메뉴 건너뛰기




Volumn 56, Issue , 2005, Pages 133-164

Solute transporters of the plastid envelope membrane

Author keywords

Bioinformatics; Genomics; Metabolism; Transport

Indexed keywords

CARRIER PROTEIN;

EID: 20444385506     PISSN: 15435008     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.arplant.56.032604.144228     Document Type: Review
Times cited : (167)

References (157)
  • 1
    • 0345307752 scopus 로고    scopus 로고
    • The lactose permease of Escherichia coli: Overall structure, the sugar-binding site and the alternating access model for transport
    • Abramson J, Smirnova I, Kasho V, Verner G, Iwata S, Kaback HR. 2003. The lactose permease of Escherichia coli: overall structure, the sugar-binding site and the alternating access model for transport. FEBS Lett. 555:96-101
    • (2003) FEBS Lett. , vol.555 , pp. 96-101
    • Abramson, J.1    Smirnova, I.2    Kasho, V.3    Verner, G.4    Iwata, S.5    Kaback, H.R.6
  • 4
    • 0033570149 scopus 로고    scopus 로고
    • A rectifying ATP-regulated solute channel in the chloroplastic outer envelope from pea
    • Bölter B, Soll J, Hill K, Hemmler R, Wagner R. 1999. A rectifying ATP-regulated solute channel in the chloroplastic outer envelope from pea. EMBO J. 18:5505-16
    • (1999) EMBO J. , vol.18 , pp. 5505-5516
    • Bölter, B.1    Soll, J.2    Hill, K.3    Hemmler, R.4    Wagner, R.5
  • 5
    • 4344624847 scopus 로고    scopus 로고
    • Plant sulphate transporters: Co-ordination of uptake, intracellular and long-distance transport
    • Buchner P, Takahashi H, Hawkesford MJ. 2004. Plant sulphate transporters: co-ordination of uptake, intracellular and long-distance transport. J. Exp. Bot. 55:1765-73
    • (2004) J. Exp. Bot. , vol.55 , pp. 1765-1773
    • Buchner, P.1    Takahashi, H.2    Hawkesford, M.J.3
  • 7
    • 1942443704 scopus 로고    scopus 로고
    • The IUBMB-endorsed transporter classification system
    • Busch W, Saier MH Jr. 2003. The IUBMB-endorsed transporter classification system. Methods Mol. Biol. 227:21-36
    • (2003) Methods Mol. Biol. , vol.227 , pp. 21-36
    • Busch, W.1    Saier Jr., M.H.2
  • 8
    • 0029186042 scopus 로고
    • Bt1, a structural gene for the major 39-44 kda amyloplast membrane polypeptides
    • Cao HP, Sullivan TD, Boyer CD, Shannon JC. 1995. Bt1, a structural gene for the major 39-44 kda amyloplast membrane polypeptides. Physiol. Plant. 95:176-86
    • (1995) Physiol. Plant. , vol.95 , pp. 176-186
    • Cao, H.P.1    Sullivan, T.D.2    Boyer, C.D.3    Shannon, J.C.4
  • 9
    • 1542272659 scopus 로고    scopus 로고
    • Expression pattern of a nuclear encoded mitochondrial arginine-ornithine translocator gene from Arabidopsis
    • Catoni E, Desimone M, Hilpert M, Wipf D, Kunze R, et al. 2003. Expression pattern of a nuclear encoded mitochondrial arginine-ornithine translocator gene from Arabidopsis. BMC Plant Biol. 3:1
    • (2003) BMC Plant Biol. , vol.3 , pp. 1
    • Catoni, E.1    Desimone, M.2    Hilpert, M.3    Wipf, D.4    Kunze, R.5
  • 10
    • 0037448455 scopus 로고    scopus 로고
    • Identification of an Arabidopsis mitochondrial succinate-fumarate translocator
    • Catoni E, Schwab R, Hilpert M, Desimone M, Schwacke R, et al. 2003. Identification of an Arabidopsis mitochondrial succinate-fumarate translocator. FEBS Lett. 534:87-92
    • (2003) FEBS Lett. , vol.534 , pp. 87-92
    • Catoni, E.1    Schwab, R.2    Hilpert, M.3    Desimone, M.4    Schwacke, R.5
  • 11
    • 0037287943 scopus 로고    scopus 로고
    • Acosmid vector containing a dominant selectable marker for cloning Chlamydomonas genes by complementation
    • Chang M, Li F, Odom OW, Lee J, Herrin DL. 2003. Acosmid vector containing a dominant selectable marker for cloning Chlamydomonas genes by complementation. Plasmid 49:75-78
    • (2003) Plasmid , vol.49 , pp. 75-78
    • Chang, M.1    Li, F.2    Odom, O.W.3    Lee, J.4    Herrin, D.L.5
  • 12
    • 11844282214 scopus 로고    scopus 로고
    • Localization and function of SulP, a nuclear-encoded chloroplast sulfate permease in Chlamydomonas reinhardtii
    • doi: 10.1007/s00425-004-1331-5
    • Chen HC, Melis A. 2004. Localization and function of SulP, a nuclear-encoded chloroplast sulfate permease in Chlamydomonas reinhardtii. Planta. doi: 10.1007/s00425-004-1331-5
    • (2004) Planta
    • Chen, H.C.1    Melis, A.2
  • 13
    • 0347300314 scopus 로고    scopus 로고
    • SulP, a nuclear gene encoding a putative chloroplast-targeted sulfate permease in Chlamydomonas reinhardtii
    • Chen HC, Yokthongwattana K, Newton AJ, Melis A. 2003. SulP, a nuclear gene encoding a putative chloroplast-targeted sulfate permease in Chlamydomonas reinhardtii. Planta 218:98-106
    • (2003) Planta , vol.218 , pp. 98-106
    • Chen, H.C.1    Yokthongwattana, K.2    Newton, A.J.3    Melis, A.4
  • 14
    • 1642416044 scopus 로고    scopus 로고
    • A cytosolic glucosyltransferase is required for conversion of starch to sucrose in Arabidopsis leaves at night
    • Chia T, Thorneycroft D, Chapple A, Messerli G, Chen J, et al. 2004. A cytosolic glucosyltransferase is required for conversion of starch to sucrose in Arabidopsis leaves at night. Plant J. 37:853-63
    • (2004) Plant J. , vol.37 , pp. 853-863
    • Chia, T.1    Thorneycroft, D.2    Chapple, A.3    Messerli, G.4    Chen, J.5
  • 15
    • 0038376077 scopus 로고    scopus 로고
    • Tic40, a membrane-anchored co-chaperone homolog in the chloroplast protein translocon
    • Chou ML, Fitzpatrick LM, Tu SL, Budziszewski G, Potter-Lewis S, et al. 2003. Tic40, a membrane-anchored co-chaperone homolog in the chloroplast protein translocon. EMBO J. 22:2970-80
    • (2003) EMBO J. , vol.22 , pp. 2970-2980
    • Chou, M.L.1    Fitzpatrick, L.M.2    Tu, S.L.3    Budziszewski, G.4    Potter-Lewis, S.5
  • 16
    • 0025977723 scopus 로고
    • Identification and structure of four yeast genes (SLY) that are able to suppress the functional loss of YPT1, a member of the RAS superfamily
    • Dascher C, Ossig R, Gallwitz D, Schmitt HD. 1991. Identification and structure of four yeast genes (SLY) that are able to suppress the functional loss of YPT1, a member of the RAS superfamily. Mol. Cell Biol. 11:872-85
    • (1991) Mol. Cell Biol. , vol.11 , pp. 872-885
    • Dascher, C.1    Ossig, R.2    Gallwitz, D.3    Schmitt, H.D.4
  • 17
    • 85047686510 scopus 로고    scopus 로고
    • The plastidic pentose phosphate translocator represents a link between the cytosolic and the plastidic pentose phosphate pathways in plants
    • Eicks M, Maurino V, Knappe S, Flügge UI, Fischer K. 2002. The plastidic pentose phosphate translocator represents a link between the cytosolic and the plastidic pentose phosphate pathways in plants. Plant Physiol. 128:512-22
    • (2002) Plant Physiol. , vol.128 , pp. 512-522
    • Eicks, M.1    Maurino, V.2    Knappe, S.3    Flügge, U.I.4    Fischer, K.5
  • 18
    • 0034697980 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins based on their N- terminal amino acid sequence
    • Emanuelsson O, Nielsen H, Brunak S, von Heijne G. 2000. Predicting subcellular localization of proteins based on their N- terminal amino acid sequence. J. Mol. Biol. 300:1005-16
    • (2000) J. Mol. Biol. , vol.300 , pp. 1005-1016
    • Emanuelsson, O.1    Nielsen, H.2    Brunak, S.3    Von Heijne, G.4
  • 19
    • 0032935861 scopus 로고    scopus 로고
    • ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites
    • Emanuelsson O, Nielsen H, von Heijne G. 1999. ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites. Protein Sci. 8:978-84
    • (1999) Protein Sci. , vol.8 , pp. 978-984
    • Emanuelsson, O.1    Nielsen, H.2    Von Heijne, G.3
  • 20
    • 0348136190 scopus 로고    scopus 로고
    • Proteomics of the chloroplast envelope membranes from Arabidopsis thaliana
    • Ferro M, Salvi D, Brugiere S, Miras S, Kowalski S, et al. 2003. Proteomics of the chloroplast envelope membranes from Arabidopsis thaliana. Mol. Cell Proteomics 2:325-45
    • (2003) Mol. Cell Proteomics , vol.2 , pp. 325-345
    • Ferro, M.1    Salvi, D.2    Brugiere, S.3    Miras, S.4    Kowalski, S.5
  • 21
    • 0037143630 scopus 로고    scopus 로고
    • Integral membrane proteins of the chloroplast envelope: Identification and subcellular localization of new transporters
    • Ferro M, Salvi D, Riviere-Rolland H, Vermat T, Seigneurin-Berny D, et al. 2002. Integral membrane proteins of the chloroplast envelope: identification and subcellular localization of new transporters. Proc. Natl. Acad. Sci. USA 99:11487-92
