol.43 , pp. 113-120
    • Willows, R.D.1    Mayer, S.M.2    Falk, M.S.3    DeLong, A.4    Hansson, K.5    Chory, J.6    Beale, S.I.7
  • 96
    • 0032856865 scopus 로고    scopus 로고
    • Feedback inhibition of chlorophyll synthesis in the phytochrome chromophore deficient aurea and yellow-green-2 mutants of tomato
    • Terry MJ, Kendrick RE. Feedback inhibition of chlorophyll synthesis in the phytochrome chromophore deficient aurea and yellow-green-2 mutants of tomato. Plant Physiol. 1999; 119:143-152.
    • (1999) Plant Physiol. , vol.119 , pp. 143-152
    • Terry, M.J.1    Kendrick, R.E.2
  • 97
    • 0029346958 scopus 로고
    • Identification of NADPH: Protochlorophyllide oxidoreductases A and B branched pathway for lightdependent chlorophyll synthesis in Arabidopsis thaliana
    • Armstrong GA, Runge S, Frick G, Sperling U, Apel K. Identification of NADPH:protochlorophyllide oxidoreductases A and B branched pathway for lightdependent chlorophyll synthesis in Arabidopsis thaliana. Plant Physiol. 1995; 108:1505-1517.
    • (1995) Plant Physiol. , vol.108 , pp. 1505-1517
    • Armstrong, G.A.1    Runge, S.2    Frick, G.3    Sperling, U.4    Apel, K.5
  • 98
    • 0028961554 scopus 로고
    • Two routes of chlorophyllide synthesis that are differentially regulated by light in barley (Hordeum vulgare L.)
    • Holtorf H, Reinbothe S, Reinbothe R, Bereza B, Apel K. Two routes of chlorophyllide synthesis that are differentially regulated by light in barley (Hordeum vulgare L.). Proc. Natl. Acad. Sci. USA 1995; 92:3254-3258.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3254-3258
    • Holtorf, H.1    Reinbothe, S.2    Reinbothe, R.3    Bereza, B.4    Apel, K.5
  • 99
    • 0029201048 scopus 로고
    • Two NADPH: Protochlorophyllide oxidoreductase in barley: Evidence for the selective disappearance of PORA during the light-induced greening of etiolated seedlings
    • Reinbothe S, Reinbothe C, Holtorf H, Apel K. Two NADPH:protochlorophyllide oxidoreductase in barley:evidence for the selective disappearance of PORA during the light-induced greening of etiolated seedlings. Plant Cell 1995; 7:1933-1940.
    • (1995) Plant Cell , vol.7 , pp. 1933-1940
    • Reinbothe, S.1    Reinbothe, C.2    Holtorf, H.3    Apel, K.4
  • 100
    • 0027422649 scopus 로고
    • Light-independent and lightdependent protochlorophyllide-reducing activities and two distinct NADPH-protochlorophyllide oxidoreductase polypeptides in mountain pine (Pinus mungo)
    • Forreiter C, Apel K. Light-independent and lightdependent protochlorophyllide-reducing activities and two distinct NADPH-protochlorophyllide oxidoreductase polypeptides in mountain pine (Pinus mungo). Planta 1993; 190:536-545.
    • (1993) Planta , vol.190 , pp. 536-545
    • Forreiter, C.1    Apel, K.2
  • 101
    • 0032143143 scopus 로고    scopus 로고
    • Loblolly pine (Pinus taeda L.) contains multiple expressed encoding light-dependent NADPH: Protochlorophyllide oxidoreductase (POR)
    • Skinner JS, Timko MP. Loblolly pine (Pinus taeda L.) contains multiple expressed encoding light-dependent NADPH:protochlorophyllide oxidoreductase (POR). Plant Cell Physiol. 1998; 39:795-806.
    • (1998) Plant Cell Physiol. , vol.39 , pp. 795-806
    • Skinner, J.S.1    Timko, M.P.2
  • 102
    • 0034595744 scopus 로고    scopus 로고
    • Identification and light-induced expression of a novel gene of NADPH-protochlorophyllide oxidoreductase isoform in Arabidopsis thaliana
    • Oosawa N, Masuda T, Awai K, Fusada N, Shimada H, Ohta H, Takamiya K. Identification and light-induced expression of a novel gene of NADPH-protochlorophyllide oxidoreductase isoform in Arabidopsis thaliana. FEBS Lett. 2000; 474:133-136.
    • (2000) FEBS Lett. , vol.474 , pp. 133-136
    • Oosawa, N.1    Masuda, T.2    Awai, K.3    Fusada, N.4    Shimada, H.5    Ohta, H.6    Takamiya, K.7
  • 103
    • 0026824270 scopus 로고
    • Molecular cloning, nuclear gene structure and developmental expression of NADPH: Protochlorophyllide oxidoreductase in pea (Pisum sativum L.)
