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Volumn 3, Issue 7, 2004, Pages 675-691

Identification of new intrinsic proteins in Arabidopsis plasma membrane proteome

Author keywords

[No Author keywords available]

Indexed keywords

ADENINE PHOSPHORIBOSYLTRANSFERASE; ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR; ALPHA TUBULIN; ARF PROTEIN; AUXIN; CARRIER PROTEIN; COTRANSPORTER; ELONGATION FACTOR 1ALPHA; GLUCOSE TRANSPORTER; GLUTATHIONE PEROXIDASE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; GUANINE NUCLEOTIDE BINDING PROTEIN; MEMBRANE PROTEIN; NODULIN; PHOSPHATE TRANSPORTER; PHOSPHATIDATE PHOSPHATASE; PHOSPHOLIPID HYDROPEROXIDE GLUTATHIONE PEROXIDASE; POLYPHOSPHOINOSITIDE; PORIN; PROTEIN KINASE; PROTEIN SERINE THREONINE KINASE; PROTEOME; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE; RAB PROTEIN; RAS PROTEIN; SNARE PROTEIN; SUPEROXIDE DISMUTASE; SYNAPTOBREVIN; SYNTAXIN;

EID: 4143128922     PISSN: 15359476     EISSN: None     Source Type: Journal    
DOI: 10.1074/mcp.M400001-MCP200     Document Type: Review
Times cited : (230)

References (107)
  • 2
    • 0034649566 scopus 로고    scopus 로고
    • Analysis of the genome sequence of the flowering plant Arabidopsis thaliana
    • Arabidopsis Genome Initiative
    • Arabidopsis Genome Initiative (2000) Analysis of the genome sequence of the flowering plant Arabidopsis thaliana. Nature 408, 796-815
    • (2000) Nature , vol.408 , pp. 796-815
  • 3
    • 0034954896 scopus 로고    scopus 로고
    • Identification of novel families of membrane proteins from the model plant Arabidopsis thaliana
    • Ward, J. M. (2001) Identification of novel families of membrane proteins from the model plant Arabidopsis thaliana. Bioinformatics 17, 560-563
    • (2001) Bioinformatics , vol.17 , pp. 560-563
    • Ward, J.M.1
  • 5
    • 0028795097 scopus 로고
    • Basic plasticity of protein expression in tobacco leaf plasma membrane
    • Masson, F., and Rossignol, M. (1995) Basic plasticity of protein expression in tobacco leaf plasma membrane. Plant J. 8, 77-85
    • (1995) Plant J. , vol.8 , pp. 77-85
    • Masson, F.1    Rossignol, M.2
  • 6
    • 0029079397 scopus 로고
    • Identification of cDNA clones encoding valosin-containing protein and other plant plasma membrane-associated proteins by a general immunoscreening strategy
    • Shi, J., Dixon, R. A., Gonzales, R. A., Kjellbom, P., and Bhattacharyya, M. K. (1995) Identification of cDNA clones encoding valosin-containing protein and other plant plasma membrane-associated proteins by a general immunoscreening strategy. Proc. Natl. Acad. Sci. U. S. A. 92, 4457-4461
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 4457-4461
    • Shi, J.1    Dixon, R.A.2    Gonzales, R.A.3    Kjellbom, P.4    Bhattacharyya, M.K.5
  • 7
    • 0033040145 scopus 로고    scopus 로고
    • Construction of two ordered cDNA libraries enriched in genes encoding plasmalemma and tonoplast proteins from a high-efficiency expression library
    • Galaud, J. P., Carriere, M., Pauly, N., Canut, H., Chalon, P., Caput, D., and Pont-Lezica, R. F. (1999) Construction of two ordered cDNA libraries enriched in genes encoding plasmalemma and tonoplast proteins from a high-efficiency expression library. Plant J. 17, 111-118
    • (1999) Plant J. , vol.17 , pp. 111-118
    • Galaud, J.P.1    Carriere, M.2    Pauly, N.3    Canut, H.4    Chalon, P.5    Caput, D.6    Pont-Lezica, R.F.7
  • 8
    • 0030561540 scopus 로고    scopus 로고
    • Signal sequence trap to clone cDNAs encoding secreted or membrane-associated plant proteins
    • Kristoffersen, P., Teichmann, T., Stracke, R., and Palme, K. (1996) Signal sequence trap to clone cDNAs encoding secreted or membrane-associated plant proteins. Anal. Biochem. 243, 127-132
    • (1996) Anal. Biochem. , vol.243 , pp. 127-132
    • Kristoffersen, P.1    Teichmann, T.2    Stracke, R.3    Palme, K.4
  • 10
    • 0030961920 scopus 로고    scopus 로고
    • Construction of a directory of tobacco plasma membrane proteins by combined two-dimensional gel electrophoresis and protein sequencing
    • Rouquie, D., Peltier, J. B., Marquis-Mansion, M., Tournaire, C., Doumas, P., and Rossignol, M. (1997) Construction of a directory of tobacco plasma membrane proteins by combined two-dimensional gel electrophoresis and protein sequencing. Electrophoresis 18, 654-660
    • (1997) Electrophoresis , vol.18 , pp. 654-660
    • Rouquie, D.1    Peltier, J.B.2    Marquis-Mansion, M.3    Tournaire, C.4    Doumas, P.5    Rossignol, M.6
  • 12
    • 0034120122 scopus 로고    scopus 로고
    • Proteomic analysis of the human colon carcinoma cell line (LIM 1215): Development of a membrane protein database
    • Simpson, R. J., Connolly, L. M., Eddes, J. S., Pereira, J. J., Moritz, R. L., and Reid, G. E. (2000) Proteomic analysis of the human colon carcinoma cell line (LIM 1215): Development of a membrane protein database. Electrophoresis 21, 1707-1732
    • (2000) Electrophoresis , vol.21 , pp. 1707-1732
    • Simpson, R.J.1    Connolly, L.M.2    Eddes, J.S.3    Pereira, J.J.4    Moritz, R.L.5    Reid, G.E.6
  • 13
    • 0031837579 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis of proteins in an immobilized pH 4-12 gradient
