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Volumn 137, Issue 1, 2005, Pages 104-116

Analysis of detergent-resistant membranes in arabidopsis. Evidence for plasma membrane lipid rafts

Author keywords

[No Author keywords available]

Indexed keywords

ELECTROPHORESIS; GAS CHROMATOGRAPHY; LIPIDS; MASS SPECTROMETRY; MOLECULES; PLANTS (BOTANY); PLASMAS; PROTEINS;

EID: 20844458248     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.104.053041     Document Type: Article
Times cited : (400)

References (84)
  • 1
    • 0030774479 scopus 로고    scopus 로고
    • On the origin of sphingolipid/ cholesterol-rich detergent-insoluble cell membranes: Physiological concentrations of cholesterol and sphingolipid induce formation of a detergent-insoluble, liquid-ordered lipid phase in model membranes
    • Ahmed SN, Brown DA, London E (1997) On the origin of sphingolipid/ cholesterol-rich detergent-insoluble cell membranes: physiological concentrations of cholesterol and sphingolipid induce formation of a detergent-insoluble, liquid-ordered lipid phase in model membranes. Biochemistry 36: 10944-10953
    • (1997) Biochemistry , vol.36 , pp. 10944-10953
    • Ahmed, S.N.1    Brown, D.A.2    London, E.3
  • 4
    • 0035661570 scopus 로고    scopus 로고
    • Plasma membrane proton ATPase Pmalp requires raft association for surface delivery in yeast
    • Bagnat M, Chang A, Simons K (2001) Plasma membrane proton ATPase Pmalp requires raft association for surface delivery in yeast. Mol Biol Cell 12: 4129-4138
    • (2001) Mol Biol Cell , vol.12 , pp. 4129-4138
    • Bagnat, M.1    Chang, A.2    Simons, K.3
  • 5
    • 0034724182 scopus 로고    scopus 로고
    • Lipid rafts function in biosynthetic delivery of proteins to the cell surface in yeast
    • USA
    • Bagnat M, Keranen S, Shevchenko A, Shevchenko A, Simons K (2000) Lipid rafts function in biosynthetic delivery of proteins to the cell surface in yeast. Proc Natl Acad Sci USA 97: 3254-3259
    • (2000) Proc Natl Acad Sci , vol.97 , pp. 3254-3259
    • Bagnat, M.1    Keranen, S.2    Shevchenko, A.3    Shevchenko, A.4    Simons, K.5
  • 6
    • 0032159175 scopus 로고    scopus 로고
    • Distinct biochemical and topological properties of the 31- and 27-kilodalton plasma membrane intrinsic protein subgroups from red beet
    • Barone LM, Mu HH, Shih CJ, Kashlan KB, Wasserman BP (1998) Distinct biochemical and topological properties of the 31- and 27-kilodalton plasma membrane intrinsic protein subgroups from red beet. Plant Physiol 118: 315-322
    • (1998) Plant Physiol , vol.118 , pp. 315-322
    • Barone, L.M.1    Mu, H.H.2    Shih, C.J.3    Kashlan, K.B.4    Wasserman, B.P.5
  • 7
    • 0034542034 scopus 로고    scopus 로고
    • Redox enzymes in the plant plasma membrane and their possible roles
    • Bérczi A, Møller IM (2000) Redox enzymes in the plant plasma membrane and their possible roles. Plant Cell Environ 23: 1287-1302
    • (2000) Plant Cell Environ , vol.23 , pp. 1287-1302
    • Bérczi, A.1    Møller, I.M.2
  • 8
    • 0037783246 scopus 로고    scopus 로고
    • Identification of glycosylphosphatidylinositol-anchored proteins in Arabidopsis. A proteomic and genomic analysis
    • Borner GHH, Lilley KS, Stevens TJ, Dupree P (2003) Identification of glycosylphosphatidylinositol-anchored proteins in Arabidopsis. A proteomic and genomic analysis. Plant Physiol 132: 568-577
    • (2003) Plant Physiol , vol.132 , pp. 568-577
    • Borner, G.H.H.1    Lilley, K.S.2    Stevens, T.J.3    Dupree, P.4
  • 9
    • 0035983610 scopus 로고    scopus 로고
