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Volumn 190, Issue , 2012, Pages 9-15

Tetraspanin genes in plants

Author keywords

Arabidopsis; Development; Gene duplication; Membrane protein; Phylogenetic tree; Tet1 trn2 mutant

Indexed keywords

TETRASPANIN; VEGETABLE PROTEIN;

EID: 84859650882     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plantsci.2012.03.005     Document Type: Review
Times cited : (33)

References (74)
  • 1
    • 27744581952 scopus 로고    scopus 로고
    • Historical perspectives on plant developmental biology
    • Van Lijsebettens M., Van Montagu M. Historical perspectives on plant developmental biology. Int. J. Dev. Biol. 2005, 49:453-465.
    • (2005) Int. J. Dev. Biol. , vol.49 , pp. 453-465
    • Van Lijsebettens, M.1    Van Montagu, M.2
  • 2
    • 0037075019 scopus 로고    scopus 로고
    • Stem cells that make stems
    • Weigel D., Jürgens G. Stem cells that make stems. Nature 2002, 415:751-754.
    • (2002) Nature , vol.415 , pp. 751-754
    • Weigel, D.1    Jürgens, G.2
  • 3
    • 0035141623 scopus 로고    scopus 로고
    • Meristems: start your signaling
    • Clark S.E. Meristems: start your signaling. Curr. Opin. Plant Biol. 2001, 4:28-32.
    • (2001) Curr. Opin. Plant Biol. , vol.4 , pp. 28-32
    • Clark, S.E.1
  • 4
    • 0033101715 scopus 로고    scopus 로고
    • The CLAVATA1 receptor-like kinase requires CLAVATA3 for its assembly into a signaling complex that includes KAPP and a Rho-related protein
    • Trotochaud A.E., Hao T., Wu G., Yang Z., Clark S.E. The CLAVATA1 receptor-like kinase requires CLAVATA3 for its assembly into a signaling complex that includes KAPP and a Rho-related protein. Plant Cell 1999, 11:393-406.
    • (1999) Plant Cell , vol.11 , pp. 393-406
    • Trotochaud, A.E.1    Hao, T.2    Wu, G.3    Yang, Z.4    Clark, S.E.5
  • 5
    • 85027938700 scopus 로고    scopus 로고
    • Stem-cell-triggered immunity through CLV3p-FLS2 signalling
    • Lee H., Chah O.-K., Sheen J. Stem-cell-triggered immunity through CLV3p-FLS2 signalling. Nature 2011, 473:376-379.
    • (2011) Nature , vol.473 , pp. 376-379
    • Lee, H.1    Chah, O.-K.2    Sheen, J.3
  • 6
    • 0029550602 scopus 로고
    • Selective trafficking of KNOTTED1 homeodomain protein and its mRNA through plasmodesmata
    • Lucas W.J., Bouché-Pillon S., Jackson D.P., Nguyen L., Baker L., Ding B., Hake S. Selective trafficking of KNOTTED1 homeodomain protein and its mRNA through plasmodesmata. Science 1995, 270:1980-1983.
    • (1995) Science , vol.270 , pp. 1980-1983
    • Lucas, W.J.1    Bouché-Pillon, S.2    Jackson, D.P.3    Nguyen, L.4    Baker, L.5    Ding, B.6    Hake, S.7
  • 7
    • 0034604413 scopus 로고    scopus 로고
    • Cell-cell signaling and movement by the floral transcription factors LEAFY and APETALA1
    • Sessions A., Yanofsky M.F., Weigel D. Cell-cell signaling and movement by the floral transcription factors LEAFY and APETALA1. Science 2000, 289:779-781.
    • (2000) Science , vol.289 , pp. 779-781
    • Sessions, A.1    Yanofsky, M.F.2    Weigel, D.3
  • 9
    • 0141996367 scopus 로고    scopus 로고
    • The ekeko mutant demonstrates a role for tetraspanin-like protein in plant development
    • Olmos E., Reiss B., Dekker K. The ekeko mutant demonstrates a role for tetraspanin-like protein in plant development. Biochem. Biophys. Res. Commun. 2003, 310:1054-1061.
