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Volumn 12, Issue 3, 2000, Pages 319-341

Proteomics of the chloroplast: Systematic identification and targeting analysis of lumenal and peripheral thylakoid proteins

Author keywords

[No Author keywords available]

Indexed keywords

PISUM SATIVUM;

EID: 0034026047     PISSN: 10404651     EISSN: None     Source Type: Journal    
DOI: 10.1105/tpc.12.3.319     Document Type: Article
Times cited : (305)

References (93)
  • 1
    • 0030471302 scopus 로고    scopus 로고
    • Protein stability and degradation in chloroplasts
    • Adam, Z. (1996). Protein stability and degradation in chloroplasts. Plant MoI. Biol. 32, 773-783.
    • (1996) Plant Moi. Biol. , vol.32 , pp. 773-783
    • Adam, Z.1
  • 4
    • 0029411638 scopus 로고
    • Evidence for the thiamine biosynthetic pathway in higher-plant plastids and its developmental regulation
    • Belanger, F.C., Leustek, T., Chu, B., and Kriz, A.L. (1995). Evidence for the thiamine biosynthetic pathway in higher-plant plastids and its developmental regulation. Plant Mol. Biol. 29, 809-821.
    • (1995) Plant Mol. Biol. , vol.29 , pp. 809-821
    • Belanger, F.C.1    Leustek, T.2    Chu, B.3    Kriz, A.L.4
  • 5
    • 0006922663 scopus 로고    scopus 로고
    • Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana
    • Bevan, M., et al., (1998). Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana. Nature 39, 485-488.
    • (1998) Nature , vol.39 , pp. 485-488
    • Bevan, M.1
  • 6
    • 0032200910 scopus 로고    scopus 로고
    • Functional genomics in plants
    • Bouchez, D., and Hofte, H. (1998). Functional genomics in plants. Plant Physiol. 118, 725-732.
    • (1998) Plant Physiol. , vol.118 , pp. 725-732
    • Bouchez, D.1    Hofte, H.2
  • 7
    • 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
  • 10
    • 0022851237 scopus 로고
    • Import of proteins into chloroplasts. Membrane integration of a thylakoid precursor protein reconstituted in chloroplast lysates
    • Cline, K. (1986). Import of proteins into chloroplasts. Membrane integration of a thylakoid precursor protein reconstituted in chloroplast lysates. J. Biol. Chem. 261, 14804-14810.
    • (1986) J. Biol. Chem. , vol.261 , pp. 14804-14810
    • Cline, K.1
  • 11
    • 0040537042 scopus 로고    scopus 로고
    • Competition between Sec- and TAT-dependent protein translocation in Escherichia coli
    • Cristobal, S., de Gier, J.W., Nielsen, H., and von Heijne, G. (1999). Competition between Sec- and TAT-dependent protein translocation in Escherichia coli. EMBO J. 18, 2982-2990.
    • (1999) EMBO J. , vol.18 , pp. 2982-2990
    • Cristobal, S.1    De Gier, J.W.2    Nielsen, H.3    Von Heijne, G.4
  • 12
    • 0030985729 scopus 로고    scopus 로고
    • Probing protein function using a combination of gene knockout and proteome analysis by mass spectrometry
    • Dainese, P., Staudenmann, W., Quadroni, M., Korostensky, C., Gonnet, G., Kertesz, M., and James, P. (1997). Probing protein function using a combination of gene knockout and proteome analysis by mass spectrometry. Electrophoresis 18, 432-442.
    • (1997) Electrophoresis , vol.18 , pp. 432-442
    • Dainese, P.1    Staudenmann, W.2    Quadroni, M.3    Korostensky, C.4    Gonnet, G.5    Kertesz, M.6    James, P.7
  • 13
    • 0032971998 scopus 로고    scopus 로고
    • Protein translocation into and across the bacterial plasma membrane and the plant thylakoid membrane
    • Dalbey, R.E., and Robinson, C. (1999). Protein translocation into and across the bacterial plasma membrane and the plant thylakoid membrane. Trends Biochem. Sci. 24, 17-22.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 17-22
    • Dalbey, R.E.1    Robinson, C.2
  • 14
    • 0022796575 scopus 로고
    • Organization of the pathway of de novo pyrimidine nucleotide biosynthesis in pea (Pisum sativum L. cv Progress No. 9) leaves
    • Doremus, H.D. (1986). Organization of the pathway of de novo pyrimidine nucleotide biosynthesis in pea (Pisum sativum L. cv Progress No. 9) leaves. Arch. Biochem. Biophys. 250, 112-119.
