메뉴 건너뛰기




Volumn 5, Issue AUG, 2014, Pages

Lectin domains at the frontiers of plant defense

Author keywords

Carbohydrate; Innate immunity; Lectin; Protein carbohydrate interaction; PRR

Indexed keywords


EID: 84907304370     PISSN: None     EISSN: 1664462X     Source Type: Journal    
DOI: 10.3389/fpls.2014.00397     Document Type: Review
Times cited : (204)

References (153)
  • 1
    • 84902009417 scopus 로고    scopus 로고
    • Transcriptional behavior of EUL-related rice lectins toward important abiotic and biotic stresses
    • doi: 10.1016/j.jplph.2014.04.004
    • Al Atalah, B., De Vleesschauwer, D., Xu, J., Fouquaert, E., Höfte, M., and Van Damme, E. J. (2014a). Transcriptional behavior of EUL-related rice lectins toward important abiotic and biotic stresses. J. Plant Physiol. 171, 986-992. doi: 10.1016/j.jplph.2014.04.004
    • (2014) J. Plant Physiol , vol.171 , pp. 986-992
    • Al Atalah, B.1    de Vleesschauwer, D.2    Xu, J.3    Fouquaert, E.4    Höfte, M.5    van Damme, E.J.6
  • 2
    • 84896747700 scopus 로고    scopus 로고
    • Characterization of a type D1A EUL-related lectin from rice expressed in Pichia pastoris
    • doi: 10.1515/hsz-2013-0267
    • Al Atalah, B., Vanderschaeghe, D., Bloch, Y., Proost, P., Plas, K., Callewaert, N., et al. (2014b). Characterization of a type D1A EUL-related lectin from rice expressed in Pichia pastoris. Biol. Chem. 395, 413-424. doi: 10.1515/hsz-2013-0267
    • (2014) Biol. Chem , vol.395 , pp. 413-424
    • Al Atalah, B.1    Vanderschaeghe, D.2    Bloch, Y.3    Proost, P.4    Plas, K.5    Callewaert, N.6
  • 3
    • 79958150155 scopus 로고    scopus 로고
    • Expression analysis of the nucleocytoplasmic lectin Orysata from rice in Pichia pastoris
    • doi: 10.1111/j.1742-4658.2011.08122.x
    • Al Atalah, B., Fouquaert, E., Vanderschaeghe, D., Proost, P., Balzarini, J., Smith, D. F., et al. (2011). Expression analysis of the nucleocytoplasmic lectin Orysata from rice in Pichia pastoris. FEBS J. 278, 2064-2079. doi: 10.1111/j.1742-4658.2011.08122.x
    • (2011) FEBS J , vol.278 , pp. 2064-2079
    • Al Atalah, B.1    Fouquaert, E.2    Vanderschaeghe, D.3    Proost, P.4    Balzarini, J.5    Smith, D.F.6
  • 4
    • 84865764022 scopus 로고    scopus 로고
    • Expression analysis of a type S2 EUL-related lectin from rice in Pichia pastoris
    • doi: 10.1007/s10719-012-9405-2
    • Al Atalah, B., Rougé, P., Smith, D. F., Proost, P., Lasanajak, Y., and Van Damme, E. J. M. (2012). Expression analysis of a type S2 EUL-related lectin from rice in Pichia pastoris. Glycoconj. J. 29, 467-479. doi: 10.1007/s10719-012-9405-2
    • (2012) Glycoconj. J , vol.29 , pp. 467-479
    • Al Atalah, B.1    Rougé, P.2    Smith, D.F.3    Proost, P.4    Lasanajak, Y.5    van Damme, E.J.M.6
  • 5
    • 84888874635 scopus 로고    scopus 로고
    • Peptides as triggers of plant defence
    • doi: 10.1093/jxb/ert275
    • Albert, M. (2013). Peptides as triggers of plant defence. J. Exp. Bot. 64, 5269-5279. doi: 10.1093/jxb/ert275
    • (2013) J. Exp. Bot , vol.64 , pp. 5269-5279
    • Albert, M.1
  • 6
    • 84857780876 scopus 로고    scopus 로고
    • Evidence for network evolution in an Arabidopsis interactome map
    • Arabidopsis Interactome Mapping Consortium, doi: 10.1126/science.1203877
    • Arabidopsis Interactome Mapping Consortium. (2011). Evidence for network evolution in an Arabidopsis interactome map. Science 333,601-607. doi: 10.1126/science.1203877
    • (2011) Science , vol.333 , pp. 601-607
  • 7
    • 77956065701 scopus 로고    scopus 로고
    • BAK1 is required for the attenuation of ethylene-inducing xylanase (Eix)-induced defense responses by the decoy receptor LeEix1
    • doi: 10.1111/j.1365-313X.2010. 04282.x
    • Bar, M., Sharfman, M., Ron, M., and Avni, A. (2010). BAK1 is required for the attenuation of ethylene-inducing xylanase (Eix)-induced defense responses by the decoy receptor LeEix1. Plant J. 63, 791-800. doi: 10.1111/j.1365-313X.2010. 04282.x
    • (2010) Plant J , vol.63 , pp. 791-800
    • Bar, M.1    Sharfman, M.2    Ron, M.3    Avni, A.4
  • 8
    • 77952717269 scopus 로고    scopus 로고