    • Prediction of glycosylphosphatidylinositol-anchored proteins in Arabidopsis. A genomic analysis
    • Borner GHH, Sherrier DJ, Stevens TJ, Arkin IT, Dupree P (2002) Prediction of glycosylphosphatidylinositol-anchored proteins in Arabidopsis. A genomic analysis. Plant Physiol 129: 486-499
    • (2002) Plant Physiol , vol.129 , pp. 486-499
    • Borner, G.H.H.1    Sherrier, D.J.2    Stevens, T.J.3    Arkin, I.T.4    Dupree, P.5
  • 10
    • 0032527642 scopus 로고    scopus 로고
    • Structure and origin of ordered lipid domains in biological membranes
    • Brown DA, London E (1998) Structure and origin of ordered lipid domains in biological membranes. J Membr Biol 164: 103-114
    • (1998) J Membr Biol , vol.164 , pp. 103-114
    • Brown, D.A.1    London, E.2
  • 11
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • Brown DA, Rose JK (1992) Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 68: 533-544
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 12
    • 0036743364 scopus 로고    scopus 로고
    • Arabidopsis mutants reveal multiple roles for sterols in plant development
    • Clouse SD (2002) Arabidopsis mutants reveal multiple roles for sterols in plant development. Plant Cell 14: 1995-2000
    • (2002) Plant Cell , vol.14 , pp. 1995-2000
    • Clouse, S.D.1
  • 14
    • 0024982237 scopus 로고
    • Protein secretion in plant cells can occur via a default pathway
    • Denecke J, Botterman J, Deblaere R (1990) Protein secretion in plant cells can occur via a default pathway. Plant Cell 2: 51-59
    • (1990) Plant Cell , vol.2 , pp. 51-59
    • Denecke, J.1    Botterman, J.2    Deblaere, R.3
  • 16
    • 0036214457 scopus 로고    scopus 로고
    • Relationship of lipid rafts to transient confinement zones detected by single particle tracking
    • Dietrich C, Yang B, Fujiwara T, Kusumi A, Jacobson K (2002) Relationship of lipid rafts to transient confinement zones detected by single particle tracking. Biophys J 82: 274-284
    • (2002) Biophys J , vol.82 , pp. 274-284
    • Dietrich, C.1    Yang, B.2    Fujiwara, T.3    Kusumi, A.4    Jacobson, K.5
  • 17
    • 2542449977 scopus 로고    scopus 로고
    • A post-genomic approach to understanding sphingolipid metabolism in Arabidopsis thaliana
    • Lond
    • Dunn TM, Lynch DV, Michaelson LV, Napier JA (2004) A post-genomic approach to understanding sphingolipid metabolism in Arabidopsis thaliana. Ann Bot (Lond) 93: 483-497
    • (2004) Ann Bot , vol.93 , pp. 483-497
    • Dunn, T.M.1    Lynch, D.V.2    Michaelson, L.V.3    Napier, J.A.4
  • 18
    • 0038557037 scopus 로고    scopus 로고
    • Lipids on the frontier: A century of cell-membrane bilayers
    • Edidin M (2003a) Lipids on the frontier: a century of cell-membrane bilayers. Nat Rev Mol Cell Biol 4: 414-418
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 414-418
    • Edidin, M.1
  • 19
    • 0037959071 scopus 로고    scopus 로고
    • The state of lipid rafts: From model membranes to cells
    • Edidin M (2003b) The state of lipid rafts: from model membranes to cells. Annu Rev Biophys Biomol Struct 32: 257-283
    • (2003) Annu Rev Biophys Biomol Struct , vol.32 , pp. 257-283
    • Edidin, M.1
  • 21
    • 0027257099 scopus 로고
    • Glycosphingolipid-enriched, detergent-insoluble complexes in protein sorting in epithelial cells
    • Fiedler K, Kobayashi T, Kurzchalia TV, Simons K (1993) Glycosphingolipid-enriched, detergent-insoluble complexes in protein sorting in epithelial cells. Biochemistry 32: 6365-6373
    • (1993) Biochemistry , vol.32 , pp. 6365-6373
    • Fiedler, K.1    Kobayashi, T.2    Kurzchalia, T.V.3    Simons, K.4
  • 22
    • 0037947831 scopus 로고    scopus 로고
    • Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors
    • USA
    • Foster LJ, De Hoog CL, Mann M (2003) Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors. Proc Natl Acad Sci USA 100: 5813-5818
    • (2003) Proc Natl Acad Sci , vol.100 , pp. 5813-5818
    • Foster, L.J.1    De Hoog, C.L.2    Mann, M.3
  • 23
    • 0032552072 scopus 로고    scopus 로고
    • Microdomains of GPI-anchored proteins in living cells revealed by crosslinking
    • Friedrichson T, Kurzchalia TV (1998) Microdomains of GPI-anchored proteins in living cells revealed by crosslinking. Nature 394: 802-805
    • (1998) Nature , vol.394 , pp. 802-805
    • Friedrichson, T.1    Kurzchalia, T.V.2
  • 24
    • 0036678454 scopus 로고    scopus 로고
    • The multidrug transporter, P-glycoprotein, actively mediates cholesterol redistribution in the cell membrane
    • USA
    • Garrigues A, Escargueil AE, Orlowski S (2002) The multidrug transporter, P-glycoprotein, actively mediates cholesterol redistribution in the cell membrane. Proc Natl Acad Sci USA 99: 10347-10352
    • (2002) Proc Natl Acad Sci , vol.99 , pp. 10347-10352
    • Garrigues, A.1    Escargueil, A.E.2    Orlowski, S.3
  • 26
    • 1842432039 scopus 로고    scopus 로고
    • Membrane domains in lymphocytes: From lipid rafts to protein scaffolds
    • Harder T, Engelhardt KR (2004) Membrane domains in lymphocytes: from lipid rafts to protein scaffolds. Traffic 5: 265-275
    • (2004) Traffic , vol.5 , pp. 265-275
    • Harder, T.1    Engelhardt, K.R.2
  • 27
    • 0002319132 scopus 로고
    • Genetic control of morphogenesis in Arabidopsis
    • Haughn GW, Somerville CR (1988) Genetic control of morphogenesis in Arabidopsis. Dev Genet 9: 73-89
    • (1988) Dev Genet , vol.9 , pp. 73-89
    • Haughn, G.W.1    Somerville, C.R.2
  • 28
    • 0036841874 scopus 로고    scopus 로고
    • Triton promotes domain formation in lipid raft mixtures
    • Heerklotz H (2002) Triton promotes domain formation in lipid raft mixtures. Biophys J 83: 2693-2701
    • (2002) Biophys J , vol.83 , pp. 2693-2701
    • Heerklotz, H.1
  • 29
    • 0038730762 scopus 로고    scopus 로고
    • The sensitivity of lipid domains to small perturbations demonstrated by the effect of Triton
    • Heerklotz H, Szadkowska H, Anderson T, Seelig J (2003) The sensitivity of lipid domains to small perturbations demonstrated by the effect of Triton. J Mol Biol 329: 793-799
    • (2003) J Mol Biol , vol.329 , pp. 793-799
    • Heerklotz, H.1    Szadkowska, H.2    Anderson, T.3    Seelig, J.4
  • 30
    • 1842588906 scopus 로고    scopus 로고
    • Lipids as targeting signals: Lipid rafts and intracellular trafficking
    • Helms JB, Zurzolo C (2004) Lipids as targeting signals: lipid rafts and intracellular trafficking. Traffic 5: 247-254
    • (2004) Traffic , vol.5 , pp. 247-254
    • Helms, J.B.1    Zurzolo, C.2
  • 31
    • 0035423556 scopus 로고    scopus 로고
    • Roles of lipid rafts in membrane transport
    • Ikonen E (2001) Roles of lipid rafts in membrane transport. Curr Opin Cell Biol 13: 470-477
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 470-477
    • Ikonen, E.1
  • 32
    • 0033735206 scopus 로고    scopus 로고
    • Sphingoid base composition of monoglucosylceramide in Brassicaceae
    • Imai H, Morimoto Y, Tamura K (2000) Sphingoid base composition of monoglucosylceramide in Brassicaceae. J Plant Physiol 157: 453-456
    • (2000) J Plant Physiol , vol.157 , pp. 453-456
    • Imai, H.1    Morimoto, Y.2    Tamura, K.3
  • 33
    • 0034075971 scopus 로고    scopus 로고
    • High-resolution FRET microscopy of cholera toxin B-subunit and GPI-anchored proteins in cell plasma membranes