    • Spano AJ, He Z, Michel H, Hunt DF, Timko MP. Molecular cloning, nuclear gene structure and developmental expression of NADPH:protochlorophyllide oxidoreductase in pea (Pisum sativum L.). Plant Mol. Biol. 1992; 18:967-972.
    • (1992) Plant Mol. Biol. , vol.18 , pp. 967-972
    • Spano, A.J.1    He, Z.2    Michel, H.3    Hunt, D.F.4    Timko, M.P.5
  • 104
    • 0028069203 scopus 로고
    • Leaf developmental age controls expression of genes encoding enzymes of chlorophyll and haem biosynthesis in pea (Pisum sativum L.)
    • He Z-H, Li J, Sundqvist C, Timko MP. Leaf developmental age controls expression of genes encoding enzymes of chlorophyll and haem biosynthesis in pea (Pisum sativum L.). Plant Physiol. 1994; 106:537-543.
    • (1994) Plant Physiol. , vol.106 , pp. 537-543
    • He, Z.-H.1    Li, J.2    Sundqvist, C.3    Timko, M.P.4
  • 105
    • 0029041173 scopus 로고
    • Light-enhanced gene expression of NADPH-protochlorophyllide oxidoreductase in cucumber
    • Kuroda H, Masuda T, Ohta H, Shioi Y, Takamiya K. Light-enhanced gene expression of NADPH-protochlorophyllide oxidoreductase in cucumber. Biochem. Biophys. Res. Commun. 1995; 210:310-316.
    • (1995) Biochem. Biophys. Res. Commun. , vol.210 , pp. 310-316
    • Kuroda, H.1    Masuda, T.2    Ohta, H.3    Shioi, Y.4    Takamiya, K.5
  • 106
    • 0034016594 scopus 로고    scopus 로고
    • Expression of NADPH-protochlorophyllide oxidoreductase gene in fully green leaves of cucumber
    • Kuroda H, Masuda T, Fusada N, Ohta H, Takamiya K. Expression of NADPH-protochlorophyllide oxidoreductase gene in fully green leaves of cucumber. Plant Cell Physiol. 2000; 41:226-229.
    • (2000) Plant Cell Physiol. , vol.41 , pp. 226-229
    • Kuroda, H.1    Masuda, T.2    Fusada, N.3    Ohta, H.4    Takamiya, K.5
  • 107
    • 0034468448 scopus 로고    scopus 로고
    • NADPH-protochlorophyllide oxidoreductase in cucumber is encoded by a single gene and its expression is transcriptionally enhanced by illumination
    • Fusada N, Masuda T, Kuroda H, Shiraishi T, Shimada H, Ohta H, Takamiya K. NADPH-protochlorophyllide oxidoreductase in cucumber is encoded by a single gene and its expression is transcriptionally enhanced by illumination. Phytosynth. Res. 2000; 64:147-154.
    • (2000) Phytosynth. Res. , vol.64 , pp. 147-154
    • Fusada, N.1    Masuda, T.2    Kuroda, H.3    Shiraishi, T.4    Shimada, H.5    Ohta, H.6    Takamiya, K.7
  • 108
    • 0028854371 scopus 로고
    • Correlated changes in the activity, amount of protein, and abundance of transcript of NADPH: Protochlorophyllide oxidoreductase and chlorophyll accumulation during greening of cucumber cotyledons
    • Yoshida K, Chen R-M, Tanaka A, Teramoto H, Tanaka R, Timko MP, Tsuji H. Correlated changes in the activity, amount of protein, and abundance of transcript of NADPH:protochlorophyllide oxidoreductase and chlorophyll accumulation during greening of cucumber cotyledons. Plant Physiol. 1995; 109:231-238.
    • (1995) Plant Physiol. , vol.109 , pp. 231-238
    • Yoshida, K.1    Chen, R.-M.2    Tanaka, A.3    Teramoto, H.4    Tanaka, R.5    Timko, M.P.6    Tsuji, H.7
  • 109
    • 0033117218 scopus 로고    scopus 로고
    • Protein import and routing systems of chloroplasts
    • Keegstra K, Cline K. Protein import and routing systems of chloroplasts. Plant Cell 1999; 11:557-570.
    • (1999) Plant Cell , vol.11 , pp. 557-570
    • Keegstra, K.1    Cline, K.2
  • 110
    • 0032971998 scopus 로고    scopus 로고
    • Protein translocation into and across the bacterial plasma membrane and the plant thylakoid membrane
    • Dalbey RE, Robinson C. Protein translocation into and across the bacterial plasma membrane and the plant thylakoid membrane. Trends Biochem. Sci. 1999; 24:17-22.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 17-22
    • Dalbey, R.E.1    Robinson, C.2
  • 111
    • 0033030860 scopus 로고    scopus 로고
    • Chloroplast precursor protein translocon
    • May T, Soll J. Chloroplast precursor protein translocon. FEBS Lett. 1999; 452:52-56.