    • Phloem protein partners of Cucurbit aphid borne yellows virus: Possible involvement of phloem proteins in virus transmission by aphids
    • doi: 10.1094/MPMI-23-6-0799
    • Bencharki, B., Boissinot, S., Revollon, S., Ziegler-Graff, V., Erdinger, M., Wiss, L., et al. (2010). Phloem protein partners of Cucurbit aphid borne yellows virus: possible involvement of phloem proteins in virus transmission by aphids. Mol. Plant Microbe Interact. 23, 799-810. doi: 10.1094/MPMI-23-6-0799
    • (2010) Mol. Plant Microbe Interact , vol.23 , pp. 799-810
    • Bencharki, B.1    Boissinot, S.2    Revollon, S.3    Ziegler-Graff, V.4    Erdinger, M.5    Wiss, L.6
  • 9
    • 77954304102 scopus 로고    scopus 로고
    • Binding properties of the N-acetylglucosamine and high-mannose N-glycan PP2-A1 phloem lectin in Arabidopsis
    • doi: 10.1104/pp.110.153882
    • Beneteau, J., Renard, D., Marché, L., Douville, E., Lavenant, L., Rahbé, Y., et al. (2010). Binding properties of the N-acetylglucosamine and high-mannose N-glycan PP2-A1 phloem lectin in Arabidopsis. Plant Physiol. 153, 1345-1361. doi: 10.1104/pp.110.153882
    • (2010) Plant Physiol , vol.153 , pp. 1345-1361
    • Beneteau, J.1    Renard, D.2    Marché, L.3    Douville, E.4    Lavenant, L.5    Rahbé, Y.6
  • 10
    • 84863645983 scopus 로고    scopus 로고
    • Screening for in planta protein-protein interactions combining bimolecular fluorescence complementation with flow cytometry
    • doi: 10.1186/1746-4811-8-25
    • Berendzen, K. W., Böhmer, M., Wallmeroth, N., Peter, S., Vesić, M., Zhou, Y., et al. (2012). Screening for in planta protein-protein interactions combining bimolecular fluorescence complementation with flow cytometry. Plant Methods 8:25. doi: 10.1186/1746-4811-8-25
    • (2012) Plant Methods , vol.8 , pp. 25
    • Berendzen, K.W.1    Böhmer, M.2    Wallmeroth, N.3    Peter, S.4    Vesić, M.5    Zhou, Y.6
  • 11
    • 79551688310 scopus 로고    scopus 로고
    • Plant targets for Pseudomonas syringae type III effectors: Virulence targets or guarded decoys
    • doi: 10.1016/j.mib.2010.12.011
    • Block, A., and Alfano, J. R. (2011). Plant targets for Pseudomonas syringae type III effectors: virulence targets or guarded decoys? Curr. Opin. Microbiol. 14, 39-46. doi: 10.1016/j.mib.2010.12.011
    • (2011) Curr. Opin. Microbiol , vol.14 , pp. 39-46
    • Block, A.1    Alfano, J.R.2
  • 12
    • 84893395487 scopus 로고    scopus 로고
    • The Pseudomonas syringae type III effector HopD1 suppresses effector-triggered immunity, localizes to the endoplasmic reticulum, and targets the Arabidopsis transcription factor NTL9
    • doi: 10.1111/nph.12626
    • Block, A., Toruño, T. Y., Elowsky, C. G., Zhang, C., Steinbrenner, J., Beynon, J., et al. (2013). The Pseudomonas syringae type III effector HopD1 suppresses effector-triggered immunity, localizes to the endoplasmic reticulum, and targets the Arabidopsis transcription factor NTL9. New Phytol. 201, 1358-1370. doi: 10.1111/nph.12626
    • (2013) New Phytol , vol.201 , pp. 1358-1370
    • Block, A.1    Toruño, T.Y.2    Elowsky, C.G.3    Zhang, C.4    Steinbrenner, J.5    Beynon, J.6
  • 13
    • 84900815207 scopus 로고    scopus 로고
    • Immune receptor complexes at the plant cell surface
    • doi: 10.1016/j.pbi.2014.04.007
    • Böhm, H., Albert, I., Fan, L., Reinhard, A., and Nürnberger, T. (2014). Immune receptor complexes at the plant cell surface. Curr. Opin. Plant Biol. 20, 47-54. doi: 10.1016/j.pbi.2014.04.007
    • (2014) Curr. Opin. Plant Biol , vol.20 , pp. 47-54
    • Böhm, H.1    Albert, I.2    Fan, L.3    Reinhard, A.4    Nürnberger, T.5
  • 14
    • 66249135697 scopus 로고    scopus 로고
    • A renaissance of elicitors: Perception of microbe-associated molecular patterns and danger signals by pattern-recognition receptors
    • doi: 10.1146/annurev.arplant.57.032905.105346
    • Boller, T., and Felix, G. (2009). A renaissance of elicitors: perception of microbe-associated molecular patterns and danger signals by pattern-recognition receptors. Annu. Rev. Plant Biol. 60,379-406. doi: 10.1146/annurev.arplant.57.032905.105346
    • (2009) Annu. Rev. Plant Biol , vol.60 , pp. 379-406
    • Boller, T.1    Felix, G.2
  • 15
    • 79953285611 scopus 로고    scopus 로고
