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Volumn 2009, Issue , 2009, Pages

Heterelogous expression of plant genes

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA (MICROORGANISMS); HEXAPODA; XENOPUS LAEVIS;

EID: 69449095020     PISSN: 16875370     EISSN: 16875389     Source Type: Journal    
DOI: 10.1155/2009/296482     Document Type: Article
Times cited : (32)

References (170)
  • 1
    • 0037791031 scopus 로고    scopus 로고
    • Overexpression of a small medicinal peptide from ginseng in the yeast Pichia pastoris
    • Yan Y., Chen J., Li J., Overexpression of a small medicinal peptide from ginseng in the yeast Pichia pastoris Protein Expression and Purification 2003 29 2 161 166
    • (2003) Protein Expression and Purification , vol.29 , Issue.2 , pp. 161-166
    • Yan, Y.1    Chen, J.2    Li, J.3
  • 2
    • 33749057675 scopus 로고    scopus 로고
    • Establishment of a heterologous system for the expression of Canavalia brasiliensis lectin: A model for the study of protein splicing
    • Bezerra W. M., Carvalho C. P., Moreira R. A., Grangeiro T. B., Establishment of a heterologous system for the expression of Canavalia brasiliensis lectin: a model for the study of protein splicing Genetics and Molecular Research 2006 5 1 216 223
    • (2006) Genetics and Molecular Research , vol.5 , Issue.1 , pp. 216-223
    • Bezerra, W.M.1    Carvalho, C.P.2    Moreira, R.A.3    Grangeiro, T.B.4
  • 3
    • 34548110776 scopus 로고    scopus 로고
    • Select what you need: A comparative evaluation of the advantages and limitations of frequently used expression systems for foreign genes
    • Yin J., Li G., Ren X., Herrler G., Select what you need: a comparative evaluation of the advantages and limitations of frequently used expression systems for foreign genes Journal of Biotechnology 2007 127 3 335 347
    • (2007) Journal of Biotechnology , vol.127 , Issue.3 , pp. 335-347
    • Yin, J.1    Li, G.2    Ren, X.3    Herrler, G.4
  • 4
    • 0037255597 scopus 로고    scopus 로고
    • Overview of tag protein fusions: From molecular and biochemical fundamentals to commercial systems
    • Terpe K., Overview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems Applied Microbiology and Biotechnology 2003 60 5 523 533
    • (2003) Applied Microbiology and Biotechnology , vol.60 , Issue.5 , pp. 523-533
    • Terpe, K.1
  • 5
    • 0032787876 scopus 로고    scopus 로고
    • Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused
    • Kapust R. B., Waugh D. S., Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused Protein Science 1999 8 8 1668 1674
    • (1999) Protein Science , vol.8 , Issue.8 , pp. 1668-1674
    • Kapust, R.B.1    Waugh, D.S.2
  • 6
    • 0032884573 scopus 로고    scopus 로고
    • Recombinant protein expression in Escherichia coli
    • Baneyx F., Recombinant protein expression in Escherichia coli Current Opinion in Biotechnology 1999 10 5 411 421
    • (1999) Current Opinion in Biotechnology , vol.10 , Issue.5 , pp. 411-421
    • Baneyx, F.1
  • 9
    • 0025259656 scopus 로고
    • The human growth hormone receptor. Secretion from Escherichia coli and disulfide bonding pattern of the extracellular binding domain
    • Fuh G., Mulkerrin M. G., Bass S., The human growth hormone receptor. Secretion from Escherichia coli and disulfide bonding pattern of the extracellular binding domain The Journal of Biological Chemistry 1990 265 6 3111 3115
    • (1990) The Journal of Biological Chemistry , vol.265 , Issue.6 , pp. 3111-3115
    • Fuh, G.1    Mulkerrin, M.G.2    Bass, S.3
  • 10
    • 0028286019 scopus 로고
    • Protein folding in the periplasm of Escherichia coli
    • Wlfing C., Plckthun A., Protein folding in the periplasm of Escherichia coli Molecular Microbiology 1994 12 5 685 692
    • (1994) Molecular Microbiology , vol.12 , Issue.5 , pp. 685-692
    • Wlfing, C.1    Plckthun, A.2
  • 11
    • 25844514728 scopus 로고    scopus 로고
    • Preparative expression of secreted proteins in bacteria: Status report and future prospects
    • Georgiou G., Segatori L., Preparative expression of secreted proteins in bacteria: status report and future prospects Current Opinion in Biotechnology 2005 16 5 538 545
    • (2005) Current Opinion in Biotechnology , vol.16 , Issue.5 , pp. 538-545
    • Georgiou, G.1    Segatori, L.2
  • 12
    • 0037294121 scopus 로고    scopus 로고
    • Cell and process design for targeting of recombinant protein into the culture medium of Escherichia coli
    • Shokri A., Sandn A. M., Larsson G., Cell and process design for targeting of recombinant protein into the culture medium of Escherichia coli Applied Microbiology and Biotechnology 2003 60 6 654 664
    • (2003) Applied Microbiology and Biotechnology , vol.60 , Issue.6 , pp. 654-664
    • Shokri, A.1    Sandn, A.M.2    Larsson, G.3
  • 13
    • 8344256552 scopus 로고    scopus 로고
    • Recombinant protein folding and misfolding in Escherichia coli
    • Baneyx F., Mujacic M., Recombinant protein folding and misfolding in Escherichia coli Nature Biotechnology 2004 22 11 1399 1408
    • (2004) Nature Biotechnology , vol.22 , Issue.11 , pp. 1399-1408
    • Baneyx, F.1    Mujacic, M.2
  • 14
    • 3042660198 scopus 로고    scopus 로고
    • Secretory and extracellular production of recombinant proteins using Escherichia coli
    • Choi J. H., Lee S. Y., Secretory and extracellular production of recombinant proteins using Escherichia coli Applied Microbiology and Biotechnology 2004 64 5 625 635
    • (2004) Applied Microbiology and Biotechnology , vol.64 , Issue.5 , pp. 625-635
    • Choi, J.H.1    Lee, S.Y.2
  • 15
    • 0035957961 scopus 로고    scopus 로고
    • Overproduction of bacterial protein disulfide isomerase (DsbC) and its modulator (DsbD) markedly enhances periplasmic production of human nerve growth factor in Escherichia coli
    • Kurokawa Y., Yanagi H., Yura T., Overproduction of bacterial protein disulfide isomerase (DsbC) and its modulator (DsbD) markedly enhances periplasmic production of human nerve growth factor in Escherichia coli The Journal of Biological Chemistry 2001 276 17 14393 14399
    • (2001) The Journal of Biological Chemistry , vol.276 , Issue.17 , pp. 14393-14399
    • Kurokawa, Y.1    Yanagi, H.2    Yura, T.3
  • 16
    • 38549143777 scopus 로고    scopus 로고
    • Production of active eukaryotic proteins through bacterial expression systems: A review of the existing biotechnology strategies
    • Sahdev S., Khattar S. K., Saini K. S., Production of active eukaryotic proteins through bacterial expression systems: a review of the existing biotechnology strategies Molecular and Cellular Biochemistry 2008 307 1-2 249 264
    • (2008) Molecular and Cellular Biochemistry , vol.307 , Issue.12 , pp. 249-264
    • Sahdev, S.1    Khattar, S.K.2    Saini, K.S.3
  • 18
    • 46149108793 scopus 로고    scopus 로고
    • Effect of folding factors in rescuing unstable heterologous lipase B to enhance its overexpression in the periplasm of Escherichia coli
    • Xu Y., Lewis D., Chou C. P., Effect of folding factors in rescuing unstable heterologous lipase B to enhance its overexpression in the periplasm of Escherichia coli Applied Microbiology and Biotechnology 2008 79 6 1035 1044
    • (2008) Applied Microbiology and Biotechnology , vol.79 , Issue.6 , pp. 1035-1044
    • Xu, Y.1    Lewis, D.2    Chou, C.P.3
  • 20
    • 0030941829 scopus 로고    scopus 로고
    • The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm
    • Prinz W. A., slund F., Holmgren A., Beckwith J., The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm The Journal of Biological Chemistry 1997 272 25 15661 15667
    • (1997) The Journal of Biological Chemistry , vol.272 , Issue.25 , pp. 15661-15667
    • Prinz, W.A.1    Slund, F.2    Holmgren, A.3    Beckwith, J.4
  • 21
    • 1842478326 scopus 로고    scopus 로고
    • Heterologous expression of barley and wheat oxalate oxidase in an E. coli trxB gor double mutant
    • Cassland P., Larsson S., Nilvebrant N.-O., Jnsson L. J., Heterologous expression of barley and wheat oxalate oxidase in an E. coli trxB gor double mutant Journal of Biotechnology 2004 109 1-2 53 62
    • (2004) Journal of Biotechnology , vol.109 , Issue.12 , pp. 53-62
    • Cassland, P.1    Larsson, S.2    Nilvebrant, N.-O.3    Jnsson, L.J.4
  • 22
    • 0034487523 scopus 로고    scopus 로고
    • An osmotin-like cryoprotective protein from the bittersweet nightshade Solanum dulcamara
    • Newton S. S., Duman J. G., An osmotin-like cryoprotective protein from the bittersweet nightshade Solanum dulcamara Plant Molecular Biology 2000 44 5 581 589
    • (2000) Plant Molecular Biology , vol.44 , Issue.5 , pp. 581-589
    • Newton, S.S.1    Duman, J.G.2
  • 23
    • 0031213622 scopus 로고    scopus 로고
    • Cloning and expression of a PR5-like protein from Arabidopsis: Inhibition of fungal growth by bacterially expressed protein
    • Hu X., Reddy A. S. N., Cloning and expression of a PR5-like protein from Arabidopsis: inhibition of fungal growth by bacterially expressed protein Plant Molecular Biology 1997 34 6 949 959
    • (1997) Plant Molecular Biology , vol.34 , Issue.6 , pp. 949-959
    • Hu, X.1    Reddy, A.S.N.2
  • 24
    • 43049159456 scopus 로고    scopus 로고