    • (1999) FEBS Lett. , vol.452 , pp. 52-56
    • May, T.1    Soll, J.2
  • 112
    • 0035852245 scopus 로고    scopus 로고
    • Toc, tic, and chloroplast protein import
    • Jarvis P, Söll J. Toc, tic, and chloroplast protein import. Biochim. Biophys. Acta 2001; 1542:64-79.
    • (2001) Biochim. Biophys. Acta , vol.1542 , pp. 64-79
    • Jarvis, P.1    Söll, J.2
  • 113
    • 0034507718 scopus 로고    scopus 로고
    • NADPH: Protochlorophyllide oxidoreductase uses the general import route into chloroplasts
    • Aronsson H, Sohrt K, Soll J. NADPH: protochlorophyllide oxidoreductase uses the general import route into chloroplasts. J. Biol. Chem. 2000; 381:1263-1267.
    • (2000) J. Biol. Chem. , vol.381 , pp. 1263-1267
    • Aronsson, H.1    Sohrt, K.2    Soll, J.3
  • 114
    • 0033527558 scopus 로고    scopus 로고
    • The C terminus of a chloroplast precursor modulates its interaction with the translocation apparatus and PIRAC
    • Dabney-Smith C, van Den Wijngaard PW, Treece Y, Vredenberg WJ, Bruce BD. The C terminus of a chloroplast precursor modulates its interaction with the translocation apparatus and PIRAC. J. Biol. Chem. 1999; 274:32351-32359.
    • (1999) J. Biol. Chem. , vol.274 , pp. 32351-32359
    • Dabney-Smith, C.1    van Den Wijngaard, P.W.2    Treece, Y.3    Vredenberg, W.J.4    Bruce, B.D.5
  • 115
    • 0035958659 scopus 로고    scopus 로고
    • The importance of the C-terminal region and Cys residues for the membrane association of NADPH: Protochlorophyllide oxidoreductase in pea
    • Aronsson H, Sundqvist C, Timko MP, Dahlin C. The importance of the C-terminal region and Cys residues for the membrane association of NADPH:protochlorophyllide oxidoreductase in pea. FEBS Lett. 2000; 502:11-15.
    • (2000) FEBS Lett. , vol.502 , pp. 11-15
    • Aronsson, H.1    Sundqvist, C.2    Timko, M.P.3    Dahlin, C.4
  • 116
    • 0029240288 scopus 로고
    • Substrate-dependent transport of the NADPH-protochlorophyllide oxidoreductase into isolated plastids
    • Reinbothe S, Runge S, Reinbothe C, Van Cleve B, Apel K. Substrate-dependent transport of the NADPH-protochlorophyllide oxidoreductase into isolated plastids. Plant Cell 1995; 7:161-172.
    • (1995) Plant Cell , vol.7 , pp. 161-172
    • Reinbothe, S.1    Runge, S.2    Reinbothe, C.3    Van Cleve, B.4    Apel, K.5
  • 117
    • 0342848648 scopus 로고    scopus 로고
    • Characterization of the plastid import reaction of the pea NADPH: Protochlorophyllide oxidoreductase (POR)
    • Argyroudi-Akoyunopglou JH, Senger H, eds, Dordrecht: Kluwer Academic Publishers
    • Aronsson H, Almkvist J, Sundqvist C, Timko MP, Dahlin C. Characterization of the plastid import reaction of the pea NADPH:protochlorophyllide oxidoreductase (POR). In: Argyroudi-Akoyunopglou JH, Senger H, eds. The Chloroplast: from Molecular Biology to Biotechnology. Dordrecht: Kluwer Academic Publishers, 1999:167-170.
    • (1999) Chloroplast: From Molecular Biology to Biotechnology. , pp. 167-170
    • Aronsson, H.1    Almkvist, J.2    Sundqvist, C.3    Timko, M.P.4    Dahlin, C.5
  • 118
    • 0034477120 scopus 로고    scopus 로고
    • Regulation of protoporphyrin IX biosynthesis by intraplastidic compartmentalization and adenosine triphosphate
    • Manohara MS, Tripathy BC. Regulation of protoporphyrin IX biosynthesis by intraplastidic compartmentalization and adenosine triphosphate. Planta 2000; 212:52-59.
    • (2000) Planta , vol.212 , pp. 52-59
    • Manohara, M.S.1    Tripathy, B.C.2
  • 119
    • 0029379838 scopus 로고
    • The in vitro assembly of the NADPH-protochlorophyllide oxidoreductase in pea chloroplasts
    • Dahlin C, Sundqvist C, Timko MP. The in vitro assembly of the NADPH-protochlorophyllide oxidoreductase in pea chloroplasts. Plant Mol. Biol. 1995; 29:317-330.