    • (1986) Arch. Biochem. Biophys. , vol.250 , pp. 112-119
    • Doremus, H.D.1
  • 16
    • 0032935861 scopus 로고    scopus 로고
    • ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites
    • Emanuelsson, O., Nielsen, H., and von Heijne, 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
    • Emanuelsson, O.1    Nielsen, H.2    Von Heijne, G.3
  • 17
    • 0032539557 scopus 로고    scopus 로고
    • Phosphate availability affects the thylakoid lipid composition and the expression of SQD1, a gene required for sulfolipid biosynthesis in Arabidopsis thaliana
    • Essigmann, B., Guler, S., Narang, R.A., Linke, D., and Banning, C. (1998). Phosphate availability affects the thylakoid lipid composition and the expression of SQD1, a gene required for sulfolipid biosynthesis in Arabidopsis thaliana. Proc. Natl. Acad. Sci. USA 95, 1950-1955.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 1950-1955
    • Essigmann, B.1    Guler, S.2    Narang, R.A.3    Linke, D.4    Banning, C.5
  • 18
    • 0032536779 scopus 로고    scopus 로고
    • A novel multi-functional chloroplast protein: Identification of a 40-kDa immunophilin-like protein located in the thylakoid lumen
    • Fulgosi, H., Vener, A.V., Altschmied, L., Herrmann, R.G., and Andersson, B. (1998). A novel multi-functional chloroplast protein: Identification of a 40-kDa immunophilin-like protein located in the thylakoid lumen. EMBO J. 17, 1577-1587.
    • (1998) EMBO J. , vol.17 , pp. 1577-1587
    • Fulgosi, H.1    Vener, A.V.2    Altschmied, L.3    Herrmann, R.G.4    Andersson, B.5
  • 19
    • 0000960808 scopus 로고
    • Light-stimulated transcription of genes for two chloroplast polypeptides in isolated pea nuclei
    • Gallagher, T.F., and Ellis, R.J. (1982). Light-stimulated transcription of genes for two chloroplast polypeptides in isolated pea nuclei. EMBO. J. 12, 1493-1498.
    • (1982) EMBO. J. , vol.12 , pp. 1493-1498
    • Gallagher, T.F.1    Ellis, R.J.2
  • 20
    • 0029788634 scopus 로고    scopus 로고
    • Characterization of a ferritin mRNA from Arabidopsis thaliana accumulated in response to iron through an oxidative pathway independent of abscisic acid
    • Gaymard, F., Boucherez, J., and Briat, J.F. (1996). Characterization of a ferritin mRNA from Arabidopsis thaliana accumulated in response to iron through an oxidative pathway independent of abscisic acid. Biochem. J. 318, 67-73.
    • (1996) Biochem. J. , vol.318 , pp. 67-73
    • Gaymard, F.1    Boucherez, J.2    Briat, J.F.3
  • 21
    • 0033057707 scopus 로고    scopus 로고
    • A sample purification and preparation technique based on nano-scale RP-columns for the sensitive analysis of complex peptide mixtures by MALDI-MS
    • Gobom, J., Nordhoff, E., Mirgorodskaya, E., Ekman, R., and Roepstorff, P. (1998). A sample purification and preparation technique based on nano-scale RP-columns for the sensitive analysis of complex peptide mixtures by MALDI-MS. J. Mass Spectrom. 34, 105-116.
    • (1998) J. Mass Spectrom. , vol.34 , pp. 105-116
    • Gobom, J.1    Nordhoff, E.2    Mirgorodskaya, E.3    Ekman, R.4    Roepstorff, P.5
  • 22
    • 0023768475 scopus 로고
    • The current state of two-dimensional electrophoresis with immobilized pH gradients
    • Görg, A., Postel, W., Günther, S. (1988). The current state of two-dimensional electrophoresis with immobilized pH gradients. Electrophoresis 9, 531-546.
    • (1988) Electrophoresis , vol.9 , pp. 531-546
    • Görg, A.1    Postel, W.2    Günther, S.3
  • 24
    • 0031587020 scopus 로고    scopus 로고
    • Postimport methylation of the small subunit of ribulose-1,5-bisphosphate carboxylase in chloroplasts
    • Grimm, R., Grimm, M., Eckerskorn, C., Pohlmeyer, K., Rohl, T., and Soil, J. (1997). Postimport methylation of the small subunit of ribulose-1,5-bisphosphate carboxylase in chloroplasts. FEBS Lett. 408, 350-354.
    • (1997) FEBS Lett. , vol.408 , pp. 350-354
    • Grimm, R.1    Grimm, M.2    Eckerskorn, C.3    Pohlmeyer, K.4    Rohl, T.5    Soil, J.6
  • 25
    • 0022666471 scopus 로고
    • Synthesis of large subunit of ribulose bisphosphate carboxylase by thylakoid-bound polyribosomes from spinach chloroplasts
    • Hattorie, T., and Margulies, M.M. (1986). Synthesis of large subunit of ribulose bisphosphate carboxylase by thylakoid-bound polyribosomes from spinach chloroplasts. Arch. Biochem. Biophys. 244, 630-640.
    • (1986) Arch. Biochem. Biophys. , vol.244 , pp. 630-640
    • Hattorie, T.1    Margulies, M.M.2
  • 27
    • 0032924894 scopus 로고    scopus 로고
    • Advances in protein solubilisation for two-dimensional electrophoresis
    • Herbert, B. (1999). Advances in protein solubilisation for two-dimensional electrophoresis. Electrophoresis 20, 660-663.