    • Expression in Escherichia coli, purification, refolding and antifungal activity of an osmotin from Solanum nigrum
    • de A Campos M., Silva M. S., Magalhes C. P., Expression in Escherichia coli, purification, refolding and antifungal activity of an osmotin from Solanum nigrum Microbial Cell Factories 2008 7 7 17
    • (2008) Microbial Cell Factories , vol.7 , pp. 7-17
    • De A Campos, M.1    Silva, M.S.2    Magalhes, C.P.3
  • 25
    • 33947530655 scopus 로고    scopus 로고
    • Soybean disease resistance protein RHG1-LRR domain expressed, purified and refolded from Escherichia coli inclusion bodies: Preparation for a functional analysis
    • Afzal A. J., Lightfoot D. A., Soybean disease resistance protein RHG1-LRR domain expressed, purified and refolded from Escherichia coli inclusion bodies: preparation for a functional analysis Protein Expression and Purification 2007 53 2 346 355
    • (2007) Protein Expression and Purification , vol.53 , Issue.2 , pp. 346-355
    • Afzal, A.J.1    Lightfoot, D.A.2
  • 26
    • 34447135632 scopus 로고    scopus 로고
    • Purification and in vitro refolding of maize chloroplast transglutaminase over-expressed in Escherichia coli
    • Carvajal-Vallejos P. K., Campos A., Fuentes-Prior P., Purification and in vitro refolding of maize chloroplast transglutaminase over-expressed in Escherichia coli Biotechnology Letters 2007 29 8 1255 1262
    • (2007) Biotechnology Letters , vol.29 , Issue.8 , pp. 1255-1262
    • Carvajal-Vallejos, P.K.1    Campos, A.2    Fuentes-Prior, P.3
  • 27
    • 33845475438 scopus 로고    scopus 로고
    • Cloning and functional expression of an acyl-ACP thioesterase FatB type from Diploknema (Madhuca) butyracea seeds in Escherichia coli
    • Jha J. K., Maiti M. K., Bhattacharjee A., Basu A., Sen P. C., Sen S. K., Cloning and functional expression of an acyl-ACP thioesterase FatB type from Diploknema (Madhuca) butyracea seeds in Escherichia coli Plant Physiology and Biochemistry 2006 44 11-12 645 655
    • (2006) Plant Physiology and Biochemistry , vol.44 , Issue.1112 , pp. 645-655
    • Jha, J.K.1    Maiti, M.K.2    Bhattacharjee, A.3    Basu, A.4    Sen, P.C.5    Sen, S.K.6
  • 28
    • 4043059910 scopus 로고    scopus 로고
    • Arabidopsis thaliana glutamate-cysteine ligase. Functional properties, kinetic mechanism, and regulation of activity
    • Jez J. M., Cahoon R. E., Chen S., Arabidopsis thaliana glutamate-cysteine ligase. Functional properties, kinetic mechanism, and regulation of activity The Journal of Biological Chemistry 2004 279 32 33463 33470
    • (2004) The Journal of Biological Chemistry , vol.279 , Issue.32 , pp. 33463-33470
    • Jez, J.M.1    Cahoon, R.E.2    Chen, S.3
  • 29
    • 38349134161 scopus 로고    scopus 로고
    • An E. coli expression system optimized for della proteins
    • Sun X., Frearson N., Kirk C., An E. coli expression system optimized for DELLA proteins Protein Expression and Purification 2008 58 1 168 174
    • (2008) Protein Expression and Purification , vol.58 , Issue.1 , pp. 168-174
    • Sun, X.1    Frearson, N.2    Kirk, C.3
  • 30
    • 0032544015 scopus 로고    scopus 로고
    • Determination of transmembrane topology of an inward-rectifying potassium channel from Arabidopsis thaliana based on functional expression in Escherichia coli
    • Uozumi N., Nakamura T., Schroeder J. I., Muto S., Determination of transmembrane topology of an inward-rectifying potassium channel from Arabidopsis thaliana based on functional expression in Escherichia coli Proceedings of the National Academy of Sciences of the United States of America 1998 95 17 9773 9778
    • (1998) Proceedings of the National Academy of Sciences of the United States of America , vol.95 , Issue.17 , pp. 9773-9778
    • Uozumi, N.1    Nakamura, T.2    Schroeder, J.I.3    Muto, S.4
  • 31
    • 2642682456 scopus 로고    scopus 로고
    • AtKUP1: An Arabidopsis gene encoding high-affinity potassium transport activity
    • Kim E. J., Kwak J. M., Uozumi N., Schroeder J. I., AtKUP1: an Arabidopsis gene encoding high-affinity potassium transport activity The Plant Cell 1998 10 1 51 62
    • (1998) The Plant Cell , vol.10 , Issue.1 , pp. 51-62
    • Kim, E.J.1    Kwak, J.M.2    Uozumi, N.3    Schroeder, J.I.4
  • 32
    • 0034003528 scopus 로고    scopus 로고
    • The Arabidopsis HKT1 gene homolog mediates inward Na+ currents in Xenopus laevis oocytes and Na+ uptake in Saccharomyces cerevisiae
    • Uozumi N., Kim E. J., Rubio F., The Arabidopsis HKT1 gene homolog mediates inward Na+ currents in Xenopus laevis oocytes and Na+ uptake in Saccharomyces cerevisiae Plant Physiology 2000 122 4 1249 1259
    • (2000) Plant Physiology , vol.122 , Issue.4 , pp. 1249-1259
    • Uozumi, N.1    Kim, E.J.2    Rubio, F.3
  • 34
    • 2642673614 scopus 로고    scopus 로고
    • Expression of a plastidic ATP/ADP transporter gene in Escherichia coli leads to a functional adenine nucleotide transport system in the bacterial cytoplasmic membrane
    • Tjaden J., Schwppe C., Mhlmann T., Quick P. W., Neuhaus H. E., Expression of a plastidic ATP/ADP transporter gene in Escherichia coli leads to a functional adenine nucleotide transport system in the bacterial cytoplasmic membrane The Journal of Biological Chemistry 1998 273 16 9630 9636
    • (1998) The Journal of Biological Chemistry , vol.273 , Issue.16 , pp. 9630-9636
    • Tjaden, J.1    Schwppe, C.2    Mhlmann, T.3    Quick, P.W.4    Neuhaus, H.E.5
  • 35
    • 0036836784 scopus 로고    scopus 로고
    • Molecular cloning and functional expression in bacteria of the potassium transporters CnHAK1 and CnHAK2 of the seagrass Cymodocea nodosa
    • Garciadeblas B., Benito B., Rodrguez-Navarro A., Molecular cloning and functional expression in bacteria of the potassium transporters CnHAK1 and CnHAK2 of the seagrass Cymodocea nodosa Plant Molecular Biology 2002 50 4-5 623 633
    • (2002) Plant Molecular Biology , vol.50 , Issue.45 , pp. 623-633
    • Garciadeblas, B.1    Benito, B.2    Rodrguez-Navarro, A.3
  • 36
    • 12144290916 scopus 로고    scopus 로고
    • A nodule-specific dicarboxylate transporter from alder is a member of the peptide transporter family
    • Jeong J., Suh S., Guan C., A nodule-specific dicarboxylate transporter from alder is a member of the peptide transporter family Plant Physiology 2004 134 3 969 978
    • (2004) Plant Physiology , vol.134 , Issue.3 , pp. 969-978
    • Jeong, J.1    Suh, S.2    Guan, C.3
  • 37
    • 20244389869 scopus 로고    scopus 로고
    • Triticum durum metallothionein: Isolation of the gene and structural characterization of the protein using solution scattering and molecular modeling
    • Bilecen K., Ozturk U. H., Duru A. D., Triticum durum metallothionein: isolation of the gene and structural characterization of the protein using solution scattering and molecular modeling The Journal of Biological Chemistry 2005 280 14 13701 13711
    • (2005) The Journal of Biological Chemistry , vol.280 , Issue.14 , pp. 13701-13711
    • Bilecen, K.1    Ozturk, U.H.2    Duru, A.D.3
  • 38
    • 8244233167 scopus 로고    scopus 로고
    • Analysis of type 1 metallothionein cDNAs in Vicia faba
    • Foley R. C., Liang Z. M., Singh K. B., Analysis of type 1 metallothionein cDNAs in Vicia faba Plant Molecular Biology 1997 33 4 583 591
    • (1997) Plant Molecular Biology , vol.33 , Issue.4 , pp. 583-591
    • Foley, R.C.1    Liang, Z.M.2    Singh, K.B.3
  • 39
    • 0031127337 scopus 로고    scopus 로고
    • Purification and immunological identification of metallothioneins 1 and 2 from Arabidopsis thaliana
    • Murphy A., Zhou J., Goldsbrough P. B., Taiz L., Purification and immunological identification of metallothioneins 1 and 2 from Arabidopsis thaliana Plant Physiology 1997 113 4 1293 1301
    • (1997) Plant Physiology , vol.113 , Issue.4 , pp. 1293-1301
    • Murphy, A.1    Zhou, J.2    Goldsbrough, P.B.3    Taiz, L.4
  • 40
    • 0036489620 scopus 로고    scopus 로고
    • Isolation and characterisation of two divergent type 3 metallothioneins from oil palm, Elaeis guineensis
    • Abdullah S. N. A., Cheah S. C., Murphy D. J., Isolation and characterisation of two divergent type 3 metallothioneins from oil palm, Elaeis guineensis Plant Physiology and Biochemistry 2002 40 3 255 263
    • (2002) Plant Physiology and Biochemistry , vol.40 , Issue.3 , pp. 255-263
    • Abdullah, S.N.A.1    Cheah, S.C.2    Murphy, D.J.3
  • 41
    • 11144281841 scopus 로고    scopus 로고
    • A plant type 2 metallothionein (MT) from cork tissue responds to oxidative stress
    • Mir G., Domnech J., Huguet G., A plant type 2 metallothionein (MT) from cork tissue responds to oxidative stress Journal of Experimental Botany 2004 55 408 2483 2493
    • (2004) Journal of Experimental Botany , vol.55 , Issue.408 , pp. 2483-2493
    • Mir, G.1    Domnech, J.2    Huguet, G.3
  • 44
    • 0035960880 scopus 로고    scopus 로고
    • Structural analysis of regulatory protein domains using GST-fusion proteins
    • Zhan Y., Song X., Zhou G. W., Structural analysis of regulatory protein domains using GST-fusion proteins Gene 2001 281 1-2 1 9
    • (2001) Gene , vol.281 , Issue.12 , pp. 1-9
    • Zhan, Y.1    Song, X.2    Zhou, G.W.3
  • 46
    • 0032970626 scopus 로고    scopus 로고
    • Identification and characterization of plant transporters using heterologous expression systems