    • Kenworthy AK, Petranova N, Edidin M (2000) High-resolution FRET microscopy of cholera toxin B-subunit and GPI-anchored proteins in cell plasma membranes. Mol Biol Cell 11: 1645-1655
    • (2000) Mol Biol Cell , vol.11 , pp. 1645-1655
    • Kenworthy, A.K.1    Petranova, N.2    Edidin, M.3
  • 34
    • 0344720879 scopus 로고
    • Inside-out plant plasma-membrane vesicles of high-purity obtained by aqueous 2-phase partitioning
    • Larsson C, Widell S, Sommarin M (1988) Inside-out plant plasma-membrane vesicles of high-purity obtained by aqueous 2-phase partitioning. FEBS Lett 229: 289-292
    • (1988) FEBS Lett , vol.229 , pp. 289-292
    • Larsson, C.1    Widell, S.2    Sommarin, M.3
  • 35
    • 85047683375 scopus 로고    scopus 로고
    • FQR1, a novel primary auxin-response gene, encodes a flavin mononucleotide-binding quinone reductase
    • Laskowski MJ, Dreher KA, Gehring MA, Abel S, Gensler AL, Sussex IM (2002) FQR1, a novel primary auxin-response gene, encodes a flavin mononucleotide-binding quinone reductase. Plant Physiol 128: 578-590
    • (2002) Plant Physiol , vol.128 , pp. 578-590
    • Laskowski, M.J.1    Dreher, K.A.2    Gehring, M.A.3    Abel, S.4    Gensler, A.L.5    Sussex, I.M.6
  • 36
    • 0037388897 scopus 로고    scopus 로고
    • Monocyte lipid rafts contain proteins implicated in vesicular trafficking and phagosome formation
    • Li N, Mak A, Richards DP, Naber C, Keller BO, Li L, Shaw AR (2003) Monocyte lipid rafts contain proteins implicated in vesicular trafficking and phagosome formation. Proteomics 3: 536-548
    • (2003) Proteomics , vol.3 , pp. 536-548
    • Li, N.1    Mak, A.2    Richards, D.P.3    Naber, C.4    Keller, B.O.5    Li, L.6    Shaw, A.R.7
  • 37
    • 0034707082 scopus 로고    scopus 로고
    • Insolubility of lipids in triton X-100: Physical origin and relationship to sphingolipid/cholesterol membrane domains (rafts)
    • London E, Brown DA (2000) Insolubility of lipids in triton X-100: physical origin and relationship to sphingolipid/cholesterol membrane domains (rafts). Biochim Biophys Acta 1508: 182-195
    • (2000) Biochim Biophys Acta , vol.1508 , pp. 182-195
    • London, E.1    Brown, D.A.2
  • 38
    • 0034604280 scopus 로고    scopus 로고
    • Effects of cholesterol and enantiomeric cholesterol on P-glycoprotein localization and function in low-density membrane domains
    • Luker GD, Pica CM, Kumar AS, Covey DF, Piwnica-Worms D (2000) Effects of cholesterol and enantiomeric cholesterol on P-glycoprotein localization and function in low-density membrane domains. Biochemistry 39: 7651-7661
    • (2000) Biochemistry , vol.39 , pp. 7651-7661
    • Luker, G.D.1    Pica, C.M.2    Kumar, A.S.3    Covey, D.F.4    Piwnica-Worms, D.5
  • 39
    • 0036673052 scopus 로고    scopus 로고
    • Auxin transport: ABC proteins join the club
    • Luschnig C (2002) Auxin transport: ABC proteins join the club. Trends Plant Sci 7: 329-332
    • (2002) Trends Plant Sci , vol.7 , pp. 329-332
    • Luschnig, C.1
  • 40
    • 0001586031 scopus 로고
    • Purification and identification of a plasma membrane associated electron transport protein from maize (Zea mays) roots
    • Luster DG, Buckhout TJ (1989) Purification and identification of a plasma membrane associated electron transport protein from maize (Zea mays) roots. Plant Physiol 91: 1014-1019
    • (1989) Plant Physiol , vol.91 , pp. 1014-1019
    • Luster, D.G.1    Buckhout, T.J.2
  • 41
    • 1842536499 scopus 로고    scopus 로고
    • Rafts: Scale-dependent, active lipid organization at the cell surface