    • The lectin receptor kinase LecRK-I.9 is a novel Phytophthora resistance component and a potential host target for a RXLR effector
    • doi: 10.1371/journal.ppat.1001327
    • Bouwmeester, K., de Sain, M., Weide, R., Gouget, A., Klamer, S., Canut, H., et al. (2011). The lectin receptor kinase LecRK-I.9 is a novel Phytophthora resistance component and a potential host target for a RXLR effector. PLoS Pathog. 7:e1001327. doi: 10.1371/journal.ppat.1001327
    • (2011) PLoS Pathog , vol.7
    • Bouwmeester, K.1    de Sain, M.2    Weide, R.3    Gouget, A.4    Klamer, S.5    Canut, H.6
  • 16
    • 70350699177 scopus 로고    scopus 로고
    • Arabidopsis L-type lectin receptor kinases: Phylogeny, classification, and expression profiles
    • doi: 10.1093/jxb/erp277
    • Bouwmeester, K., and Govers, F. (2009). Arabidopsis L-type lectin receptor kinases: phylogeny, classification, and expression profiles. J. Exp. Bot. 60, 4383-4396. doi: 10.1093/jxb/erp277
    • (2009) J. Exp. Bot , vol.60 , pp. 4383-4396
    • Bouwmeester, K.1    Govers, F.2
  • 17
    • 84866384889 scopus 로고    scopus 로고
    • The LysM receptor-like kinase LysM RLK1 is required to activate defense and abiotic-stress responses induced by overexpression of fungal chitinases in Arabidopsis plants
    • doi: 10.1093/mp/sss021
    • Brotman, Y., Landau, U., Pnini, S., Lisec, J., Balazadeh, S., Mueller-Roeber, B., et al. (2012). The LysM receptor-like kinase LysM RLK1 is required to activate defense and abiotic-stress responses induced by overexpression of fungal chitinases in Arabidopsis plants. Mol. Plant 5, 1113-1124. doi: 10.1093/mp/sss021
    • (2012) Mol. Plant , vol.5 , pp. 1113-1124
    • Brotman, Y.1    Landau, U.2    Pnini, S.3    Lisec, J.4    Balazadeh, S.5    Mueller-Roeber, B.6
  • 18
    • 42549103340 scopus 로고    scopus 로고
    • LysM, a widely distributed protein motif for binding to (peptido)glycans
    • doi: 10.1111/j.1365-2958.2008.06211.x
    • Buist, G., Steen, A., Kok, J., and Kuipers, O. P. (2008). LysM, a widely distributed protein motif for binding to (peptido)glycans. Mol. Microbiol. 68, 838-847. doi: 10.1111/j.1365-2958.2008.06211.x
    • (2008) Mol. Microbiol , vol.68 , pp. 838-847
    • Buist, G.1    Steen, A.2    Kok, J.3    Kuipers, O.P.4
  • 19
    • 15944390196 scopus 로고    scopus 로고
    • How C-type lectins detect pathogens
    • doi: 10.1111/j.1462-5822.2005.00506.x
    • Cambi, A., Koopman, M., and Figdor, C. G. (2005). How C-type lectins detect pathogens. Cell. Microbiol. 7, 481-488. doi: 10.1111/j.1462-5822.2005.00506.x
    • (2005) Cell. Microbiol , vol.7 , pp. 481-488
    • Cambi, A.1    Koopman, M.2    Figdor, C.G.3
  • 20
    • 84901331667 scopus 로고    scopus 로고
    • Extracellular ATP is a central signaling molecule in plant stress responses
    • doi: 10.1016/j.pbi.2014.04.009
    • Cao, Y., Tanaka, K., Nguyen, C. T., and Stacey, G. (2014). Extracellular ATP is a central signaling molecule in plant stress responses. Curr. Opin. Plant Biol. 20, 82-87. doi: 10.1016/j.pbi.2014.04.009
    • (2014) Curr. Opin. Plant Biol , vol.20 , pp. 82-87
    • Cao, Y.1    Tanaka, K.2    Nguyen, C.T.3    Stacey, G.4
  • 21
    • 84899131887 scopus 로고    scopus 로고
    • An XA21-associated kinase (OsSERK2) regulates immunity mediated by the XA21 and XA3 immune receptors
    • doi: 10.1093/mp/ssu003
    • Chen, X., Zuo, S., Schwessinger, B., Chern, M., Canlas, P. E., Ruan, D., et al. (2014). An XA21-associated kinase (OsSERK2) regulates immunity mediated by the XA21 and XA3 immune receptors. Mol. Plant 7, 874-892. doi: 10.1093/mp/ssu003
    • (2014) Mol. Plant , vol.7 , pp. 874-892
    • Chen, X.1    Zuo, S.2    Schwessinger, B.3    Chern, M.4    Canlas, P.E.5    Ruan, D.6
  • 22
    • 0036616781 scopus 로고    scopus 로고
    • Jasmonic acid methyl ester induces the synthesis of a cytoplasmic/nuclear chitooligosaccharide-binding lectin in tobacco leaves
    • Chen, Y., Peumans, W. J., Hause, B., Bras, J., Kumar, M., Proost, P., et al. (2002a). Jasmonic acid methyl ester induces the synthesis of a cytoplasmic/nuclear chitooligosaccharide-binding lectin in tobacco leaves. FASEB J. 16, 905-907.