    • Dreyer I., Horeau C., Lemaillet G., Identification and characterization of plant transporters using heterologous expression systems Journal of Experimental Botany 1999 50 1073 1087
    • (1999) Journal of Experimental Botany , vol.50 , pp. 1073-1087
    • Dreyer, I.1    Horeau, C.2    Lemaillet, G.3
  • 47
    • 0028914005 scopus 로고
    • Use of Saccharomyces cerevisiae for patch-clamp analysis of heterologous membrane proteins: Characterization of Kat1, an inward-rectifying K+ channel from Arabidopsis thaliana, and comparison with endogeneous yeast channels and carriers
    • Bertl A., Anderson J. A., Slayman C. L., Gaber R. F., Use of Saccharomyces cerevisiae for patch-clamp analysis of heterologous membrane proteins: characterization of Kat1, an inward-rectifying K+ channel from Arabidopsis thaliana, and comparison with endogeneous yeast channels and carriers Proceedings of the National Academy of Sciences of the United States of America 1995 92 7 2701 2705
    • (1995) Proceedings of the National Academy of Sciences of the United States of America , vol.92 , Issue.7 , pp. 2701-2705
    • Bertl, A.1    Anderson, J.A.2    Slayman, C.L.3    Gaber, R.F.4
  • 49
    • 0031421317 scopus 로고    scopus 로고
    • The HAK1 gene of barley is a member of a large gene family and encodes a high-affinity potassium transporter
    • Santa-Mara G. E., Rubio F., Dubcovsky J., Rodrguez-Navarro A., The HAK1 gene of barley is a member of a large gene family and encodes a high-affinity potassium transporter The Plant Cell 1997 9 12 2281 2289
    • (1997) The Plant Cell , vol.9 , Issue.12 , pp. 2281-2289
    • Santa-Mara, G.E.1    Rubio, F.2    Dubcovsky, J.3    Rodrguez-Navarro, A.4
  • 50
    • 0031590324 scopus 로고    scopus 로고
    • A new family of K+ transporters from Arabidopsis that are conserved across phyla
    • Quintero F. J., Blatt M. R., A new family of K+ transporters from Arabidopsis that are conserved across phyla FEBS Letters 1997 415 2 206 211
    • (1997) FEBS Letters , vol.415 , Issue.2 , pp. 206-211
    • Quintero, F.J.1    Blatt, M.R.2
  • 51
    • 0031832283 scopus 로고    scopus 로고
    • AtKUP1: A dual-affinity K+ transporter from arabidopsis
    • Fu H.-H., Luan S., AtKUP1: a dual-affinity K+ transporter from arabidopsis The Plant Cell 1998 10 1 63 73
    • (1998) The Plant Cell , vol.10 , Issue.1 , pp. 63-73
    • Fu, H.-H.1    Luan, S.2
  • 52
    • 0028114234 scopus 로고
    • Structure and transport mechanism of a high-affinity potassium uptake transporter from higher plants
    • Schachtman D. P., Schroeder J. I., Structure and transport mechanism of a high-affinity potassium uptake transporter from higher plants Nature 1994 370 6491 655 658
    • (1994) Nature , vol.370 , Issue.6491 , pp. 655-658
    • Schachtman, D.P.1    Schroeder, J.I.2
  • 53
    • 0029583478 scopus 로고
    • Sodium-driven potassium uptake by the plant potassium transporter HKT1 and mutations conferring salt tolerance
    • Rubio F., Gassmann W., Schroeder J. I., Sodium-driven potassium uptake by the plant potassium transporter HKT1 and mutations conferring salt tolerance Science 1995 270 5242 1660 1663
    • (1995) Science , vol.270 , Issue.5242 , pp. 1660-1663
    • Rubio, F.1    Gassmann, W.2    Schroeder, J.I.3
  • 54
    • 0346669802 scopus 로고    scopus 로고
    • Cloning of two contrasting high-affinity sulfate transporters from tomato induced by low sulfate and infection by the vascular pathogen Verticillium dahliae
    • Howarth J. R., Fourcroy P., Davidian J.-C., Smith F. W., Hawkesford M. J., Cloning of two contrasting high-affinity sulfate transporters from tomato induced by low sulfate and infection by the vascular pathogen Verticillium dahliae Planta 2003 218 1 58 64
    • (2003) Planta , vol.218 , Issue.1 , pp. 58-64
    • Howarth, J.R.1    Fourcroy, P.2    Davidian, J.-C.3    Smith, F.W.4    Hawkesford, M.J.5
  • 56
    • 8444249373 scopus 로고    scopus 로고
    • AtPTR1, a plasma membrane peptide transporter expressed during seed germination and in vascular tissue of Arabidopsis
    • Dietrich D., Hammes U., Thor K., AtPTR1, a plasma membrane peptide transporter expressed during seed germination and in vascular tissue of Arabidopsis The Plant Journal 2004 40 4 488 499
    • (2004) The Plant Journal , vol.40 , Issue.4 , pp. 488-499
    • Dietrich, D.1    Hammes, U.2    Thor, K.3
  • 57
    • 33845755468 scopus 로고    scopus 로고
    • Arabidopsis thaliana CHX17 gene complements the kha1 deletion phenotypes in Saccharomyces cerevisiae
    • Maresova L., Sychrova H., Arabidopsis thaliana CHX17 gene complements the kha1 deletion phenotypes in Saccharomyces cerevisiae Yeast 2006 23 16 1167 1171
    • (2006) Yeast , vol.23 , Issue.16 , pp. 1167-1171
    • Maresova, L.1    Sychrova, H.2
  • 58
    • 34547652462 scopus 로고    scopus 로고
    • Isolation, functional characterization, and expression analysis of grapevine (Vitis vinifera L.) hexose transporters: Differential roles in sink and source tissues
    • Hayes M. A., Davies C., Dry I. B., Isolation, functional characterization, and expression analysis of grapevine (Vitis vinifera L.) hexose transporters: differential roles in sink and source tissues Journal of Experimental Botany 2007 58 8 1985 1997
    • (2007) Journal of Experimental Botany , vol.58 , Issue.8 , pp. 1985-1997
    • Hayes, M.A.1    Davies, C.2    Dry, I.B.3
  • 59
    • 37249039463 scopus 로고    scopus 로고
    • Arabidopsis Inositol Transporter2 mediates H+ symport of different inositol epimers and derivatives across the plasma membrane
    • Schneider S., Schneidereit A., Udvardi P., Arabidopsis Inositol Transporter2 mediates H+ symport of different inositol epimers and derivatives across the plasma membrane Plant Physiology 2007 145 4 1395 1407
    • (2007) Plant Physiology , vol.145 , Issue.4 , pp. 1395-1407
    • Schneider, S.1    Schneidereit, A.2    Udvardi, P.3
  • 60
    • 33646342506 scopus 로고    scopus 로고
    • AtGAT1, a high affinity transporter for -aminobutyric acid in Arabidopsis thaliana
    • Meyer A., Eskandari S., Grallath S., Rentsch D., AtGAT1, a high affinity transporter for -aminobutyric acid in Arabidopsis thaliana The Journal of Biological Chemistry 2006 281 11 7197 7204
    • (2006) The Journal of Biological Chemistry , vol.281 , Issue.11 , pp. 7197-7204
    • Meyer, A.1    Eskandari, S.2    Grallath, S.3    Rentsch, D.4
  • 61
    • 19044393297 scopus 로고    scopus 로고
    • Tonoplast intrinsic proteins AtTIP2;1 and AtTIP2;3 facilitate NH3 transport into the vacuole
    • Loqu D., Ludewig U., Yuan L., von Wirn N., Tonoplast intrinsic proteins AtTIP2;1 and AtTIP2;3 facilitate NH3 transport into the vacuole Plant Physiology 2005 137 2 671 680
    • (2005) Plant Physiology , vol.137 , Issue.2 , pp. 671-680
    • Loqu, D.1    Ludewig, U.2    Yuan, L.3    Von Wirn, N.4
  • 62
    • 0842285689 scopus 로고    scopus 로고
    • Differential expression of sucrose transporter and polyol transporter genes during maturation of common plantain companion cells
    • Ramsperger-Gleixner M., Geiger D., Hedrich R., Sauer N., Differential expression of sucrose transporter and polyol transporter genes during maturation of common plantain companion cells Plant Physiology 2004 134 1 147 160
    • (2004) Plant Physiology , vol.134 , Issue.1 , pp. 147-160
    • Ramsperger-Gleixner, M.1    Geiger, D.2    Hedrich, R.3    Sauer, N.4
  • 63
    • 2642607849 scopus 로고    scopus 로고
    • Ectopic potassium uptake in trk1 trk2 mutants of Saccharomyces cerevisiae correlates with a highly hyperpolarized membrane potential
    • Madrid R., Gmez M. J., Ramos J., Rodrguez-Navarro A., Ectopic potassium uptake in trk1 trk2 mutants of Saccharomyces cerevisiae correlates with a highly hyperpolarized membrane potential The Journal of Biological Chemistry 1998 273 24 14838 14844
    • (1998) The Journal of Biological Chemistry , vol.273 , Issue.24 , pp. 14838-14844
    • Madrid, R.1    Gmez, M.J.2    Ramos, J.3    Rodrguez-Navarro, A.4
  • 64
    • 0033955337 scopus 로고    scopus 로고
    • Heterologous protein expression in the methylotrophic yeast Pichia pastoris
    • Cereghino J. L., Cregg J. M., Heterologous protein expression in the methylotrophic yeast Pichia pastoris FEMS Microbiology Reviews 2000 24 1 45 66
    • (2000) FEMS Microbiology Reviews , vol.24 , Issue.1 , pp. 45-66
    • Cereghino, J.L.1    Cregg, J.M.2
  • 65
    • 17244363998 scopus 로고    scopus 로고
    • Heterologous protein production using the Pichia pastoris expression system
    • Macauley-Patrick S., Fazenda M. L., McNeil B., Harvey L. M., Heterologous protein production using the Pichia pastoris expression system Yeast 2005 22 4 249 270
    • (2005) Yeast , vol.22 , Issue.4 , pp. 249-270
    • MacAuley-Patrick, S.1    Fazenda, M.L.2    McNeil, B.3    Harvey, L.M.4
  • 66
    • 0024637162 scopus 로고
    • Size distribution and general structural features of N-linked oligosaccharides from the methylotrophic yeast, Pichia pastoris
    • Grinna L. S., Tschopp J. F., Size distribution and general structural features of N-linked oligosaccharides from the methylotrophic yeast, Pichia pastoris Yeast 1989 5 2 107 115
    • (1989) Yeast , vol.5 , Issue.2 , pp. 107-115
    • Grinna, L.S.1    Tschopp, J.F.2
  • 67