    • Mayor S, Rao M (2004) Rafts: scale-dependent, active lipid organization at the cell surface. Traffic 5: 231-240
    • (2004) Traffic , vol.5 , pp. 231-240
    • Mayor, S.1    Rao, M.2
  • 42
    • 0032031499 scopus 로고    scopus 로고
    • Changes in the levels of seven proteins involved in polypeptide folding and transport during endosperm development of two barley genotypes differing in storage protein localisation
    • Mogelsvang S, Simpson DJ (1998) Changes in the levels of seven proteins involved in polypeptide folding and transport during endosperm development of two barley genotypes differing in storage protein localisation. Plant Mol Biol 6: 541-552
    • (1998) Plant Mol Biol , vol.6 , pp. 541-552
    • Mogelsvang, S.1    Simpson, D.J.2
  • 44
    • 0037073697 scopus 로고    scopus 로고
    • Flotillin-1/reggie-2 traffics to surface raft domains via a novel Golgi-independent pathway. Identification of a novel membrane targeting domain and a role for palmitoylation
    • Morrow IC, Rea S, Martin S, Prior IA, Prohaska R, Hancock JF, James DE, Parton RG (2002) Flotillin-1/reggie-2 traffics to surface raft domains via a novel Golgi-independent pathway. Identification of a novel membrane targeting domain and a role for palmitoylation. J Biol Chem 277: 48834-48841
    • (2002) J Biol Chem , vol.277 , pp. 48834-48841
    • Morrow, I.C.1    Rea, S.2    Martin, S.3    Prior, I.A.4    Prohaska, R.5    Hancock, J.F.6    James, D.E.7    Parton, R.G.8
  • 45
    • 10544225382 scopus 로고    scopus 로고
    • Single point mutations in various domains of a plant plasma membrane H(+)-ATPase expressed in Saccharomyces cerevisiae increase H(+)-pumping and permit yeast growth at low pH
    • Morsomme P, de Kerchove d'Exaerde A, De Meester S, Thines D, Goffeau A, Boutry M (1996) Single point mutations in various domains of a plant plasma membrane H(+)-ATPase expressed in Saccharomyces cerevisiae increase H(+)-pumping and permit yeast growth at low pH. EMBO J 15: 5513-5526
    • (1996) EMBO J , vol.15 , pp. 5513-5526
    • Morsomme, P.1    De Kerchove D'Exaerde, A.2    De Meester, S.3    Thines, D.4    Goffeau, A.5    Boutry, M.6
  • 46
    • 0005946413 scopus 로고    scopus 로고
    • Intracellular transport of GPI-anchored proteins
    • Muniz M, Riezman H (2000) Intracellular transport of GPI-anchored proteins. EMBO J 19: 10-15
    • (2000) EMBO J , vol.19 , pp. 10-15
    • Muniz, M.1    Riezman, H.2
  • 48
    • 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 GS, Simmons CR (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
  • 49
    • 0037044851 scopus 로고    scopus 로고
    • Proteomic analysis of a detergent-resistant membrane skeleton from neutrophil plasma membranes
    • Nebl T, Pestonjamasp KN, Leszyk JD, Crowley JL, Oh SW, Luna EJ (2002) Proteomic analysis of a detergent-resistant membrane skeleton from neutrophil plasma membranes. J Biol Chem 277: 43399-43409
    • (2002) J Biol Chem , vol.277 , pp. 43399-43409
    • Nebl, T.1    Pestonjamasp, K.N.2    Leszyk, J.D.3    Crowley, J.L.4    Oh, S.W.5    Luna, E.J.6
  • 50
    • 0036481562 scopus 로고    scopus 로고
    • The vacuolar (H+)-ATPases: Nature's most versatile proton pumps
    • Nishi T, Forgac M (2002) The vacuolar (H+)-ATPases: nature's most versatile proton pumps. Nat Rev Mol Cell Biol 3: 94-103
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 94-103
    • Nishi, T.1    Forgac, M.2
  • 51
    • 0141567909 scopus 로고    scopus 로고
    • Compositional changes in lipid microdomains of air-blood barrier plasma membranes in pulmonary interstitial edema