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11487-11492
    • Ferro, M.1    Salvi, D.2    Riviere-Rolland, H.3    Vermat, T.4    Seigneurin-Berny, D.5
  • 22
    • 0031105611 scopus 로고    scopus 로고
    • A new class of plastidic phosphate translocators: A putative link between primary and secondary metabolism by the phosphoenolpyruvate/phosphate antiporter
    • Fischer K, Kammerer N, Gutensohn M, Arbinger B, Weber A, et al. 1997. A new class of plastidic phosphate translocators: a putative link between primary and secondary metabolism by the phosphoenolpyruvate/phosphate antiporter. Plant Cell 9:453-62
    • (1997) Plant Cell , vol.9 , pp. 453-462
    • Fischer, K.1    Kammerer, N.2    Gutensohn, M.3    Arbinger, B.4    Weber, A.5
  • 23
    • 0036674475 scopus 로고    scopus 로고
    • Transport of carbon in non-green plastids
    • Fischer K, Weber A. 2002. Transport of carbon in non-green plastids. Trends Plant Sci. 7:345-51
    • (2002) Trends Plant Sci. , vol.7 , pp. 345-351
    • Fischer, K.1    Weber, A.2
  • 26
    • 0025914006 scopus 로고
    • The major chloroplast envelope polypeptide is the phosphate translocator and not the protein import receptor
    • Flügge UI, Weber A, Fischer K, Lottspeich F, Eckerskorn C, et al. 1991. The major chloroplast envelope polypeptide is the phosphate translocator and not the protein import receptor. Nature 353:364-67
    • (1991) Nature , vol.353 , pp. 364-367
    • Flügge, U.I.1    Weber, A.2    Fischer, K.3    Lottspeich, F.4    Eckerskorn, C.5
  • 27
    • 1042279117 scopus 로고    scopus 로고
    • In-depth analysis of the thylakoid membrane proteome of Arabidopsis thaliana chloroplasts: New proteins, new functions, and a plastid proteome database
    • Friso G, Giacomelli L, Ytterberg AJ, Peltier JB, Rudella A, et al. 2004. In-depth analysis of the thylakoid membrane proteome of Arabidopsis thaliana chloroplasts: new proteins, new functions, and a plastid proteome database. Plant Cell 16:478-99
    • (2004) Plant Cell , vol.16 , pp. 478-499
    • Friso, G.1    Giacomelli, L.2    Ytterberg, A.J.3    Peltier, J.B.4    Rudella, A.5
  • 28
    • 0041733229 scopus 로고    scopus 로고
    • Proteomic study of the Arabidopsis thaliana chloroplastic envelope membrane utilizing alternatives to traditional two-dimensional electrophoresis
    • Froehlich JE, Wilkerson CG, Ray WK, McAndrew RS, Osteryoung KW, et al. 2003. Proteomic study of the Arabidopsis thaliana chloroplastic envelope membrane utilizing alternatives to traditional two-dimensional electrophoresis. J. Proteome Res. 2:413-25
    • (2003) J. Proteome Res. , vol.2 , pp. 413-425
    • Froehlich, J.E.1    Wilkerson, C.G.2    Ray, W.K.3    McAndrew, R.S.4    Osteryoung, K.W.5
  • 29
    • 0033761347 scopus 로고    scopus 로고
    • Structure of a glycerol-conducting channel and the basis for its selectivity
    • Fu D, Libson A, Miercke LJ, Weitzman C, Nollert P, et al. 2000. Structure of a glycerol-conducting channel and the basis for its selectivity. Science 290:481-86
    • (2000) Science , vol.290 , pp. 481-486
    • Fu, D.1    Libson, A.2    Miercke, L.J.3    Weitzman, C.4    Nollert, P.5
  • 30
    • 0026609104 scopus 로고
    • The distribution of charged amino acids in mitochondrial inner-membrane proteins suggests different modes of membrane integration for nuclearly and mitochondrially encoded proteins
    • Gavel Y, von Heijne G. 1992. The distribution of charged amino acids in mitochondrial inner-membrane proteins suggests different modes of membrane integration for nuclearly and mitochondrially encoded proteins. Eur. J. Biochem. 205:1207-15
    • (1992) Eur. J. Biochem. , vol.205 , pp. 1207-1215
    • Gavel, Y.1    Von Heijne, G.2
  • 31
    • 0033133448 scopus 로고    scopus 로고
    • Three functional transporters for constitutive, diurnally regulated, and starvation-induced uptake of ammonium into Arabidopsis roots
    • Gazzarrini S, Lejay L, Gojon A, Ninnemann O, Frommer WB, von Wiren N. 1999. Three functional transporters for constitutive, diurnally regulated, and starvation-induced uptake of ammonium into Arabidopsis roots. Plant Cell 11:937-48
    • (1999) Plant Cell , vol.11 , pp. 937-948
    • Gazzarrini, S.1    Lejay, L.2    Gojon, A.3    Ninnemann, O.4    Frommer, W.B.5    Von Wiren, N.6
  • 32
    • 0034143440 scopus 로고    scopus 로고
    • A new familiy of high-affinity transporters for adenine, cytosine, and purine derivatives in Arabidopsis
    • Gillissen B, Bürkle L, André B, Kühn C, Rentsch D, et al. 2000. A new familiy of high-affinity transporters for adenine, cytosine, and purine derivatives in Arabidopsis. Plant Cell 12:291-300
    • (2000) Plant Cell , vol.12 , pp. 291-300
    • Gillissen, B.1    Bürkle, L.2    André, B.3    Kühn, C.4    Rentsch, D.5
  • 33
    • 0032437390 scopus 로고    scopus 로고
    • Stable isotope distribution in the major metabolites of source and sink organs of Solanum tuberosum L.: A powerful tool in the study of metabolic partitioning in intact plants
    • Gleixner G, Scrimgeour C, Schmidt HL, Viola R. 1998. Stable isotope distribution in the major metabolites of source and sink organs of Solanum tuberosum L.: a powerful tool in the study of metabolic partitioning in intact plants. Planta 207:241-45
    • (1998) Planta , vol.207 , pp. 241-245
    • Gleixner, G.1    Scrimgeour, C.2    Schmidt, H.L.3    Viola, R.4
  • 36
    • 0031401179 scopus 로고    scopus 로고
    • Antisense repression of both ADP-glucose pyrophosphorylase and triose phosphate translocator modifies carbohydrate partitioning in potato leaves
    • Hattenbach A, Müller-Röber B, Nast G, Heineke D. 1997. Antisense repression of both ADP-glucose pyrophosphorylase and triose phosphate translocator modifies carbohydrate partitioning in potato leaves. Plant Physiol. 115:471-75
    • (1997) Plant Physiol. , vol.115 , pp. 471-475
    • Hattenbach, A.1    Müller-Röber, B.2    Nast, G.3    Heineke, D.4
  • 37
    • 0033666207 scopus 로고    scopus 로고
    • Plastidic metabolite transporters and their physiological functions in the inducible crassulacean acid metabolism plant Mesembryanthemum crystallinum
    • Häusler RE, Baur B, Scharte J, Teichmann T, Eicks M, et al. 2000. Plastidic metabolite transporters and their physiological functions in the inducible crassulacean acid metabolism plant Mesembryanthemum crystallinum. Plant J. 24:285-96
    • (2000) Plant J. , vol.24 , pp. 285-296
    • Häusler, R.E.1    Baur, B.2    Scharte, J.3    Teichmann, T.4    Eicks, M.5
  • 38
    • 0343485024 scopus 로고    scopus 로고
    • Control of carbon partitioning and photosynthesis by the triose phosphate/phosphate translocator in transgenic tobacco plants (Nicotiana tabacum). II. Assessment of control coefficients of the triose phosphate/phosphate translocator
    • Häusler RE, Schlieben NH, Flügge UI. 2000. Control of carbon partitioning and photosynthesis by the triose phosphate/phosphate translocator in transgenic tobacco plants (Nicotiana tabacum). II. Assessment of control coefficients of the triose phosphate/phosphate translocator. Planta 210:383-90
    • (2000) Planta , vol.210 , pp. 383-390
    • Häusler, R.E.1    Schlieben, N.H.2    Flügge, U.I.3
  • 39
    • 0343485026 scopus 로고    scopus 로고
    • Control of carbon partitioning and photosynthesis by the triose phosphate/phosphate translocator in transgenic tobacco plants (Nicotiana tabacum L.). I. Comparative physiological analysis of tobacco plants with antisense repression and overexpression of the triose phosphate/phosphate translocator
    • Häusler RE, Schlieben NH, Nicolay P, Fischer K, Fischer KL, Flügge UI. 2000. Control of carbon partitioning and photosynthesis by the triose phosphate/phosphate translocator in transgenic tobacco plants (Nicotiana tabacum L.). I. Comparative physiological analysis of tobacco plants with antisense repression and overexpression of the triose phosphate/phosphate translocator. Planta 210:371-82
    • (2000) Planta , vol.210 , pp. 371-382
    • Häusler, R.E.1    Schlieben, N.H.2    Nicolay, P.3    Fischer, K.4    Fischer, K.L.5    Flügge, U.I.6
  • 40
    • 0028039332 scopus 로고
    • Effect of antisense repression of the chloroplast triose-phosphate translocator on photosynthetic metabolism in transgenic potato plants