    • 14744299579 scopus 로고
    • Recent advances in the expression of foreign genes in Pichia pastoris
    • Cregg J. M., Vedvick T. S., Raschke W. C., Recent advances in the expression of foreign genes in Pichia pastoris Nature Biotechnology 1993 11 8 905 910
    • (1993) Nature Biotechnology , vol.11 , Issue.8 , pp. 905-910
    • Cregg, J.M.1    Vedvick, T.S.2    Raschke, W.C.3
  • 69
    • 0034097952 scopus 로고    scopus 로고
    • Recombinant expression of molybdenum reductase fragments of plant nitrate reductase at high levels in Pichia pastoris
    • Mertens J. A., Shiraishi N., Campbell W. H., Recombinant expression of molybdenum reductase fragments of plant nitrate reductase at high levels in Pichia pastoris Plant Physiology 2000 123 2 743 756
    • (2000) Plant Physiology , vol.123 , Issue.2 , pp. 743-756
    • Mertens, J.A.1    Shiraishi, N.2    Campbell, W.H.3
  • 71
    • 0033197613 scopus 로고    scopus 로고
    • Molecular characterisation of a membrane-bound galactosyltransferase of plant cell wall matrix polysaccharide biosynthesis
    • Edwards M. E., Dickson C. A., Chengappa S., Sidebottom C., Gidley M. J., Reid J. S. G., Molecular characterisation of a membrane-bound galactosyltransferase of plant cell wall matrix polysaccharide biosynthesis The Plant Journal 1999 19 6 691 697
    • (1999) The Plant Journal , vol.19 , Issue.6 , pp. 691-697
    • Edwards, M.E.1    Dickson, C.A.2    Chengappa, S.3    Sidebottom, C.4    Gidley, M.J.5    Reid, J.S.G.6
  • 73
    • 0037518458 scopus 로고    scopus 로고
    • Expression of eukaryotic glycosyltransferases in the yeast Pichia pastoris
    • Bencrov M., Rendi D., Fabini G., Kopecky E.-M., Altmann F., Wilson I. B. H., Expression of eukaryotic glycosyltransferases in the yeast Pichia pastoris Biochimie 2003 85 3-4 413 422
    • (2003) Biochimie , vol.85 , Issue.34 , pp. 413-422
    • Bencrov, M.1    Rendi, D.2    Fabini, G.3    Kopecky, E.-M.4    Altmann, F.5    Wilson, I.B.H.6
  • 74
    • 0141788512 scopus 로고    scopus 로고
    • A cDNA encoding vacuolar type -D-fructofuranosidase (Os fruct3) of rice and its expression in Pichia pastoris
    • Fu R.-H., Wang A.-Y., Wang Y.-C., Sung H.-Y., A cDNA encoding vacuolar type -D-fructofuranosidase (Os fruct3) of rice and its expression in Pichia pastoris Biotechnology Letters 2003 25 18 1525 1530
    • (2003) Biotechnology Letters , vol.25 , Issue.18 , pp. 1525-1530
    • Fu, R.-H.1    Wang, A.-Y.2    Wang, Y.-C.3    Sung, H.-Y.4
  • 75
    • 0037296231 scopus 로고    scopus 로고
    • Methylotrophic yeast Pichia pastoris as a host for production of ATP-diphosphohydrolase (apyrase) from potato tubers (Solanum tuberosum)
    • Nourizad N., Ehn M., Gharizadeh B., Hober S., Nyrn P., Methylotrophic yeast Pichia pastoris as a host for production of ATP-diphosphohydrolase (apyrase) from potato tubers (Solanum tuberosum) Protein Expression and Purification 2003 27 2 229 237
    • (2003) Protein Expression and Purification , vol.27 , Issue.2 , pp. 229-237
    • Nourizad, N.1    Ehn, M.2    Gharizadeh, B.3    Hober, S.4    Nyrn, P.5
  • 76
    • 0036371346 scopus 로고    scopus 로고
    • Characterization of recombinant barley oxalate oxidase expressed by Pichia pastoris
    • Whittaker M. M., Whittaker J. W., Characterization of recombinant barley oxalate oxidase expressed by Pichia pastoris Journal of Biological Inorganic Chemistry 2002 7 1-2 136 145
    • (2002) Journal of Biological Inorganic Chemistry , vol.7 , Issue.12 , pp. 136-145
    • Whittaker, M.M.1    Whittaker, J.W.2
  • 78
    • 69449105347 scopus 로고    scopus 로고
    • Expression of A. thaliana G protein alpha subunit in P. pastoris
    • supplement 1
    • Kaplan B., Tunca S., Sayers Z., Expression of A. thaliana G protein alpha subunit in P. pastoris FEBS Journal 2005 272 supplement 1 1 11
    • (2005) FEBS Journal , vol.272 , pp. 1-11
    • Kaplan, B.1    Tunca, S.2    Sayers, Z.3
  • 80
    • 33646147815 scopus 로고    scopus 로고
    • Expression and transport characterisation of the wheat low-affinity cation transporter (LCT1) in the methylotrophic yeast Pichia pastoris
    • Diatloff E., Forde B. G., Roberts S. K., Expression and transport characterisation of the wheat low-affinity cation transporter (LCT1) in the methylotrophic yeast Pichia pastoris Biochemical and Biophysical Research Communications 2006 344 3 807 813
    • (2006) Biochemical and Biophysical Research Communications , vol.344 , Issue.3 , pp. 807-813
    • Diatloff, E.1    Forde, B.G.2    Roberts, S.K.3
  • 81
    • 0024287753 scopus 로고
    • Characterization of the lipid acyl hydrolase activity of the major potato (Solanum tuberosum) tuber protein, patatin, by cloning and abundant expression in a baculovirus vector
    • Andrews D. L., Beames B., Summers M. D., Park W. D., Characterization of the lipid acyl hydrolase activity of the major potato (Solanum tuberosum) tuber protein, patatin, by cloning and abundant expression in a baculovirus vector Biochemical Journal 1988 252 1 199 206
    • (1988) Biochemical Journal , vol.252 , Issue.1 , pp. 199-206
    • Andrews, D.L.1    Beames, B.2    Summers, M.D.3    Park, W.D.4
  • 82
    • 0031594283 scopus 로고    scopus 로고
    • Two isoforms of NAPDH: Cytochrome p450 reductase in Arabidopsis thaliana gene structure, heterologous expression in insect cells, and differential regulation
    • Mizutani M., Ohta D., Two isoforms of NAPDH: cytochrome p450 reductase in Arabidopsis thaliana gene structure, heterologous expression in insect cells, and differential regulation Plant Physiology 1998 116 1 357 367
    • (1998) Plant Physiology , vol.116 , Issue.1 , pp. 357-367
    • Mizutani, M.1    Ohta, D.2
  • 84
    • 35448945700 scopus 로고    scopus 로고
    • Phosphorylation of threonine 161 in plant cyclin-dependent kinase A is required for cell division by activation of its associated kinase
    • Harashima H., Shinmyo A., Sekine M., Phosphorylation of threonine 161 in plant cyclin-dependent kinase A is required for cell division by activation of its associated kinase The Plant Journal 2007 52 3 435 448
    • (2007) The Plant Journal , vol.52 , Issue.3 , pp. 435-448
    • Harashima, H.1    Shinmyo, A.2    Sekine, M.3
  • 85
    • 0032817558 scopus 로고    scopus 로고
    • Microsomal electron transfer in higher plants: Cloning and heterologous expression of NADH-cytochrome b5 reductase from Arabidopsis
    • Fukuchi-Mizutani M., Mizutani M., Tanaka Y., Kusumi T., Ohta D., Microsomal electron transfer in higher plants: cloning and heterologous expression of NADH-cytochrome b5 reductase from Arabidopsis Plant Physiology 1999 119 1 353 361
    • (1999) Plant Physiology , vol.119 , Issue.1 , pp. 353-361
    • Fukuchi-Mizutani, M.1    Mizutani, M.2    Tanaka, Y.3    Kusumi, T.4    Ohta, D.5
  • 86
    • 0034870820 scopus 로고    scopus 로고
    • Efficient prenylation by a plant geranylgeranyltransferase-I requires a functional Caal box motif and a proximal polybasic domain
    • Caldelari D., Sternberg H., Rodrguez-Concepcin M., Gruissem W., Yalovsky S., Efficient prenylation by a plant geranylgeranyltransferase-I requires a functional Caal box motif and a proximal polybasic domain Plant Physiology 2001 126 4 1416 1429
    • (2001) Plant Physiology , vol.126 , Issue.4 , pp. 1416-1429
    • Caldelari, D.1    Sternberg, H.2    Rodrguez-Concepcin, M.3    Gruissem, W.4    Yalovsky, S.5
  • 87
    • 0036909919 scopus 로고    scopus 로고
    • Molecular characterization of an Arabidopsis acyl-coenzyme a synthetase localized on glyoxysomal membranes
    • Hayashi H., De Bellis L., Hayashi Y., Molecular characterization of an Arabidopsis acyl-coenzyme a synthetase localized on glyoxysomal membranes Plant Physiology 2002 130 4 2019 2026
    • (2002) Plant Physiology , vol.130 , Issue.4 , pp. 2019-2026
    • Hayashi, H.1    De Bellis, L.2    Hayashi, Y.3
  • 88
    • 0036000055 scopus 로고    scopus 로고
    • Isolation and characterization of homogentisate phytyltransferase genes from Synechocystis sp. PCC 6803 and Arabidopsis
    • Savidge B., Weiss J. D., Wong Y.-H. H., Isolation and characterization of homogentisate phytyltransferase genes from Synechocystis sp. PCC 6803 and Arabidopsis Plant Physiology 2002 129 1 321 332
    • (2002) Plant Physiology , vol.129 , Issue.1 , pp. 321-332
    • Savidge, B.1    Weiss, J.D.2    Wong, Y.-H.H.3
  • 89
    • 1942469580 scopus 로고    scopus 로고
    • Arabidopsis CYP707As encode (+)-abscisic acid 8′ -hydroxylase, a key enzyme in the oxidative catabolism of abscisic acid
    • Saito S., Hirai N., Matsumoto C., Arabidopsis CYP707As encode (+)-abscisic acid 8′ -hydroxylase, a key enzyme in the oxidative catabolism of abscisic acid Plant Physiology 2004 134 4 1439 1449
    • (2004) Plant Physiology , vol.134 , Issue.4 , pp. 1439-1449
    • Saito, S.1    Hirai, N.2    Matsumoto, C.3
  • 90
    • 0037237680 scopus 로고    scopus 로고
    • Structural requirements for Arabidopsis 1, 2-xylosyltransferase activity and targeting to the Golgi
    • Pagny S., Bouissonnie F., Sarkar M., Structural requirements for Arabidopsis 1, 2-xylosyltransferase activity and targeting to the Golgi The Plant Journal 2003 33 1 189 203
    • (2003) The Plant Journal , vol.33 , Issue.1 , pp. 189-203
    • Pagny, S.1    Bouissonnie, F.2    Sarkar, M.3
  • 91