    • (1999) Electrophoresis , vol.20 , pp. 660-663
    • Herbert, B.1
  • 28
    • 0031861787 scopus 로고    scopus 로고
    • Improved protein solubility in two-dimensional electrophoresis using tributyl phosphine as reducing agent
    • Herbert, B.R., Molloy, M.P., Gooley, A.A., Walsh, B.J., Bryson, W.G., and Williams, K.L. (1998). Improved protein solubility in two-dimensional electrophoresis using tributyl phosphine as reducing agent. Electrophoresis 19, 845-851.
    • (1998) Electrophoresis , vol.19 , pp. 845-851
    • Herbert, B.R.1    Molloy, M.P.2    Gooley, A.A.3    Walsh, B.J.4    Bryson, W.G.5    Williams, K.L.6
  • 29
    • 0033574431 scopus 로고    scopus 로고
    • Plastidic pathway of serine biosynthesis. Molecular cloning and expression of 3-phosphoserine phosphatase from Arabidopsis thaliana
    • Ho, C.L., Noji, M., and Saito, K. (1999). Plastidic pathway of serine biosynthesis. Molecular cloning and expression of 3-phosphoserine phosphatase from Arabidopsis thaliana. J. Biol. Chem. 274, 11007-11012.
    • (1999) J. Biol. Chem. , vol.274 , pp. 11007-11012
    • Ho, C.L.1    Noji, M.2    Saito, K.3
  • 30
    • 0024185105 scopus 로고
    • Catalyst for polyacrylamide gel polymerization and detection of proteins by silver staining
    • Hochstrasser, D.F., and Merril, C.R. (1988). Catalyst for polyacrylamide gel polymerization and detection of proteins by silver staining. Appl. Theor. Electrophor. 1, 35-40.
    • (1988) Appl. Theor. Electrophor. , vol.1 , pp. 35-40
    • Hochstrasser, D.F.1    Merril, C.R.2
  • 31
    • 0026828458 scopus 로고
    • Photo-system II 23 kDa polypeptide of oxygen-evolving complex is encoded by a multigene family in tobacco
    • Hua, S., Dube, S.K., Barnett, N.M., and Kung, S.D. (1992). Photo-system II 23 kDa polypeptide of oxygen-evolving complex is encoded by a multigene family in tobacco. Plant Mol. Biol. 18, 997-999.
    • (1992) Plant Mol. Biol. , vol.18 , pp. 997-999
    • Hua, S.1    Dube, S.K.2    Barnett, N.M.3    Kung, S.D.4
  • 32
    • 0000784856 scopus 로고
    • Rough thylakoids: Translation on photosynthetic membranes
    • Jagendorf, A., and Michaels, A. (1990). Rough thylakoids: Translation on photosynthetic membranes. Plant Sci. 71, 137-145.
    • (1990) Plant Sci. , vol.71 , pp. 137-145
    • Jagendorf, A.1    Michaels, A.2
  • 33
    • 0033117218 scopus 로고    scopus 로고
    • Protein import and routing systems of chloroplasts
    • Keegstra, K., and Cline, K. (1999). Protein import and routing systems of chloroplasts. Plant Cell 11, 557-570.
    • (1999) Plant Cell , vol.11 , pp. 557-570
    • Keegstra, K.1    Cline, K.2
  • 34
    • 0032518315 scopus 로고    scopus 로고
    • Metabolic compartmentation of plastid prenyllipid biosynthesis -evidence for the involvement of a multifunctional geranylgeranyl reductase
    • Keller, Y., Bouvier, F., d'Harlingue, A., and Camara, B. (1998). Metabolic compartmentation of plastid prenyllipid biosynthesis -Evidence for the involvement of a multifunctional geranylgeranyl reductase. Eur. J. Biochem. 251, 413-417.
    • (1998) Eur. J. Biochem. , vol.251 , pp. 413-417
    • Keller, Y.1    Bouvier, F.2    D'Harlingue, A.3    Camara, B.4
  • 35
    • 0033103281 scopus 로고    scopus 로고
    • Identification of proteins associated with plastoglobules isolated from pea (Pisum sativum L.) chloroplasts
    • Kessler, F., Schnell, D., and Blobel, G. (1999). Identification of proteins associated with plastoglobules isolated from pea (Pisum sativum L.) chloroplasts. Planta 208, 107-113.