    • Heineke D, Kruse A, Flügge UI, Frommer WB, Riesmeier JW, et al. 1994. Effect of antisense repression of the chloroplast triose-phosphate translocator on photosynthetic metabolism in transgenic potato plants. Planta 193:174-80
    • (1994) Planta , vol.193 , pp. 174-180
    • Heineke, D.1    Kruse, A.2    Flügge, U.I.3    Frommer, W.B.4    Riesmeier, J.W.5
  • 41
    • 0035059568 scopus 로고    scopus 로고
    • A small decrease of plastid transketolase activity in antisense tobacco transformants has dramatic effects on photosynthesis and phenylpropanoid metabolism
    • Henkes S, Sonnewald U, Badur R, Flachmann R, Stitt M. 2001. A small decrease of plastid transketolase activity in antisense tobacco transformants has dramatic effects on photosynthesis and phenylpropanoid metabolism. Plant Cell 13:535-51
    • (2001) Plant Cell , vol.13 , pp. 535-551
    • Henkes, S.1    Sonnewald, U.2    Badur, R.3    Flachmann, R.4    Stitt, M.5
  • 42
    • 85047684869 scopus 로고    scopus 로고
    • When simpler is better. Unicellular green algae for discovering new genes and functions in carbohydrate metabolism
    • Hicks GR, Hironaka CM, Dauvillee D, Funke RP, D'Hulst C, et al. 2001. When simpler is better. Unicellular green algae for discovering new genes and functions in carbohydrate metabolism. Plant Physiol. 127:1334-38
    • (2001) Plant Physiol. , vol.127 , pp. 1334-1338
    • Hicks, G.R.1    Hironaka, C.M.2    Dauvillee, D.3    Funke, R.P.4    D'Hulst, C.5
  • 43
    • 0002420821 scopus 로고
    • The gluconeogenetic metabolism of pyruvate during deacification in plants with crassulacean acid metabolism
    • Holtum JAM, Osmond CB. 1981. The gluconeogenetic metabolism of pyruvate during deacification in plants with crassulacean acid metabolism. Aust. J. Plant Physiol. 8:31-44
    • (1981) Aust. J. Plant Physiol. , vol.8 , pp. 31-44
    • Holtum, J.A.M.1    Osmond, C.B.2
  • 44
    • 0041489951 scopus 로고    scopus 로고
    • Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli
    • Huang Y, Lemieux MJ, Song J, Auer M, Wang DN. 2003. Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli. Science 301:616-20
    • (2003) Science , vol.301 , pp. 616-620
    • Huang, Y.1    Lemieux, M.J.2    Song, J.3    Auer, M.4    Wang, D.N.5
  • 45
    • 0032568826 scopus 로고    scopus 로고
    • The hydrophilic domain of Tic110, an inner envelope membrane component of the chloroplastic protein translocation apparatus, faces the stromal compartment
    • Jackson DT, Froehlich JE, Keegstra K. 1998. The hydrophilic domain of Tic110, an inner envelope membrane component of the chloroplastic protein translocation apparatus, faces the stromal compartment. J. Biol. Chem. 273:16583-88
    • (1998) J. Biol. Chem. , vol.273 , pp. 16583-16588
    • Jackson, D.T.1    Froehlich, J.E.2    Keegstra, K.3
  • 46
    • 0035037171 scopus 로고    scopus 로고
    • Arabidopsis genes encoding components of the chloroplastic protein import apparatus
    • Jackson-Constan D, Keegstra K. 2001. Arabidopsis genes encoding components of the chloroplastic protein import apparatus. Plant Physiol. 125:1567-76
    • (2001) Plant Physiol. , vol.125 , pp. 1567-1576
    • Jackson-Constan, D.1    Keegstra, K.2
  • 47
    • 0035816712 scopus 로고    scopus 로고
    • Functional analysis of the protein-interacting domains of chloroplast SRP43
    • Jonas-Straube E, Hutin C, Hoffman NE, Schünemann D. 2001. Functional analysis of the protein-interacting domains of chloroplast SRP43. J. Biol. Chem. 276:24654-60
    • (2001) J. Biol. Chem. , vol.276 , pp. 24654-24660
    • Jonas-Straube, E.1    Hutin, C.2    Hoffman, N.E.3    Schünemann, D.4
  • 48
    • 0031834277 scopus 로고    scopus 로고
    • Molecular characterization of a carbon transporter in plastids from heterotrophic tissues: The glucose6-phosphate/phosphate antiporter
    • Kammerer B, Fischer K, Hilpert B, Schubert S, Gutensohn M, et al. 1998. Molecular characterization of a carbon transporter in plastids from heterotrophic tissues: the glucose6-phosphate/phosphate antiporter. Plant Cell 10:105-17
    • (1998) Plant Cell , vol.10 , pp. 105-117
    • Kammerer, B.1    Fischer, K.2    Hilpert, B.3    Schubert, S.4    Gutensohn, M.5
  • 49
    • 0028818858 scopus 로고
    • Molecular characterization of a putative Arabidopsis thaliana copper transporter and its yeast homologue
    • Kampfenkel K, Kushnir S, Babiychuk E, Inze D, Van Montagu M. 1995. Molecular characterization of a putative Arabidopsis thaliana copper transporter and its yeast homologue. J. Biol. Chem. 270:28479-86
    • (1995) J. Biol. Chem. , vol.270 , pp. 28479-28486
    • Kampfenkel, K.1    Kushnir, S.2    Babiychuk, E.3    Inze, D.4    Van Montagu, M.5
  • 50
    • 0028822675 scopus 로고
    • Molecular characterization of an Arabidopsis thaliana cDNA encoding a novel putative adenylate translocator of higher plants
    • Kampfenkel KH, Möhlmann T, Batz O, van Montague M, Inzé D, Neuhaus HE. 1995. Molecular characterization of an Arabidopsis thaliana cDNA encoding a novel putative adenylate translocator of higher plants. FEBS Lett. 374:351-55
    • (1995) FEBS Lett. , vol.374 , pp. 351-355
    • Kampfenkel, K.H.1    Möhlmann, T.2    Batz, O.3    Van Montague, M.4    Inzé, D.5    Neuhaus, H.E.6
  • 51
    • 1842432608 scopus 로고    scopus 로고
    • The Arabidopsis thaliana chloroplast proteome reveals pathway abundance and novel protein functions
    • Kleffmann T, Russenberger D, von Zychlinski A, Christopher W, Sjolander K, et al. 2004. The Arabidopsis thaliana chloroplast proteome reveals pathway abundance and novel protein functions. Curr. Biol. 14:354-62
    • (2004) Curr. Biol. , vol.14 , pp. 354-362
    • Kleffmann, T.1    Russenberger, D.2    Von Zychlinski, A.3    Christopher, W.4    Sjolander, K.5
  • 52
    • 0019875964 scopus 로고
    • Membrane protein oligomeric structure and transport function
    • Klingenberg M. 1981. Membrane protein oligomeric structure and transport function. Nature 290:449-54
    • (1981) Nature , vol.290 , pp. 449-454
    • Klingenberg, M.1
  • 53
    • 0347895062 scopus 로고    scopus 로고
    • Analysis of the plastidic phosphate translocator gene family in Arabidopsis and identification of new phosphate translocator-homologous transporters, classified by their putative substrate-binding site
    • Knappe S, Flügge UI, Fischer K. 2003. Analysis of the plastidic phosphate translocator gene family in Arabidopsis and identification of new phosphate translocator-homologous transporters, classified by their putative substrate-binding site. Plant Physiol. 131:1178-90
    • (2003) Plant Physiol. , vol.131 , pp. 1178-1190
    • Knappe, S.1    Flügge, U.I.2    Fischer, K.3
  • 54
    • 0345495698 scopus 로고    scopus 로고
    • Characterization of two functional phosphoenolpyruvate/phosphate translocator (PPT) genes in Arabidopsis-AtPPT1 may be involved in the provision of signals for correct mesophyll development
    • Knappe S, Löttgert T, Schneider A, Voll L, Flügge UI, Fischer K. 2003. Characterization of two functional phosphoenolpyruvate/phosphate translocator (PPT) genes in Arabidopsis-AtPPT1 may be involved in the provision of signals for correct mesophyll development. Plant J. 36:411-20
    • (2003) Plant J. , vol.36 , pp. 411-420
    • Knappe, S.1    Löttgert, T.2    Schneider, A.3    Voll, L.4    Flügge, U.I.5    Fischer, K.6
  • 55
    • 0036016255 scopus 로고    scopus 로고
    • Tissue-specific, light-regulated and plastid-regulated expression of the single-copy nuclear gene encoding the chloroplast Rieske FeS protein of Arabidopsis thaliana
    • Knight JS, Duckett CM, Sullivan JA, Walker AR, Gray JC. 2002. Tissue-specific, light-regulated and plastid-regulated expression of the single-copy nuclear gene encoding the chloroplast Rieske FeS protein of Arabidopsis thaliana. Plant Cell Physiol. 43:522-31
    • (2002) Plant Cell Physiol. , vol.43 , pp. 522-531
    • Knight, J.S.1    Duckett, C.M.2    Sullivan, J.A.3    Walker, A.R.4    Gray, J.C.5
  • 56
    • 0037795745 scopus 로고    scopus 로고
    • The oxidative pentose phosphate pathway: Structure and organisation
    • Kruger NJ, von Schaewen A. 2003. The oxidative pentose phosphate pathway: structure and organisation. Curr. Opin. Plant Biol. 6:236-46
    • (2003) Curr. Opin. Plant Biol. , vol.6 , pp. 236-246
    • Kruger, N.J.1    Von Schaewen, A.2
  • 57
    • 0033391482 scopus 로고    scopus 로고
    • T-DNA as an insertional mutagen in Arabidopsis