    • (2002) FASEB J , vol.16 , pp. 905-907
    • Chen, Y.1    Peumans, W.J.2    Hause, B.3    Bras, J.4    Kumar, M.5    Proost, P.6
  • 23
    • 0037051943 scopus 로고    scopus 로고
    • The Sambucus nigra type-2 ribosome-inactivating protein SNA-I' exhibits in planta antiviral activity in transgenic tobacco
    • doi: 10.1016/S0014-5793(02) 02455-9
    • Chen, Y., Peumans, W. J., and Van Damme, E. J. M. (2002b). The Sambucus nigra type-2 ribosome-inactivating protein SNA-I' exhibits in planta antiviral activity in transgenic tobacco. FEBS Lett. 516, 27-30. doi: 10.1016/S0014-5793(02) 02455-9
    • (2002) FEBS Lett , vol.516 , pp. 27-30
    • Chen, Y.1    Peumans, W.J.2    van Damme, E.J.M.3
  • 24
    • 33644749576 scopus 로고    scopus 로고
    • The Arabidopsis receptor kinase FLS2 binds flg22 and determines the specificity of flagellin perception
    • doi: 10.1105/tpc.105.036574
    • Chinchilla, D., Bauer, Z., Regenass, M., Boller, T., and Felix, G. (2006). The Arabidopsis receptor kinase FLS2 binds flg22 and determines the specificity of flagellin perception. Plant Cell 18, 465-476. doi: 10.1105/tpc.105.036574
    • (2006) Plant Cell , vol.18 , pp. 465-476
    • Chinchilla, D.1    Bauer, Z.2    Regenass, M.3    Boller, T.4    Felix, G.5
  • 25
    • 34547151023 scopus 로고    scopus 로고
    • A flagellin-induced complex of the receptor FLS2 and BAK1 initiates plant defence
    • doi: 10.1038/nature05999
    • Chinchilla, D., Zipfel, C., Robatzek, S., Kemmerling, B., Nürnberger, T., Jones, J. D., et al. (2007). A flagellin-induced complex of the receptor FLS2 and BAK1 initiates plant defence. Nature 448, 497-500. doi: 10.1038/nature05999
    • (2007) Nature , vol.448 , pp. 497-500
    • Chinchilla, D.1    Zipfel, C.2    Robatzek, S.3    Kemmerling, B.4    Nürnberger, T.5    Jones, J.D.6
  • 26
    • 84892572037 scopus 로고    scopus 로고
    • Identification of a plant receptor for extracellular ATP
    • doi: 10.1126/science.343.6168.290
    • Choi, J., Tanaka, K., Cao, Y., Qi, Y., Qiu, J., Liang, Y., et al. (2014). Identification of a plant receptor for extracellular ATP. Science 343, 290-294. doi: 10.1126/science.343.6168.290
    • (2014) Science , vol.343 , pp. 290-294
    • Choi, J.1    Tanaka, K.2    Cao, Y.3    Qi, Y.4    Qiu, J.5    Liang, Y.6
  • 27
    • 84878433740 scopus 로고    scopus 로고
    • The Pseudomonas syringae type III effector AvrRpt2 promotes pathogen virulence via stimulating Arabidopsis auxin/indole acetic acid protein turnover
    • doi: 10.1104/pp.113.219659
    • Cui, F., Wu, S., Sun, W., Coaker, G., Kunkel, B., He, P., et al. (2013). The Pseudomonas syringae type III effector AvrRpt2 promotes pathogen virulence via stimulating Arabidopsis auxin/indole acetic acid protein turnover. Plant Physiol. 162, 1018-1029. doi: 10.1104/pp.113.219659
    • (2013) Plant Physiol , vol.162 , pp. 1018-1029
    • Cui, F.1    Wu, S.2    Sun, W.3    Coaker, G.4    Kunkel, B.5    He, P.6
  • 28
    • 80053623860 scopus 로고    scopus 로고
    • R-type lectins
    • 2nd Edn, Chap. 28, eds E. Varki, R. D. Cummings, J. D. Esko, H. H. Freeze, P. Stanley, C. R. Bertozzi., et al. (Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press)
    • Cummings, R. D., and Etzler, M. E. (2009). R-type lectins, in Essentials of Glycobiology, 2nd Edn, Chap. 28, eds E. Varki, R. D. Cummings, J. D. Esko, H. H. Freeze, P. Stanley, C. R. Bertozzi., et al. (Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press).
    • (2009) Essentials of Glycobiology
    • Cummings, R.D.1    Etzler, M.E.2
  • 29
    • 84881413993 scopus 로고    scopus 로고
    • Pivoting the plant immune system from dissection to deployment
    • doi: 10.1126/science.1236011
    • Dangl, J. L., Horvath, D. M., and Staskawicz, B. J. (2013). Pivoting the plant immune system from dissection to deployment. Science 341, 746-751. doi: 10.1126/science.1236011
    • (2013) Science , vol.341 , pp. 746-751
    • Dangl, J.L.1    Horvath, D.M.2    Staskawicz, B.J.3
  • 30
    • 84884511250 scopus 로고    scopus 로고
    • Molecular assembly of the aerolysin pore reveals a swirling membrane-insertion mechanism
    • doi: 10.1038/nchembio.1312
    • Degiacomi, M. T., Iacovache, I., Pernot, L., Chami, M., Kudryashev, M., Stahlberg, H., et al. (2013). Molecular assembly of the aerolysin pore reveals a swirling membrane-insertion mechanism. Nat. Chem. Biol. 9, 623-629. doi: 10.1038/nchembio.1312
    • (2013) Nat. Chem. Biol , vol.9 , pp. 623-629
    • Degiacomi, M.T.1    Iacovache, I.2    Pernot, L.3    Chami, M.4    Kudryashev, M.5    Stahlberg, H.6
  • 31
    • 84903167621 scopus 로고    scopus 로고
    • In vivo interaction between the tobacco lectin and the core histone proteins
    • doi: 10.1016/j.jplph.2014.04.008
    • Delporte, A., De Vos, W. H., and Van Damme, E. J. M. (2014a). In vivo interaction between the tobacco lectin and the core histone proteins. J. Plant Physiol. 171, 986-992. doi: 10.1016/j.jplph.2014.04.008
    • (2014) J. Plant Physiol , vol.171 , pp. 986-992
    • Delporte, A.1    de Vos, W.H.2    van Damme, E.J.M.3
  • 33
    • 0037394625 scopus 로고    scopus 로고
    • Accumulation of SALT protein in rice plants as a response to environmental stresses
    • doi: 10.1016/S0168-9452(03)00014-1
    • de Souza Filho, G. A., Ferreira, B. S., Dias, J. M. R., Queiroz, K. S., Branco, A. T., Bressan-Smith, R. E., et al. (2003). Accumulation of SALT protein in rice plants as a response to environmental stresses. Plant Sci. 164, 623-628. doi: 10.1016/S0168-9452(03)00014-1
    • (2003) Plant Sci , vol.164 , pp. 623-628
    • de Souza, F.G.A.1    Ferreira, B.S.2    Dias, J.M.R.3    Queiroz, K.S.4    Branco, A.T.5    Bressan-Smith, R.E.6
  • 34
    • 84962011254 scopus 로고    scopus 로고
    • Chapter 6: Nonself perception in plant innate immunity
    • ed. C. López-Larrea (Austin, TX: Landes Bioscience; New York, NY: Springer Science+Business Media)
    • Dubery, I. A., Sanabria, N. M., and Huang, J.-C. (2012). Chapter 6: nonself perception in plant innate immunity, in Self and Nonself, ed. C. López-Larrea (Austin, TX: Landes Bioscience; New York, NY: Springer Science+Business Media).