    • (1999) Planta , vol.208 , pp. 107-113
    • Kessler, F.1    Schnell, D.2    Blobel, G.3
  • 36
    • 0032549515 scopus 로고    scopus 로고
    • The thylakoid lumen of chloroplasts. Isolation and characterization
    • Kieselbach, T., Hagman, Å., Andersson, B., and Schröder, W.P. (1998). The thylakoid lumen of chloroplasts. Isolation and characterization. J. Biol. Chem. 273, 6710-6716.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6710-6716
    • Kieselbach, T.1    Hagman, Å.2    Andersson, B.3    Schröder, W.P.4
  • 37
    • 0032538436 scopus 로고    scopus 로고
    • Purification and properties of a novel chloroplast stromal peptidase. Processing of polyphenol oxidase and other imported precursors
    • Koussevitzky, S., Ne'eman, E., Sommer, A., Steffens, J.C., and Harel, E. (1998). Purification and properties of a novel chloroplast stromal peptidase. Processing of polyphenol oxidase and other imported precursors. J. Biol. Chem. 273, 27064-27069.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27064-27069
    • Koussevitzky, S.1    Ne'eman, E.2    Sommer, A.3    Steffens, J.C.4    Harel, E.5
  • 38
    • 0032102792 scopus 로고    scopus 로고
    • Identifying proteins and post-translational modifications by mass spectrometry
    • Küster, B., and Mann, M. (1998). Identifying proteins and post-translational modifications by mass spectrometry. Curr. Opin. Struct. Biol. 8, 393-400.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 393-400
    • Küster, B.1    Mann, M.2
  • 39
    • 0032055343 scopus 로고    scopus 로고
    • Molecular biology of gibberellin synthesis
    • Lange, T. (1998). Molecular biology of gibberellin synthesis. Planta 204, 409-419.
    • (1998) Planta , vol.204 , pp. 409-419
    • Lange, T.1
  • 40
    • 0026668598 scopus 로고
    • Information for targeting to the chloroplast inner envelope membrane is contained in the mature region of the maize bt1-encoded protein
    • Li, H.M., Sullivan, T.D., and Keegstra, K. (1992). Information for targeting to the chloroplast inner envelope membrane is contained in the mature region of the maize Bt1-encoded protein. J. Biol. Chem. 267, 18999-19004.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18999-19004
    • Li, H.M.1    Sullivan, T.D.2    Keegstra, K.3
  • 41
    • 0026720015 scopus 로고
    • The spinach chloroplast chromosome is bound to the thylakoid membrane in the region of the inverted repeat
    • Liu, J.W., and Rose, R.J. (1992). The spinach chloroplast chromosome is bound to the thylakoid membrane in the region of the inverted repeat. Biochem. Biophys. Res. Commun. 184, 993-1000.
    • (1992) Biochem. Biophys. Res. Commun. , vol.184 , pp. 993-1000
    • Liu, J.W.1    Rose, R.J.2
  • 42
    • 0025970277 scopus 로고
    • Ferritin accumulation and degradation in different organs of pea (Pisum sativum) during development
    • Lobreaux, S., and Briat, J.F. (1991). Ferritin accumulation and degradation in different organs of pea (Pisum sativum) during development. Biochem. J. 274, 601-606.
    • (1991) Biochem. J. , vol.274 , pp. 601-606
    • Lobreaux, S.1    Briat, J.F.2
  • 43
    • 0345678951 scopus 로고    scopus 로고
    • Protein import into chloroplasts
    • Lubeck, J., Heins, L., and Soil, J. (1997). Protein import into chloroplasts. Physiol. Plant. 100, 53-64.
    • (1997) Physiol. Plant. , vol.100 , pp. 53-64
    • Lubeck, J.1    Heins, L.2    Soil, J.3
  • 44
    • 0021448826 scopus 로고
    • Partial deglycosylation of chloroplast coupling factor 1 (CF-) prevents the reconstitution of photophosphorylation
    • Maione, I.E., and Jagendorf, A.T. (1984). Partial deglycosylation of chloroplast coupling factor 1 (CF-) prevents the reconstitution of photophosphorylation. Proc. Natl. Acad. Sci. USA 81, 3733-3736.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 3733-3736
    • Maione, I.E.1    Jagendorf, A.T.2
  • 45
    • 0030836047 scopus 로고    scopus 로고
    • Stromal and thylakoid-bound ascorbate peroxidases are produced by alternative splicing in pumpkin
    • Mano, S., Yamaguchi, K., Hayashi, M., and Nishimura, M. (1997). Stromal and thylakoid-bound ascorbate peroxidases are produced by alternative splicing in pumpkin. FEBS Lett. 413, 21-26.
    • (1997) FEBS Lett. , vol.413 , pp. 21-26
    • Mano, S.1    Yamaguchi, K.2    Hayashi, M.3    Nishimura, M.4
  • 46
    • 0033082633 scopus 로고    scopus 로고
    • Characterisation of an Arabidopsis thaliana cDNA encoding a novel thylakoid lumen protein imported by the A pH-dependent pathway
    • Mant, A., Kieselbach, T., Schröder, W.P., and Robinson, C. (1999). Characterisation of an Arabidopsis thaliana cDNA encoding a novel thylakoid lumen protein imported by the A pH-dependent pathway. Planta 207, 624-627.
    • (1999) Planta , vol.207 , pp. 624-627
    • Mant, A.1    Kieselbach, T.2    Schröder, W.P.3    Robinson, C.4
  • 47
    • 0029873984 scopus 로고    scopus 로고
    • Molecular identification of zeaxanthin epoxidase of Nicotiana plumbaginifolia, a gene involved in abscisic acid biosynthesis and corresponding to the ABA locus of Arabidopsis thaliana
    • Marin, E., Nussaume, L., Quesada, A., Gonneau, M., Sotta, B., Hugueney, P., Frey, A., and Marion-Poll, A. (1996). Molecular identification of zeaxanthin epoxidase of Nicotiana plumbaginifolia, a gene involved in abscisic acid biosynthesis and corresponding to the ABA locus of Arabidopsis thaliana. EMBO J. 15, 2331-2342.