    • Gorg, A., Boguth, G., Obermaier, C., and Weiss, W. (1998) Two-dimensional electrophoresis of proteins in an immobilized pH 4-12 gradient. Electrophoresis 19, 1516-1519
    • (1998) Electrophoresis , vol.19 , pp. 1516-1519
    • Gorg, A.1    Boguth, G.2    Obermaier, C.3    Weiss, W.4
  • 14
    • 0037347236 scopus 로고    scopus 로고
    • Evaluation of nonionic and zwitterionic detergents as membrane protein solubilizers in two-dimensional electrophoresis
    • Luche, S., Santoni, V., and Rabilloud, T. (2003) Evaluation of nonionic and zwitterionic detergents as membrane protein solubilizers in two-dimensional electrophoresis. Proteomics 3, 249-253
    • (2003) Proteomics , vol.3 , pp. 249-253
    • Luche, S.1    Santoni, V.2    Rabilloud, T.3
  • 15
    • 0031026920 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis of membrane proteins: A current challenge for immobilized pH gradients
    • Adessi, C., Miege, C., Albrieux, C., and Rabilloud, T. (1997) Two-dimensional electrophoresis of membrane proteins: a current challenge for immobilized pH gradients. Electrophoresis 18, 127-135
    • (1997) Electrophoresis , vol.18 , pp. 127-135
    • Adessi, C.1    Miege, C.2    Albrieux, C.3    Rabilloud, T.4
  • 16
    • 0031861758 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis for proteome projects: The effects of protein hydrophobicity and copy number
    • Wilkins, M. R., Gasteiger, E., Sanchez, J. C., Bairoch, A., and Hochstrasser, D. F. (1998) Two-dimensional gel electrophoresis for proteome projects: The effects of protein hydrophobicity and copy number. Electrophoresis 19, 1501-1505
    • (1998) Electrophoresis , vol.19 , pp. 1501-1505
    • Wilkins, M.R.1    Gasteiger, E.2    Sanchez, J.C.3    Bairoch, A.4    Hochstrasser, D.F.5
  • 19
    • 0033778077 scopus 로고    scopus 로고
    • Membrane proteomics: Use of additive main effects with multiplicative interaction model to classify plasma membrane proteins according to their solubility and electrophoretic properties
    • Santoni, V., Kieffer, S., Desclaux, D., Masson, F., and Rabilloud, T. (2000) Membrane proteomics: Use of additive main effects with multiplicative interaction model to classify plasma membrane proteins according to their solubility and electrophoretic properties. Electrophoresis 21, 3329-3344
    • (2000) Electrophoresis , vol.21 , pp. 3329-3344
    • Santoni, V.1    Kieffer, S.2    Desclaux, D.3    Masson, F.4    Rabilloud, T.5
  • 20
    • 0034066471 scopus 로고    scopus 로고
    • Membrane proteins and proteomics: Un amour impossible?
    • Santoni, V., Molloy, M., and Rabilloud, T. (2000) Membrane proteins and proteomics: Un amour impossible? Electrophoresis 21, 1054-1070
    • (2000) Electrophoresis , vol.21 , pp. 1054-1070
    • Santoni, V.1    Molloy, M.2    Rabilloud, T.3
  • 21
    • 0037934549 scopus 로고    scopus 로고
    • Subcellular proteomics
    • Dreger, M. (2003) Subcellular proteomics. Mass Spectrom. Rev. 22, 27-56
    • (2003) Mass Spectrom Rev. , vol.22 , pp. 27-56
    • Dreger, M.1
  • 24
    • 0037667409 scopus 로고    scopus 로고
    • A proteomic study reveals novel insights into the diversity of aquaporin forms expressed in the plasma membrane of plant roots
    • Santoni, V., Vinh, J., Pflieger, D., Sommerer, N., and Maurel, C. (2003) A proteomic study reveals novel insights into the diversity of aquaporin forms expressed in the plasma membrane of plant roots. Biochem. J. 373, 289-296
    • (2003) Biochem. J. , vol.373 , pp. 289-296
    • Santoni, V.1    Vinh, J.2    Pflieger, D.3    Sommerer, N.4    Maurel, C.5
  • 25
    • 0035044161 scopus 로고    scopus 로고
    • A novel subfractionation approach for mitochondrial proteins: A three-dimensional mitochondrial proteome map
    • Hanson, B. J., Schulenberg, B., Patton, W. F., and Capaldi, R. A. (2001) A novel subfractionation approach for mitochondrial proteins: A three-dimensional mitochondrial proteome map. Electrophoresis 22, 950-959
    • (2001) Electrophoresis , vol.22 , pp. 950-959
    • Hanson, B.J.1    Schulenberg, B.2    Patton, W.F.3    Capaldi, R.A.4
  • 26
    • 85047683107 scopus 로고    scopus 로고
    • Proteomic approach to identify novel mitochondrial proteins in Arabidopsis
    • Kruft, V., Eubel, H., Jansch, L., Werhahn, W., and Braun, H. P. (2001) Proteomic approach to identify novel mitochondrial proteins in Arabidopsis. Plant Physiol. 127, 1694-1710
    • (2001) Plant Physiol. , vol.127 , pp. 1694-1710
    • Kruft, V.1    Eubel, H.2    Jansch, L.3    Werhahn, W.4    Braun, H.P.5
  • 27
    • 0032881817 scopus 로고    scopus 로고
    • Technical Advance: Differential extraction of hydrophobic proteins from chloroplast envelope membranes: A subcellular-specific proteomic approach to identify rare intrinsic membrane proteins
    • Seigneurin-Berny, D., Rolland, N., Garin, J., and Joyard, J. (1999) Technical Advance: Differential extraction of hydrophobic proteins from chloroplast envelope membranes: A subcellular-specific proteomic approach to identify rare intrinsic membrane proteins. Plant J. 19, 217-228
    • (1999) Plant J. , vol.19 , pp. 217-228
    • Seigneurin-Berny, D.1    Rolland, N.2    Garin, J.3    Joyard, J.4
  • 28