    • (2003) Biochem. Biophys. Res. Commun. , vol.310 , pp. 1054-1061
    • Olmos, E.1    Reiss, B.2    Dekker, K.3
  • 10
    • 33947136790 scopus 로고    scopus 로고
    • Mutations in the TORNADO2 gene affect cellular decisions in the peripheral zone of the shoot apical meristem of Arabidopsis thaliana
    • Chiu W.-H., Chandler J., Cnops G., Van Lijsebettens M., Werr W. Mutations in the TORNADO2 gene affect cellular decisions in the peripheral zone of the shoot apical meristem of Arabidopsis thaliana. Plant Mol. Biol. 2007, 63:731-744.
    • (2007) Plant Mol. Biol. , vol.63 , pp. 731-744
    • Chiu, W.-H.1    Chandler, J.2    Cnops, G.3    Van Lijsebettens, M.4    Werr, W.5
  • 12
    • 0033841205 scopus 로고    scopus 로고
    • TORNADO1 and TORNADO2 are required for the specification of radial and circumferential pattern in the Arabidopsis root
    • Cnops G., Wang X., Linstead P., Van Montagu M., Van Lijsebettens M., Dolan L. TORNADO1 and TORNADO2 are required for the specification of radial and circumferential pattern in the Arabidopsis root. Development 2000, 127:3385-3394.
    • (2000) Development , vol.127 , pp. 3385-3394
    • Cnops, G.1    Wang, X.2    Linstead, P.3    Van Montagu, M.4    Van Lijsebettens, M.5    Dolan, L.6
  • 14
    • 28644444179 scopus 로고    scopus 로고
    • The phylogenetic analysis of tetraspanins projects the evolution of cell-cell interactions from unicellular to multicellular organisms
    • Huang S., Yuan S., Dong M., Su J., Yu C., Shen Y., Xie X., Yu Y., Yu X., Chen S., Zhang S., Pontarotti P., Xu A. The phylogenetic analysis of tetraspanins projects the evolution of cell-cell interactions from unicellular to multicellular organisms. Genomics 2005, 86:674-684.
    • (2005) Genomics , vol.86 , pp. 674-684
    • Huang, S.1    Yuan, S.2    Dong, M.3    Su, J.4    Yu, C.5    Shen, Y.6    Xie, X.7    Yu, Y.8    Yu, X.9    Chen, S.10    Zhang, S.11    Pontarotti, P.12    Xu, A.13
  • 15
    • 77957736749 scopus 로고    scopus 로고
    • The evolution of vertebrate tetraspanins: gene loss, retention, and massive positive selection after whole genome duplications
    • Huang S., Tian H., Chen Z., Yu T., Xu A. The evolution of vertebrate tetraspanins: gene loss, retention, and massive positive selection after whole genome duplications. BMC Evol. Biol. 2010, 10:306.
    • (2010) BMC Evol. Biol. , vol.10 , pp. 306
    • Huang, S.1    Tian, H.2    Chen, Z.3    Yu, T.4    Xu, A.5
  • 16
    • 33748886363 scopus 로고    scopus 로고
    • Origin of the tetraspanin uroplakins and their co-evolution with associated proteins: implications for uroplakin structure and function
    • Garcia-España A., Chung P.-J., Zhao X., Lee A., Pellicer A., Yu J., Sun T.-T., DeSalle R. Origin of the tetraspanin uroplakins and their co-evolution with associated proteins: implications for uroplakin structure and function. Mol. Phylogenet. Evol. 2006, 41:355-367.
    • (2006) Mol. Phylogenet. Evol. , vol.41 , pp. 355-367
    • Garcia-España, A.1    Chung, P.-J.2    Zhao, X.3    Lee, A.4    Pellicer, A.5    Yu, J.6    Sun, T.-T.7    DeSalle, R.8
  • 17
    • 77953139574 scopus 로고    scopus 로고
    • Evolution of cysteine patterns in the large extracellular loop of tetraspanins from animals, fungi, plants and single-celled eukaryotes
    • DeSalle R., Mares R., Garcia-España A. Evolution of cysteine patterns in the large extracellular loop of tetraspanins from animals, fungi, plants and single-celled eukaryotes. Mol. Phylogenet. Evol. 2010, 56:486-491.