    • (1996) EMBO J. , vol.15 , pp. 2331-2342
    • Marin, E.1    Nussaume, L.2    Quesada, A.3    Gonneau, M.4    Sotta, B.5    Hugueney, P.6    Frey, A.7    Marion-Poll, A.8
  • 48
    • 0023303085 scopus 로고
    • Intramembrane translocation and post-translational palmitoylation of the chloroplast 32-kDa herbicide-binding protein
    • Mattoo, A.K., and Edelman, M. (1987). Intramembrane translocation and post-translational palmitoylation of the chloroplast 32-kDa herbicide-binding protein. Proc. Natl. Acad. Sci. USA 84, 1497-1501.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 1497-1501
    • Mattoo, A.K.1    Edelman, M.2
  • 51
    • 0344404400 scopus 로고    scopus 로고
    • A nuclear-encoded protein of prokaryotic origin is essential for the stability of photosystem II in Arabidopsis thaliana
    • Meurer, J., Plucken, H., Kowallik, K.V., and Westhoff, P. (1998). A nuclear-encoded protein of prokaryotic origin is essential for the stability of photosystem II in Arabidopsis thaliana. EMBO J. 17, 5286-5297.
    • (1998) EMBO J. , vol.17 , pp. 5286-5297
    • Meurer, J.1    Plucken, H.2    Kowallik, K.V.3    Westhoff, P.4
  • 52
    • 0026540832 scopus 로고
    • Arabidopsis mutants deficient in polyunsaturated fatty acid synthesis. Biochemical and genetic characterization of a plant oleoyl-phosphatidylcholine desaturase
    • Miquel, M., and Browse, J. (1992). Arabidopsis mutants deficient in polyunsaturated fatty acid synthesis. Biochemical and genetic characterization of a plant oleoyl-phosphatidylcholine desaturase. J. Biol. Chem. 267, 1502-1509.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1502-1509
    • Miquel, M.1    Browse, J.2
  • 54
    • 0033549567 scopus 로고    scopus 로고
    • Component specificity for the thylakoidal sec and delta pH-dependent protein transport pathways
    • Mori, H., Summer, E.J., Ma, X., and Cline, K. (1999). Component specificity for the thylakoidal sec and delta pH-dependent protein transport pathways. J. Cell Biol. 146, 45-56.
    • (1999) J. Cell Biol. , vol.146 , pp. 45-56
    • Mori, H.1    Summer, E.J.2    Ma, X.3    Cline, K.4
  • 55
    • 0032972509 scopus 로고    scopus 로고
    • PSORT: A program for detecting sorting signals in proteins and predicting their subcellular localization
    • Nakai, K., and Horton, P. (1999). PSORT: A program for detecting sorting signals in proteins and predicting their subcellular localization. Trends Biochem. Sci. 24, 34-36.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 34-36
    • Nakai, K.1    Horton, P.2
  • 57
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen, H., Engelbrecht, J., Brunak, S., and von Heijne, G. (1997). Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10, 1-6.
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 59
    • 0031854295 scopus 로고    scopus 로고
    • Identification of yeast proteins from two-dimensional gels: Working out spot cross-contamination
    • Parker, K.C., Garrels, J.I., Hines, W., Butler, E.M., McKee, A.M., Patterson, D., and Martin, S. (1998). Identification of yeast proteins from two-dimensional gels: Working out spot cross-contamination. Electrophoresis 19, 1920-1932.
    • (1998) Electrophoresis , vol.19 , pp. 1920-1932
    • Parker, K.C.1    Garrels, J.I.2    Hines, W.3    Butler, E.M.4    McKee, A.M.5    Patterson, D.6    Martin, S.7
  • 60
    • 26044440113 scopus 로고
    • Determination of accurate extinction coefficients and simultaneous equations for assaying chlorophylls a and b extracted with four different solvents: Verification of the concentration of chlorophyll standards by atomic absorption spectroscopy
    • Porra, R.J., Thompson, W.A., and Kriedemann, P.E. (1989). Determination of accurate extinction coefficients and simultaneous equations for assaying chlorophylls a and b extracted with four different solvents: Verification of the concentration of chlorophyll standards by atomic absorption spectroscopy. Biochim. Biophys. Acta 975, 384-394.
    • (1989) Biochim. Biophys. Acta , vol.975 , pp. 384-394
    • Porra, R.J.1    Thompson, W.A.2    Kriedemann, P.E.3
  • 61
    • 0031277489 scopus 로고    scopus 로고
    • A ubiquitous plant housekeeping gene, PAP, encodes a major protein component of bell pepper chromoplasts
    • Pozueta-Romero, J., Rafia, F., Houlne, G., Cheniclet, C., Carde, J.P., Schantz, M.L., and Schantz, R. (1997). A ubiquitous plant housekeeping gene, PAP, encodes a major protein component of bell pepper chromoplasts. Plant Physiol. 115, 1185-1194.