    • 0033213680 scopus 로고    scopus 로고
    • A point mutation in the ethylene-inducing xylanase elicitor inhibits the -1-4-endoxylanase activity but not the elicitation activity
    • Furman-Matarasso N., Cohen E., Du Q., Chejanovsky N., Hanania U., Avni A., A point mutation in the ethylene-inducing xylanase elicitor inhibits the -1-4-endoxylanase activity but not the elicitation activity Plant Physiology 1999 121 2 345 351
    • (1999) Plant Physiology , vol.121 , Issue.2 , pp. 345-351
    • Furman-Matarasso, N.1    Cohen, E.2    Du, Q.3    Chejanovsky, N.4    Hanania, U.5    Avni, A.6
  • 92
    • 0032711802 scopus 로고    scopus 로고
    • The allosterically unregulated isoform of ADP-glucose pyrophosphorylase from barley endosperm is the most likely source of ADP-glucose incorporated into endosperm starch
    • Doan D. N. P., Rudi H., Olsen O.-A., The allosterically unregulated isoform of ADP-glucose pyrophosphorylase from barley endosperm is the most likely source of ADP-glucose incorporated into endosperm starch Plant Physiology 1999 121 3 965 975
    • (1999) Plant Physiology , vol.121 , Issue.3 , pp. 965-975
    • Doan, D.N.P.1    Rudi, H.2    Olsen, O.-A.3
  • 93
    • 0029787242 scopus 로고    scopus 로고
    • The baculovirus/insect cell system as an alternative to Xenopus oocytes. First characterization of the AKT1 K+ channel from Arabidopsis thaliana
    • Gaymard F., Cerutti M., Horeau C., The baculovirus/insect cell system as an alternative to Xenopus oocytes. First characterization of the AKT1 K+ channel from Arabidopsis thaliana The Journal of Biological Chemistry 1996 271 37 22863 22870
    • (1996) The Journal of Biological Chemistry , vol.271 , Issue.37 , pp. 22863-22870
    • Gaymard, F.1    Cerutti, M.2    Horeau, C.3
  • 95
    • 0030919991 scopus 로고    scopus 로고
    • New structure and function in plant K+ channels: KCO1, an outward rectifier with a steep Ca2+ dependency
    • Czempinski K., Zimmermann S., Ehrhardt T., Mller-Rber B., New structure and function in plant K+ channels: KCO1, an outward rectifier with a steep Ca2+ dependency The EMBO Journal 1997 16 10 2565 2575
    • (1997) The EMBO Journal , vol.16 , Issue.10 , pp. 2565-2575
    • Czempinski, K.1    Zimmermann, S.2    Ehrhardt, T.3    Mller-Rber, B.4
  • 96
    • 0030971291 scopus 로고    scopus 로고
    • Association of plant K+ (in) channels is mediated by conserved and does not affect subunit assembly
    • Ehrhardt T., Zimmermann S., Mller-Rber B., Association of plant K+ (in) channels is mediated by conserved and does not affect subunit assembly FEBS Letters 1997 409 2 166 170
    • (1997) FEBS Letters , vol.409 , Issue.2 , pp. 166-170
    • Ehrhardt, T.1    Zimmermann, S.2    Mller-Rber, B.3
  • 97
    • 0032013194 scopus 로고    scopus 로고
    • Characterization of SKT1, an inwardly rectifying potassium channel from potato, by heterologous in insect cells
    • Zimmermann S., Talke I., Ehrhardt T., Nast G., Mller-Rber B., Characterization of SKT1, an inwardly rectifying potassium channel from potato, by heterologous in insect cells Plant Physiology 1998 116 3 879 890
    • (1998) Plant Physiology , vol.116 , Issue.3 , pp. 879-890
    • Zimmermann, S.1    Talke, I.2    Ehrhardt, T.3    Nast, G.4    Mller-Rber, B.5
  • 98
    • 55549109761 scopus 로고    scopus 로고
    • The binding of auxin to the Arabidopsis auxin influx transporter AUX1
    • Carrier D. J., Bakar N. T. A., Swarup R., The binding of auxin to the Arabidopsis auxin influx transporter AUX1 Plant Physiology 2008 148 1 529 535
    • (2008) Plant Physiology , vol.148 , Issue.1 , pp. 529-535
    • Carrier, D.J.1    Bakar, N.T.A.2    Swarup, R.3
  • 99
    • 0034192562 scopus 로고    scopus 로고
    • Xenopus oocytes as an expression system for plant transporters
    • Miller A. J., Zhou J. J., Xenopus oocytes as an expression system for plant transporters Biochimica et Biophysica Acta 2000 1465 1-2 343 358
    • (2000) Biochimica et Biophysica Acta , vol.1465 , Issue.12 , pp. 343-358
    • Miller, A.J.1    Zhou, J.J.2
  • 100
    • 15944402496 scopus 로고    scopus 로고
    • The Xenopus oocyte: System for the study of functional expression and modulation of proteins
    • Sigel E., The Xenopus oocyte: system for the study of functional expression and modulation of proteins Molecular Nutrition and Food Research 2005 49 3 228 234
    • (2005) Molecular Nutrition and Food Research , vol.49 , Issue.3 , pp. 228-234
    • Sigel, E.1
  • 101
    • 0026582987 scopus 로고
    • Functional expression of a plant plasma membrane transporter in Xenopus oocytes
    • Boorer K. J., Forde B. G., Leigh R. A., Miller A. J., Functional expression of a plant plasma membrane transporter in Xenopus oocytes FEBS Letters 1992 302 2 166 168
    • (1992) FEBS Letters , vol.302 , Issue.2 , pp. 166-168
    • Boorer, K.J.1    Forde, B.G.2    Leigh, R.A.3    Miller, A.J.4
  • 102
    • 33751088799 scopus 로고    scopus 로고
    • Characterization of a two-component high-affinity nitrate uptake system in Arabidopsis. Physiology and protein-protein interaction
    • Orsel M., Chopin F., Leleu O., Characterization of a two-component high-affinity nitrate uptake system in Arabidopsis. Physiology and protein-protein interaction Plant Physiology 2006 142 3 1304 1317
    • (2006) Plant Physiology , vol.142 , Issue.3 , pp. 1304-1317
    • Orsel, M.1    Chopin, F.2    Leleu, O.3
  • 103
    • 0034830558 scopus 로고    scopus 로고
    • Characterization of two HKT1 homologues from Eucalyptus camaldulensis that display intrinsic osmosensing capability
    • Liu W., Fairbairn D. J., Reid R. J., Schachtman D. P., Characterization of two HKT1 homologues from Eucalyptus camaldulensis that display intrinsic osmosensing capability Plant Physiology 2001 127 1 283 294
    • (2001) Plant Physiology , vol.127 , Issue.1 , pp. 283-294
    • Liu, W.1    Fairbairn, D.J.2    Reid, R.J.3    Schachtman, D.P.4
  • 104
    • 11144357502 scopus 로고    scopus 로고
    • Glycine residues in potassium channel-like selectivity filters determine potassium selectivity in four-loop-per-subunit HKT transporters from plants
    • Mser P., Hosoo Y., Goshima S., Glycine residues in potassium channel-like selectivity filters determine potassium selectivity in four-loop-per-subunit HKT transporters from plants Proceedings of the National Academy of Sciences of the United States of America 2002 99 9 6428 6433
    • (2002) Proceedings of the National Academy of Sciences of the United States of America , vol.99 , Issue.9 , pp. 6428-6433
    • Mser, P.1    Hosoo, Y.2    Goshima, S.3
  • 105
    • 0242580829 scopus 로고    scopus 로고
    • Homo- and heterooligomerization of ammonium transporter-1 NH4+ uniporters
    • Ludewig U., Wilken S., Wu B., Homo- and heterooligomerization of ammonium transporter-1 NH4+ uniporters The Journal of Biological Chemistry 2003 278 46 45603 45610
    • (2003) The Journal of Biological Chemistry , vol.278 , Issue.46 , pp. 45603-45610
    • Ludewig, U.1    Wilken, S.2    Wu, B.3
  • 106
    • 34248144236 scopus 로고    scopus 로고
    • Regulation of NH4+ transport by essential cross talk between AMT monomers through the carboxyl tails
    • Neuhuser B., Dynowski M., Mayer M., Ludewig U., Regulation of NH4+ transport by essential cross talk between AMT monomers through the carboxyl tails Plant Physiology 2007 143 4 1651 1659
    • (2007) Plant Physiology , vol.143 , Issue.4 , pp. 1651-1659
    • Neuhuser, B.1    Dynowski, M.2    Mayer, M.3    Ludewig, U.4
  • 107
    • 0242666390 scopus 로고    scopus 로고
    • Substrate specificity of the Arabidopsis thaliana sucrose transporter AtSUC2
    • Chandran D., Reinders A., Ward J. M., Substrate specificity of the Arabidopsis thaliana sucrose transporter AtSUC2 The Journal of Biological Chemistry 2003 278 45 44320 44325
    • (2003) The Journal of Biological Chemistry , vol.278 , Issue.45 , pp. 44320-44325
    • Chandran, D.1    Reinders, A.2    Ward, J.M.3
  • 108
    • 33846399443 scopus 로고    scopus 로고
    • Arabidopsis sucrose transporter AtSUC9. High-affinity transport activity, intragenic control of expression, and early flowering mutant phenotype
    • Sivitz A. B., Reinders A., Johnson M. E., Arabidopsis sucrose transporter AtSUC9. High-affinity transport activity, intragenic control of expression, and early flowering mutant phenotype Plant Physiology 2007 143 1 188 198
    • (2007) Plant Physiology , vol.143 , Issue.1 , pp. 188-198
    • Sivitz, A.B.1    Reinders, A.2    Johnson, M.E.3
  • 109
    • 50249180796 scopus 로고    scopus 로고
    • Functional analysis of LjSUT4, a vacuolar sucrose transporter from Lotus japonicus
    • Reinders A., Sivitz A. B., Starker C. G., Gantt J. S., Ward J. M., Functional analysis of LjSUT4, a vacuolar sucrose transporter from Lotus japonicus Plant Molecular Biology 2008 68 3 289 299
    • (2008) Plant Molecular Biology , vol.68 , Issue.3 , pp. 289-299
    • Reinders, A.1    Sivitz, A.B.2    Starker, C.G.3    Gantt, J.S.4    Ward, J.M.5
  • 110
    • 1542318969 scopus 로고    scopus 로고
    • A wheat gene encoding an aluminum-activated malate transporter
    • Sasaki T., Yamamoto Y., Ezaki B., A wheat gene encoding an aluminum-activated malate transporter The Plant Journal 2004 37 5 645 653
    • (2004) The Plant Journal , vol.37 , Issue.5 , pp. 645-653