    • (2012) Self and Nonself
    • Dubery, I.A.1    Sanabria, N.M.2    Huang, J.-C.3
  • 35
    • 2442629457 scopus 로고    scopus 로고
    • Calnexin, calreticulin, and ERp57: Teammates in glycoprotein folding
    • doi: 10.1385/CBB:39:3:223
    • Ellgaard, L., and Frickel, E. M. (2003). Calnexin, calreticulin, and ERp57: teammates in glycoprotein folding. Cell Biochem. Biophys. 39, 223-247. doi: 10.1385/CBB:39:3:223
    • (2003) Cell Biochem. Biophys , vol.39 , pp. 223-247
    • Ellgaard, L.1    Frickel, E.M.2
  • 36
    • 0037182855 scopus 로고    scopus 로고
    • A receptor kinase gene regulating symbiotic nodule development
    • doi: 10.1038/nature00842
    • Endre, G., Kereszt, A., Kevei, Z., Mihacea, S., Kaló, P., and Kiss, G. B. (2002). A receptor kinase gene regulating symbiotic nodule development. Nature 417, 962-966. doi: 10.1038/nature00842
    • (2002) Nature , vol.417 , pp. 962-966
    • Endre, G.1    Kereszt, A.2    Kevei, Z.3    Mihacea, S.4    Kaló, P.5    Kiss, G.B.6
  • 37
    • 0034144354 scopus 로고    scopus 로고
    • A specific β-glucosidase-aggregating factor is responsible for the β-glucosidase null phenotype in maize
    • doi: 10.1104/pp.122.2.563
    • Esen, A., and Blanchard, D. J. (2000). A specific β-glucosidase-aggregating factor is responsible for the β-glucosidase null phenotype in maize. Plant Physiol. 122, 563-572. doi: 10.1104/pp.122.2.563
    • (2000) Plant Physiol , vol.122 , pp. 563-572
    • Esen, A.1    Blanchard, D.J.2
  • 38
    • 66949163724 scopus 로고    scopus 로고
    • Transcriptional regulation of wheat VER2 promoter in rice in response to abscisic acid, jasmonate, and light
    • doi: 10.1016/S1673-8527(08)60126-5
    • Feng, H., Xu, W.-Z., Lin, H.-H., and Chong, K. (2009). Transcriptional regulation of wheat VER2 promoter in rice in response to abscisic acid, jasmonate, and light. J. Genet. Genomics 36, 371-377. doi: 10.1016/S1673-8527(08)60126-5
    • (2009) J. Genet. Genomics , vol.36 , pp. 371-377
    • Feng, H.1    Xu, W.-Z.2    Lin, H.-H.3    Chong, K.4
  • 39
    • 51549094455 scopus 로고    scopus 로고
    • The old Euonymus europaeus agglutinin represents a novel family of ubiquitous plant proteins
    • doi: 10.1104/pp.108.116764
    • Fouquaert, E., Peumans, W. J., Smith, D. F., Proost, P., Savvides, S. N., and Van Damme, E. J. M. (2008). The old Euonymus europaeus agglutinin represents a novel family of ubiquitous plant proteins. Plant Physiol. 147, 1316-1324. doi: 10.1104/pp.108.116764
    • (2008) Plant Physiol , vol.147 , pp. 1316-1324
    • Fouquaert, E.1    Peumans, W.J.2    Smith, D.F.3    Proost, P.4    Savvides, S.N.5    van Damme, E.J.M.6
  • 40
    • 85016377357 scopus 로고    scopus 로고
    • Promiscuity of the euonymus carbohydrate-binding domain
    • doi: 10.3390/biom2040415
    • Fouquaert, E., and Van Damme, E. J. M. (2012). Promiscuity of the euonymus carbohydrate-binding domain. Biomolecules 2, 415-434. doi: 10.3390/biom2040415
    • (2012) Biomolecules , vol.2 , pp. 415-434
    • Fouquaert, E.1    van Damme, E.J.M.2
  • 41
    • 66149095785 scopus 로고    scopus 로고
    • Genetic dissection of Verticillium wilt resistance mediated by tomato Ve1
    • doi: 10.1104/pp.109.136762
    • Fradin, E. F., Zhang, Z., Juarez Ayala, J. C., Castroverde, C. D., Nazar, R. N., Robb, J., et al. (2009). Genetic dissection of Verticillium wilt resistance mediated by tomato Ve1. Plant Physiol. 150, 320-332. doi: 10.1104/pp.109.136762
    • (2009) Plant Physiol , vol.150 , pp. 320-332
    • Fradin, E.F.1    Zhang, Z.2    Juarez, A.J.C.3    Castroverde, C.D.4    Nazar, R.N.5    Robb, J.6
  • 42
    • 80055000869 scopus 로고    scopus 로고
    • Nicotiana attenuata LECTIN RECEPTOR KINASE 1 suppresses the insect-mediated inhibition of induced defense responses during Manduca sexta herbivory
    • doi: 10.1105/tpc.111.088229
    • Gilardoni, P. A., Hettenhausen, C., Baldwin, I. T., and Bonaventure, G. (2011). Nicotiana attenuata LECTIN RECEPTOR KINASE 1 suppresses the insect-mediated inhibition of induced defense responses during Manduca sexta herbivory. Plant Cell 23, 3512-3532. doi: 10.1105/tpc.111.088229
    • (2011) Plant Cell , vol.23 , pp. 3512-3532
    • Gilardoni, P.A.1    Hettenhausen, C.2    Baldwin, I.T.3    Bonaventure, G.4
  • 43
    • 0035006480 scopus 로고    scopus 로고
    • Both the extracellular leucine-rich repeat domain and the kinase activity of FLS2 are required for flagellin binding and signaling in Arabidopsis
    • doi: 10.1105/tpc.13.5.1155