    • Palestini P, Calvi C, Conforti E, Daffara R, Botto L, Miserocchi G (2003) Compositional changes in lipid microdomains of air-blood barrier plasma membranes in pulmonary interstitial edema. J Appl Physiol 95: 1446-1452
    • (2003) J Appl Physiol , vol.95 , pp. 1446-1452
    • Palestini, P.1    Calvi, C.2    Conforti, E.3    Daffara, R.4    Botto, L.5    Miserocchi, G.6
  • 52
    • 0034536003 scopus 로고    scopus 로고
    • Identification of low-density Triton X-100-insoluble plasma membrane microdomains in higher plants
    • Peskan T, Westermann M, Oelmuller R (2000) Identification of low-density Triton X-100-insoluble plasma membrane microdomains in higher plants. Eur J Biochem 267: 6989-6995
    • (2000) Eur J Biochem , vol.267 , pp. 6989-6995
    • Peskan, T.1    Westermann, M.2    Oelmuller, R.3
  • 53
    • 1642354334 scopus 로고    scopus 로고
    • Lipid rafts: Heterogeneity on the high seas
    • Pike LJ (2004) Lipid rafts: heterogeneity on the high seas. Biochem J 378: 281-292
    • (2004) Biochem J , vol.378 , pp. 281-292
    • Pike, L.J.1
  • 54
    • 0034611005 scopus 로고    scopus 로고
    • Sphingolipid-cholesterol rafts diffuse as small entities in the plasma membrane of mammalian cells
    • Pralle A, Keller P, Florin EL, Simons K, Horber JK (2000) Sphingolipid-cholesterol rafts diffuse as small entities in the plasma membrane of mammalian cells. J Cell Biol 148: 997-1008
    • (2000) J Cell Biol , vol.148 , pp. 997-1008
    • Pralle, A.1    Keller, P.2    Florin, E.L.3    Simons, K.4    Horber, J.K.5
  • 56
    • 0037455589 scopus 로고    scopus 로고
    • Direct visualization of Ras proteins in spatially distinct cell surface microdomains
    • Prior IA, Muncke C, Parton RG, Hancock JF (2003) Direct visualization of Ras proteins in spatially distinct cell surface microdomains. J Cell Biol 160: 165-170
    • (2003) J Cell Biol , vol.160 , pp. 165-170
    • Prior, I.A.1    Muncke, C.2    Parton, R.G.3    Hancock, J.F.4
  • 57
    • 0032875098 scopus 로고    scopus 로고
    • Fatty acylation of proteins: New insights into membrane targeting of myristoylated and palmitoylated proteins
    • Resh MD (1999) Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins. Biochim Biophys Acta 1451: 1-16
    • (1999) Biochim Biophys Acta , vol.1451 , pp. 1-16
    • Resh, M.D.1
  • 58
    • 0030020125 scopus 로고    scopus 로고
    • Immunological detection of tonoplast polypeptides in the plasma membrane of pea cotyledons
    • Robinson DG, Haschke HP, Hinz G, Hoh B, Maeshima M, 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
  • 60
    • 0035336735 scopus 로고    scopus 로고
    • COBRA encodes a putative GPI-anchored protein, which is polarly localized and necessary for oriented cell expansion in Arabidopsis
    • Schindelman G, Morikami A, Jung J, Baskin TI, Carpita NC, Derbyshire P, McCann MC, Benfey PN (2001) COBRA encodes a putative GPI-anchored protein, which is polarly localized and necessary for oriented cell expansion in Arabidopsis. Genes Dev 15: 1115-1127
    • (2001) Genes Dev , vol.15 , pp. 1115-1127
    • Schindelman, G.1    Morikami, A.2    Jung, J.3    Baskin, T.I.4    Carpita, N.C.5    Derbyshire, P.6    McCann, M.C.7    Benfey, P.N.8
  • 61
    • 0028151351 scopus 로고
    • Interactions between saturated acyl chains confer detergent resistance on lipids and glycosylphosphatidylinositol (GPI)-anchored proteins: GPI-anchored proteins in liposomes and cells show similar behavior
    • USA
    • Schroeder R, London E, Brown D (1994) Interactions between saturated acyl chains confer detergent resistance on lipids and glycosylphosphatidylinositol (GPI)-anchored proteins: GPI-anchored proteins in liposomes and cells show similar behavior. Proc Natl Acad Sci USA 91: 12130-12134