    • (2010) Mol. Phylogenet. Evol. , vol.56 , pp. 486-491
    • DeSalle, R.1    Mares, R.2    Garcia-España, A.3
  • 23
    • 33644820905 scopus 로고    scopus 로고
    • Complete predicted three-dimensional structure of the facilitator transmembrane protein and hepatitis C virus receptor CD81: conserved and variable structural domains in the tetraspanin superfamily
    • Seigneuret M. Complete predicted three-dimensional structure of the facilitator transmembrane protein and hepatitis C virus receptor CD81: conserved and variable structural domains in the tetraspanin superfamily. Biophys. J. 2006, 90:212-227.
    • (2006) Biophys. J. , vol.90 , pp. 212-227
    • Seigneuret, M.1
  • 24
    • 0036302083 scopus 로고    scopus 로고
    • Infertility of CD9-deficient mouse eggs is reversed by mouse CD9, human CD9, or mouse CD81; polyadenylated mRNA injection developed for molecular analysis of sperm-egg fusion
    • Kaji K., Oda S., Miyazaki S., Kudo A. Infertility of CD9-deficient mouse eggs is reversed by mouse CD9, human CD9, or mouse CD81; polyadenylated mRNA injection developed for molecular analysis of sperm-egg fusion. Dev. Biol. 2002, 247:327-334.
    • (2002) Dev. Biol. , vol.247 , pp. 327-334
    • Kaji, K.1    Oda, S.2    Miyazaki, S.3    Kudo, A.4
  • 25
    • 79953201597 scopus 로고    scopus 로고
    • The complexity of tetraspanins
    • Rubinstein E. The complexity of tetraspanins. Biochem. Soc. Trans. 2011, 39:501-505.
    • (2011) Biochem. Soc. Trans. , vol.39 , pp. 501-505
    • Rubinstein, E.1
  • 27
    • 40349091686 scopus 로고    scopus 로고
    • An " electronic Fluorescent Pictograph" browser for exploring and analyzing large-scale biological data sets
    • Winter D., Vinegar B., Nahal H., Ammar R., Wilson G.V., Provart N.J. An " electronic Fluorescent Pictograph" browser for exploring and analyzing large-scale biological data sets. PLoS One 2007, 2:e718.
    • (2007) PLoS One , vol.2
    • Winter, D.1    Vinegar, B.2    Nahal, H.3    Ammar, R.4    Wilson, G.V.5    Provart, N.J.6
  • 29
    • 79959354582 scopus 로고    scopus 로고
    • Arabidopsis WIH1 and WIH2 genes act in the transition from somatic to reproductive cell fate
    • Lieber D., Lora J., Schrempp S., Lenhard M., Laux T. Arabidopsis WIH1 and WIH2 genes act in the transition from somatic to reproductive cell fate. Curr. Biol. 2011, 21:1009-1017.
    • (2011) Curr. Biol. , vol.21 , pp. 1009-1017
    • Lieber, D.1    Lora, J.2    Schrempp, S.3    Lenhard, M.4    Laux, T.5
  • 30
    • 24044439517 scopus 로고    scopus 로고
    • Protein-protein interactions in the tetraspanin web
    • Levy S., Shoham T. Protein-protein interactions in the tetraspanin web. Physiology 2005, 20:218-224.
    • (2005) Physiology , vol.20 , pp. 218-224
    • Levy, S.1    Shoham, T.2
  • 31
    • 75149121861 scopus 로고    scopus 로고
    • The role of tetraspanins in the pathogenesis of infectious diseases
    • van Spriel A.B., Figdor C.G. The role of tetraspanins in the pathogenesis of infectious diseases. Microbes Infect. 2010, 12:106-112.