    • 0034026047 scopus 로고    scopus 로고
    • Proteomics of the chloroplast: Systematic identification and targeting analysis of lumenal and peripheral thylakoid proteins
    • Peltier, J. B., Friso, G., Kalume, D. E., Roepstorff, P., Nilsson, F., Adamska, I., and van Wijk, K. J. (2000) Proteomics of the chloroplast: Systematic identification and targeting analysis of lumenal and peripheral thylakoid proteins. Plant Cell 12, 319-341
    • (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    Adamska, I.6    van Wijk, K.J.7
  • 31
    • 0036051481 scopus 로고    scopus 로고
    • The chloroplast grana proteome defined by intact mass measurements from liquid chromatography mass spectrometry
    • Gomez, S. M., Nishio, J. N., Faull, K. F., and Whitelegge, J. P. (2002) The chloroplast grana proteome defined by intact mass measurements from liquid chromatography mass spectrometry. Mol. Cell. Proteomics 1, 46-59
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 46-59
    • Gomez, S.M.1    Nishio, J.N.2    Faull, K.F.3    Whitelegge, J.P.4
  • 32
    • 2642529334 scopus 로고    scopus 로고
    • Two-dimensional blue native/SDS gel electrophoresis of multi-protein complexes from whole cellular lysates: A proteomics approach
    • Camacho-Carvajal, M. M., Wollscheid, B., Aebersold, R., Steimle, V., and Schamel, W. W. (2004) Two-dimensional blue native/SDS gel electrophoresis of multi-protein complexes from whole cellular lysates: A proteomics approach. Mol. Cell. Proteomics 3, 176-182
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 176-182
    • Camacho-Carvajal, M.M.1    Wollscheid, B.2    Aebersold, R.3    Steimle, V.4    Schamel, W.W.5
  • 34
    • 84980140250 scopus 로고
    • Croissance et synthèse des protéines de suspensions cellulaires de tabac sensibles à la kinétine
    • Jouanneau, J. P., and Péaud-Lenoël, C. (1967) Croissance et synthèse des protéines de suspensions cellulaires de tabac sensibles à la kinétine. Physiol. Plantarum 20, 834-850
    • (1967) Physiol. Plantarum , vol.20 , pp. 834-850
    • Jouanneau, J.P.1    Péaud-Lenoël, C.2
  • 35
    • 0040290255 scopus 로고
    • Preparation of sealed tonoplast and plasma-membrane vesicles from Catharanthus roseus (L.) G. Don. cells by free-flow electrophoresis
    • Canut, H., Baudracco, S., Cabané, M., Boudet, A. M., and Marigo, G. (1991) Preparation of sealed tonoplast and plasma-membrane vesicles from Catharanthus roseus (L.) G. Don. cells by free-flow electrophoresis. Planta 184, 448-456
    • (1991) Planta , vol.184 , pp. 448-456
    • Canut, H.1    Baudracco, S.2    Cabané, M.3    Boudet, A.M.4    Marigo, G.5
  • 36
    • 77957095712 scopus 로고
    • Preparation of high-purity plasma membranes
    • Larsson, C., Widell, S., and Kjellbom, P. (1987) Preparation of high-purity plasma membranes. Methods Enzymol. 148, 558-568
    • (1987) Methods Enzymol. , vol.148 , pp. 558-568
    • Larsson, C.1    Widell, S.2    Kjellbom, P.3
  • 37
    • 0019149326 scopus 로고
    • Removal of polyethylene glycol from proteins by salt-induced phase separation
    • Busby, T. F., and Ingham, K. C. (1980) Removal of polyethylene glycol from proteins by salt-induced phase separation. Vox Sang. 39, 93-100
    • (1980) Vox Sang. , vol.39 , pp. 93-100
    • Busby, T.F.1    Ingham, K.C.2
  • 38
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 39
    • 77957077486 scopus 로고
    • Isolation of the plasma membrane: Membrane markers and general principles
    • Briskin, D. P., Leonard, R. T., and Hodges, T. K. (1987) Isolation of the plasma membrane: Membrane markers and general principles. Methods Enzymol. 148, 542-558
    • (1987) Methods Enzymol. , vol.148 , pp. 542-558
    • Briskin, D.P.1    Leonard, R.T.2    Hodges, T.K.3
  • 41
    • 0033773868 scopus 로고    scopus 로고
    • Organic solvent extraction as a versatile procedure to identify hydrophobic chloroplast membrane proteins
    • Ferro, M., Seigneurin-Berny, D., Rolland, N., Chapel, A., Salvi, D., Garin, J., and Joyard, J. (2000) Organic solvent extraction as a versatile procedure to identify hydrophobic chloroplast membrane proteins. Electrophoresis 21, 3517-3526
    • (2000) Electrophoresis , vol.21 , pp. 3517-3526
    • Ferro, M.1    Seigneurin-Berny, D.2    Rolland, N.3    Chapel, A.4    Salvi, D.5    Garin, J.6    Joyard, J.7
  • 42
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., and Doolittle, R. F. (1982) A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157, 105-132
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 43
    • 0030989517 scopus 로고    scopus 로고
    • Removal of a cryptic intron and subcellular localization of green fluorescent protein are required to mark transgenic Arabidopsis plants brightly
    • Haseloff, J., Siemering, K. R., Prasher, D. C., and Hodge, S. (1997) Removal of a cryptic intron and subcellular localization of green fluorescent protein are required to mark transgenic Arabidopsis plants brightly. Proc. Natl. Acad. Sci. U. S. A. 94, 2122-2127
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 2122-2127
    • Haseloff, J.1    Siemering, K.R.2    Prasher, D.C.3    Hodge, S.4
  • 44
    • 0032030760 scopus 로고    scopus 로고