    • (1997) Plant Physiol. , vol.115 , pp. 1185-1194
    • Pozueta-Romero, J.1    Rafia, F.2    Houlne, G.3    Cheniclet, C.4    Carde, J.P.5    Schantz, M.L.6    Schantz, R.7
  • 62
    • 0031807109 scopus 로고    scopus 로고
    • Use of thiourea to increase the solubility of membrane proteins in two-dimensional electrophoresis
    • Rabilloud, T. (1998). Use of thiourea to increase the solubility of membrane proteins in two-dimensional electrophoresis. Electrophoresis 19, 758-760.
    • (1998) Electrophoresis , vol.19 , pp. 758-760
    • Rabilloud, T.1
  • 63
    • 0028603364 scopus 로고
    • Sample application by in-gel rehydration improves the resolution of two-dimensional electrophoresis with immobilized pH gradients in the first dimension
    • Rabilloud, T., Valette, C., and Lawrence, J.-J. (1994a). Sample application by in-gel rehydration improves the resolution of two-dimensional electrophoresis with immobilized pH gradients in the first dimension. Electrophoresis 15, 1552-1558.
    • (1994) Electrophoresis , vol.15 , pp. 1552-1558
    • Rabilloud, T.1    Valette, C.2    Lawrence, J.-J.3
  • 64
    • 0002476741 scopus 로고
    • Silver-staining of proteins in polyacrylamide gels: A general overview
    • Rabilloud, T., Vuillard, L., Gilly, C., and Lawrence, J.-J. (1994b). Silver-staining of proteins in polyacrylamide gels: A general overview. Cell. Mol. Biol. 40, 57-75.
    • (1994) Cell. Mol. Biol. , vol.40 , pp. 57-75
    • Rabilloud, T.1    Vuillard, L.2    Gilly, C.3    Lawrence, J.-J.4
  • 65
    • 0030957650 scopus 로고    scopus 로고
    • Improvement of the solubilization of proteins in two-dimensional electrophoresis with immobilized pH gradients
    • Rabilloud, T., Adessi, C., Giraudel, A., and Lunardi, J. (1997). Improvement of the solubilization of proteins in two-dimensional electrophoresis with immobilized pH gradients. Electrophoresis 18, 307-316.
    • (1997) Electrophoresis , vol.18 , pp. 307-316
    • Rabilloud, T.1    Adessi, C.2    Giraudel, A.3    Lunardi, J.4
  • 66
    • 0032560485 scopus 로고    scopus 로고
    • A chloroplast processing enzyme functions as the general stromal processing peptidase
    • Richter, S., and Lamppa, G.K. (1998). A chloroplast processing enzyme functions as the general stromal processing peptidase. Proc. Natl. Acad. Sci. USA 95, 7463-7468.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7463-7468
    • Richter, S.1    Lamppa, G.K.2
  • 67
    • 0031013294 scopus 로고    scopus 로고
    • Mass spectrometry in protein studies: From genome to function
    • Roepstorff, P. (1997). Mass spectrometry in protein studies: From genome to function. Curr. Opin. Biotechnol. 8, 6-13.
    • (1997) Curr. Opin. Biotechnol. , vol.8 , pp. 6-13
    • Roepstorff, P.1
  • 68
    • 0030961920 scopus 로고    scopus 로고
    • Construction of a directory of tobacco plasma membrane proteins by combined two-dimensional gel electrophoresis and protein sequencing
    • Rouquié, D., Peltier, J.B., Marquis-Mansion, M., Tournaire, C., Doumas, P., and Rossignol, M. (1997). Construction of a directory of tobacco plasma membrane proteins by combined two-dimensional gel electrophoresis and protein sequencing. Electrophoresis 18, 654-660.
    • (1997) Electrophoresis , vol.18 , pp. 654-660
    • Rouquié, D.1    Peltier, J.B.2    Marquis-Mansion, M.3    Tournaire, C.4    Doumas, P.5    Rossignol, M.6
  • 69
    • 0027511159 scopus 로고
    • Detection and characterization of a plastid envelope DMA-binding protein which may anchor plastid nucleoids
    • Sato, N., Albrieux, C., Joyard, J., Douce, R., and Kuroiwa, T. (1993). Detection and characterization of a plastid envelope DMA-binding protein which may anchor plastid nucleoids. EMBO J. 12, 555-561.
    • (1993) EMBO J. , vol.12 , pp. 555-561
    • Sato, N.1    Albrieux, C.2    Joyard, J.3    Douce, R.4    Kuroiwa, T.5
  • 70
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H., and von Jagow, G. (1987). Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166, 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 71
    • 0030026850 scopus 로고    scopus 로고
    • Molecular chaperones are present in the thylakoid lumen of pea chloroplasts
    • Schlichter, T., and Soll, J. (1996). Molecular chaperones are present in the thylakoid lumen of pea chloroplasts. FEBS Lett. 379, 302-304.