    • (2010) Microbes Infect. , vol.12 , pp. 106-112
    • van Spriel, A.B.1    Figdor, C.G.2
  • 32
    • 33846165776 scopus 로고    scopus 로고
    • Integrity of all four transmembrane domains of the tetraspanin uroplakin Ib is required for its exit from the ER
    • Tu L., Kong X.-P., Sun T.-T., Kreibich G. Integrity of all four transmembrane domains of the tetraspanin uroplakin Ib is required for its exit from the ER. J. Cell Sci. 2006, 119:5077-5086.
    • (2006) J. Cell Sci. , vol.119 , pp. 5077-5086
    • Tu, L.1    Kong, X.-P.2    Sun, T.-T.3    Kreibich, G.4
  • 33
    • 0035207920 scopus 로고    scopus 로고
    • Complexes of tetraspanins with integrins: more than meets the eye
    • Berditchevski F. Complexes of tetraspanins with integrins: more than meets the eye. J. Cell Sci. 2001, 114:4143-4151.
    • (2001) J. Cell Sci. , vol.114 , pp. 4143-4151
    • Berditchevski, F.1
  • 34
    • 0033431676 scopus 로고    scopus 로고
    • Association of a tetraspanin CD9 with CD5 on the T cell surface: role of particular transmembrane domains in the association
    • Toyo-oka K., Yashiro-Ohtani Y., Park C.-S., Tai X.-G., Miyake K., Hamaoka T., Fujiwara H. Association of a tetraspanin CD9 with CD5 on the T cell surface: role of particular transmembrane domains in the association. Int. Immunol. 1999, 11:2043-2052.
    • (1999) Int. Immunol. , vol.11 , pp. 2043-2052
    • Toyo-oka, K.1    Yashiro-Ohtani, Y.2    Park, C.-S.3    Tai, X.-G.4    Miyake, K.5    Hamaoka, T.6    Fujiwara, H.7
  • 35
    • 33846226473 scopus 로고    scopus 로고
    • Tetraspanins as regulators of protein trafficking
    • Berditchevski F., Odintsova E. Tetraspanins as regulators of protein trafficking. Traffic 2007, 8:89-96.
    • (2007) Traffic , vol.8 , pp. 89-96
    • Berditchevski, F.1    Odintsova, E.2
  • 38
    • 0035955657 scopus 로고    scopus 로고
    • Structure of the tetraspanin main extracellular domain. A partially conserved fold with a structurally variable domain insertion
    • Seigneuret M., Delaguillaumie A., Lagaudrière-Gesbert C., Conjeaud H. Structure of the tetraspanin main extracellular domain. A partially conserved fold with a structurally variable domain insertion. J. Biol. Chem. 2001, 276:40055-40064.
    • (2001) J. Biol. Chem. , vol.276 , pp. 40055-40064
    • Seigneuret, M.1    Delaguillaumie, A.2    Lagaudrière-Gesbert, C.3    Conjeaud, H.4
  • 39
    • 0031660652 scopus 로고    scopus 로고
    • Highly stoichiometric, stable, and specific association of integrin α3β1 with CD151 provides a major link to phosphatidylinositol 4-kinase, and may regulate cell migration
    • Yauch R.L., Berditchevski F., Harler M.B., Reichner J., Hemler M.E. Highly stoichiometric, stable, and specific association of integrin α3β1 with CD151 provides a major link to phosphatidylinositol 4-kinase, and may regulate cell migration. Mol. Biol. Cell 1998, 9:2751-2765.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 2751-2765
    • Yauch, R.L.1    Berditchevski, F.2    Harler, M.B.3    Reichner, J.4    Hemler, M.E.5
  • 41
    • 0037051906 scopus 로고    scopus 로고
    • Differential stability of tetraspanin/tetraspanin interactions: role of palmitoylation
    • Charrin S., Manié S., Oualid M., Billard M., Boucheix C., Rubinstein E. Differential stability of tetraspanin/tetraspanin interactions: role of palmitoylation. FEBS Lett. 2002, 516:139-144.