    • Sasaki, T.1    Yamamoto, Y.2    Ezaki, B.3
  • 111
    • 33751078302 scopus 로고    scopus 로고
    • The BnALMT1 and BnALMT2 genes from rape encode aluminum-activated malate transporters that enhance the aluminum resistance of plant cells
    • Ligaba A., Katsuhara M., Ryan P. R., Shibasaka M., Matsumoto H., The BnALMT1 and BnALMT2 genes from rape encode aluminum-activated malate transporters that enhance the aluminum resistance of plant cells Plant Physiology 2006 142 3 1294 1303
    • (2006) Plant Physiology , vol.142 , Issue.3 , pp. 1294-1303
    • Ligaba, A.1    Katsuhara, M.2    Ryan, P.R.3    Shibasaka, M.4    Matsumoto, H.5
  • 112
    • 22144483650 scopus 로고    scopus 로고
    • Arabidopsis POLYOL TRANSPORTERS, a new member of the monosaccharide transporter-like superfamily, mediates H+ -symport of numerous substrates, including myo -inositol, glycerol, and ribose
    • Klepek Y.-S., Geiger D., Stadler R., Arabidopsis POLYOL TRANSPORTERS, a new member of the monosaccharide transporter-like superfamily, mediates H+ -symport of numerous substrates, including myo -inositol, glycerol, and ribose The Plant Cell 2005 17 1 204 218
    • (2005) The Plant Cell , vol.17 , Issue.1 , pp. 204-218
    • Klepek, Y.-S.1    Geiger, D.2    Stadler, R.3
  • 113
    • 0842285689 scopus 로고    scopus 로고
    • Differential expression of sucrose transporter and polyol transporter genes during maturation of common plantain companion cells
    • Ramsperger-Gleixner M., Geiger D., Hedrich R., Sauer N., Differential expression of sucrose transporter and polyol transporter genes during maturation of common plantain companion cells Plant Physiology 2004 134 1 147 160
    • (2004) Plant Physiology , vol.134 , Issue.1 , pp. 147-160
    • Ramsperger-Gleixner, M.1    Geiger, D.2    Hedrich, R.3    Sauer, N.4
  • 114
    • 33745649000 scopus 로고    scopus 로고
    • Arabidopsis INOSITOL TRANSPORTER4 mediates high-affinity H+ symport of myoinositol across the plasma membrane
    • Schneider S., Schneidereit A., Konrad K. R., Arabidopsis INOSITOL TRANSPORTER4 mediates high-affinity H+ symport of myoinositol across the plasma membrane Plant Physiology 2006 141 2 567 577
    • (2006) Plant Physiology , vol.141 , Issue.2 , pp. 567-577
    • Schneider, S.1    Schneidereit, A.2    Konrad, K.R.3
  • 115
    • 37249039463 scopus 로고    scopus 로고
    • Arabidopsis INOSITOL TRANSPORTER2 mediates H+ symport of different inositol epimers and derivatives across the plasma membrane
    • Schneider S., Schneidereit A., Udvardi P., Arabidopsis INOSITOL TRANSPORTER2 mediates H+ symport of different inositol epimers and derivatives across the plasma membrane Plant Physiology 2007 145 4 1395 1407
    • (2007) Plant Physiology , vol.145 , Issue.4 , pp. 1395-1407
    • Schneider, S.1    Schneidereit, A.2    Udvardi, P.3
  • 116
    • 33750015785 scopus 로고    scopus 로고
    • AtCAT6, a sink-tissue-localized transporter for essential amino acids in Arabidopsis
    • Hammes U. Z., Nielsen E., Honaas L. A., Taylor C. G., Schachtman D. P., AtCAT6, a sink-tissue-localized transporter for essential amino acids in Arabidopsis The Plant Journal 2006 48 3 414 426
    • (2006) The Plant Journal , vol.48 , Issue.3 , pp. 414-426
    • Hammes, U.Z.1    Nielsen, E.2    Honaas, L.A.3    Taylor, C.G.4    Schachtman, D.P.5
  • 117
    • 34247264463 scopus 로고    scopus 로고
    • Identification and functional characterization of cation-chloride cotransporters in plants
    • Colmenero-Flores J. M., Martnez G., Gamba G., Identification and functional characterization of cation-chloride cotransporters in plants The Plant Journal 2007 50 2 278 292
    • (2007) The Plant Journal , vol.50 , Issue.2 , pp. 278-292
    • Colmenero-Flores, J.M.1    Martnez, G.2    Gamba, G.3
  • 118
    • 37749035651 scopus 로고    scopus 로고
    • Not all ALMT1-type transporters mediate aluminum-activated organic acid responses: The case of ZmALMT1 an anion-selective transporter
    • Pieros M. A., Canado G. M. A., Maron L. G., Lyi S. M., Menossi M., Kochian L. V., Not all ALMT1-type transporters mediate aluminum-activated organic acid responses: the case of ZmALMT1 an anion-selective transporter The Plant Journal 2008 53 2 352 367
    • (2008) The Plant Journal , vol.53 , Issue.2 , pp. 352-367
    • Pieros, M.A.1    Canado, G.M.A.2    Maron, L.G.3    Lyi, S.M.4    Menossi, M.5    Kochian, L.V.6
  • 119
    • 0026579591 scopus 로고
    • Cloning and expression in yeast of a plant potassium ion transport system
    • Sentenac H., Bonneaud N., Minet M., Cloning and expression in yeast of a plant potassium ion transport system Science 1992 256 5057 663 665
    • (1992) Science , vol.256 , Issue.5057 , pp. 663-665
    • Sentenac, H.1    Bonneaud, N.2    Minet, M.3
  • 120
    • 0030998539 scopus 로고    scopus 로고
    • Plant K+ channel -subunits assemble indiscriminately
    • Dreyer I., Antunes S., Hoshi T., Plant K+ channel -subunits assemble indiscriminately Biophysical Journal 1997 72 5 2143 2150
    • (1997) Biophysical Journal , vol.72 , Issue.5 , pp. 2143-2150
    • Dreyer, I.1    Antunes, S.2    Hoshi, T.3
  • 121
    • 0034000565 scopus 로고    scopus 로고
    • Enhancement of Na+ uptake currents, time-dependent inward-rectifying K+ channel currents, and K+ channel transcripts by K+ starvation in wheat root cells
    • Buschmann P. H., Vaidyanathan R., Gassmann W., Schroeder J. I., Enhancement of Na+ uptake currents, time-dependent inward-rectifying K+ channel currents, and K+ channel transcripts by K+ starvation in wheat root cells Plant Physiology 2000 122 4 1387 1397
    • (2000) Plant Physiology , vol.122 , Issue.4 , pp. 1387-1397
    • Buschmann, P.H.1    Vaidyanathan, R.2    Gassmann, W.3    Schroeder, J.I.4
  • 122
    • 4344559464 scopus 로고    scopus 로고
    • DKT1, a novel K+ channel from carrot, forms functional heteromeric channels with KDC1
    • Formentin E., Varotto S., Costa A., DKT1, a novel K+ channel from carrot, forms functional heteromeric channels with KDC1 FEBS Letters 2004 573 13 61 67
    • (2004) FEBS Letters , vol.573 , Issue.13 , pp. 61-67
    • Formentin, E.1    Varotto, S.2    Costa, A.3
  • 123
    • 18644380098 scopus 로고    scopus 로고
    • Rice K+ uptake channel Os AKT1 is sensitive to salt stress
    • Fuchs I., Stlzle S., Ivashikina N., Hedrich R., Rice K+ uptake channel Os AKT1 is sensitive to salt stress Planta 2005 221 2 212 221
    • (2005) Planta , vol.221 , Issue.2 , pp. 212-221
    • Fuchs, I.1    Stlzle, S.2    Ivashikina, N.3    Hedrich, R.4
  • 124
    • 51749095497 scopus 로고    scopus 로고
    • Maize plasma membrane aquaporins belonging to the PIP1 and PIP2 subgroups are in vivo phosphorylated
    • Van Wilder V., Miecielica U., Degand H., Derua R., Waelkens E., Chaumont F., Maize plasma membrane aquaporins belonging to the PIP1 and PIP2 subgroups are in vivo phosphorylated Plant and Cell Physiology 2008 49 9 1364 1377
    • (2008) Plant and Cell Physiology , vol.49 , Issue.9 , pp. 1364-1377
    • Van Wilder, V.1    Miecielica, U.2    Degand, H.3    Derua, R.4    Waelkens, E.5    Chaumont, F.6
  • 125
    • 46449119266 scopus 로고    scopus 로고
    • Expression and purification of intact and functional soybean (Glycine max) seed ferritin complex in Escherichia coli
    • Dong X., Tang B., Li J., Xu Q., Fang S., Hua Z., Expression and purification of intact and functional soybean (Glycine max) seed ferritin complex in Escherichia coli Journal of Microbiology and Biotechnology 2008 18 2 299 307
    • (2008) Journal of Microbiology and Biotechnology , vol.18 , Issue.2 , pp. 299-307
    • Dong, X.1    Tang, B.2    Li, J.3    Xu, Q.4    Fang, S.5    Hua, Z.6
  • 126
    • 2342476496 scopus 로고    scopus 로고
    • The expression and processing of two recombinant 2S albumins from soybean (Glycine max) in the yeast Pichia pastoris
    • Lin J., Fido R., Shewry P., Archer D. B., Alcocer M. J. C., The expression and processing of two recombinant 2S albumins from soybean (Glycine max) in the yeast Pichia pastoris Biochimica et Biophysica Acta 2004 1698 2 203 212
    • (2004) Biochimica et Biophysica Acta , vol.1698 , Issue.2 , pp. 203-212
    • Lin, J.1    Fido, R.2    Shewry, P.3    Archer, D.B.4    Alcocer, M.J.C.5
  • 128
    • 0024461833 scopus 로고
    • The putative transposase of transposable element Ac from Zea mays L. interacts with subterminal sequences of Ac
    • Kunze R., Starlinger P., The putative transposase of transposable element Ac from Zea mays L. interacts with subterminal sequences of Ac The EMBO Journal 1989 8 11 3177 3185
    • (1989) The EMBO Journal , vol.8 , Issue.11 , pp. 3177-3185
    • Kunze, R.1    Starlinger, P.2
  • 129
    • 0025131867 scopus 로고
    • Secretion of functional papain precursor from insect cells. Requirement for N-glycosylation of the pro-region
    • Vernet T., Tessier D. C., Richardson C., Secretion of functional papain precursor from insect cells. Requirement for N-glycosylation of the pro-region The Journal of Biological Chemistry 1990 265 27 16661 16666
    • (1990) The Journal of Biological Chemistry , vol.265 , Issue.27 , pp. 16661-16666
    • Vernet, T.1    Tessier, D.C.2    Richardson, C.3
  • 130
  • 131
    • 0028500825 scopus 로고