    • (1996) FEBS Lett. , vol.379 , pp. 302-304
    • Schlichter, T.1    Soll, J.2
  • 72
    • 0025008168 scopus 로고
    • Sequence logos: A new way to display consensus sequences
    • Schneider, G., and Stephens, R.M. (1990). Sequence logos: A new way to display consensus sequences. Nucleic Acids Res. 18, 6097-6100.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 6097-6100
    • Schneider, G.1    Stephens, R.M.2
  • 73
    • 0031736218 scopus 로고    scopus 로고
    • Old and new pathways of protein export in chloroplasts and bacteria
    • Settles, A.M., and Martienssen, R. (1998). Old and new pathways of protein export in chloroplasts and bacteria. Trends Cell Biol. 8, 494-501.
    • (1998) Trends Cell Biol. , vol.8 , pp. 494-501
    • Settles, A.M.1    Martienssen, R.2
  • 74
    • 0025830411 scopus 로고
    • Transport of proteins into chloroplasts. The thylakoidal processing peptidase is a signal-type peptidase with stringent substrate requirements at the -3 and -1 positions
    • Shackleton, J.B., and Robinson, C. (1991). Transport of proteins into chloroplasts. The thylakoidal processing peptidase is a signal-type peptidase with stringent substrate requirements at the -3 and -1 positions. J. Biol. Chem. 266, 12152-12156.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12152-12156
    • Shackleton, J.B.1    Robinson, C.2
  • 76
    • 0024299367 scopus 로고
    • Subtle alteration of the active site of ribulose bisphosphate carboxylase/oxy-genase by concerted site-directed mutagenesis and chemical modification
    • Smith, H.B., Larimer, F.W., and Hartman, F.C. (1988). Subtle alteration of the active site of ribulose bisphosphate carboxylase/oxy-genase by concerted site-directed mutagenesis and chemical modification. Biochem. Biophys. Res. Commun. 152, 579-584.
    • (1988) Biochem. Biophys. Res. Commun. , vol.152 , pp. 579-584
    • Smith, H.B.1    Larimer, F.W.2    Hartman, F.C.3
  • 77
    • 0032055825 scopus 로고    scopus 로고
    • AIR synthetase in cowpea nodules: A single gene product targeted to two organelles?
    • Smith, P.M., Mann, A.J., Goggin, D.E., and Atkins, C.A. (1998). AIR synthetase in cowpea nodules: A single gene product targeted to two organelles? Plant Mol. Biol. 36, 811-820.
    • (1998) Plant Mol. Biol. , vol.36 , pp. 811-820
    • Smith, P.M.1    Mann, A.J.2    Goggin, D.E.3    Atkins, C.A.4
  • 78
    • 0033515448 scopus 로고    scopus 로고
    • TAKs, thylakoid membrane protein kinases associated with energy transduction
    • Snyders, S., and Kohorn, B.D. (1999). TAKs, thylakoid membrane protein kinases associated with energy transduction. J. Biol. Chem. 274, 9137-9140.
    • (1999) J. Biol. Chem. , vol.274 , pp. 9137-9140
    • Snyders, S.1    Kohorn, B.D.2
  • 79
    • 0028198721 scopus 로고
    • Substrate- and species-specific processing enzymes for chloroplast precursor proteins
    • Su, Q., and Boschetti, A. (1994). Substrate- and species-specific processing enzymes for chloroplast precursor proteins. Biochem. J. 300, 787-792.
    • (1994) Biochem. J. , vol.300 , pp. 787-792
    • Su, Q.1    Boschetti, A.2
  • 80
    • 0030267939 scopus 로고    scopus 로고
    • Regulation of gene expression in chloroplasts of higher plants
    • Sugita, M., and Sugiura, M. (1996). Regulation of gene expression in chloroplasts of higher plants. Plant Mol. Biol. 32, 315-326.
    • (1996) Plant Mol. Biol. , vol.32 , pp. 315-326
    • Sugita, M.1    Sugiura, M.2
  • 81
    • 0028980954 scopus 로고
    • The maize brittle 1 gene encodes amyloplast membrane polypeptides
    • Sullivan, T.D., and Kaneko, Y. (1995). The maize brittle 1 gene encodes amyloplast membrane polypeptides. Plant J. 196, 477-484.
    • (1995) Plant J. , vol.196 , pp. 477-484
    • Sullivan, T.D.1    Kaneko, Y.2
  • 82
    • 0026291471 scopus 로고
    • Analysis of maize brittle-1 alleles and a defective Suppressor-mutator-induced mutable allele
    • Sullivan, T.D., Strelow, L.I., Illingworth, C.A., Phillips, R.L., and Nelson, O.E., Jr. (1991). Analysis of maize brittle-1 alleles and a defective Suppressor-mutator-induced mutable allele. Plant Cell 3, 1337-1348.