    • (1995) Plant Mol. Biol. , vol.29 , pp. 317-330
    • Dahlin, C.1    Sundqvist, C.2    Timko, M.P.3
  • 120
    • 0034469955 scopus 로고    scopus 로고
    • ADP/ATP and protein phosphorylation dependence of phototransformable protochlorophyllide in isolated etioplast membranes
    • Kovacheva S, Ryberg M, Sundqvist C. ADP/ATP and protein phosphorylation dependence of phototransformable protochlorophyllide in isolated etioplast membranes. Photosynth. Res. 2000; 64:127-136.
    • (2000) Photosynth. Res. , vol.64 , pp. 127-136
    • Kovacheva, S.1    Ryberg, M.2    Sundqvist, C.3
  • 121
    • 0007011418 scopus 로고
    • Benzyladenine as a regulator of the chlorophyll synthesis in cucumber cotyledons
    • Fletcher RAA, McCullogh D. Benzyladenine as a regulator of the chlorophyll synthesis in cucumber cotyledons. Can. J. Bot. 1971; 49:2197-2201.
    • (1971) Can. J. Bot. , vol.49 , pp. 2197-2201
    • Fletcher, R.A.A.1    McCullogh, D.2
  • 122
    • 0002352058 scopus 로고    scopus 로고
    • Effects of light, development age and phytohormones on the expression of NADPH-protochlorophyllide oxidoreductase gene in Cucumis sativus
    • Kuroda H, Masuda T, Ohta H, Shioi Y, Takamiya K-I. Effects of light, development age and phytohormones on the expression of NADPH-protochlorophyllide oxidoreductase gene in Cucumis sativus. Plant Physiol. Biochem. 1996; 34:17-22.
    • (1996) Plant Physiol. Biochem. , vol.34 , pp. 17-22
    • Kuroda, H.1    Masuda, T.2    Ohta, H.3    Shioi, Y.4    Takamiya, K.-I.5
  • 123
    • 0033118449 scopus 로고    scopus 로고
    • Sequence analysis of expressed sequence tags from an ABA-treated cDNA library identifies stress responses genes in the moss Phycomitrella patens
    • Macuka J, Bashiardes S, Ruben E, Spooner K, Cuming A, Knight C, Cove D. Sequence analysis of expressed sequence tags from an ABA-treated cDNA library identifies stress responses genes in the moss Phycomitrella patens. Plant Cell Physiol. 1999; 40:378-387.
    • (1999) Plant Cell Physiol. , vol.40 , pp. 378-387
    • Macuka, J.1    Bashiardes, S.2    Ruben, E.3    Spooner, K.4    Cuming, A.5    Knight, C.6    Cove, D.7
  • 124
    • 0031705795 scopus 로고    scopus 로고
    • Cytokinin stimulates and abscisic acid inhibits greening in etiolated Lupinus luteus cotyledons by affecting the expression of the light-sensitive protochlorophyllide oxidoreductase
    • Kusnetsov V, Herrmann RG, Kulaeva ON, Oelmüller R. Cytokinin stimulates and abscisic acid inhibits greening in etiolated Lupinus luteus cotyledons by affecting the expression of the light-sensitive protochlorophyllide oxidoreductase. Mol. Gen. Genet. 1998; 259:21-28.
    • (1998) Mol. Gen. Genet. , vol.259 , pp. 21-28
    • Kusnetsov, V.1    Herrmann, R.G.2    Kulaeva, O.N.3    Oelmüller, R.4
  • 125
    • 0032744118 scopus 로고    scopus 로고
    • Regreening of scenescent Nicotiana leaves. I. Reappearance of NADPHprotochlorophyllide oxidoreductase and light-harvesting chlorophyll a/b-binding protein
    • Zavaleta-Mancera HA, Franklin KA, Ougham HJ, Thomas H, Scott IM. Regreening of scenescent Nicotiana leaves. I. Reappearance of NADPHprotochlorophyllide oxidoreductase and light-harvesting chlorophyll a/b-binding protein. J. Exp. Bot. 1999; 50:1677-1682.
    • (1999) J. Exp. Bot. , vol.50 , pp. 1677-1682
    • Zavaleta-Mancera, H.A.1    Franklin, K.A.2    Ougham, H.J.3    Thomas, H.4    Scott, I.M.5
  • 126
    • 0035285152 scopus 로고    scopus 로고
    • Cytokinin-induced transcriptional activition of NADPH-protochlorophyllide oxidoreductase gene in cucumber
    • Kuroda H, Masuda T, Fusada N, Ohta H, Takamiya K. Cytokinin-induced transcriptional activition of NADPH-protochlorophyllide oxidoreductase gene in cucumber. J. Plant Res. 2001; 114:1-7.