    • Krysan PJ, Young JC, Sussman MR. 1999. T-DNA as an insertional mutagen in Arabidopsis. Plant Cell 11:2283-90
    • (1999) Plant Cell , vol.11 , pp. 2283-2290
    • Krysan, P.J.1    Young, J.C.2    Sussman, M.R.3
  • 58
    • 0033377070 scopus 로고    scopus 로고
    • Plant mitochondrial carriers: An overview
    • Laloi M. 1999, Plant mitochondrial carriers: an overview. Cell Mol. Life Sci. 56:918-44
    • (1999) Cell Mol. Life Sci. , vol.56 , pp. 918-944
    • Laloi, M.1
  • 59
    • 0029188092 scopus 로고
    • Cue1: A mesophyll cell-specific positive regulator of light-controlled gene expression in Arabidopsis
    • Li H-m, Culligan K, Dixon RA, Chory J. 1995. Cue1: a mesophyll cell-specific positive regulator of light-controlled gene expression in Arabidopsis. Plant Cell 7:1599-610
    • (1995) Plant Cell , vol.7 , pp. 1599-1610
    • Li, H.-M.1    Culligan, K.2    Dixon, R.A.3    Chory, J.4
  • 60
    • 0037085468 scopus 로고    scopus 로고
    • Functional cloning and characterization of a plant efflux carrier for multidrug and heavy metal detoxification
    • Li L, He Z, Pandey GK, Tsuchiya T, Luan S. 2002. Functional cloning and characterization of a plant efflux carrier for multidrug and heavy metal detoxification. J. Biol. Chem. 277:5360-68
    • (2002) J. Biol. Chem. , vol.277 , pp. 5360-5368
    • Li, L.1    He, Z.2    Pandey, G.K.3    Tsuchiya, T.4    Luan, S.5
  • 62
    • 0027411773 scopus 로고
    • Expression of the functional mature chloroplast triose phosphate translocator in yeast internal membranes and purification of the histidine-tagged protein by a single metal-affinity chromatography step
    • Loddenkötter B, Kammerer B, Fischer K, Flügge UI. 1993. Expression of the functional mature chloroplast triose phosphate translocator in yeast internal membranes and purification of the histidine-tagged protein by a single metal-affinity chromatography step. Proc. Natl. Acad. Sci. USA 90:2155-59
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2155-2159
    • Loddenkötter, B.1    Kammerer, B.2    Fischer, K.3    Flügge, U.I.4
  • 63
    • 0742319992 scopus 로고    scopus 로고
    • The role of amylomaltase in maltose metabolism in the cytosol of photosynthetic cells
    • Lu Y, Sharkey TD. 2004. The role of amylomaltase in maltose metabolism in the cytosol of photosynthetic cells. Planta 218:466-73
    • (2004) Planta , vol.218 , pp. 466-473
    • Lu, Y.1    Sharkey, T.D.2
  • 64
    • 0029775088 scopus 로고    scopus 로고
    • Topology of IEP110, a component of the chloroplastic protein import machinery present in the inner envelope membrane
    • Lübeck J, Soll J, Akita M, Nielsen E, Keegstra K. 1996. Topology of IEP110, a component of the chloroplastic protein import machinery present in the inner envelope membrane. EMBO J. 15:4230-38
    • (1996) EMBO J. , vol.15 , pp. 4230-4238
    • Lübeck, J.1    Soll, J.2    Akita, M.3    Nielsen, E.4    Keegstra, K.5
  • 65
    • 4143128922 scopus 로고    scopus 로고
    • Identification of new intrinsic proteins in Arabidopsis plasma membrane proteome
    • Marmagne A, Rouet MA, Ferro M, Rolland N, Alcon C, et al. 2004. Identification of new intrinsic proteins in Arabidopsis plasma membrane proteome. Mol. Cell Proteomics 3:675-91
    • (2004) Mol. Cell Proteomics , vol.3 , pp. 675-691
    • Marmagne, A.1    Rouet, M.A.2    Ferro, M.3    Rolland, N.4    Alcon, C.5
  • 66
    • 0037853748 scopus 로고    scopus 로고
    • Phylogenetic relationships within cation transporter families of Arabidopsis
    • Maser P, Thomine S, Schroeder JI, Ward JM, Hirschi K, et al. 2001. Phylogenetic relationships within cation transporter families of Arabidopsis. Plant Physiol. 126:1646-67
    • (2001) Plant Physiol. , vol.126 , pp. 1646-1667
    • Maser, P.1    Thomine, S.2    Schroeder, J.I.3    Ward, J.M.4    Hirschi, K.5
  • 67
    • 11144354393 scopus 로고    scopus 로고
    • Genome sequence of the ultrasmall unicellular red alga Cyanidioschyzon merolae 10D
    • Matsuzaki M, Misumi O, Shin IT, Maruyama S, Takahara M, et al. 2004. Genome sequence of the ultrasmall unicellular red alga Cyanidioschyzon merolae 10D. Nature 428:653-57
    • (2004) Nature , vol.428 , pp. 653-657
    • Matsuzaki, M.1    Misumi, O.2    Shin, I.T.3    Maruyama, S.4    Takahara, M.5
  • 68
    • 3142603413 scopus 로고    scopus 로고
    • Improvement of culture conditions and evidence for nuclear transformation by homologous recombination in a red alga, Cyanidioschyzon merolae 10D
    • Minoda A, Sakagami R, Yagisawa F, Kuroiwa T, Tanaka K. 2004. Improvement of culture conditions and evidence for nuclear transformation by homologous recombination in a red alga, Cyanidioschyzon merolae 10D. Plant Cell Physiol. 45:667-71
    • (2004) Plant Cell Physiol. , vol.45 , pp. 667-671
    • Minoda, A.1    Sakagami, R.2    Yagisawa, F.3    Kuroiwa, T.4    Tanaka, K.5
  • 69
    • 0037033102 scopus 로고    scopus 로고
    • Non-canonical transit peptide for import into the chloroplast
    • Miras S, Salvi D, Ferro M, Grunwald D, Garin J, et al. 2002. Non-canonical transit peptide for import into the chloroplast. J. Biol. Chem. 277:47770-78
    • (2002) J. Biol. Chem. , vol.277 , pp. 47770-47778
    • Miras, S.1    Salvi, D.2    Ferro, M.3    Grunwald, D.4    Garin, J.5
  • 70
    • 2942681146 scopus 로고    scopus 로고
    • 2-responsive genes regulated by CCM1 controlling a carbon-concentrating mechanism in Chlamydomonas reinhardtii
    • 2-responsive genes regulated by CCM1 controlling a carbon-concentrating mechanism in Chlamydomonas reinhardtii. Plant Physiol. 135:1595-607
    • (2004) Plant Physiol. , vol.135 , pp. 1595-1607
    • Miura, K.1    Yamano, T.2    Yoshioka, S.3    Kohinata, T.4    Inoue, Y.5
  • 71
    • 0032521666 scopus 로고    scopus 로고
    • Occurrence of two plastidic ATP/ADP transporters in Arabidopsis thaliana L.-molecular characterisation and comparative structural analysis of similar ATP/ADP translocators from plastids and Rickettsia prowazekii
    • Möhlmann T, Tjaden J, Schwoppe C, Winkler HH, Kampfenkel K, Neuhaus HE. 1998. Occurrence of two plastidic ATP/ADP transporters in Arabidopsis thaliana L.-molecular characterisation and comparative structural analysis of similar ATP/ADP translocators from plastids and Rickettsia prowazekii. Eur. J. Biochem. 252:353-59
    • (1998) Eur. J. Biochem. , vol.252 , pp. 353-359
    • Möhlmann, T.1    Tjaden, J.2    Schwoppe, C.3    Winkler, H.H.4    Kampfenkel, K.5    Neuhaus, H.E.6
  • 72
    • 0035190234 scopus 로고    scopus 로고
    • A plastidic ABC protein involved in intercompartmental communication of light signaling
    • Møller SG, Kunkel T, Chua NH. 2001. A plastidic ABC protein involved in intercompartmental communication of light signaling. Genes Dev. 15:90-103
    • (2001) Genes Dev. , vol.15 , pp. 90-103
    • Møller, S.G.1    Kunkel, T.2    Chua, N.H.3
  • 73
    • 0035964205 scopus 로고    scopus 로고
    • An essential role of a TatC homologue of a Delta pH-dependent protein transporter in thylakoid membrane formation during chloroplast development in Arabidopsis thaliana
    • Motohashi R, Nagata N, Ito T, Takahashi S, Hobo T, et al. 2001. An essential role of a TatC homologue of a Delta pH-dependent protein transporter in thylakoid membrane formation during chloroplast development in Arabidopsis thaliana. Proc. Natl. Acad. Sci. USA 98:10499-504
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 10499-10504
    • Motohashi, R.1    Nagata, N.2    Ito, T.3    Takahashi, S.4    Hobo, T.5
  • 74
    • 0037057652 scopus 로고    scopus 로고
    • Crystal structure of bacterial multidrug efflux transporter AcrB
    • Murakami S, Nakashima R, Yamashita E, Yamaguchi A. 2002. Crystal structure of bacterial multidrug efflux transporter AcrB. Nature 419:587-93
    • (2002) Nature , vol.419 , pp. 587-593
    • Murakami, S.1    Nakashima, R.2    Yamashita, E.3    Yamaguchi, A.4
  • 75
    • 4444230596 scopus 로고    scopus 로고
    • Inner envelope protein 32 is imported into chloroplasts by a novel pathway
    • Nada A, Soll J. 2004. Inner envelope protein 32 is imported into chloroplasts by a novel pathway. J. Cell Sci. 117:3975-82
    • (2004) J. Cell Sci. , vol.117 , pp. 3975-3982
    • Nada, A.1    Soll, J.2
  • 76
    • 0031036197 scopus 로고    scopus 로고
    • Characterization of a novel eukaryotic ATP/ADP translocator located in the plastid envelope of Arabidopsis thaliana L.