    • LAT52 protein is essential for tomato pollen development: Pollen expressing antisense LAT52 RNA hydrates and germinates abnormally and cannot achieve fertilization
    • DOI 10.1046/j.1365-313X.1994.06030321.x
    • Muschietti J., Dircks L., Vancanneyt G., McCormick S., LAT52 protein is essential for tomato pollen development: pollen expressing antisense LAT52 RNA hydrates and germinates abnormally and cannot achieve fertilization The Plant Journal 1994 6 3 321 328 (Pubitemid 2135128)
    • (1994) Plant Journal , vol.6 , Issue.3 , pp. 321-328
    • Muschietti, J.1    Dircks, L.2    Vancanneyt, G.3    McCormick, S.4
  • 132
    • 0028486254 scopus 로고
    • Authentic processing and targeting of active maize auxin-binding protein in the baculovirus expression system
    • MacDonald H., Henderson J., Napier R. M., Venis M. A., Hawes C., Lazarus C. M., Authentic processing and targeting of active maize auxin-binding protein in the baculovirus expression system Plant Physiology 1994 105 4 1049 1057
    • (1994) Plant Physiology , vol.105 , Issue.4 , pp. 1049-1057
    • MacDonald, H.1    Henderson, J.2    Napier, R.M.3    Venis, M.A.4    Hawes, C.5    Lazarus, C.M.6
  • 133
    • 0033738566 scopus 로고    scopus 로고
    • Overexpression of auxin-binding protein enhances the sensitivity of guard cells to auxin
    • Bauly J. M., Sealy I. M., Macdonald H., Overexpression of auxin-binding protein enhances the sensitivity of guard cells to auxin Plant Physiology 2000 124 3 1229 1238
    • (2000) Plant Physiology , vol.124 , Issue.3 , pp. 1229-1238
    • Bauly, J.M.1    Sealy, I.M.2    MacDonald, H.3
  • 135
    • 0031105483 scopus 로고    scopus 로고
    • Isolation of a cDNA and a genomic clone encoding cinnamate 4-hydroxylase from Arabidopsis and its expression manner in planta
    • Mizutani M., Ohta D., Sato R., Isolation of a cDNA and a genomic clone encoding cinnamate 4-hydroxylase from Arabidopsis and its expression manner in planta Plant Physiology 1997 113 3 755 763
    • (1997) Plant Physiology , vol.113 , Issue.3 , pp. 755-763
    • Mizutani, M.1    Ohta, D.2    Sato, R.3
  • 136
    • 0038375339 scopus 로고    scopus 로고
    • Novel ATP-binding and autophosphorylation activity associated with Arabidopsis and human cryptochrome-1
    • Bouly J.-P., Giovani B., Djamei A., Novel ATP-binding and autophosphorylation activity associated with Arabidopsis and human cryptochrome-1 European Journal of Biochemistry 2003 270 14 2921 2928
    • (2003) European Journal of Biochemistry , vol.270 , Issue.14 , pp. 2921-2928
    • Bouly, J.-P.1    Giovani, B.2    Djamei, A.3
  • 137
    • 33846377245 scopus 로고    scopus 로고
    • Physiological roles of the light, oxygen, or voltage domains of phototropin 1 and phototropin 2 in Arabidopsis
    • Cho H.-Y., Tseng T.-S., Kaiserli E., Sullivan S., Christie J. M., Briggs W. R., Physiological roles of the light, oxygen, or voltage domains of phototropin 1 and phototropin 2 in Arabidopsis Plant Physiology 2007 143 1 517 529
    • (2007) Plant Physiology , vol.143 , Issue.1 , pp. 517-529
    • Cho, H.-Y.1    Tseng, T.-S.2    Kaiserli, E.3    Sullivan, S.4    Christie, J.M.5    Briggs, W.R.6
  • 138
    • 0026664116 scopus 로고
    • Overexpression of plant histidinol dehydrogenase using a baculovirus expression vector system
    • Nagai A., Suzuki K., Ward E., Overexpression of plant histidinol dehydrogenase using a baculovirus expression vector system Archives of Biochemistry and Biophysics 1992 295 2 235 239
    • (1992) Archives of Biochemistry and Biophysics , vol.295 , Issue.2 , pp. 235-239
    • Nagai, A.1    Suzuki, K.2    Ward, E.3
  • 139
    • 0028486021 scopus 로고
    • Cloning and expression of soluble epoxide hydrolase from potato
    • Stapleton A., Beetham J. K., Pinot F., Cloning and expression of soluble epoxide hydrolase from potato The Plant Journal 1994 6 2 251 258
    • (1994) The Plant Journal , vol.6 , Issue.2 , pp. 251-258
    • Stapleton, A.1    Beetham, J.K.2    Pinot, F.3
  • 140
    • 0029360768 scopus 로고
    • Insect cell expression of recombinant imidazoleglycerolphosphate dehydratase of Arabidopsis and wheat and inhibition by triazole herbicides
    • Tada S., Hatano M., Nakayama Y., Insect cell expression of recombinant imidazoleglycerolphosphate dehydratase of Arabidopsis and wheat and inhibition by triazole herbicides Plant Physiology 1995 109 1 153 159
    • (1995) Plant Physiology , vol.109 , Issue.1 , pp. 153-159
    • Tada, S.1    Hatano, M.2    Nakayama, Y.3
  • 141
    • 0030295013 scopus 로고    scopus 로고
    • Phytoene synthase from Narcissus pseudonarcissus: Functional expression, galactolipid requirement, topological distribution in chromoplasts and induction during flowering
    • Schledz M., Al-Babili S., von Lintig J., Phytoene synthase from Narcissus pseudonarcissus: functional expression, galactolipid requirement, topological distribution in chromoplasts and induction during flowering The Plant Journal 1996 10 5 781 792
    • (1996) The Plant Journal , vol.10 , Issue.5 , pp. 781-792
    • Schledz, M.1    Al-Babili, S.2    Von Lintig, J.3
  • 142
    • 0030138514 scopus 로고    scopus 로고
    • A novel, soluble form of phytoene desaturase from Narcissus pseudonarcissus chromoplasts is Hsp70-complexed and competent for flavinylation, membrane association and enzymatic activation
    • Al-Babili S., von Lintig J., Haubruck H., Beyer P., A novel, soluble form of phytoene desaturase from Narcissus pseudonarcissus chromoplasts is Hsp70-complexed and competent for flavinylation, membrane association and enzymatic activation The Plant Journal 1996 9 5 601 612
    • (1996) The Plant Journal , vol.9 , Issue.5 , pp. 601-612
    • Al-Babili, S.1    Von Lintig, J.2    Haubruck, H.3    Beyer, P.4
  • 143
    • 0031990783 scopus 로고    scopus 로고
    • 4-coumarate:coenzyme a ligase in hybrid poplar. Properties of native enzymes, cDNA cloning, and analysis of recombinant enzymes
    • Allina S. M., Pri-Hadash A., Theilmann D. A., Ellis B. E., Douglas C. J., 4-coumarate:coenzyme a ligase in hybrid poplar. Properties of native enzymes, cDNA cloning, and analysis of recombinant enzymes Plant Physiology 1998 116 2 743 754
    • (1998) Plant Physiology , vol.116 , Issue.2 , pp. 743-754
    • Allina, S.M.1    Pri-Hadash, A.2    Theilmann, D.A.3    Ellis, B.E.4    Douglas, C.J.5
  • 144
    • 85047684611 scopus 로고    scopus 로고
    • A grapevine gene encoding a guard cell K+ channel displays developmental regulation in the grapevine berry
    • Pratelli R., Lacombe B., Torregrosa L., A grapevine gene encoding a guard cell K+ channel displays developmental regulation in the grapevine berry Plant Physiology 2002 128 2 564 577
    • (2002) Plant Physiology , vol.128 , Issue.2 , pp. 564-577
    • Pratelli, R.1    Lacombe, B.2    Torregrosa, L.3
  • 145
    • 0037931738 scopus 로고    scopus 로고
    • The K+ channel KZM1 mediates potassium uptake into the phloem and guard cells of the C4 grass Zea mays
    • Philippar K., Bchsenschtz K., Abshagen M., The K+ channel KZM1 mediates potassium uptake into the phloem and guard cells of the C4 grass Zea mays The Journal of Biological Chemistry 2003 278 19 16973 16981
    • (2003) The Journal of Biological Chemistry , vol.278 , Issue.19 , pp. 16973-16981
    • Philippar, K.1    Bchsenschtz, K.2    Abshagen, M.3
  • 147
    • 0034117309 scopus 로고    scopus 로고
    • Functional characterisation of LKT1, a K+ uptake channel from tomato root hairs, and comparison with the closely related potato inwardly rectifying K+ channel SKT1 after expression in Xenopus oocytes
    • Hartje S., Zimmermann S., Klonus D., Mueller-Roeber B., Functional characterisation of LKT1, a K+ uptake channel from tomato root hairs, and comparison with the closely related potato inwardly rectifying K+ channel SKT1 after expression in Xenopus oocytes Planta 2000 210 5 723 731
    • (2000) Planta , vol.210 , Issue.5 , pp. 723-731
    • Hartje, S.1    Zimmermann, S.2    Klonus, D.3    Mueller-Roeber, B.4
  • 148
    • 33846979782 scopus 로고    scopus 로고
    • Increased functional diversity of plant K+ channels by preferential heteromerization of the Shaker-like subunits AKT2 and KAT2
    • Xicluna J., Lacombe B., Dreyer I., Increased functional diversity of plant K+ channels by preferential heteromerization of the Shaker-like subunits AKT2 and KAT2 The Journal of Biological Chemistry 2007 282 1 486 494
    • (2007) The Journal of Biological Chemistry , vol.282 , Issue.1 , pp. 486-494
    • Xicluna, J.1    Lacombe, B.2    Dreyer, I.3
  • 149
    • 33845966427 scopus 로고    scopus 로고
    • The potassium channel KAT1 is activated by plant and animal 14-3-3 proteins
    • Sottocornola B., Visconti S., Orsi S., The potassium channel KAT1 is activated by plant and animal 14-3-3 proteins The Journal of Biological Chemistry 2006 281 47 35735 35741
    • (2006) The Journal of Biological Chemistry , vol.281 , Issue.47 , pp. 35735-35741
    • Sottocornola, B.1    Visconti, S.2    Orsi, S.3
  • 150
    • 85047682135 scopus 로고    scopus 로고
    • Electrophysiological analysis of cloned cyclic nucleotide-gated ion channels
    • Leng Q., Mercier R. W., Hua B.-G., Fromm H., Berkowitz G. A., Electrophysiological analysis of cloned cyclic nucleotide-gated ion channels Plant Physiology 2002 128 2 400 410