    • (2001) J. Plant Res. , vol.114 , pp. 1-7
    • Kuroda, H.1    Masuda, T.2    Fusada, N.3    Ohta, H.4    Takamiya, K.5
  • 127
    • 0030174971 scopus 로고    scopus 로고
    • Identification of three cDNA clones expressed in the leaf extension zone and with altered patterns in the slender mutant of barley: A tonoplast intrinsic protein, a putative structural protein and protochlorophyllide oxidoreductase
    • Schünmann PHD, Ougham HJ. Identification of three cDNA clones expressed in the leaf extension zone and with altered patterns in the slender mutant of barley: a tonoplast intrinsic protein, a putative structural protein and protochlorophyllide oxidoreductase. Plant Mol. Biol. 1996; 31:529-537.
    • (1996) Plant Mol. Biol. , vol.31 , pp. 529-537
    • Schünmann, P.H.D.1    Ougham, H.J.2
  • 128
    • 0034935145 scopus 로고    scopus 로고
    • Both light-dependent protochlorophyllide oxidoreductase A and protochlorophyllide oxidoreductase B are down-regulated in the slender mutant of barley
    • Ougham HJ, Thomas AM, Thomas BJ, Frick GA, Armstrong GA. Both light-dependent protochlorophyllide oxidoreductase A and protochlorophyllide oxidoreductase B are down-regulated in the slender mutant of barley. J. Exp. Bot. 2001; 52:1447-1454.
    • (2001) J. Exp. Bot. , vol.52 , pp. 1447-1454
    • Ougham, H.J.1    Thomas, A.M.2    Thomas, B.J.3    Frick, G.A.4    Armstrong, G.A.5
  • 129
    • 0032006920 scopus 로고    scopus 로고
    • Cloning of the gene encoding a protochlorophyllide reductase: The physiological significance of co-existence of light-dependent and -independent protochlorophyllide reduction systems in the cyanobacterium Plectonema boryanum
    • Fujita Y, Takagi H, Hase T. Cloning of the gene encoding a protochlorophyllide reductase: the physiological significance of co-existence of light-dependent and -independent protochlorophyllide reduction systems in the cyanobacterium Plectonema boryanum. Plant Cell Physiol. 1998; 39:177-185.
    • (1998) Plant Cell Physiol. , vol.39 , pp. 177-185
    • Fujita, Y.1    Takagi, H.2    Hase, T.3
  • 130
    • 0034604647 scopus 로고    scopus 로고
    • Reconstitution of light-independent protochlorophyllide reductase from purified BchL and BchN-BchB subunits. In vitro confirmation of nitrogenase-like features of a bacteriochlorophyll biosynthesis enzymes
    • Fujita Y, Bauer CE. Reconstitution of light-independent protochlorophyllide reductase from purified BchL and BchN-BchB subunits. In vitro confirmation of nitrogenase-like features of a bacteriochlorophyll biosynthesis enzymes. J. Biol. Chem. 2000; 275:23583-23588.
    • (2000) J. Biol. Chem. , vol.275 , pp. 23583-23588
    • Fujita, Y.1    Bauer, C.E.2
  • 131
    • 0034022990 scopus 로고    scopus 로고
    • Yellow-in-the-dark mutants of Chlamydomonas lacks the ChlL subunit of lightindependent protochlorophyllide reductase
    • Cahoon AB, Timko MP. Yellow-in-the-dark mutants of Chlamydomonas lacks the ChlL subunit of lightindependent protochlorophyllide reductase. Plant Cell 2000; 12:559-568.
    • (2000) Plant Cell , vol.12 , pp. 559-568
    • Cahoon, A.B.1    Timko, M.P.2
  • 132
    • 84989699852 scopus 로고
    • Temperature dependence of chlorophyll(ide) spectral shifts and photoactive protochlorophyllide regeneration after flash in etiolated barley leaves
    • Eullaffroy P, Salvetat R, Franck F, Popovic R. Temperature dependence of chlorophyll(ide) spectral shifts and photoactive protochlorophyllide regeneration after flash in etiolated barley leaves. J. Photochem. Photobiol. B 1995; 62:751-756.
    • (1995) J. Photochem. Photobiol. B , vol.62 , pp. 751-756
    • Eullaffroy, P.1    Salvetat, R.2    Franck, F.3    Popovic, R.4
  • 133
    • 0034672466 scopus 로고    scopus 로고
    • The formation of chlorophyll from chlorophyllide in leaves containing proplastids is a four-step process
    • erratum appears in FEBS Lett. 2001; 494:261
    • Schoefs B, Bertrand M. The formation of chlorophyll from chlorophyllide in leaves containing proplastids is a four-step process. FEBS Lett. 2000; 486:243-246 (erratum appears in FEBS Lett. 2001; 494:261).
    • (2000) FEBS Lett. , vol.486 , pp. 243-246
    • Schoefs, B.1    Bertrand, M.2
  • 134
    • 0034083087 scopus 로고    scopus 로고
    • Evidence of chlorophyll synthesis pathway alteration in desiccated barley leaves
    • Le Lay P, Eullaffroy P, Juneau P, Popovic R. Evidence of chlorophyll synthesis pathway alteration in desiccated barley leaves. Plant Cell Physiol. 2000; 41:565-570.