    • (1994) Proc Natl Acad Sci , vol.91 , pp. 12130-12134
    • Schroeder, R.1    London, E.2    Brown, D.3
  • 63
    • 0037008178 scopus 로고    scopus 로고
    • Using genomic resources to guide research directions. The arabinogalactan protein gene family as a test case
    • Schultz CJ, Rumsewicz MP, Johnson KL, Jones BJ, Gaspar YM, Bacic A (2002) Using genomic resources to guide research directions. The arabinogalactan protein gene family as a test case. Plant Physiol 129: 1448-1463
    • (2002) Plant Physiol , vol.129 , pp. 1448-1463
    • Schultz, C.J.1    Rumsewicz, M.P.2    Johnson, K.L.3    Jones, B.J.4    Gaspar, Y.M.5    Bacic, A.6
  • 64
    • 0035984061 scopus 로고    scopus 로고
    • The Arabidopsis SKU5 gene encodes an extracellular glycosyl phosphatidylinositol-anchored glycoprotein involved in directional root growth
    • Sedbrook JC, Carroll KL, Hung KF, Masson PH, Somerville CR (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
  • 65
    • 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 JA, Navas P, Villalba JM (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
  • 67
    • 13044289297 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol-anchored cell-surface proteins from Arabidopsis
    • Sherrier DJ, Prime TA, Dupree P (1999) Glycosylphosphatidylinositol- anchored cell-surface proteins from Arabidopsis. Electrophoresis 20: 2027-2035
    • (1999) Electrophoresis , vol.20 , pp. 2027-2035
    • Sherrier, D.J.1    Prime, T.A.2    Dupree, P.3
  • 68
    • 0141828502 scopus 로고    scopus 로고
    • Use of detergents to study membrane rafts: The good, the bad, and the ugly
    • Shogomori H, Brown DA (2003) Use of detergents to study membrane rafts: the good, the bad, and the ugly. Biol Chem 384: 1259-1263
    • (2003) Biol Chem , vol.384 , pp. 1259-1263
    • Shogomori, H.1    Brown, D.A.2
  • 69
    • 0034788422 scopus 로고    scopus 로고
    • Arabinogalactan-proteins: Structure, expression and function
    • Showalter AE (2001) Arabinogalactan-proteins: structure, expression and function. Cell Mol Life Sci 58: 1399-1417
    • (2001) Cell Mol Life Sci , vol.58 , pp. 1399-1417
    • Showalter, A.E.1
  • 70
    • 0042845804 scopus 로고    scopus 로고
    • Fluorescence energy transfer reveals microdomain formation at physiological temperatures in lipid mixtures modeling the outer leaflet of the plasma membrane
    • Silvius JR (2003) Fluorescence energy transfer reveals microdomain formation at physiological temperatures in lipid mixtures modeling the outer leaflet of the plasma membrane. Biophys J 85: 1034-1045
    • (2003) Biophys J , vol.85 , pp. 1034-1045
    • Silvius, J.R.1
  • 71
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K, Ikonen E (1997) Functional rafts in cell membranes. Nature 387: 569-572
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 72
    • 0034304851 scopus 로고    scopus 로고
    • Lipid rafts and signal transduction
    • Simons K, Toomre D (2000) Lipid rafts and signal transduction. Nat Rev Mol Cell Biol 1: 31-39
    • (2000) Nat Rev Mol Cell Biol , vol.1 , pp. 31-39
    • Simons, K.1    Toomre, D.2
  • 73
    • 0023788823 scopus 로고
    • Lipid sorting in epithelial cells
    • Simons K, van Meer G (1988) Lipid sorting in epithelial cells. Biochemistry 27: 6197-6202
    • (1988) Biochemistry , vol.27 , pp. 6197-6202
    • Simons, K.1    Van Meer, G.2
  • 74
    • 0028038501 scopus 로고
    • Localization of cell-wall poteins in relation to the developmental anatomy of the carrot root apex