    • Neuhaus HE, Thom E, Möhlmann T, Steup M, Kampfenkel K. 1997. Characterization of a novel eukaryotic ATP/ADP translocator located in the plastid envelope of Arabidopsis thaliana L. Plant J. 11:73-82
    • (1997) Plant J. , vol.11 , pp. 73-82
    • Neuhaus, H.E.1    Thom, E.2    Möhlmann, T.3    Steup, M.4    Kampfenkel, K.5
  • 77
    • 0034193582 scopus 로고    scopus 로고
    • Solute pores, ion channels, and metabolite transporters in the outer and inner envelope membranes of higher plant plastids
    • Neuhaus HE, Wagner R. 2000. Solute pores, ion channels, and metabolite transporters in the outer and inner envelope membranes of higher plant plastids. Biochim. Biophys. Acta 1465:307-23
    • (2000) Biochim. Biophys. Acta , vol.1465 , pp. 307-323
    • Neuhaus, H.E.1    Wagner, R.2
  • 78
    • 0346096943 scopus 로고    scopus 로고
    • A previously unknown maltose transporter essential for starch degradation in leaves
    • Niittyla T, Messerli G, Trevisan M, Chen J, Smith AM, Zeeman SC. 2004. A previously unknown maltose transporter essential for starch degradation in leaves. Science 303:87-89
    • (2004) Science , vol.303 , pp. 87-89
    • Niittyla, T.1    Messerli, G.2    Trevisan, M.3    Chen, J.4    Smith, A.M.5    Zeeman, S.C.6
  • 81
    • 0037225279 scopus 로고    scopus 로고
    • Characterization of the ABCA transporter subfamily: Identification of prokaryotic and eukaryotic members, phylogeny and topology
    • Peelman F, Labeur C, Vanloo B, Roosbeek S, Devaud C, et al. 2003. Characterization of the ABCA transporter subfamily: identification of prokaryotic and eukaryotic members, phylogeny and topology. J. Mol. Biol. 325:259-74
    • (2003) J. Mol. Biol. , vol.325 , pp. 259-274
    • Peelman, F.1    Labeur, C.2    Vanloo, B.3    Roosbeek, S.4    Devaud, C.5
  • 82
    • 0034026047 scopus 로고    scopus 로고
    • Proteomics of the chloroplast: Systematic identification and targeting analysis of lumenal and peripheral thylakoid proteins
    • Peltier JB, Friso G, Kalume DE, Roepstorff P, Nilsson F, et al. 2000. Proteomics of the chloroplast: systematic identification and targeting analysis of lumenal and peripheral thylakoid proteins. Plant Cell 12:319-41
    • (2000) Plant Cell , vol.12 , pp. 319-341
    • Peltier, J.B.1    Friso, G.2    Kalume, D.E.3    Roepstorff, P.4    Nilsson, F.5
  • 83
    • 1042289735 scopus 로고    scopus 로고
    • Clp protease complexes from photosynthetic and non-photosynthetic plastids and mitochondria of plants, their predicted three-dimensional structures, and functional implications
    • Peltier JB, Ripoll DR, Friso G, Rudella A, Cai Y, et al. 2004. Clp protease complexes from photosynthetic and non-photosynthetic plastids and mitochondria of plants, their predicted three-dimensional structures, and functional implications. J. Biol. Chem. 279:4768-81
    • (2004) J. Biol. Chem. , vol.279 , pp. 4768-4781
    • Peltier, J.B.1    Ripoll, D.R.2    Friso, G.3    Rudella, A.4    Cai, Y.5
  • 85
    • 0032125382 scopus 로고    scopus 로고
    • A high-conductance solute channel in the chloroplastic outer envelope from Pea
    • Pohlmeyer K, Soll J, Grimm R, Hill K, Wagner R. 1998. A high-conductance solute channel in the chloroplastic outer envelope from Pea. Plant Cell 10:1207-16
    • (1998) Plant Cell , vol.10 , pp. 1207-1216
    • Pohlmeyer, K.1    Soll, J.2    Grimm, R.3    Hill, K.4    Wagner, R.5
  • 86
    • 0030787877 scopus 로고    scopus 로고
    • Isolation and characterization of an amino acid-selective channel protein present in the chloroplastic outer envelope membrane
    • Pohlmeyer K, Soll J, Steinkamp T, Hinnah S, Wagner R. 1997. Isolation and characterization of an amino acid-selective channel protein present in the chloroplastic outer envelope membrane. Proc. Natl. Acad. Sci. USA 94:9504-9
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9504-9509
    • Pohlmeyer, K.1    Soll, J.2    Steinkamp, T.3    Hinnah, S.4    Wagner, R.5
  • 87
    • 0033548261 scopus 로고    scopus 로고
    • The preprotein translocase of the mitochondrial inner membrane: Function and evolution
    • Rassow J, Dekker PJ, van Wilpe S, Meijer M, Soll J. 1999. The preprotein translocase of the mitochondrial inner membrane: function and evolution. J. Mol. Biol. 286:105-20
    • (1999) J. Mol. Biol. , vol.286 , pp. 105-120
    • Rassow, J.1    Dekker, P.J.2    Van Wilpe, S.3    Meijer, M.4    Soll, J.5
  • 88
    • 1242319241 scopus 로고    scopus 로고
    • Identification of plastid envelope proteins required for import of protochlorophyllide oxidoreductase A into the chloroplast of barley
    • Reinbothe S, Quigley F, Gray J, Schemenewitz A, Reinbothe C. 2004. Identification of plastid envelope proteins required for import of protochlorophyllide oxidoreductase A into the chloroplast of barley. Proc. Natl. Acad. Sci. USA 101:2197-202
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2197-2202
    • Reinbothe, S.1    Quigley, F.2    Gray, J.3    Schemenewitz, A.4    Reinbothe, C.5
  • 89
    • 1242341913 scopus 로고    scopus 로고
    • The outer plastid envelope protein OEP16: Role as precursor translocase in import of protochlorophyllide oxidoreductase A
    • Reinbothe S, Quigley F, Springer A, Schemenewitz A, Reinbothe C. 2004. The outer plastid envelope protein OEP16: role as precursor translocase in import of protochlorophyllide oxidoreductase A. Proc. Natl. Acad. Sci. USA 101:2203-8
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2203-2208
    • Reinbothe, S.1    Quigley, F.2    Springer, A.3    Schemenewitz, A.4    Reinbothe, C.5
  • 90
    • 0043067995 scopus 로고    scopus 로고
    • The Arabidopsis mutant dct is deficient in the plastidic glutamate/malate translocator DiT2
    • Renné P, Dreßen U, Hebbeker U, Hille D, Flügge UI, et al. 2003. The Arabidopsis mutant dct is deficient in the plastidic glutamate/malate translocator DiT2. Plant J. 35:316-31
    • (2003) Plant J. , vol.35 , pp. 316-331
    • Renné, P.1    Dreßen, U.2    Hebbeker, U.3    Hille, D.4    Flügge, U.I.5
  • 92
    • 0033829519 scopus 로고    scopus 로고
    • The Chlamydomonas reinhardtii nar1 gene encodes a chloroplast membrane protein involved in nitrite transport
    • Rexach J, Fernández E, Galván A. 2000. The Chlamydomonas reinhardtii nar1 gene encodes a chloroplast membrane protein involved in nitrite transport. Plant Cell 12:1441-53
    • (2000) Plant Cell , vol.12 , pp. 1441-1453
    • Rexach, J.1    Fernández, E.2    Galván, A.3
  • 93
    • 0142152446 scopus 로고    scopus 로고
    • The sulfolipids 2′-O-acylsulfoquinovosyldiacylglycerol and sulfoquinovosyldiacylglycerol are absent from a Chlamydomonas reinhardtii mutant deleted in SQD1
    • Riekhof WR, Ruckle ME, Lydic TA, Sears BB, Benning C. 2003. The sulfolipids 2′-O-acylsulfoquinovosyldiacylglycerol and sulfoquinovosyldiacylglycerol are absent from a Chlamydomonas reinhardtii mutant deleted in SQD1. Plant Physiol. 133:864-74
    • (2003) Plant Physiol. , vol.133 , pp. 864-874
    • Riekhof, W.R.1    Ruckle, M.E.2    Lydic, T.A.3    Sears, B.B.4    Benning, C.5
  • 94
    • 0027302147 scopus 로고
    • Antisense repression of the chloroplast triose phosphate translocator affects carbon partitioning in transgenic potato plants
    • Riesmeier JW, Flügge UI, Schulz B, Heineke D, Heldt HW, et al. 1993. Antisense repression of the chloroplast triose phosphate translocator affects carbon partitioning in transgenic potato plants. Proc. Natl. Acad. Sci. USA 90:6160-64
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6160-6164
    • Riesmeier, J.W.1    Flügge, U.I.2    Schulz, B.3    Heineke, D.4    Heldt, H.W.5
  • 95
    • 0027092284 scopus 로고
    • Isolation and characterization of a sucrose carrier cDNA from spinach by functional expression in yeast
    • Riesmeier JW, Willmitzer L, Frommer WB. 1992. Isolation and characterization of a sucrose carrier cDNA from spinach by functional expression in yeast. EMBO J. 11:4705-13
    • (1992) EMBO J. , vol.11 , pp. 4705-4713