    • Gómez-Gómez, L., Bauer, Z., and Boller, T. (2001). Both the extracellular leucine-rich repeat domain and the kinase activity of FLS2 are required for flagellin binding and signaling in Arabidopsis. Plant Cell 13, 1155-1163. doi: 10.1105/tpc.13.5.1155
    • (2001) Plant Cell , vol.13 , pp. 1155-1163
    • Gómez-Gómez, L.1    Bauer, Z.2    Boller, T.3
  • 44
    • 33750097480 scopus 로고    scopus 로고
    • Subterfuge and manipulation: Type III effector proteins of phytopathogenic bacteria
    • doi: 10.1146/annurev.micro.60.080805. 142251
    • Grant, S. R., Fisher, E. J., Chang, J. H., Mole, B. M., and Dangl, J. L. (2006). Subterfuge and manipulation: type III effector proteins of phytopathogenic bacteria. Annu. Rev. Microbiol. 60, 425-449. doi: 10.1146/annurev.micro.60.080805. 142251
    • (2006) Annu. Rev. Microbiol , vol.60 , pp. 425-449
    • Grant, S.R.1    Fisher, E.J.2    Chang, J.H.3    Mole, B.M.4    Dangl, J.L.5
  • 45
    • 60249091268 scopus 로고    scopus 로고
    • Xanthomonas campestris overcomes Arabidopsis stomatal innate immunity through a DSF cell-to-cell signal-regulated virulence factor
    • doi: 10.1104/pp.108.126870
    • Gudesblat, G. E., Torres, P. S., and Vojnov, A. A. (2009). Xanthomonas campestris overcomes Arabidopsis stomatal innate immunity through a DSF cell-to-cell signal-regulated virulence factor. Plant Physiol. 149, 1017-1027. doi: 10.1104/pp.108.126870
    • (2009) Plant Physiol , vol.149 , pp. 1017-1027
    • Gudesblat, G.E.1    Torres, P.S.2    Vojnov, A.A.3
  • 46
    • 84864385295 scopus 로고    scopus 로고
    • Plant LysM proteins: Modules mediating symbiosis and immunity
    • doi: 10.1016/j.tplants.2012.04.003
    • Gust, A. A., Willmann, R., Desaki, Y., Grabherr, H. M., and Nürnberger, T. (2012). Plant LysM proteins: modules mediating symbiosis and immunity. Trends Plant Sci. 17, 495-502. doi: 10.1016/j.tplants.2012.04.003
    • (2012) Trends Plant Sci , vol.17 , pp. 495-502
    • Gust, A.A.1    Willmann, R.2    Desaki, Y.3    Grabherr, H.M.4    Nürnberger, T.5
  • 47
    • 84892819254 scopus 로고    scopus 로고
    • The leucine-rich repeat receptor kinase BIR2 is a negative regulator of BAK1 in plant immunity
    • doi: 10.1016/j.cub.2013.11.047
    • Halter, T., Imkampe, J., Mazzotta, S., Wierzba, M., Postel, S., Bücherl, C., et al. (2014). The leucine-rich repeat receptor kinase BIR2 is a negative regulator of BAK1 in plant immunity. Curr. Biol. 24, 134-143. doi: 10.1016/j.cub.2013.11.047
    • (2014) Curr. Biol , vol.24 , pp. 134-143
    • Halter, T.1    Imkampe, J.2    Mazzotta, S.3    Wierzba, M.4    Postel, S.5    Bücherl, C.6
  • 48
    • 84900827562 scopus 로고    scopus 로고
    • Structural insight into the activation of plant receptor kinases
    • doi: 10.1016/j.pbi.2014.04.008
    • Han, Z., Sun, Y., and Chai, J. (2014). Structural insight into the activation of plant receptor kinases. Curr. Opin. Plant Biol. 20, 55-63. doi: 10.1016/j.pbi.2014.04.008
    • (2014) Curr. Opin. Plant Biol , vol.20 , pp. 55-63
    • Han, Z.1    Sun, Y.2    Chai, J.3
  • 49
    • 77951157392 scopus 로고    scopus 로고
    • Pattern recognition receptors require N-glycosylation to mediate plant immunity
    • doi: 10.1074/jbc.M109.063073
    • Häweker, H., Rips, S., Koiwa, H., Salomon, S., Saijo, Y., Chinchilla, D., et al. (2010). Pattern recognition receptors require N-glycosylation to mediate plant immunity. J. Biol. Chem. 285, 4629-4636. doi: 10.1074/jbc.M109.063073
    • (2010) J. Biol. Chem , vol.285 , pp. 4629-4636
    • Häweker, H.1    Rips, S.2    Koiwa, H.3    Salomon, S.4    Saijo, Y.5    Chinchilla, D.6
  • 50
    • 84892922883 scopus 로고    scopus 로고
    • Chitin-induced activation of immune signaling by the rice receptor CEBiP relies on a unique sandwich-type dimerization
    • doi: 10.1073/pnas.1312099111
    • Hayafune, M., Berisio, R., Marchetti, R., Silipo, A., Kayama, M., Desaki, Y., et al. (2014). Chitin-induced activation of immune signaling by the rice receptor CEBiP relies on a unique sandwich-type dimerization. Proc. Natl. Acad. Sci. U.S.A. 111, E404-E413. doi: 10.1073/pnas.1312099111
    • (2014) Proc. Natl. Acad. Sci. U.S.A , vol.111
    • Hayafune, M.1    Berisio, R.2    Marchetti, R.3    Silipo, A.4    Kayama, M.5    Desaki, Y.6
  • 51
    • 84877341291 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress responses in plants
    • doi: 10.1146/annurev-arplant-050312-120053