    • (2002) Plant Physiology , vol.128 , Issue.2 , pp. 400-410
    • Leng, Q.1    Mercier, R.W.2    Hua, B.-G.3    Fromm, H.4    Berkowitz, G.A.5
  • 151
    • 0038715131 scopus 로고    scopus 로고
    • Plants do it differently. A new basis for potassium/sodium selectivity in the pore of an ion channel
    • Hua B.-G., Mercier R. W., Leng Q., Berkowitz G. A., Plants do it differently. A new basis for potassium/sodium selectivity in the pore of an ion channel Plant Physiology 2003 132 3 1353 1361
    • (2003) Plant Physiology , vol.132 , Issue.3 , pp. 1353-1361
    • Hua, B.-G.1    Mercier, R.W.2    Leng, Q.3    Berkowitz, G.A.4
  • 152
    • 20444489270 scopus 로고    scopus 로고
    • GmN70 and LjN70. Anion transporters of the symbiosome membrane of nodules with a transport preference for nitrate
    • Vincill E. D., Szczyglowski K., Roberts D. M., GmN70 and LjN70. Anion transporters of the symbiosome membrane of nodules with a transport preference for nitrate Plant Physiology 2005 137 4 1435 1444
    • (2005) Plant Physiology , vol.137 , Issue.4 , pp. 1435-1444
    • Vincill, E.D.1    Szczyglowski, K.2    Roberts, D.M.3
  • 153
    • 51749103887 scopus 로고    scopus 로고
    • Novel properties of the wheat aluminum tolerance organic acid transporter (TaALMT1) revealed by electrophysiological characterization in Xenopus oocytes: Functional and structural implications
    • Pieros M. A., Canado G. M. A., Kochian L. V., Novel properties of the wheat aluminum tolerance organic acid transporter (TaALMT1) revealed by electrophysiological characterization in Xenopus oocytes: functional and structural implications Plant Physiology 2008 147 4 2131 2146
    • (2008) Plant Physiology , vol.147 , Issue.4 , pp. 2131-2146
    • Pieros, M.A.1    Canado, G.M.A.2    Kochian, L.V.3
  • 154
    • 33646342506 scopus 로고    scopus 로고
    • AtGAT1, a high affinity transporter for -aminobutyric acid in Arabidopsis thaliana
    • Meyer A., Eskandari S., Grallath S., Rentsch D., AtGAT1, a high affinity transporter for -aminobutyric acid in Arabidopsis thaliana The Journal of Biological Chemistry 2006 281 11 7197 7204
    • (2006) The Journal of Biological Chemistry , vol.281 , Issue.11 , pp. 7197-7204
    • Meyer, A.1    Eskandari, S.2    Grallath, S.3    Rentsch, D.4
  • 155
    • 0033996879 scopus 로고    scopus 로고
    • Plasma membrane intrinsic proteins from maize cluster in two sequence subgroups with differential aquaporin activity
    • Chaumont F., Barrieu F., Jung R., Chrispeels M. J., Plasma membrane intrinsic proteins from maize cluster in two sequence subgroups with differential aquaporin activity Plant Physiology 2000 122 4 1025 1034
    • (2000) Plant Physiology , vol.122 , Issue.4 , pp. 1025-1034
    • Chaumont, F.1    Barrieu, F.2    Jung, R.3    Chrispeels, M.J.4
  • 156
    • 0033737020 scopus 로고    scopus 로고
    • Permeability and channel-mediated transport of boric acid across membrane vesicles isolated from squash roots
    • Dordas C., Chrispeels M. J., Brown P. H., Permeability and channel-mediated transport of boric acid across membrane vesicles isolated from squash roots Plant Physiology 2000 124 3 1349 1361
    • (2000) Plant Physiology , vol.124 , Issue.3 , pp. 1349-1361
    • Dordas, C.1    Chrispeels, M.J.2    Brown, P.H.3
  • 157
    • 0034850787 scopus 로고    scopus 로고
    • Characterization of two tomato aquaporins and expression during the incompatible interaction of tomato with the plant parasite Cuscuta reflexa
    • Werner M., Uehlein N., Proksch P., Kaldenhoff R., Characterization of two tomato aquaporins and expression during the incompatible interaction of tomato with the plant parasite Cuscuta reflexa Planta 2001 213 4 550 555
    • (2001) Planta , vol.213 , Issue.4 , pp. 550-555
    • Werner, M.1    Uehlein, N.2    Proksch, P.3    Kaldenhoff, R.4
  • 158
    • 0142214660 scopus 로고    scopus 로고
    • Plasma membrane aquaporins are involved in winter embolism recovery in walnut tree
    • Sakr S., Alves G., Morillon R., Plasma membrane aquaporins are involved in winter embolism recovery in walnut tree Plant Physiology 2003 133 2 630 641
    • (2003) Plant Physiology , vol.133 , Issue.2 , pp. 630-641
    • Sakr, S.1    Alves, G.2    Morillon, R.3
  • 159
    • 0345392686 scopus 로고    scopus 로고
    • Urea transport by nitrogen-regulated tonoplast intrinsic proteins in Arabidopsis
    • Liu L.-H., Ludewig U., Gassert B., Frommer W. B., von Wirn N., Urea transport by nitrogen-regulated tonoplast intrinsic proteins in Arabidopsis Plant Physiology 2003 133 3 1220 1228
    • (2003) Plant Physiology , vol.133 , Issue.3 , pp. 1220-1228
    • Liu, L.-H.1    Ludewig, U.2    Gassert, B.3    Frommer, W.B.4    Von Wirn, N.5
  • 160
    • 19044393297 scopus 로고    scopus 로고
    • Tonoplast intrinsic proteins AtTIP2;1 and AtTIP2;3 facilitate NH3 transport into the vacuole
    • Loqu D., Ludewig U., Yuan L., von Wirn N., Tonoplast intrinsic proteins AtTIP2;1 and AtTIP2;3 facilitate NH3 transport into the vacuole Plant Physiology 2005 137 2 671 680
    • (2005) Plant Physiology , vol.137 , Issue.2 , pp. 671-680
    • Loqu, D.1    Ludewig, U.2    Yuan, L.3    Von Wirn, N.4
  • 163
    • 34247254303 scopus 로고    scopus 로고
    • Isolation and functional characterization of PgTIP1, a hormone-autotrophic cells-specific tonoplast aquaporin in ginseng
    • Lin W., Peng Y., Li G., Isolation and functional characterization of PgTIP1, a hormone-autotrophic cells-specific tonoplast aquaporin in ginseng Journal of Experimental Botany 2007 58 5 947 956
    • (2007) Journal of Experimental Botany , vol.58 , Issue.5 , pp. 947-956
    • Lin, W.1    Peng, Y.2    Li, G.3
  • 164
    • 34548227925 scopus 로고    scopus 로고
    • Arabidopsis NIP2;1, a major intrinsic protein transporter of lactic acid induced by anoxic stress
    • Choi W.-G., Roberts D. M., Arabidopsis NIP2;1, a major intrinsic protein transporter of lactic acid induced by anoxic stress The Journal of Biological Chemistry 2007 282 33 24209 24218
    • (2007) The Journal of Biological Chemistry , vol.282 , Issue.33 , pp. 24209-24218
    • Choi, W.-G.1    Roberts, D.M.2
  • 165
    • 44449104056 scopus 로고    scopus 로고
    • Drought stress alters water relations and expression of PIP -type aquaporin genes in Nicotiana tabacum plants
    • Mahdieh M., Mostajeran A., Horie T., Katsuhara M., Drought stress alters water relations and expression of PIP -type aquaporin genes in Nicotiana tabacum plants Plant and Cell Physiology 2008 49 5 801 813
    • (2008) Plant and Cell Physiology , vol.49 , Issue.5 , pp. 801-813
    • Mahdieh, M.1    Mostajeran, A.2    Horie, T.3    Katsuhara, M.4
  • 166
    • 0037457993 scopus 로고    scopus 로고
    • Involvement of CjMDR1, a plant multidrugresistance-type ATP-binding cassette protein, in alkaloid transport in Coptis japonica
    • Shitan N., Bazin I., Dan K., Involvement of CjMDR1, a plant multidrugresistance-type ATP-binding cassette protein, in alkaloid transport in Coptis japonica Proceedings of the National Academy of Sciences of the United States of America 2003 100 2 751 756
    • (2003) Proceedings of the National Academy of Sciences of the United States of America , vol.100 , Issue.2 , pp. 751-756
    • Shitan, N.1    Bazin, I.2    Dan, K.3
  • 167
    • 33644808731 scopus 로고    scopus 로고
    • A novel plant major intrinsic protein in Physcomitrella patens most similar to bacterial glycerol channels
    • Gustavsson S., Lebrun A.-S., Nordn K., Chaumont F., Johanson U., A novel plant major intrinsic protein in Physcomitrella patens most similar to bacterial glycerol channels Plant Physiology 2005 139 1 287 295
    • (2005) Plant Physiology , vol.139 , Issue.1 , pp. 287-295
    • Gustavsson, S.1    Lebrun, A.-S.2    Nordn, K.3    Chaumont, F.4    Johanson, U.5
  • 168
    • 8144228134 scopus 로고    scopus 로고
    • AtTPK4, an Arabidopsis tandem-pore K+ channel, poised to control the pollen membrane voltage in a pH- and Ca2+ -dependent manner
    • Becker D., Geiger D., Dunkel M., AtTPK4, an Arabidopsis tandem-pore K+ channel, poised to control the pollen membrane voltage in a pH- and Ca2+ -dependent manner Proceedings of the National Academy of Sciences of the United States of America 2004 101 44 15621 15626
    • (2004) Proceedings of the National Academy of Sciences of the United States of America , vol.101 , Issue.44 , pp. 15621-15626
    • Becker, D.1    Geiger, D.2    Dunkel, M.3
  • 169
    • 34248185333 scopus 로고    scopus 로고
    • The FRD3-mediated efflux of citrate into the root vasculature is necessary for efficient iron translocation
    • Durrett T. P., Gassmann W., Rogers E. E., The FRD3-mediated efflux of citrate into the root vasculature is necessary for efficient iron translocation Plant Physiology 2007 144 1 197 205
    • (2007) Plant Physiology , vol.144 , Issue.1 , pp. 197-205
    • Durrett, T.P.1    Gassmann, W.2    Rogers, E.E.3
  • 170
    • 0034003618 scopus 로고    scopus 로고
    • Plant cells are not just green yeast
    • Bassham D. C., Raikhel N. V., Plant cells are not just green yeast Plant Physiology 2000 122 4 999 1001
    • (2000) Plant Physiology , vol.122 , Issue.4 , pp. 999-1001
    • Bassham, D.C.1    Raikhel, N.V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.