    • Riesmeier, J.W.1    Willmitzer, L.2    Frommer, W.B.3
  • 97
    • 0032705240 scopus 로고    scopus 로고
    • The outer envelope protein OEP24 from pea chloroplasts can functionally replace the mitochondrial VDAC in yeast
    • Rohl T, Motzkus M, Soll J. 1999. The outer envelope protein OEP24 from pea chloroplasts can functionally replace the mitochondrial VDAC in yeast. FEBS Lett. 460:491-94
    • (1999) FEBS Lett. , vol.460 , pp. 491-494
    • Rohl, T.1    Motzkus, M.2    Soll, J.3
  • 99
    • 0030733162 scopus 로고    scopus 로고
    • Disruption of the plastid ycf10 open reading frame affects uptake of inorganic carbon in the chloroplast of Chlamydomonas
    • 97a. Rolland N, Dorne AJ, Amoroso G, Sültemeyer DF, Joyard J, Rochaix JD. 1997. Disruption of the plastid ycf10 open reading frame affects uptake of inorganic carbon in the chloroplast of Chlamydomonas. EMBO J. 16:6713-26
    • (1997) EMBO J. , vol.16 , pp. 6713-6726
    • Rolland, N.1    Dorne, A.J.2    Amoroso, G.3    Sültemeyer, D.F.4    Joyard, J.5    Rochaix, J.D.6
  • 100
    • 0742267789 scopus 로고    scopus 로고
    • Characterization of a protein of the plastid inner envelope having homology to animal inorganic phosphate, chloride and organic-anion transporters
    • Roth C, Menzel G, Petetot JM, Rochat-Hacker S, Poirier Y. 2004. Characterization of a protein of the plastid inner envelope having homology to animal inorganic phosphate, chloride and organic-anion transporters. Planta 218:406-16
    • (2004) Planta , vol.218 , pp. 406-416
    • Roth, C.1    Menzel, G.2    Petetot, J.M.3    Rochat-Hacker, S.4    Poirier, Y.5
  • 101
  • 103
    • 0035839555 scopus 로고    scopus 로고
    • The Arabidopsis thaliana ABC protein superfamily, a complete inventory
    • Sanchez-Fernandez R, Davies TG, Coleman JO, Rea PA. 2001. The Arabidopsis thaliana ABC protein superfamily, a complete inventory. J. Biol. Chem. 276:30231-44
    • (2001) J. Biol. Chem. , vol.276 , pp. 30231-30244
    • Sanchez-Fernandez, R.1    Davies, T.G.2    Coleman, J.O.3    Rea, P.A.4
  • 105
    • 0034066471 scopus 로고    scopus 로고
    • Membrane proteins and proteomics: Un amour impossible?
    • Santoni V, Molloy M, Rabilloud T. 2000. Membrane proteins and proteomics: un amour impossible? Electrophoresis 21:1054-70
    • (2000) Electrophoresis , vol.21 , pp. 1054-1070
    • Santoni, V.1    Molloy, M.2    Rabilloud, T.3
  • 106
    • 5144233908 scopus 로고    scopus 로고
    • AtSUC8 and AtSUC9 encode functional sucrose transporters, but the closely related AtSUC6 and AtSUC7 genes encode aberrant proteins in different Arabidopsis ecotypes
    • Sauer N, Ludwig A, Knoblauch A, Rothe P, Gahrtz M, Klebl F. 2004. AtSUC8 and AtSUC9 encode functional sucrose transporters, but the closely related AtSUC6 and AtSUC7 genes encode aberrant proteins in different Arabidopsis ecotypes. Plant J. 40:120-30
    • (2004) Plant J. , vol.40 , pp. 120-130
    • Sauer, N.1    Ludwig, A.2    Knoblauch, A.3    Rothe, P.4    Gahrtz, M.5    Klebl, F.6
  • 107
    • 17344395359 scopus 로고    scopus 로고
    • Chloroplast transit peptide prediction: A peek inside the black box
    • Schein AI, Kissinger JC, Ungar LH. 2001. Chloroplast transit peptide prediction: a peek inside the black box. Nucleic Acids Res. 29:E82
    • (2001) Nucleic Acids Res. , vol.29
    • Schein, A.I.1    Kissinger, J.C.2    Ungar, L.H.3
  • 109
    • 0347264778 scopus 로고    scopus 로고
    • An Arabidopsis thaliana knock-out mutant of the chloroplast triose phosphate/phosphate translocator is severely compromised only when starch synthesis, but not starch mobilisation is abolished
    • Schneider A, Häusler RE, Kolukisaoglu U, Kunze R, van der Graaff E, et al. 2002. An Arabidopsis thaliana knock-out mutant of the chloroplast triose phosphate/phosphate translocator is severely compromised only when starch synthesis, but not starch mobilisation is abolished. Plant J. 32:685-99
    • (2002) Plant J. , vol.32 , pp. 685-699
    • Schneider, A.1    Häusler, R.E.2    Kolukisaoglu, U.3    Kunze, R.4    Van Der Graaff, E.5
  • 110
    • 0025013880 scopus 로고
    • The chloroplast import receptor is an integral membrane protein of the chloroplast envelope contact sites
    • Schnell DJ, Blobel G, Pain D. 1990. The chloroplast import receptor is an integral membrane protein of the chloroplast envelope contact sites. J. Cell Biol. 111:1825-38
    • (1990) J. Cell Biol. , vol.111 , pp. 1825-1838
    • Schnell, D.J.1    Blobel, G.2    Pain, D.3
  • 111
    • 0011340184 scopus 로고
    • Pyruvate-derived amino acids in spinach chloroplasts: Synthesis and regulation during photosynthetic carbon metabolism
    • Schulze-Siebert D, Heineke D, Scharf H, Schulz G. 1984. Pyruvate-derived amino acids in spinach chloroplasts: synthesis and regulation during photosynthetic carbon metabolism. Plant Physiol. 76:465-71
    • (1984) Plant Physiol. , vol.76 , pp. 465-471
    • Schulze-Siebert, D.1    Heineke, D.2    Scharf, H.3    Schulz, G.4
  • 113
    • 0026579591 scopus 로고
    • Cloning and expression in yeast of plant potassium ion transport system
    • Sentenac H, Bonneaud N, Minet M, Lacroute F, Salmon J-M, et al. 1992. Cloning and expression in yeast of plant potassium ion transport system. Science 256:663-65
    • (1992) Science , vol.256 , pp. 663-665
    • Sentenac, H.1    Bonneaud, N.2    Minet, M.3    Lacroute, F.4    Salmon, J.-M.5
  • 115
    • 0031893765 scopus 로고    scopus 로고
    • High-efficiency transformation of Chlamydomonas reinhardtii by electroporation
    • Shimogawara K, Fujiwara S, Grossman A, Usuda H. 1998. High-efficiency transformation of Chlamydomonas reinhardtii by electroporation. Genetics 148:1821-28
    • (1998) Genetics , vol.148 , pp. 1821-1828
    • Shimogawara, K.1    Fujiwara, S.2    Grossman, A.3    Usuda, H.4
  • 116
    • 12244286739 scopus 로고    scopus 로고
    • Chlamydomonas reinhardtii genome project. A guide to the generation and use of the cDNA information
    • Shrager J, Hauser C, Chang CW, Harris EH, Davies J, et al. 2003. Chlamydomonas reinhardtii genome project. A guide to the generation and use of the cDNA information. Plant Physiol. 131:401-8
    • (2003) Plant Physiol. , vol.131 , pp. 401-408
    • Shrager, J.1    Hauser, C.2    Chang, C.W.3    Harris, E.H.4    Davies, J.5
  • 117
    • 0034193760 scopus 로고    scopus 로고
    • Molecular mechanisms of phosphate and sulphate transport in plants
    • Smith FW, Rae AL, Hawkesford MJ. 2000. Molecular mechanisms of phosphate and sulphate transport in plants. Biochim. Biophys. Acta 1465:236-45
    • (2000) Biochim. Biophys. Acta , vol.1465 , pp. 236-245
    • Smith, F.W.1    Rae, A.L.2    Hawkesford, M.J.3
  • 119
    • 0000348258 scopus 로고
    • An Arabidopsis thaliana mutant defective in chloroplast dicarboxylate transport
    • Somerville SC, Ogren WL. 1983. An Arabidopsis thaliana mutant defective in chloroplast dicarboxylate transport. Proc. Natl. Acad. Sci. USA 80:1290-94
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 1290-1294
    • Somerville, S.C.1    Ogren, W.L.2
  • 120
    • 0003269891 scopus 로고
    • A mutant of Arabidopsis deficient in chloroplast dicarboxylate transport is missing an envelope protein
    • Somerville SC, Somerville CR. 1985. A mutant of Arabidopsis deficient in chloroplast dicarboxylate transport is missing an envelope protein. Plant Sci. 37:217-20
    • (1985) Plant Sci. , vol.37 , pp. 217-220
    • Somerville, S.C.1    Somerville, C.R.2
  • 121
    • 3042711950 scopus 로고    scopus 로고
    • A probable Na+(K+)/H+ exchanger on the chloroplast envelope functions in pH homeostasis and chloroplast development in Arabidopsis thaliana
    • Song CP, Guo Y, Qiu Q, Lambert G, Galbraith DW, et al. 2004. A probable Na+(K+)/H+ exchanger on the chloroplast envelope functions in pH homeostasis and chloroplast development in Arabidopsis thaliana. Proc. Natl. Acad. Sci. USA 101:10211-16
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 10211-10216