    • (2002) FEBS Lett. , vol.516 , pp. 139-144
    • Charrin, S.1    Manié, S.2    Oualid, M.3    Billard, M.4    Boucheix, C.5    Rubinstein, E.6
  • 42
    • 67349207886 scopus 로고    scopus 로고
    • Mutation of juxtamembrane cysteines in the tetraspanin CD81 affects palmitoylation and alters interaction with other proteins at the cell surface
    • Delandre C., Penabaz T.R., Passarelli A.L., Chapes S.K., Clem R.J. Mutation of juxtamembrane cysteines in the tetraspanin CD81 affects palmitoylation and alters interaction with other proteins at the cell surface. Exp. Cell Res. 2009, 315:1953-1963.
    • (2009) Exp. Cell Res. , vol.315 , pp. 1953-1963
    • Delandre, C.1    Penabaz, T.R.2    Passarelli, A.L.3    Chapes, S.K.4    Clem, R.J.5
  • 43
    • 0036198534 scopus 로고    scopus 로고
    • Palmitoylation of tetraspanin proteins: modulation of CD151 lateral interactions, subcellular distribution, and integrin-dependent cell morphology
    • Yang X., Claas C., Kraeft S.-K., Chen L.B., Wang Z., Kreidberg J.A., Hemler M.E. Palmitoylation of tetraspanin proteins: modulation of CD151 lateral interactions, subcellular distribution, and integrin-dependent cell morphology. Mol. Biol. Cell 2002, 13:767-781.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 767-781
    • Yang, X.1    Claas, C.2    Kraeft, S.-K.3    Chen, L.B.4    Wang, Z.5    Kreidberg, J.A.6    Hemler, M.E.7
  • 44
    • 0037020085 scopus 로고    scopus 로고
    • Expression of the palmitoylation-deficient CD151 weakens the association of α3β1 integrin with the tetraspanin-enriched microdomains and affects integrin-dependent signaling
    • Berditchevski F., Odintsova E., Sawada S., Gilbert E. Expression of the palmitoylation-deficient CD151 weakens the association of α3β1 integrin with the tetraspanin-enriched microdomains and affects integrin-dependent signaling. J. Biol. Chem. 2002, 277:36991-37000.
    • (2002) J. Biol. Chem. , vol.277 , pp. 36991-37000
    • Berditchevski, F.1    Odintsova, E.2    Sawada, S.3    Gilbert, E.4
  • 45
    • 79961142381 scopus 로고    scopus 로고
    • The C-terminal tail of tetraspanin protein CD9 contributes to its function and molecular organization
    • Wang H.-X., Kolesnikova T.V., Denison C., Gygi S.P., Hemler M.E. The C-terminal tail of tetraspanin protein CD9 contributes to its function and molecular organization. J. Cell Sci. 2011, 124:2702-2710.
    • (2011) J. Cell Sci. , vol.124 , pp. 2702-2710
    • Wang, H.-X.1    Kolesnikova, T.V.2    Denison, C.3    Gygi, S.P.4    Hemler, M.E.5
  • 46
    • 33947664480 scopus 로고    scopus 로고
    • Calcium-dependent association of calmodulin with the C-terminal domain of the tetraspanin protein peripherin/rds
    • Edrington T.C.t., Yeagle P.L., Gretzula C.L., Boesze-Battaglia K. Calcium-dependent association of calmodulin with the C-terminal domain of the tetraspanin protein peripherin/rds. Biochemistry 2007, 46:3862-3871.
    • (2007) Biochemistry , vol.46 , pp. 3862-3871
    • Edrington, T.1    Yeagle, P.L.2    Gretzula, C.L.3    Boesze-Battaglia, K.4
  • 47
    • 0037466459 scopus 로고    scopus 로고
    • Tetraspanin CD63 promotes targeting and lysosomal proteolysis of membrane-type 1 matrix metalloproteinase
    • Takino T., Miyamori H., Kawaguchi N., Uekita T., Seiki M., Sato H. Tetraspanin CD63 promotes targeting and lysosomal proteolysis of membrane-type 1 matrix metalloproteinase. Biochem. Biophys. Res. Commun. 2003, 304:160-166.