    • Soluble, highly fluorescent variants of green fluorescent protein (GFP) for use in higher plants
    • Davis, S. J., and Vierstra, R. D. (1998) Soluble, highly fluorescent variants of green fluorescent protein (GFP) for use in higher plants. Plant Mol. Biol. 36, 521-528
    • (1998) Plant Mol. Biol. , vol.36 , pp. 521-528
    • Davis, S.J.1    Vierstra, R.D.2
  • 45
    • 0038468540 scopus 로고    scopus 로고
    • AtNRAMP3, a multispecific vacuolar metal transporter involved in plant responses to iron deficiency
    • Thomine, S., Lelievre, F., Debarbieux, E., Schroeder, J. I., and Barbier-Brygoo, H. (2003) AtNRAMP3, a multispecific vacuolar metal transporter involved in plant responses to iron deficiency. Plant J. 34, 685-695
    • (2003) Plant J. , vol.34 , pp. 685-695
    • Thomine, S.1    Lelievre, F.2    Debarbieux, E.3    Schroeder, J.I.4    Barbier-Brygoo, H.5
  • 46
    • 0020490258 scopus 로고
    • Characterization of envelope membrane polypeptides from spinach chloroplasts
    • Joyard, J., Grossman, A., Bartlett, S. G., Douce, R., and Chua, N. H. (1982) Characterization of envelope membrane polypeptides from spinach chloroplasts. J. Biol. Chem. 257, 1095-1101
    • (1982) J. Biol. Chem. , vol.257 , pp. 1095-1101
    • Joyard, J.1    Grossman, A.2    Bartlett, S.G.3    Douce, R.4    Chua, N.H.5
  • 47
    • 0026582987 scopus 로고
    • Functionalexpression of a plant plasma membrane transporter in Xenopus, oocytes
    • Boorer, K. J., Forde, B. G., Leigh, R. A., and Miller, A. J. (1992) Functional expression of a plant plasma membrane transporter in Xenopus, oocytes. FEBS Lett. 302, 166-168
    • (1992) FEBS Lett. , vol.302 , pp. 166-168
    • Boorer, K.J.1    Forde, B.G.2    Leigh, R.A.3    Miller, A.J.4
  • 48
    • 0029132614 scopus 로고
    • +-ATPase (a highly regulated enzyme with multiple physiological functions)
    • +-ATPase (a highly regulated enzyme with multiple physiological functions). Plant Physiol. 108, 1-6
    • (1995) Plant Physiol. , vol.108 , pp. 1-6
    • Michelet, B.1    Boutry, M.2
  • 50
    • 0035984061 scopus 로고    scopus 로고
    • The Arabidopsis SKU5 gene encodes an extracellular glycosyl phosphatidylinositol-anchored glycoprotein involved in directional root growth
    • Sedbrook, J. C., Carroll, K. L., Hung, K. F., Masson, P. H., and Somerville, C. R. (2002) The Arabidopsis SKU5 gene encodes an extracellular glycosyl phosphatidylinositol-anchored glycoprotein involved in directional root growth. Plant Cell 14, 1635-1648
    • (2002) Plant Cell , vol.14 , pp. 1635-1648
    • Sedbrook, J.C.1    Carroll, K.L.2    Hung, K.F.3    Masson, P.H.4    Somerville, C.R.5
  • 51
    • 0034724178 scopus 로고    scopus 로고
    • Random GFP::CDNA fusions enable visualization of subcellular structures in cells of Arabidopsis at a high frequency
    • Cutler, S. R., Ehrhardt, D. W., Griffitts, J. S., and Somerville, C. R. (2000) Random GFP::cDNA fusions enable visualization of subcellular structures in cells of Arabidopsis at a high frequency. Proc. Natl. Acad. Sci. U. S. A. 97, 3718-3723
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 3718-3723
    • Cutler, S.R.1    Ehrhardt, D.W.2    Griffitts, J.S.3    Somerville, C.R.4
  • 52
    • 0037353653 scopus 로고    scopus 로고
    • Proteome analysis. Novel proteins identified at the peribacteroid membrane from Lotus japonicus root nodules
    • Wienkoop, S., and Saalbach, G. (2003) Proteome analysis. Novel proteins identified at the peribacteroid membrane from Lotus japonicus root nodules. Plant Physiol. 131, 1080-1090
    • (2003) Plant Physiol. , vol.131 , pp. 1080-1090
    • Wienkoop, S.1    Saalbach, G.2
  • 53
    • 0030339016 scopus 로고    scopus 로고
    • Cloning of a cDNA encoding a plasma membrane-associated, uronide binding phosphoprotein with physical properties similar to viral movement proteins
    • Reymond, P., Kunz, B., Paul-Pletzer, K., Grimm, R., Eckerskorn, C., and Farmer, E. E. (1996) Cloning of a cDNA encoding a plasma membrane-associated, uronide binding phosphoprotein with physical properties similar to viral movement proteins. Plant Cell. 8, 2265-2276
    • (1996) Plant Cell. , vol.8 , pp. 2265-2276
    • Reymond, P.1    Kunz, B.2    Paul-Pletzer, K.3    Grimm, R.4    Eckerskorn, C.5    Farmer, E.E.6
  • 54
    • 0033545926 scopus 로고    scopus 로고
    • Transcriptional regulation of plant phosphate transporters
    • Muchhal, U. S., and Raghothama, K. G. (1999) Transcriptional regulation of plant phosphate transporters. Proc. Natl. Acad. Sci. U. S. A. 96, 5868-5872
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 5868-5872
    • Muchhal, U.S.1    Raghothama, K.G.2
  • 55
    • 0033671251 scopus 로고    scopus 로고
    • Localization and control of expression of Nt-Syr1, a tobacco SNARE protein
    • Leyman, B., Geelen, D., and Blatt, M. R. (2000) Localization and control of expression of Nt-Syr1, a tobacco SNARE protein. Plant J. 24, 369-381
    • (2000) Plant J. , vol.24 , pp. 369-381
    • Leyman, B.1    Geelen, D.2    Blatt, M.R.3
  • 56
    • 0141676481 scopus 로고    scopus 로고
    • A plasma membrane zinc transporter from Medicago truncatula is up-regulated in roots by Zn fertilization, yet down-regulated by arbuscular mycorrhizal colonization