    • Song, C.P.1    Guo, Y.2    Qiu, Q.3    Lambert, G.4    Galbraith, D.W.5
  • 122
    • 0034697040 scopus 로고    scopus 로고
    • Identification of the poreforming region of the outer chloroplast envelope protein OEP16
    • Steinkamp T, Hill K, Hinnah SC, Wagner R, Rohl T, et al. 2000. Identification of the poreforming region of the outer chloroplast envelope protein OEP16. J. Biol. Chem. 275:11758-64
    • (2000) J. Biol. Chem. , vol.275 , pp. 11758-11764
    • Steinkamp, T.1    Hill, K.2    Hinnah, S.C.3    Wagner, R.4    Rohl, T.5
  • 123
    • 0000713345 scopus 로고
    • Capacities of pea chloroplasts to catalyse the oxidative pentose phosphate and glycolysis
    • Stitt M, ap Rees T. 1979. Capacities of pea chloroplasts to catalyse the oxidative pentose phosphate and glycolysis. Phytochemistry 18:1905-11
    • (1979) Phytochemistry , vol.18 , pp. 1905-1911
    • Stitt, M.1    Ap Rees, T.2
  • 124
    • 0033197510 scopus 로고    scopus 로고
    • The phosphoenolpyruvate/phosphate translocator is required for phenolic metabolism, palisade cell development, and plastid- dependent nuclear gene expression
    • Streatfield SJ, Weber A, Kinsman EA, Häusler RE, Li JM, et al. 1999. The phosphoenolpyruvate/phosphate translocator is required for phenolic metabolism, palisade cell development, and plastid- dependent nuclear gene expression. Plant Cell 11:1609-21
    • (1999) Plant Cell , vol.11 , pp. 1609-1621
    • Streatfield, S.J.1    Weber, A.2    Kinsman, E.A.3    Häusler, R.E.4    Li, J.M.5
  • 125
    • 0028980954 scopus 로고
    • The maize brittle1 gene encodes amyloplast membrane polypeptides
    • Sullivan TD, Kaneko Y. 1995. The maize brittle1 gene encodes amyloplast membrane polypeptides. Planta 196:477-84
    • (1995) Planta , vol.196 , pp. 477-484
    • Sullivan, T.D.1    Kaneko, Y.2
  • 126
    • 0031131609 scopus 로고    scopus 로고
    • ALBINO3, an Arabidopsis nuclear gene essential for chloroplast differentiation, encodes a chloroplast protein that shows homology to proteins present in bacterial membranes and yeast mitochondria
    • Sundberg E, Slagter JG, Fridborg I, Cleary SP, Robinson C, Coupland G. 1997. ALBINO3, an Arabidopsis nuclear gene essential for chloroplast differentiation, encodes a chloroplast protein that shows homology to proteins present in bacterial membranes and yeast mitochondria. Plant Cell 9:717-30
    • (1997) Plant Cell , vol.9 , pp. 717-730
    • Sundberg, E.1    Slagter, J.G.2    Fridborg, I.3    Cleary, S.P.4    Robinson, C.5    Coupland, G.6
  • 127
    • 0034649566 scopus 로고    scopus 로고
    • Analysis of the genome sequence of the flowering plant Arabidopsis thaliana
    • TAGI. 2000. Analysis of the genome sequence of the flowering plant Arabidopsis thaliana. Nature 408:796-815
    • (2000) Nature , vol.408 , pp. 796-815
  • 128
    • 0032693542 scopus 로고    scopus 로고
    • Cloning of an Arabidopsis cDNA encoding a chloroplast localizing sulphate transporter isoform
    • Takahashi H, Asanuma W, Saito K. 1999. Cloning of an Arabidopsis cDNA encoding a chloroplast localizing sulphate transporter isoform. J. Exp. Bot. 50:1713-14
    • (1999) J. Exp. Bot. , vol.50 , pp. 1713-1714
    • Takahashi, H.1    Asanuma, W.2    Saito, K.3
  • 129
    • 0031768569 scopus 로고    scopus 로고
    • The AmMYB308 and AmMYB330 transcription factors from antirrhinum regulate phenylpropanoid and lignin biosynthesis in transgenic tobacco
    • Tamagnone L, Merida A, Parr A, Mackay S, Culianez-Macia FA, et al. 1998. The AmMYB308 and AmMYB330 transcription factors from antirrhinum regulate phenylpropanoid and lignin biosynthesis in transgenic tobacco. Plant Cell 10:135-54
    • (1998) Plant Cell , vol.10 , pp. 135-154
    • Tamagnone, L.1    Merida, A.2    Parr, A.3    Mackay, S.4    Culianez-Macia, F.A.5
  • 130
    • 0032301062 scopus 로고    scopus 로고
    • Inhibition of phenolic acid metabolism results in precocious cell death and altered cell morphology in leaves of transgenic tobacco plants
    • Tamagnone L, Merida A, Stacey N, Plaskitt K, Parr A, et al. 1998. Inhibition of phenolic acid metabolism results in precocious cell death and altered cell morphology in leaves of transgenic tobacco plants. Plant Cell 10:1801-16
    • (1998) Plant Cell , vol.10 , pp. 1801-1816
    • Tamagnone, L.1    Merida, A.2    Stacey, N.3    Plaskitt, K.4    Parr, A.5
  • 131
    • 0036345904 scopus 로고    scopus 로고
    • Identifying and characterizing plastidic 2-oxoglutarate/malate and dicarboxylate transporters in Arabidopsis thaliana
    • Taniguchi M, Taniguchi Y, Kawasaki M, Takeda S, Kato T, et al. 2002. Identifying and characterizing plastidic 2-oxoglutarate/malate and dicarboxylate transporters in Arabidopsis thaliana. Plant Cell Physiol. 43:706-17
    • (2002) Plant Cell Physiol. , vol.43 , pp. 706-717
    • Taniguchi, M.1    Taniguchi, Y.2    Kawasaki, M.3    Takeda, S.4    Kato, T.5
  • 133
    • 0035979797 scopus 로고    scopus 로고
    • Overexpression of mammalian integral membrane proteins for structural studies
    • Tate CG. 2001. Overexpression of mammalian integral membrane proteins for structural studies. FEBS Lett. 504:94-98
    • (2001) FEBS Lett. , vol.504 , pp. 94-98
    • Tate, C.G.1
  • 134
    • 0001596403 scopus 로고
    • Activity and accumulation of cell division-promoting phenolics in tobacco tissue-cultures
    • Teutonico RA, Dudley MW, Orr JD, Lynn DG, Binns AN. 1991. Activity and accumulation of cell division-promoting phenolics in tobacco tissue-cultures. Plant Physiol. 97:288-97
    • (1991) Plant Physiol. , vol.97 , pp. 288-297
    • Teutonico, R.A.1    Dudley, M.W.2    Orr, J.D.3    Lynn, D.G.4    Binns, A.N.5
  • 135
    • 0033520470 scopus 로고    scopus 로고
    • The envelope anion channel involved in chloroplast protein import is associated with Tic110
    • van den Wijngaard PW, Vredenberg WJ. 1999. The envelope anion channel involved in chloroplast protein import is associated with Tic110. J. Biol. Chem. 274:25201-4
    • (1999) J. Biol. Chem. , vol.274 , pp. 25201-25204
    • Van Den Wijngaard, P.W.1    Vredenberg, W.J.2
  • 136
    • 0034789243 scopus 로고    scopus 로고
    • Post-transcriptional gene silencing in plants
    • Vaucheret H, Beclin C, Fagard M. 2001. Post-transcriptional gene silencing in plants. J. Cell Sci. 114:3083-91
    • (2001) J. Cell Sci. , vol.114 , pp. 3083-3091
    • Vaucheret, H.1    Beclin, C.2    Fagard, M.3
  • 137
    • 0036670270 scopus 로고    scopus 로고
    • A chloroplast phosphate transporter, PHT2;1, influences allocation of phosphate within the plant and phosphate-starvation responses
    • Versaw WK, Harrison MJ. 2002. A chloroplast phosphate transporter, PHT2;1, influences allocation of phosphate within the plant and phosphate-starvation responses. Plant Cell 14:1751-66
    • (2002) Plant Cell , vol.14 , pp. 1751-1766
    • Versaw, W.K.1    Harrison, M.J.2
  • 138
    • 0344633613 scopus 로고    scopus 로고
    • The phenotype of the Arabidopsis cue1 mutant is not simply caused by a general restriction of the shikimate pathway
    • Voll L, Häusler RE, Hecker R, Weber A, Weissenbock G, et al. 2003. The phenotype of the Arabidopsis cue1 mutant is not simply caused by a general restriction of the shikimate pathway. Plant J. 36:301-17
    • (2003) Plant J. , vol.36 , pp. 301-317
    • Voll, L.1    Häusler, R.E.2    Hecker, R.3    Weber, A.4    Weissenbock, G.5
  • 139
    • 0000651660 scopus 로고
    • The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology
    • von Heijne G. 1986. The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology. EMBO J. 5:3021-27
    • (1986) EMBO J. , vol.5 , pp. 3021-3027
    • Von Heijne, G.1
  • 140
    • 0023676242 scopus 로고
    • Topogenic signals in integral membrane proteins
    • von Heijne G, Gavel Y. 1988. Topogenic signals in integral membrane proteins. Eur. J. Biochem. 174:671-78
    • (1988) Eur. J. Biochem. , vol.174 , pp. 671-678
    • Von Heijne, G.1    Gavel, Y.2
  • 141
    • 0038157455 scopus 로고
    • Insights into the structure of the chloroplast phosphate translocator protein