    • Smallwood M, Beven A, Donovan N, Neill SJ, Peart J, Roberts K, Knox JP (1994) Localization of cell-wall poteins in relation to the developmental anatomy of the carrot root apex. Plant J 5: 237-246
    • (1994) Plant J , vol.5 , pp. 237-246
    • Smallwood, M.1    Beven, A.2    Donovan, N.3    Neill, S.J.4    Peart, J.5    Roberts, K.6    Knox, J.P.7
  • 75
    • 0038356303 scopus 로고    scopus 로고
    • Plant sphingolipids: Structural diversity, biosynthesis, first genes and functions
    • Sperling P, Heinz E (2003) Plant sphingolipids: structural diversity, biosynthesis, first genes and functions. Biochim Biophys Acta 1632: 1-15
    • (2003) Biochim Biophys Acta , vol.1632 , pp. 1-15
    • Sperling, P.1    Heinz, E.2
  • 77
    • 0027968068 scopus 로고
    • CLUSTALW: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ (1994) CLUSTALW: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22: 4673-4680
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 78
    • 0029053516 scopus 로고
    • A component of the chloroplastic protein import apparatus is targeted to the outer envelope membrane via a novel pathway
    • Tranel PJ, Froehlich J, Goyal A, Keegstra K (1995) A component of the chloroplastic protein import apparatus is targeted to the outer envelope membrane via a novel pathway. EMBO J 14: 2436-2446
    • (1995) EMBO J , vol.14 , pp. 2436-2446
    • Tranel, P.J.1    Froehlich, J.2    Goyal, A.3    Keegstra, K.4
  • 79
    • 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, 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
  • 80
    • 0032552054 scopus 로고    scopus 로고
    • GPI-anchored proteins are organized in submicron domains at the cell surface
    • Varma R, Mayor S (1998) GPI-anchored proteins are organized in submicron domains at the cell surface. Nature 394: 798-801
    • (1998) Nature , vol.394 , pp. 798-801
    • Varma, R.1    Mayor, S.2
  • 81
    • 0038039171 scopus 로고    scopus 로고
    • Recently discovered functions of glucosylceramides in plants and fungi
    • Warnecke D, Heinz E (2003) Recently discovered functions of glucosylceramides in plants and fungi. Cell Mol Life Sci 60: 919-941
    • (2003) Cell Mol Life Sci , vol.60 , pp. 919-941
    • Warnecke, D.1    Heinz, E.2
  • 82
    • 0032191992 scopus 로고    scopus 로고
    • Targeting of active sialyltransferase to the plant Golgi apparatus
    • Wee EG, Sherrier DJ, Prime TA, Dupree P (1998) Targeting of active sialyltransferase to the plant Golgi apparatus. Plant Cell 10: 1759-1768
    • (1998) Plant Cell , vol.10 , pp. 1759-1768
    • Wee, E.G.1    Sherrier, D.J.2    Prime, T.A.3    Dupree, P.4
  • 83
    • 0346665865 scopus 로고    scopus 로고
    • Cell polarity and PIN protein positioning in Arabidopsis require sterol methyltransferase1 function
    • Willemsen V, Friml J, Grebe M, van den Toorn A, Palme K, Scheres B (2003) Cell polarity and PIN protein positioning in Arabidopsis require sterol methyltransferase1 function. Plant Cell 15: 612-625
    • (2003) Plant Cell , vol.15 , pp. 612-625
    • Willemsen, V.1    Friml, J.2    Grebe, M.3    Van Den Toorn, A.4    Palme, K.5    Scheres, B.6
  • 84
    • 0037012847 scopus 로고    scopus 로고
    • Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells
    • Zacharias DA, Violin JD, Newton AC, Tsien RY (2002) Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells. Science 296: 913-916
    • (2002) Science , vol.296 , pp. 913-916
    • Zacharias, D.A.1    Violin, J.D.2    Newton, A.C.3    Tsien, R.Y.4


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