    • Burleigh, S. H., Kristensen, B. K., and Bechmann, I. E. (2003) A plasma membrane zinc transporter from Medicago truncatula is up-regulated in roots by Zn fertilization, yet down-regulated by arbuscular mycorrhizal colonization. Plant Mol. Biol. 52, 1077-1088
    • (2003) Plant Mol. Biol. , vol.52 , pp. 1077-1088
    • Burleigh, S.H.1    Kristensen, B.K.2    Bechmann, I.E.3
  • 57
    • 0027536034 scopus 로고
    • The specific subcellular localization of two isoforms of cytochrome b5 suggests novel targeting pathways
    • D'Arrigo, A., Manera, E., Longhi, R., and Borgese, N. (1993) The specific subcellular localization of two isoforms of cytochrome b5 suggests novel targeting pathways. J. Biol. Chem. 268, 2802-2808
    • (1993) J. Biol. Chem. , vol.268 , pp. 2802-2808
    • D'Arrigo, A.1    Manera, E.2    Longhi, R.3    Borgese, N.4
  • 58
    • 0020210950 scopus 로고
    • Relationship between endoplasmic reticulum and Golgi membranes: Evidence for a heterogeneous localization of cytochrome b5 in the Golgi membranes
    • Collot, M., Kalff, M., and Remacle, J. (1982) Relationship between endoplasmic reticulum and Golgi membranes: Evidence for a heterogeneous localization of cytochrome b5 in the Golgi membranes. Eur J. Cell Biol. 29, 34-42
    • (1982) Eur. J. Cell Biol. , vol.29 , pp. 34-42
    • Collot, M.1    Kalff, M.2    Remacle, J.3
  • 59
    • 0242285732 scopus 로고    scopus 로고
    • VDAC is a conserved element of death pathways in plant and animal systems
    • Godbole, A., Varghese, J., Sarin, A., and Mathew, M. K. (2003) VDAC is a conserved element of death pathways in plant and animal systems. Biochim. Biophys. Acta 1642, 87-96
    • (2003) Biochim. Biophys. Acta , vol.1642 , pp. 87-96
    • Godbole, A.1    Varghese, J.2    Sarin, A.3    Mathew, M.K.4
  • 60
    • 0031448082 scopus 로고    scopus 로고
    • Minireview: On the structure and gating mechanism of the mitochondrial channel, VDAC
    • Mannella, C. A. (1997) Minireview: On the structure and gating mechanism of the mitochondrial channel, VDAC. J. Bioenerg. Biomembr. 29, 525-531
    • (1997) J. Bioenerg. Biomembr. , vol.29 , pp. 525-531
    • Mannella, C.A.1
  • 61
    • 0032946360 scopus 로고    scopus 로고
    • Vacuolar and plasma membrane proton-adenosinetriphosphatases
    • Nelson, N., and Harvey, W. R. (1999) Vacuolar and plasma membrane proton-adenosinetriphosphatases. Physiol. Rev. 79, 361-385
    • (1999) Physiol. Rev. , vol.79 , pp. 361-385
    • Nelson, N.1    Harvey, W.R.2
  • 62
    • 0030839304 scopus 로고    scopus 로고
    • +-ATPase: A universal proton pump of eukaryotes
    • +-ATPase: A universal proton pump of eukaryotes. Biochem. J. 324(Pt 3), 697-712
    • (1997) Biochem. J. , vol.324 , Issue.PART 3 , pp. 697-712
    • Finbow, M.E.1    Harrison, M.A.2
  • 65
    • 0032711298 scopus 로고    scopus 로고
    • Tonoplast intrinsic protein isoforms as markers for vacuolar functions
    • Jauh, G. Y., Phillips, T. E., and Rogers, J. C. (1999) Tonoplast intrinsic protein isoforms as markers for vacuolar functions. Plant Cell 11, 1867-1882
    • (1999) Plant Cell , vol.11 , pp. 1867-1882
    • Jauh, G.Y.1    Phillips, T.E.2    Rogers, J.C.3
  • 66
    • 0030020125 scopus 로고    scopus 로고
    • Immunological detection of tonoplast polypeptides in the plasma membrane of pea cotyledons
    • Robinson, D. G., Haschke, H. P., Hinz, G., Hoh, B., Maeshima, M., and Marty, F. (1996) Immunological detection of tonoplast polypeptides in the plasma membrane of pea cotyledons. Planta 198, 95-103
    • (1996) Planta , vol.198 , pp. 95-103
    • Robinson, D.G.1    Haschke, H.P.2    Hinz, G.3    Hoh, B.4    Maeshima, M.5    Marty, F.6
  • 69
    • 0032561256 scopus 로고    scopus 로고
    • Cloning of the V-ATPase subunit G in plant: Functional expression and sub-cellular localization
    • Rouquie, D., Tournaire-Roux, C., Szponarski, W., Rossignol, M., and Doumas, P. (1998) Cloning of the V-ATPase subunit G in plant: Functional expression and sub-cellular localization. FEBS Lett. 437, 287-292
    • (1998) FEBS Lett. , vol.437 , pp. 287-292
    • Rouquie, D.1    Tournaire-Roux, C.2    Szponarski, W.3    Rossignol, M.4    Doumas, P.5
  • 73
    • 0028675704 scopus 로고
    • The plasma membrane of Arabidopsis thaliana contains a mercury-insensitive aquaporin that is a homolog of the tonoplast water channel protein TIP
    • Daniels, M. J., Mirkov, T. E., and Chrispeels, M. J. (1994) The plasma membrane of Arabidopsis thaliana contains a mercury-insensitive aquaporin that is a homolog of the tonoplast water channel protein TIP. Plant Physiol. 106, 1325-1333
    • (1994) Plant Physiol. , vol.106 , pp. 1325-1333
    • Daniels, M.J.1    Mirkov, T.E.2    Chrispeels, M.J.3
  • 74
    • 0026555536 scopus 로고
    • Evidence for extra-mitochondrial localization of the VDAC/porin channel in eucaryotic cells
    • Thinnes, F. P. (1992) Evidence for extra-mitochondrial localization of the VDAC/porin channel in eucaryotic cells. J. Bioenerg. Biomembr. 24, 71-75
    • (1992) J. Bioenerg. Biomembr. , vol.24 , pp. 71-75
    • Thinnes, F.P.1
  • 75
    • 0030006030 scopus 로고    scopus 로고
    • Is there VDAC in cell compartments other than the mitochondria?