    • (2000) Plant Cell Physiol. , vol.41 , pp. 565-570
    • Le Lay, P.1    Eullaffroy, P.2    Juneau, P.3    Popovic, R.4
  • 135
    • 0034824411 scopus 로고    scopus 로고
    • Spectroscopic analysis of desiccationinduced alterations of the chlorophyllide transformation pathway in etiolated barley leaves
    • Le Lay P, Böddi B, Kovacevic D, Juneau P, Dewez D, Popovic R. Spectroscopic analysis of desiccationinduced alterations of the chlorophyllide transformation pathway in etiolated barley leaves. Plant Physiol. 2001; 127:202-211.
    • (2001) Plant Physiol. , vol.127 , pp. 202-211
    • Le Lay, P.1    Böddi, B.2    Kovacevic, D.3    Juneau, P.4    Dewez, D.5    Popovic, R.6
  • 136
    • 0015535621 scopus 로고
    • Control of the synthesis of major polypeptide of chloroplast membranes in Chlamydomonas reinhardtii
    • Hoober JK, Stegman WJ. Control of the synthesis of major polypeptide of chloroplast membranes in Chlamydomonas reinhardtii. J. Cell Biol. 1973; 56:1-12.
    • (1973) J. Cell Biol. , vol.56 , pp. 1-12
    • Hoober, J.K.1    Stegman, W.J.2
  • 137
    • 0035852789 scopus 로고    scopus 로고
    • Arabidopsis genomes uncoupled 5 (GUN5) mutant reveals the involvement of Mg-chelatase H subunit in plastid-to-nucleus signal transduction
    • Mochizuki N, Brusslan JA, Larkin R, Nagatani A, Chory J. Arabidopsis genomes uncoupled 5 (GUN5) mutant reveals the involvement of Mg-chelatase H subunit in plastid-to-nucleus signal transduction. Proc. Natl. Acad. Sci. USA 2001; 98:2053-2058.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2053-2058
    • Mochizuki, N.1    Brusslan, J.A.2    Larkin, R.3    Nagatani, A.4    Chory, J.5
  • 138
    • 0021739749 scopus 로고
    • Regulation of lightharvesting chlorophyll-binding protein mRNA accumulation in Chlamydomonas reinhardtii
    • Johanningmeier U, Howell SH. Regulation of lightharvesting chlorophyll-binding protein mRNA accumulation in Chlamydomonas reinhardtii. J. Biol. Chem. 1984; 259:13541-13549.
    • (1984) J. Biol. Chem. , vol.259 , pp. 13541-13549
    • Johanningmeier, U.1    Howell, S.H.2
  • 139
    • 85047690585 scopus 로고
    • Possible control of transcript levels by chlorophyll precursors in Chlamydomonas
    • Johanningmeier U. Possible control of transcript levels by chlorophyll precursors in Chlamydomonas. Eur. J. Biochem. 1988; 177:417-424.
    • (1988) Eur. J. Biochem. , vol.177 , pp. 417-424
    • Johanningmeier, U.1
  • 140
    • 0034989707 scopus 로고    scopus 로고
    • Amitrole treatment of etiolated barley seedlings leafs to deregulation of tetrapyrrole synthesis and to reduced expression of lhc and rbcS genes
    • La Rocca N, Rascio N, Oster U, Rüdiger W. Amitrole treatment of etiolated barley seedlings leafs to deregulation of tetrapyrrole synthesis and to reduced expression of lhc and rbcS genes. Planta 2001; 213:101-108.
    • (2001) Planta , vol.213 , pp. 101-108
    • La Rocca, N.1    Rascio, N.2    Oster, U.3    Rüdiger, W.4
  • 141
    • 0026781940 scopus 로고
    • Regulation of chlorophyll apoprotein expression and accumulation
    • Herrin DL, Battey JF, Greer K, Schmidt GW. Regulation of chlorophyll apoprotein expression and accumulation. J. Biol. Chem. 1992; 267:8260-8269.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8260-8269
    • Herrin, D.L.1    Battey, J.F.2    Greer, K.3    Schmidt, G.W.4
  • 143
    • 84989726707 scopus 로고
    • The greening process in cress seedlings. II. Complexing agents and 5-aminolevulinate inhibition of cab-mRNA coding for the light-harvesting chlorophyll a/b protein
    • Kittsteiner U, Brunner H, Rüdiger W. The greening process in cress seedlings. II. Complexing agents and 5-aminolevulinate inhibition of cab-mRNA coding for the light-harvesting chlorophyll a/b protein. Physiol. Plant. 1991; 81:190-196.