    • Howell, S. H. (2013). Endoplasmic reticulum stress responses in plants. Annu. Rev. Plant Biol. 64, 477-499. doi: 10.1146/annurev-arplant-050312-120053
    • (2013) Annu. Rev. Plant Biol , vol.64 , pp. 477-499
    • Howell, S.H.1
  • 52
    • 84873272792 scopus 로고    scopus 로고
    • Overexpression of L-type lectin-like protein kinase 1 confers pathogen resistance and regulates salinity response in Arabidopsis thaliana
    • doi: 10.1016/j.plantsci.2012.12.019
    • Huang, P., Ju, H.-W., Min, J.-H., Zhang, X., Kim, S.-H., Yang, K.-Y., et al. (2013). Overexpression of L-type lectin-like protein kinase 1 confers pathogen resistance and regulates salinity response in Arabidopsis thaliana. Plant Sci. 203-204, 98-106. doi: 10.1016/j.plantsci.2012.12.019
    • (2013) Plant Sci , vol.203-204 , pp. 98-106
    • Huang, P.1    Ju, H.-W.2    Min, J.-H.3    Zhang, X.4    Kim, S.-H.5    Yang, K.-Y.6
  • 53
    • 84904050452 scopus 로고    scopus 로고
    • The Arabidopsis LecRK-VI.2 associates with the pattern-recognition receptor FLS2 and primes Nicotiana benthamiana pattern-triggered immunity
    • doi: 10.1111/tpj.12557
    • Huang, P.-Y., Yeh, Y.-H., Liu, A.-C., Cheng, C.-P., and Zimmerli, L. (2014). The Arabidopsis LecRK-VI.2 associates with the pattern-recognition receptor FLS2 and primes Nicotiana benthamiana pattern-triggered immunity. Plant J. 79, 243-255. doi: 10.1111/tpj.12557
    • (2014) Plant J , vol.79 , pp. 243-255
    • Huang, P.-Y.1    Yeh, Y.-H.2    Liu, A.-C.3    Cheng, C.-P.4    Zimmerli, L.5
  • 54
    • 29944445545 scopus 로고    scopus 로고
    • Cloning and expression of a novel cDNA encoding a mannose-specific jacalin-related lectin from Oryza sativa
    • doi: 10.1016/j.toxicon. 2005.10.010
    • Jiang, J. F., Han, Y., Xing, L. J., Xu, Y. Y., Xu, Z. H., and Chong, K. (2006). Cloning and expression of a novel cDNA encoding a mannose-specific jacalin-related lectin from Oryza sativa. Toxicon 47, 133-139. doi: 10.1016/j.toxicon. 2005.10.010
    • (2006) Toxicon , vol.47 , pp. 133-139
    • Jiang, J.F.1    Han, Y.2    Xing, L.J.3    Xu, Y.Y.4    Xu, Z.H.5    Chong, K.6
  • 55
    • 33947676369 scopus 로고    scopus 로고
    • Overexpression of OsJAC1, a lectin gene, suppresses the coleoptiles and stem elongation in rice
    • doi: 10.1111/j.1744-7909.2007.00428.x
    • Jiang, J. F., Xu, Y. Y., and Chong, K. (2007). Overexpression of OsJAC1, a lectin gene, suppresses the coleoptiles and stem elongation in rice. J. Integr. Plant Biol. 49, 230-237. doi: 10.1111/j.1744-7909.2007.00428.x
    • (2007) J. Integr. Plant Biol , vol.49 , pp. 230-237
    • Jiang, J.F.1    Xu, Y.Y.2    Chong, K.3
  • 56
    • 69449095737 scopus 로고    scopus 로고
    • A plant-specific calreticulin is a key retention factor for a defective brassinosteroid receptor in the endoplasmic reticulum
    • doi: 10.1073/pnas. 0906144106
    • Jin, H., Hong, Z., Su, W., and Li, J. (2009). A plant-specific calreticulin is a key retention factor for a defective brassinosteroid receptor in the endoplasmic reticulum. Proc. Natl. Acad. Sci. U.S.A. 106, 13612-13617. doi: 10.1073/pnas. 0906144106
    • (2009) Proc. Natl. Acad. Sci. U.S.A , vol.106 , pp. 13612-13617
    • Jin, H.1    Hong, Z.2    Su, W.3    Li, J.4
  • 57
    • 33746582708 scopus 로고    scopus 로고
    • Plant cells recognize chitin fragments for defense signaling through a plasma membrane receptor
    • doi: 10.1073/pnas. 0508882103
    • Kaku, H., Nishizawa, Y., Ishii-Minami, N., Akimoto-Tomiyama, C., Dohmae, N., Takio, K., et al. (2006). Plant cells recognize chitin fragments for defense signaling through a plasma membrane receptor. Proc. Natl. Acad. Sci. U.S.A. 103, 11086-11091. doi: 10.1073/pnas. 0508882103
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 11086-11091
    • Kaku, H.1    Nishizawa, Y.2    Ishii-Minami, N.3    Akimoto-Tomiyama, C.4    Dohmae, N.5    Takio, K.6
  • 58
    • 84902440215 scopus 로고    scopus 로고
    • Structural basis for multiple sugar recognition of jacalin-related human ZG16p lectin
    • doi: 10.1074/jbc.M113.539114
    • Kanagawa, M., Liu, Y., Hanashima, S., Ikeda, A., Chai, W., Nakano, Y., et al. (2014). Structural basis for multiple sugar recognition of jacalin-related human ZG16p lectin. J. Biol. Chem. 289, 16954-16965. doi: 10.1074/jbc.M113.539114
    • (2014) J. Biol. Chem , vol.289 , pp. 16954-16965
    • Kanagawa, M.1    Liu, Y.2    Hanashima, S.3    Ikeda, A.4    Chai, W.5    Nakano, Y.6
  • 59
    • 55849138714 scopus 로고    scopus 로고