    • Yu, W. H., and Forte, M. (1996) Is there VDAC in cell compartments other than the mitochondria? J. Bioenerg. Biomembr. 28, 93-100
    • (1996) J. Bioenerg. Biomembr. , vol.28 , pp. 93-100
    • Yu, W.H.1    Forte, M.2
  • 77
    • 1042301383 scopus 로고    scopus 로고
    • VDAC1 is a transplasma membrane NADH: Ferricyanide reductase
    • Baker, M. A., Lane, D. J., Ly, J. D., De Pinto, V., and Lawen, A. (2004) VDAC1 is a transplasma membrane NADH:ferricyanide reductase. J. Biol. Chem. 279, 4811-4819
    • (2004) J. Biol. Chem. , vol.279 , pp. 4811-4819
    • Baker, M.A.1    Lane, D.J.2    Ly, J.D.3    De Pinto, V.4    Lawen, A.5
  • 80
    • 0037008335 scopus 로고    scopus 로고
    • ADP-ribosylation factor 1 of Arabidopsis plays a critical role in intracellular trafficking and maintenance of endoplasmic reticulum morphology in Arabidopsis
    • Lee, M. H., Min, M. K., Lee, Y. J., Jin, J. B., Shin, D. H., Kim, D. H., Lee, K. H., and Hwang, I. (2002) ADP-ribosylation factor 1 of Arabidopsis plays a critical role in intracellular trafficking and maintenance of endoplasmic reticulum morphology in Arabidopsis. Plant Physiol. 129, 1507-1520
    • (2002) Plant Physiol. , vol.129 , pp. 1507-1520
    • Lee, M.H.1    Min, M.K.2    Lee, Y.J.3    Jin, J.B.4    Shin, D.H.5    Kim, D.H.6    Lee, K.H.7    Hwang, I.8
  • 81
    • 0028170814 scopus 로고
    • Role of protein modification reactions in programming interactions between ras-related GTPases and cell membranes
    • Glomset, J. A., and Farnsworth, C. C. (1994) Role of protein modification reactions in programming interactions between ras-related GTPases and cell membranes. Annu. Rev. Cell Biol. 10, 181-205
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 181-205
    • Glomset, J.A.1    Farnsworth, C.C.2
  • 82
    • 0036270260 scopus 로고    scopus 로고
    • Small GTPases: Versatile signaling switches in plants
    • Yang, Z. (2002) Small GTPases: versatile signaling switches in plants. Plant Cell 14, (suppl.) S375-388
    • (2002) Plant Cell , vol.14 , Issue.SUPPL.
    • Yang, Z.1
  • 83
    • 0242290313 scopus 로고    scopus 로고
    • Unexpected protein families including cell defense components feature in the N-myristoylome of a higher eukaryote
    • Boisson, B., Giglione, C., and Meinnel, T. (2003) Unexpected protein families including cell defense components feature in the N-myristoylome of a higher eukaryote. J. Biol. Chem. 278, 43418-43429
    • (2003) J. Biol. Chem. , vol.278 , pp. 43418-43429
    • Boisson, B.1    Giglione, C.2    Meinnel, T.3
  • 84
    • 0032972509 scopus 로고    scopus 로고
    • PSORT: A program for detecting the sorting signals of proteins and predicting their subcellular localization
    • Nakai, K., and Horton, P. (1999) PSORT: a program for detecting the sorting signals of proteins and predicting their subcellular localization. Trends Biochem. Sci. 24, 34-35
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 34-35
    • Nakai, K.1    Horton, P.2
  • 85
    • 0023716253 scopus 로고
    • Identification of GTP-binding proteins in the plasma membrane of higher plants
    • Blum, W., Hinsch, K. D., Schultz, G., and Weiler, E. W. (1988) Identification of GTP-binding proteins in the plasma membrane of higher plants. Biochem. Biophys. Res. Commun. 156, 954-959
    • (1988) Biochem. Biophys. Res. Commun. , vol.156 , pp. 954-959
    • Blum, W.1    Hinsch, K.D.2    Schultz, G.3    Weiler, E.W.4
  • 86
    • 0027105865 scopus 로고
    • Characterization of GTP binding and hydrolysis in plasma membranes of zucchini
    • Perdue, D. O., and Lomax, T. L. (1992) Characterization of GTP binding and hydrolysis in plasma membranes of zucchini. Plant Physiol. Biochem. 30, 163-172
    • (1992) Plant Physiol. Biochem. , vol.30 , pp. 163-172
    • Perdue, D.O.1    Lomax, T.L.2
  • 87
    • 0033779962 scopus 로고    scopus 로고
    • Maize ROP7 GTPase contains a unique, CaaX box-independent plasma membrane targeting signal
    • Ivanchenko, M., Vejlupkova, Z., Quatrano, R. S., and Fowler, J. E. (2000) Maize ROP7 GTPase contains a unique, CaaX box-independent plasma membrane targeting signal. Plant J. 24, 79-90
    • (2000) Plant J. , vol.24 , pp. 79-90
    • Ivanchenko, M.1    Vejlupkova, Z.2    Quatrano, R.S.3    Fowler, J.E.4
  • 88
    • 0035801358 scopus 로고    scopus 로고
    • Ara6, a plant-unique novel type Rab GTPase, functions in the endocytic pathway of Arabidopsis thaliana
    • Ueda, T., Yamaguchi, M., Uchimiya, H., and Nakano, A. (2001) Ara6, a plant-unique novel type Rab GTPase, functions in the endocytic pathway of Arabidopsis thaliana. EMBO J. 20, 4730-4741
    • (2001) EMBO J. , vol.20 , pp. 4730-4741
    • Ueda, T.1    Yamaguchi, M.2    Uchimiya, H.3    Nakano, A.4