    • (2003) Biochem. Biophys. Res. Commun. , vol.304 , pp. 160-166
    • Takino, T.1    Miyamori, H.2    Kawaguchi, N.3    Uekita, T.4    Seiki, M.5    Sato, H.6
  • 48
    • 33947496629 scopus 로고    scopus 로고
    • The inner loop of tetraspanins CD82 and CD81 mediates interactions with human T cell lymphotrophic virus type 1 Gag protein
    • Mazurov D., Heidecker G., Derse D. The inner loop of tetraspanins CD82 and CD81 mediates interactions with human T cell lymphotrophic virus type 1 Gag protein. J. Biol. Chem. 2007, 282:3896-3903.
    • (2007) J. Biol. Chem. , vol.282 , pp. 3896-3903
    • Mazurov, D.1    Heidecker, G.2    Derse, D.3
  • 51
    • 28444441957 scopus 로고    scopus 로고
    • Tetraspanin functions and associated microdomains
    • Hemler M.E. Tetraspanin functions and associated microdomains. Nat. Rev. Mol. Cell Biol. 2005, 6:801-811.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 801-811
    • Hemler, M.E.1
  • 52
    • 11244304502 scopus 로고    scopus 로고
    • Palmitoylation supports assembly and function of integrin-tetraspanin complexes
    • Yang X., Kovalenko O.V., Tang W., Claas C., Stipp C.S., Hemler M.E. Palmitoylation supports assembly and function of integrin-tetraspanin complexes. J. Cell Biol. 2004, 167:1231-1240.
    • (2004) J. Cell Biol. , vol.167 , pp. 1231-1240
    • Yang, X.1    Kovalenko, O.V.2    Tang, W.3    Claas, C.4    Stipp, C.S.5    Hemler, M.E.6
  • 55
    • 33644977667 scopus 로고    scopus 로고
    • CD9 controls the formation of clusters that contain tetraspanins and the integrin α6β1, which are involved in human and mouse gamete fusion
    • Ziyyat A., Rubinstein E., Monier-Gavelle F., Barraud V., Kulski O., Prenant M., Boucheix C., Bomsel M., Wolf J.-P. CD9 controls the formation of clusters that contain tetraspanins and the integrin α6β1, which are involved in human and mouse gamete fusion. J. Cell Sci. 2006, 119:416-424.
    • (2006) J. Cell Sci. , vol.119 , pp. 416-424
    • Ziyyat, A.1    Rubinstein, E.2    Monier-Gavelle, F.3    Barraud, V.4    Kulski, O.5    Prenant, M.6    Boucheix, C.7    Bomsel, M.8    Wolf, J.-P.9
  • 56
    • 84861234216 scopus 로고    scopus 로고
    • Gamete interactions during double fertilization in flowering plants
    • Sprunck S., Dresselhaus T. Gamete interactions during double fertilization in flowering plants. Zellbiologie Aktuell 2009, 35:22-27.
    • (2009) Zellbiologie Aktuell , vol.35 , pp. 22-27
    • Sprunck, S.1    Dresselhaus, T.2
  • 59
    • 84859161891 scopus 로고    scopus 로고
    • Structural and functional relationships between photoreceptor tetraspanins and other superfamily members
    • Conley S.M., Stuck M.W., Naash M.I. Structural and functional relationships between photoreceptor tetraspanins and other superfamily members. Cell. Mol. Life Sci. 2011, 69:1035-1047.
    • (2011) Cell. Mol. Life Sci. , vol.69 , pp. 1035-1047
    • Conley, S.M.1    Stuck, M.W.2    Naash, M.I.3
  • 60
    • 77952099176 scopus 로고    scopus 로고
    • Expression and structural characterization of peripherin/RDS, a membrane protein implicated in photoreceptor outer segment morphology
    • Vos W.L., Vaughan S., Lall P.Y., McCaffrey J.G., Wysocka-Kapcinska M., Findlay J.B.C. Expression and structural characterization of peripherin/RDS, a membrane protein implicated in photoreceptor outer segment morphology. Eur. Biophys. J. 2010, 39:679-688.