    • (1991) Physiol. Plant. , vol.81 , pp. 190-196
    • Kittsteiner, U.1    Brunner, H.2    Rüdiger, W.3
  • 144
    • 0030500420 scopus 로고    scopus 로고
    • The greening process in cress seedlings. II. Possible interference of chlorophyll precursors, accumulated after thujaplicin treatment, with light-regulated expression in LHC genes
    • Oster U, Brünner H, Rüdiger W. The greening process in cress seedlings. II. Possible interference of chlorophyll precursors, accumulated after thujaplicin treatment, with light-regulated expression in LHC genes. J. Photochem. Photobiol. 1996; 36:255-261.
    • (1996) J. Photochem. Photobiol. , vol.36 , pp. 255-261
    • Oster, U.1    Brünner, H.2    Rüdiger, W.3
  • 146
    • 0028865421 scopus 로고
    • Light intensity regulation of cab gene transcription is signaled by the redox state of the plastoquinone pool
    • Escoubas JM, Lomas M, La Roche J, Falkowski PG. Light intensity regulation of cab gene transcription is signaled by the redox state of the plastoquinone pool. Proc. Natl. Acad. Sci. USA 1995; 92:10237-10241.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10237-10241
    • Escoubas, J.M.1    Lomas, M.2    La Roche, J.3    Falkowski, P.G.4
  • 147
    • 0032695704 scopus 로고    scopus 로고
    • Plastid translation is required for the expression of nuclear photosynthesis genes in the dark and in roots in pea lip1 mutant
    • Sullivan JA, Gray JC. Plastid translation is required for the expression of nuclear photosynthesis genes in the dark and in roots in pea lip1 mutant. Plant Cell 1999; 11:901-910.
    • (1999) Plant Cell , vol.11 , pp. 901-910
    • Sullivan, J.A.1    Gray, J.C.2
  • 148
    • 0031439546 scopus 로고    scopus 로고
    • Chlorophyll precursors are signals of chloroplast origin involved in light induction of nuclear heat-shock genes
    • Kropat J, Oster U, Rüdiger W, Beck CF. Chlorophyll precursors are signals of chloroplast origin involved in light induction of nuclear heat-shock genes. Proc. Natl. Acad. Sci. USA 1997; 94:14168-14172.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 14168-14172
    • Kropat, J.1    Oster, U.2    Rüdiger, W.3    Beck, C.F.4
  • 149
    • 0000001787 scopus 로고    scopus 로고
    • Identification of Mg-protoporphyrin IX as a chloroplast signal that mediates the expression of nuclear genes
    • Wagner E, Normann J, Greppin H, Hackstein JHP, Herrmann RG, Kowallik KV, Shenk HEA, Seckbach J, eds, Geneva: Geneva University Press
    • Kropat J, Oster U, Pöpperl G, Rüdiger W, Beck CF. Identification of Mg-protoporphyrin IX as a chloroplast signal that mediates the expression of nuclear genes. In: Wagner E, Normann J, Greppin H, Hackstein JHP, Herrmann RG, Kowallik KV, Shenk HEA, Seckbach J, eds. From Symbiosis to Eukaryotism -Endocytobiology VII. Geneva: Geneva University Press, 1999:341-348.
    • (1999) From Symbiosis to Eukaryotism -Endocytobiology VII. , pp. 341-348
    • Kropat, J.1    Oster, U.2    Pöpperl, G.3    Rüdiger, W.4    Beck, C.F.5
  • 150
    • 0034538403 scopus 로고    scopus 로고
    • Chloroplast signalling in the light induction of nuclear HSP70 genes requires the accumulation of chlorophyll precursors and their accessibility to cytoplasm nucleus
    • Kropat J, Oster U, Rüdiger W, Beck CF. Chloroplast signalling in the light induction of nuclear HSP70 genes requires the accumulation of chlorophyll precursors and their accessibility to cytoplasm nucleus. Plant J. 2000; 24:523-531.
    • (2000) Plant J. , vol.24 , pp. 523-531
    • Kropat, J.1    Oster, U.2    Rüdiger, W.3    Beck, C.F.4
  • 151
  • 153
    • 0027214202 scopus 로고
    • Signal transduction mutant of Arabidopsis uncouple nuclear CAB and RBCS gene expression from chloroplast development
    • Susek RE, Ausubel FM, Chory J. Signal transduction mutant of Arabidopsis uncouple nuclear CAB and RBCS gene expression from chloroplast development. Cell 1993; 74:787-799.
    • (1993) Cell , vol.74 , pp. 787-799
    • Susek, R.E.1    Ausubel, F.M.2    Chory, J.3
  • 154
    • 0023881275 scopus 로고
    • Light-regulated translation of chloroplast proteins. I. Transcripts of psaA-psaB, psbA, and rbcL are associated with polysomes in dark-grown and illuminated barley seedlings
    • Klein RR, Mason HS, Mullet JE. Light-regulated translation of chloroplast proteins. I. Transcripts of psaA-psaB, psbA, and rbcL are associated with polysomes in dark-grown and illuminated barley seedlings J. Cell Biol. 1988; 106:289-301.