  • 89
    • 0034703012 scopus 로고    scopus 로고
    • Prohibitins, stomatins, and plant disease response genes compose a protein superfamily that controls cell proliferation, ion channel regulation, and death
    • Nadimpalli, R., Yalpani, N., Johal, G. S., and Simmons, C. R. (2000) Prohibitins, stomatins, and plant disease response genes compose a protein superfamily that controls cell proliferation, ion channel regulation, and death. J. Biol. Chem. 275, 29579-29586
    • (2000) J. Biol. Chem. , vol.275 , pp. 29579-29586
    • Nadimpalli, R.1    Yalpani, N.2    Johal, G.S.3    Simmons, C.R.4
  • 90
    • 0028965228 scopus 로고
    • Prohibitin: Potential role in senescence, development, and tumor suppression
    • McClung, J. K., Jupe, E. R., Liu, X. T., and Dell'Orco, R. T. (1995) Prohibitin: Potential role in senescence, development, and tumor suppression. Exp Gerontol. 30, 99-124
    • (1995) Exp. Gerontol. , vol.30 , pp. 99-124
    • McClung, J.K.1    Jupe, E.R.2    Liu, X.T.3    Dell'Orco, R.T.4
  • 91
    • 0028000374 scopus 로고
    • The IgM antigen receptor of B lymphocytes is associated with prohibitin and a prohibitin-related protein
    • Terashima, M., Kim, K. M., Adachi, T., Nielsen, P. J., Reth, M., Kohler, G., and Lamers, M. C. (1994) The IgM antigen receptor of B lymphocytes is associated with prohibitin and a prohibitin-related protein. EMBO J. 13, 3782-3792
    • (1994) EMBO J. , vol.13 , pp. 3782-3792
    • Terashima, M.1    Kim, K.M.2    Adachi, T.3    Nielsen, P.J.4    Reth, M.5    Kohler, G.6    Lamers, M.C.7
  • 92
    • 0028088668 scopus 로고
    • Purification and characterization of phospholipid hydroperoxide glutathione peroxidase from rat testis mitochondrial membranes
    • Roveri, A., Maiorino, M., Nisii, C., and Ursini, F. (1994) Purification and characterization of phospholipid hydroperoxide glutathione peroxidase from rat testis mitochondrial membranes. Biochim. Biophys. Acta 1208, 211-221
    • (1994) Biochim. Biophys. Acta , vol.1208 , pp. 211-221
    • Roveri, A.1    Maiorino, M.2    Nisii, C.3    Ursini, F.4
  • 94
    • 0025223272 scopus 로고
    • Electron-transport components of the 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine delta 12-desaturase (delta 12-desaturase) in microsomal preparations from developing safflower (Carthamus tinctorius L.) cotyledons
    • Smith, M. A., Cross, A. R., Jones, O. T., Griffiths, W. T., Stymne, S., and Stobart, K. (1990) Electron-transport components of the 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine delta 12-desaturase (delta 12-desaturase) in microsomal preparations from developing safflower (Carthamus tinctorius L.) cotyledons. Biochem. J. 272, 23-29
    • (1990) Biochem. J. , vol.272 , pp. 23-29
    • Smith, M.A.1    Cross, A.R.2    Jones, O.T.3    Griffiths, W.T.4    Stymne, S.5    Stobart, K.6
  • 95
    • 0028140643 scopus 로고
    • Purification and characterization of two distinct NAD(P)H dehydrogenases from onion (Allium cepa L.) root plasma membrane
    • Serrano, A., Cordoba, F., Gonzalez-Reyes, J. A., Navas, P., and Villalba, J. M. (1994) Purification and characterization of two distinct NAD(P)H dehydrogenases from onion (Allium cepa L.) root plasma membrane. Plant Physiol. 106, 87-96
    • (1994) Plant Physiol. , vol.106 , pp. 87-96
    • Serrano, A.1    Cordoba, F.2    Gonzalez-Reyes, J.A.3    Navas, P.4    Villalba, J.M.5
  • 96
    • 0031397296 scopus 로고    scopus 로고
    • Dissecting the diphenylene iodonium-sensitive NAD(P)H:quinone oxidoreductase of zucchini plasma membrane
    • Trost, P., Foscarini, S., Preger, V., Bonora, P., Vitale, L., and Pupillo, P. (1997) Dissecting the diphenylene iodonium-sensitive NAD(P)H:quinone oxidoreductase of zucchini plasma membrane. Plant Physiol. 114, 737-746
    • (1997) Plant Physiol. , vol.114 , pp. 737-746
    • Trost, P.1    Foscarini, S.2    Preger, V.3    Bonora, P.4    Vitale, L.5    Pupillo, P.6
  • 97
    • 0035832861 scopus 로고    scopus 로고
    • Two cinnamoyl-CoA reductase (CCR) genes from Arabidopsis thaliana are differentially expressed during development and in response to infection with pathogenic bacteria
    • Lauvergeat, V., Lacomme, C., Lacombe, E., Lasserre, E., Roby, D., and Grima-Pettenati, J. (2001) Two cinnamoyl-CoA reductase (CCR) genes from Arabidopsis thaliana are differentially expressed during development and in response to infection with pathogenic bacteria. Phytochemistry 57, 1187-1195
    • (2001) Phytochemistry , vol.57 , pp. 1187-1195
    • Lauvergeat, V.1    Lacomme, C.2    Lacombe, E.3    Lasserre, E.4    Roby, D.5    Grima-Pettenati, J.6
  • 98
    • 0032004726 scopus 로고    scopus 로고