    • (2010) Eur. Biophys. J. , vol.39 , pp. 679-688
    • Vos, W.L.1    Vaughan, S.2    Lall, P.Y.3    McCaffrey, J.G.4    Wysocka-Kapcinska, M.5    Findlay, J.B.C.6
  • 61
    • 0032512412 scopus 로고    scopus 로고
    • Cysteine residues of photoreceptor peripherin/rds: role in subunit assembly and autosomal dominant retinitis pigmentosa
    • Goldberg A.F.X., Loewen C.J.R., Molday R.S. Cysteine residues of photoreceptor peripherin/rds: role in subunit assembly and autosomal dominant retinitis pigmentosa. Biochemistry 1998, 37:680-685.
    • (1998) Biochemistry , vol.37 , pp. 680-685
    • Goldberg, A.F.X.1    Loewen, C.J.R.2    Molday, R.S.3
  • 62
    • 16344379189 scopus 로고    scopus 로고
    • The PIN auxin efflux facilitators: evolutionary and functional perspectives
    • Paponov I.A., Teale W.D., Trebar M., Blilou I., Palme K. The PIN auxin efflux facilitators: evolutionary and functional perspectives. Trends Plant Sci. 2005, 10:170-177.
    • (2005) Trends Plant Sci. , vol.10 , pp. 170-177
    • Paponov, I.A.1    Teale, W.D.2    Trebar, M.3    Blilou, I.4    Palme, K.5
  • 65
    • 1242342962 scopus 로고    scopus 로고
    • The tetraspanin BcPls1 is required for appressorium-mediated penetration of Botrytis cinerea into host plant leaves
    • Gourgues M., Brunet-Simon A., Lebrun M.-H., Levis C. The tetraspanin BcPls1 is required for appressorium-mediated penetration of Botrytis cinerea into host plant leaves. Mol. Microbiol. 2004, 51:619-629.
    • (2004) Mol. Microbiol. , vol.51 , pp. 619-629
    • Gourgues, M.1    Brunet-Simon, A.2    Lebrun, M.-H.3    Levis, C.4
  • 66
    • 33845975257 scopus 로고    scopus 로고
    • Membrane microdomains and proteomics: lessons from tetraspanin microdomains and comparison with lipid rafts
    • Le Naour F., André M., Boucheix C., Rubinstein E. Membrane microdomains and proteomics: lessons from tetraspanin microdomains and comparison with lipid rafts. Proteomics 2006, 6:6447-6454.
    • (2006) Proteomics , vol.6 , pp. 6447-6454
    • Le Naour, F.1    André, M.2    Boucheix, C.3    Rubinstein, E.4
  • 69
    • 84857780876 scopus 로고    scopus 로고
    • Evidence for network evolution in an Arabidopsis interactome map
    • Arabidopsis Interactome Mapping Consortium
    • Evidence for network evolution in an Arabidopsis interactome map. Science 2011, 333:601-607. Arabidopsis Interactome Mapping Consortium.
    • (2011) Science , vol.333 , pp. 601-607
  • 72
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: multiple sequence alignment with high accuracy and high throughput
    • Edgar R.C. MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res. 2004, 32:1792-1797.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 74
    • 85115107592 scopus 로고
    • Agrobacterium tumefaciens-mediated transformation of Arabidopsis thaliana root explants by using kanamycin selection
    • Valvekens D., Van Montagu M., Van Lijsebettens M. Agrobacterium tumefaciens-mediated transformation of Arabidopsis thaliana root explants by using kanamycin selection. Proc. Natl. Acad. Sci. U.S.A. 1988, 85:5536-5540.
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 5536-5540
    • Valvekens, D.1    Van Montagu, M.2    Van Lijsebettens, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.