    • (1988) J. Cell Biol. , vol.106 , pp. 289-301
    • Klein, R.R.1    Mason, H.S.2    Mullet, J.E.3
  • 155
    • 0025108852 scopus 로고
    • In vitro synthesis of chlorophyll a in the dark triggers accumulation of chlorophyll a apoproteins in barley etioplasts
    • Eichacker LA, Soll J, Lauterbach P, Rüdiger W, Klein RR, Mullet JE. In vitro synthesis of chlorophyll a in the dark triggers accumulation of chlorophyll a apoproteins in barley etioplasts. J. Biol. Chem. 1990; 265:13566-13571.
    • (1990) J. Biol. Chem. , vol.265 , pp. 13566-13571
    • Eichacker, L.A.1    Soll, J.2    Lauterbach, P.3    Rüdiger, W.4    Klein, R.R.5    Mullet, J.E.6
  • 156
    • 0026515088 scopus 로고
    • Synthesis of chlorophyll a regulates translation of chlorophyll a apoproteins P700, CP47, CP43 and D2 in barley etioplasts
    • Eichacker LA, Paulsen H, Rüdiger W. Synthesis of chlorophyll a regulates translation of chlorophyll a apoproteins P700, CP47, CP43 and D2 in barley etioplasts. Eur. J. Biochem. 1992; 205:17-24.
    • (1992) Eur. J. Biochem. , vol.205 , pp. 17-24
    • Eichacker, L.A.1    Paulsen, H.2    Rüdiger, W.3
  • 157
    • 0032054667 scopus 로고    scopus 로고
    • Chlorophyll a synthesis upon interruption and deletion of por coding for the light-dependent NADPH: Protochlorophyllide oxidoreductase in a photosystem-I-less/chlL-strain of Synechocystis sp. PCC 6803
    • He Q, Brune D, Nieman R, Vermaas W. Chlorophyll a synthesis upon interruption and deletion of por coding for the light-dependent NADPH:protochlorophyllide oxidoreductase in a photosystem-I-less/chlL-strain of Synechocystis sp. PCC 6803 Eur. J. Biochem. 1998; 253:161-172.
    • (1998) Eur. J. Biochem. , vol.253 , pp. 161-172
    • He, Q.1    Brune, D.2    Nieman, R.3    Vermaas, W.4
  • 158
    • 0037276001 scopus 로고    scopus 로고
    • Arrest of chlorophyll synthesis and differential decrease of photosystem I and II in a cyanobacterial mutant lacking light-independent protochlorophyllide reductase
    • Kada S, Koike H, Satoh K, Hase T, Fujita Y. Arrest of chlorophyll synthesis and differential decrease of photosystem I and II in a cyanobacterial mutant lacking light-independent protochlorophyllide reductase. Plant Mol. Biol. 2003; 51:225-235.
    • (2003) Plant Mol. Biol. , vol.51 , pp. 225-235
    • Kada, S.1    Koike, H.2    Satoh, K.3    Hase, T.4    Fujita, Y.5
  • 159
    • 0000721821 scopus 로고    scopus 로고
    • Chlorophyll synthesis in darkgrown pine primary needles
    • Schoefs, B, Franck F. Chlorophyll synthesis in darkgrown pine primary needles. Plant Physiol. 1998; 118:1159-1168.
    • (1998) Plant Physiol. , vol.118 , pp. 1159-1168
    • Schoefs, B.1    Franck, F.2
  • 160
    • 0034622999 scopus 로고    scopus 로고
    • Molecular evidence for the early evolution of photosynthesis
    • Xiong J, Fischer WM, Inoue K, Nakahara M, Bauer CE. Molecular evidence for the early evolution of photosynthesis. Science 2000; 289:1724-1730.
    • (2000) Science , vol.289 , pp. 1724-1730
    • Xiong, J.1    Fischer, W.M.2    Inoue, K.3    Nakahara, M.4    Bauer, C.E.5
  • 161
    • 0034492246 scopus 로고    scopus 로고
    • Is photosynthesis really derived from purple bacteria?
    • Green BR, Gantt E. Is photosynthesis really derived from purple bacteria? J Phycol. 2000; 36:983-985.
    • (2000) J Phycol. , vol.36 , pp. 983-985
    • Green, B.R.1    Gantt, E.2
  • 162
    • 0030160204 scopus 로고    scopus 로고
    • Developmental and light-regulated expression of individual members of the light-harvesting complex b gene family in Pinus palustris
    • Peer W, Silverthorne J, Peters JL. Developmental and light-regulated expression of individual members of the light-harvesting complex b gene family in Pinus palustris. Plant Physiol. 1996; 111:627-634.
    • (1996) Plant Physiol. , vol.111 , pp. 627-634
    • Peer, W.1    Silverthorne, J.2    Peters, J.L.3


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