    • (1991) Plant Cell , vol.3 , pp. 1337-1348
    • Sullivan, T.D.1    Strelow, L.I.2    Illingworth, C.A.3    Phillips, R.L.4    Nelson O.E., Jr.5
  • 83
    • 0030047467 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis of plant proteins and standardization of gel patterns
    • Tsugita, A., Kamo, M., Kawakami, T., and Ohki, Y. (1996). Two-dimensional electrophoresis of plant proteins and standardization of gel patterns. Electrophoresis 17, 855-865.
    • (1996) Electrophoresis , vol.17 , pp. 855-865
    • Tsugita, A.1    Kamo, M.2    Kawakami, T.3    Ohki, Y.4
  • 84
    • 0032083023 scopus 로고    scopus 로고
    • Protein phosphorylation and redox sensing in chloroplast thylakoids
    • Vener, A.V., Ohad, I., and Andersson, B. (1998). Protein phosphorylation and redox sensing in chloroplast thylakoids. Curr. Opin. Plant Biol. 1, 217-223.
    • (1998) Curr. Opin. Plant Biol. , vol.1 , pp. 217-223
    • Vener, A.V.1    Ohad, I.2    Andersson, B.3
  • 86
    • 0000168857 scopus 로고
    • The extrinsic 33 kDa polypeptide of the oxygen-evolving complex of photosystem II is a putative calcium-binding protein and is encoded by a multi-gene family in pea
    • Wales, R., Newman, B.J., Pappin, D., and Gray, J.C. (1989). The extrinsic 33 kDa polypeptide of the oxygen-evolving complex of photosystem II is a putative calcium-binding protein and is encoded by a multi-gene family in pea. Plant Mol. Biol. 12, 439-451.
    • (1989) Plant Mol. Biol. , vol.12 , pp. 439-451
    • Wales, R.1    Newman, B.J.2    Pappin, D.3    Gray, J.C.4
  • 87
    • 0031776931 scopus 로고    scopus 로고
    • Electrospray-ionization mass spectrometry of intact intrinsic membrane proteins
    • Whitelegge, J.P., Gundersen, C.B., and Faull, K.F. (1998). Electrospray-ionization mass spectrometry of intact intrinsic membrane proteins. Protein Sci. 7, 1423-1430.
    • (1998) Protein Sci. , vol.7 , pp. 1423-1430
    • Whitelegge, J.P.1    Gundersen, C.B.2    Faull, K.F.3
  • 89
    • 0032910388 scopus 로고    scopus 로고
    • The biogenesis and assembly of photosynthetic proteins in thylakoid membranes
    • Wollman, F.A., Minai, L., and Nechushtai, R. (1999). The biogenesis and assembly of photosynthetic proteins in thylakoid membranes. Biochim. Biophys. Acta 1411, 21-85.
    • (1999) Biochim. Biophys. Acta , vol.1411 , pp. 21-85
    • Wollman, F.A.1    Minai, L.2    Nechushtai, R.3
  • 90
    • 0031962612 scopus 로고    scopus 로고
    • Mass spectrometry and the age of the pro-teome
    • Yates III, J.R. (1998). Mass spectrometry and the age of the pro-teome. J. Mass Spectrom. 33, 1-19.
    • (1998) J. Mass Spectrom. , vol.33 , pp. 1-19
    • Yates J.R. III1
  • 91
    • 0033557879 scopus 로고    scopus 로고
    • Alternatively spliced mRNA variants of chloroplast ascorbate peroxidase isoenzymes in spinach leaves
    • Yoshimura, K., Yabuta, Y., Tamoi, M., Ishikawa, T., and Shigeoka, S. (1999). Alternatively spliced mRNA variants of chloroplast ascorbate peroxidase isoenzymes in spinach leaves. Biochem. J. 338, 41-48.
    • (1999) Biochem. J. , vol.338 , pp. 41-48
    • Yoshimura, K.1    Yabuta, Y.2    Tamoi, M.3    Ishikawa, T.4    Shigeoka, S.5
  • 92
    • 0029553767 scopus 로고
    • Nucleoids of pea chloroplasts: Microscopic and chemical characterization. Occurrence of histone-like proteins
    • Yurina, N.P., Belkina, G.G., Karapetyan, N.V., and Odintsova, M.S. (1995). Nucleoids of pea chloroplasts: Microscopic and chemical characterization. Occurrence of histone-like proteins. Biochem. Mol. Biol. Int. 36, 145-154.
    • (1995) Biochem. Mol. Biol. Int. , vol.36 , pp. 145-154
    • Yurina, N.P.1    Belkina, G.G.2    Karapetyan, N.V.3    Odintsova, M.S.4
  • 93
    • 0032568955 scopus 로고    scopus 로고
    • Isolation and characterization of monomeric and dimeric CP47-reaction center photosystem II complexes
    • Zheleva, D., Sharma, J., Panico, M., Morris, H.R., and Barber, J. (1998). Isolation and characterization of monomeric and dimeric CP47-reaction center photosystem II complexes. J. Biol. Chem 273, 16122-16127.
    • (1998) J. Biol. Chem , vol.273 , pp. 16122-16127
    • Zheleva, D.1    Sharma, J.2    Panico, M.3    Morris, H.R.4    Barber, J.5


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