    • S-nitrosylation of glyceraldehyde-3-phosphate dehydrogenase decreases the enzyme affinity to the erythrocyte membrane
    • Galli, F., Rovidati, S., Ghibelli, L., and Canestrari, F. (1998) S-nitrosylation of glyceraldehyde-3-phosphate dehydrogenase decreases the enzyme affinity to the erythrocyte membrane. Nitric Oxide 2, 17-27
    • (1998) Nitric Oxide , vol.2 , pp. 17-27
    • Galli, F.1    Rovidati, S.2    Ghibelli, L.3    Canestrari, F.4
  • 99
    • 0037195125 scopus 로고    scopus 로고
    • Tubulin is the endogenous inhibitor of the glyceraldehyde 3-phosphate dehydrogenase isoform that catalyzes membrane fusion: Implications for the coordinated regulation of glycolysis and membrane fusion
    • Glaser, P. E., Han, X., and Gross, R. W. (2002) Tubulin is the endogenous inhibitor of the glyceraldehyde 3-phosphate dehydrogenase isoform that catalyzes membrane fusion: Implications for the coordinated regulation of glycolysis and membrane fusion. Proc. Natl. Acad. Sci. U. S. A. 99, 14104-14109
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 14104-14109
    • Glaser, P.E.1    Han, X.2    Gross, R.W.3
  • 100
    • 0040194270 scopus 로고    scopus 로고
    • Identification, cloning, and properties of cytosolic d-ribulose-5-phosphate 3-epimerase from higher plants
    • Kopriva, S., Koprivova, A., and Suss, K. H. (2000) Identification, cloning, and properties of cytosolic d-ribulose-5-phosphate 3-epimerase from higher plants. J. Biol. Chem. 275, 1294-1299
    • (2000) J. Biol. Chem. , vol.275 , pp. 1294-1299
    • Kopriva, S.1    Koprivova, A.2    Suss, K.H.3
  • 101
    • 0036707560 scopus 로고    scopus 로고
    • Effects of low chronic doses of ionizing radiation on antioxidant enzymes and G6PDH activities in Stipa capillata (Poaceae)
    • Zaka, R., Vandecasteele, C. M., and Misset, M. T. (2002) Effects of low chronic doses of ionizing radiation on antioxidant enzymes and G6PDH activities in Stipa capillata (Poaceae). J. Exp. Bot. 53, 1979-1987
    • (2002) J. Exp. Bot. , vol.53 , pp. 1979-1987
    • Zaka, R.1    Vandecasteele, C.M.2    Misset, M.T.3
  • 102
    • 0036262189 scopus 로고    scopus 로고
    • Adenine phosphoribosyltransferase isoforms of Arabidopsis and their potential contributions to adenine and cytokinin metabolism
    • Allen, M., Qin, W., Moreau, F., and Moffatt, B. (2002) Adenine phosphoribosyltransferase isoforms of Arabidopsis and their potential contributions to adenine and cytokinin metabolism. Physiol. Plant. 115, 56-68
    • (2002) Physiol. Plant. , vol.115 , pp. 56-68
    • Allen, M.1    Qin, W.2    Moreau, F.3    Moffatt, B.4
  • 104
    • 0029744530 scopus 로고    scopus 로고
    • Identification and cDNA cloning of 35-kDa phosphatidic acid phosphatase (type 2) bound to plasma membranes. Polymerase chain reaction amplification of mouse H2O2-inducible hic53 clone yielded the cDNA encoding phosphatidic acid phosphatase
    • Kai, M., Wada, I., Imai, S., Sakane, F., and Kanoh, H. (1996) Identification and cDNA cloning of 35-kDa phosphatidic acid phosphatase (type 2) bound to plasma membranes. Polymerase chain reaction amplification of mouse H2O2-inducible hic53 clone yielded the cDNA encoding phosphatidic acid phosphatase. J. Biol. Chem. 271, 18931-18938
    • (1996) J. Biol. Chem. , vol.271 , pp. 18931-18938
    • Kai, M.1    Wada, I.2    Imai, S.3    Sakane, F.4    Kanoh, H.5
  • 105
    • 0035884207 scopus 로고    scopus 로고
    • Pulmonary lipid phosphate phosphohydrolase in plasma membrane signalling platforms
    • Nanjundan, M., and Possmayer, F. (2001) Pulmonary lipid phosphate phosphohydrolase in plasma membrane signalling platforms. Biochem. J. 358, 637-646
    • (2001) Biochem. J. , vol.358 , pp. 637-646
    • Nanjundan, M.1    Possmayer, F.2
  • 106
    • 0030833046 scopus 로고    scopus 로고
    • A new family of plasma membrane polypeptides differentially regulated during plant development
    • Logan, D. C., Domergue, O., Teyssendier de la Serve, B., and Rossignol, M. (1997) A new family of plasma membrane polypeptides differentially regulated during plant development. Biochem. Mol. Biol. Int. 43, 1051-1062
    • (1997) Biochem. Mol. Biol. Int. , vol.43 , pp. 1051-1062
    • Logan, D.C.1    Domergue, O.2    Teyssendier de la Serve, B.3    Rossignol, M.4
  • 107
    • 0032853036 scopus 로고    scopus 로고
    • Identification of new early markers of the hypersensitive response in Arabidopsis thaliana
    • Lacomme, C., and Roby, D. (1999) Identification of new early markers of the hypersensitive response in Arabidopsis thaliana. FEBS Lett. 459, 149-153
    • (1999) FEBS Lett. , vol.459 , pp. 149-153
    • Lacomme, C.1    Roby, D.2


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