    • ed. DT Clakson, DT Cooke, NewYork: Plenum
    • Wallmeier H, Weber A, Gross A, Flügge UI. 1992. Insights into the structure of the chloroplast phosphate translocator protein. In Transport and Receptor Proteins of Plant Membranes, ed. DT Clakson, DT Cooke, pp. 77-89. NewYork: Plenum
    • (1992) Transport and Receptor Proteins of Plant Membranes , pp. 77-89
    • Wallmeier, H.1    Weber, A.2    Gross, A.3    Flügge, U.I.4
  • 142
    • 0036010131 scopus 로고    scopus 로고
    • Interaction of cytosolic and plastidic nitrogen metabolism in plants
    • Weber A, Flügge UI. 2002. Interaction of cytosolic and plastidic nitrogen metabolism in plants. J. Exp. Bot. 53:865-74
    • (2002) J. Exp. Bot. , vol.53 , pp. 865-874
    • Weber, A.1    Flügge, U.I.2
  • 143
    • 0028917799 scopus 로고
    • The 2-oxoglutarate/malate translocator of chloroplast envelope membranes: Molecular cloning of a transporter containing a 12-helix motif and expression of the functional protein in yeast cells
    • Weber A, Menzlaff E, Arbinger B, Gutensohn M, Eckerskorn C, Flügge UI. 1995. The 2-oxoglutarate/malate translocator of chloroplast envelope membranes: molecular cloning of a transporter containing a 12-helix motif and expression of the functional protein in yeast cells. Biochemistry 34:2621-27
    • (1995) Biochemistry , vol.34 , pp. 2621-2627
    • Weber, A.1    Menzlaff, E.2    Arbinger, B.3    Gutensohn, M.4    Eckerskorn, C.5    Flügge, U.I.6
  • 144
    • 0034094933 scopus 로고    scopus 로고
    • Identification, purification, and molecular cloning of a putative plastidic glucose translocator
    • Weber A, Servaites JC, Geiger DR, Kofler H, Hille D, et al. 2000. Identification, purification, and molecular cloning of a putative plastidic glucose translocator. Plant Cell 12:787-801
    • (2000) Plant Cell , vol.12 , pp. 787-801
    • Weber, A.1    Servaites, J.C.2    Geiger, D.R.3    Kofler, H.4    Hille, D.5
  • 145
    • 2442480656 scopus 로고    scopus 로고
    • Solute transporters as connecting elements between cytosol and plastid stroma
    • Weber APM. 2004. Solute transporters as connecting elements between cytosol and plastid stroma. Curr. Opin. Plant Biol. 7:247-53
    • (2004) Curr. Opin. Plant Biol. , vol.7 , pp. 247-253
    • Weber, A.P.M.1
  • 146
    • 33845330845 scopus 로고    scopus 로고
    • Synthesis, export, and partitioning of the end products of photosynthesis
    • ed. RR Wise, JK Hoober. Dordrecht, Netherlands: Kluwer Academics
    • Weber APM. 2005. Synthesis, export, and partitioning of the end products of photosynthesis. In The Structure and Function of Plastids, ed. RR Wise, JK Hoober. Dordrecht, Netherlands: Kluwer Academics
    • (2005) The Structure and Function of Plastids
    • Weber, A.P.M.1
  • 147
    • 19944432176 scopus 로고    scopus 로고
    • EST-analysis of the thermo-acidophilic red microalga Galdieria sulphuraria reveals potential for lipid A biosynthesis and unveils the pathway of carbon export from rhodoplasts
    • Weber APM, Oesterhelt C, Gross W, Bräutigam A, Imboden LA, et al. 2004. EST-analysis of the thermo-acidophilic red microalga Galdieria sulphuraria reveals potential for lipid A biosynthesis and unveils the pathway of carbon export from rhodoplasts. Plant Mol. Biol. 55:17-32
    • (2004) Plant Mol. Biol. , vol.55 , pp. 17-32
    • Weber, A.P.M.1    Oesterhelt, C.2    Gross, W.3    Bräutigam, A.4    Imboden, L.A.5
  • 148
    • 2442484711 scopus 로고    scopus 로고
    • Using mutants to probe the in vivo function of plastid envelope membrane metabolite transporters
    • Weber APM, Schneidereit J, Voll LM. 2004. Using mutants to probe the in vivo function of plastid envelope membrane metabolite transporters. J. Exp. Bot. 55:1231-44
    • (2004) J. Exp. Bot. , vol.55 , pp. 1231-1244
    • Weber, A.P.M.1    Schneidereit, J.2    Voll, L.M.3
  • 149
    • 0742267790 scopus 로고    scopus 로고
    • Maltose is the major form of carbon exported from the chloroplast at night
    • Weise SE, Weber APM, Sharkey TD. 2004. Maltose is the major form of carbon exported from the chloroplast at night. Planta 218:474-82
    • (2004) Planta , vol.218 , pp. 474-482
    • Weise, S.E.1    Weber, A.P.M.2    Sharkey, T.D.3
  • 150
    • 0034800385 scopus 로고    scopus 로고
    • Construct design for efficient, effective and high-throughput gene silencing in plants
    • Wesley SV, Helliwell CA, Smith NA, Wang M, Rouse DT, et al. 2001. Construct design for efficient, effective and high-throughput gene silencing in plants. Plant J. 27:581-90
    • (2001) Plant J. , vol.27 , pp. 581-590
    • Wesley, S.V.1    Helliwell, C.A.2    Smith, N.A.3    Wang, M.4    Rouse, D.T.5
  • 151
    • 0000939796 scopus 로고
    • Molecular cloning and structural analysis of the phosphate translocator from pea chloroplasts and its comparison to the spinach phosphate translocator
    • Willey DL, Fischer K, Wachter E, Link TA, Flügge UI. 1991. Molecular cloning and structural analysis of the phosphate translocator from pea chloroplasts and its comparison to the spinach phosphate translocator. Planta 183:451-61
    • (1991) Planta , vol.183 , pp. 451-461
    • Willey, D.L.1    Fischer, K.2    Wachter, E.3    Link, T.A.4    Flügge, U.I.5
  • 152
    • 0038242363 scopus 로고    scopus 로고
    • A permease-like protein involved in ER to thylakoid lipid transfer in Arabidopsis
    • Xu C, Fan J, Riekhof W, Froehlich JE, Benning C. 2003. A permease-like protein involved in ER to thylakoid lipid transfer in Arabidopsis. EMBO J. 22:2370-79
    • (2003) EMBO J. , vol.22 , pp. 2370-2379
    • Xu, C.1    Fan, J.2    Riekhof, W.3    Froehlich, J.E.4    Benning, C.5
  • 153
    • 0036008984 scopus 로고    scopus 로고
    • Two distinct high-affinity sulfate transporters with different inducibilities mediate uptake of sulfate in Arabidopsis roots
    • Yoshimoto N, Takahashi H, Smith FW, Yamaya T, Saito K. 2002. Two distinct high-affinity sulfate transporters with different inducibilities mediate uptake of sulfate in Arabidopsis roots. Plant J. 29:465-73
    • (2002) Plant J. , vol.29 , pp. 465-473
    • Yoshimoto, N.1    Takahashi, H.2    Smith, F.W.3    Yamaya, T.4    Saito, K.5
  • 154
    • 17944366026 scopus 로고    scopus 로고
    • The Arabidopsis sex1 mutant is defective in the R1 protein, a general regulator of starch degradation in plants, and not in the chloroplast hexose transporter
    • Yu TS, Kofler H, Häusler RE, Hille D, Flügge UI, et al. 2001. The Arabidopsis sex1 mutant is defective in the R1 protein, a general regulator of starch degradation in plants, and not in the chloroplast hexose transporter. Plant Cell 13:1907-18
    • (2001) Plant Cell , vol.13 , pp. 1907-1918
    • Yu, T.S.1    Kofler, H.2    Häusler, R.E.3    Hille, D.4    Flügge, U.I.5
  • 155
    • 2642578319 scopus 로고    scopus 로고
    • New approach for plant proteomics - Characterization of chloroplast proteins of Arabidopsis thaliana by top-down mass spectrometry
    • Zabrouskov V, Giacomelli L, van Wijk KJ, McLafferty FW. 2003. New approach for plant proteomics - characterization of chloroplast proteins of Arabidopsis thaliana by top-down mass spectrometry. Mol. Cell. Proteomics 2:1253-60
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 1253-1260
    • Zabrouskov, V.1    Giacomelli, L.2    Van Wijk, K.J.3    McLafferty, F.W.4
  • 157
    • 3042539829 scopus 로고    scopus 로고
    • Plastidial alpha-glucan phosphorylase is not required for starch degradation in Arabidopsis leaves but has a role in the tolerance of abiotic stress
    • Zeeman SC, Thorneycroft D, Schupp N, Chapple A, Weck M, et al. 2004. Plastidial alpha-glucan phosphorylase is not required for starch degradation in Arabidopsis leaves but has a role in the tolerance of abiotic stress. Plant Physiol. 135:849-58
    • (2004) Plant Physiol. , vol.135 , pp. 849-858
    • Zeeman, S.C.1    Thorneycroft, D.2    Schupp, N.3    Chapple, A.4    Weck, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.