    • NbLRK1, a lectin-like receptor kinase protein of Nicotiana benthamiana, interacts with Phytophthora infestans INF1 elicitin and mediates INF1-induced cell death
    • doi: 10.1007/s00425-008-0797-y
    • Kanzaki, H., Saitoh, H., Takahashi, Y., Berberich, T., Ito, A., Kamoun, S., et al. (2008). NbLRK1, a lectin-like receptor kinase protein of Nicotiana benthamiana, interacts with Phytophthora infestans INF1 elicitin and mediates INF1-induced cell death. Planta 228, 977-987. doi: 10.1007/s00425-008-0797-y
    • (2008) Planta , vol.228 , pp. 977-987
    • Kanzaki, H.1    Saitoh, H.2    Takahashi, Y.3    Berberich, T.4    Ito, A.5    Kamoun, S.6
  • 60
    • 0346727443 scopus 로고    scopus 로고
    • Mutational analysis provides molecular insight into the carbohydrate-binding region of calreticulin: Pivotal roles of tyrosine-109 and aspartate-135 in carbohydrate recognition
    • doi: 10.1021/bi0355286
    • Kapoor, M., Ellgaard, L., Gopalakrishnapai, J., Schirra, C., Gemma, E., Oscarson, S., et al. (2004). Mutational analysis provides molecular insight into the carbohydrate-binding region of calreticulin: pivotal roles of tyrosine-109 and aspartate-135 in carbohydrate recognition. Biochemistry 43, 97-106. doi: 10.1021/bi0355286
    • (2004) Biochemistry , vol.43 , pp. 97-106
    • Kapoor, M.1    Ellgaard, L.2    Gopalakrishnapai, J.3    Schirra, C.4    Gemma, E.5    Oscarson, S.6
  • 61
    • 77950901883 scopus 로고    scopus 로고
    • Isolation and characterization of NgRLK1, a receptor-like kinase of Nicotiana glutinosa that interacts with the elicitin of Phytophthora capsici
    • doi: 10.1007/s11033-009-9570-y
    • Kim, Y. T., Oh, J., Kim, K. H., Uhm, J. Y., and Lee, B. M. (2009). Isolation and characterization of NgRLK1, a receptor-like kinase of Nicotiana glutinosa that interacts with the elicitin of Phytophthora capsici. Mol. Biol. Rep. 37, 717-727. doi: 10.1007/s11033-009-9570-y
    • (2009) Mol. Biol. Rep , vol.37 , pp. 717-727
    • Kim, Y.T.1    Oh, J.2    Kim, K.H.3    Uhm, J.Y.4    Lee, B.M.5
  • 62
    • 58949099400 scopus 로고    scopus 로고
    • Homolog of the maize β-glucosidase aggregating factor from sorghum is a jacalin-related GalNAc-specific lectin but lacks protein aggregating activity
    • doi: 10.1093/glycob/cwn132
    • Kittur, F. S., Yu, H. Y., Bevan, D. R., and Esen, A. (2009). Homolog of the maize β-glucosidase aggregating factor from sorghum is a jacalin-related GalNAc-specific lectin but lacks protein aggregating activity. Glycobiology 19,277-287. doi: 10.1093/glycob/cwn132
    • (2009) Glycobiology , vol.19 , pp. 277-287
    • Kittur, F.S.1    Yu, H.Y.2    Bevan, D.R.3    Esen, A.4
  • 63
    • 33746603069 scopus 로고    scopus 로고
    • LysM receptors recognize friend and foe
    • doi: 10.1073/pnas.0604601103
    • Knogge, W., and Scheel, D. (2006). LysM receptors recognize friend and foe. Proc. Natl. Acad. Sci. U.S.A. 103, 10829-10830. doi: 10.1073/pnas.0604601103
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 10829-10830
    • Knogge, W.1    Scheel, D.2
  • 64
    • 84893786939 scopus 로고    scopus 로고
    • CEBiP is the major chitin oligomers-binding protein in rice and plays a main role in the perception of chitin oligomers
    • doi: 10.1007/s11103-013-0149-6
    • Kouzai, Y., Nakajima, K., Hayafune, M., Ozawa, K., Kaku, H., Shibuya, N., et al. (2014). CEBiP is the major chitin oligomers-binding protein in rice and plays a main role in the perception of chitin oligomers. Plant Mol. Biol. 84, 519-528. doi: 10.1007/s11103-013-0149-6
    • (2014) Plant Mol. Biol , vol.84 , pp. 519-528
    • Kouzai, Y.1    Nakajima, K.2    Hayafune, M.3    Ozawa, K.4    Kaku, H.5    Shibuya, N.6
  • 65
    • 77951517299 scopus 로고    scopus 로고
    • Perception of the Arabidopsis danger signal peptide 1 involves the pattern recognition receptor AtPEPR1 and its close homologue AtPEPR2
    • doi: 10.1074/jbc.M109.097394
    • Krol, E., Mentzel, T., Chinchilla, D., Boller, T., Felix, G., Kemmerling, B., et al. (2010). Perception of the Arabidopsis danger signal peptide 1 involves the pattern recognition receptor AtPEPR1 and its close homologue AtPEPR2. J. Biol. Chem. 285, 13471-13479. doi: 10.1074/jbc.M109.097394
    • (2010) J. Biol. Chem , vol.285 , pp. 13471-13479
    • Krol, E.1    Mentzel, T.2    Chinchilla, D.3    Boller, T.4    Felix, G.5    Kemmerling, B.6
  • 66
    • 53849102959 scopus 로고    scopus 로고
    • Do F-box proteins with a C-terminal domain homologous with the tobacco lectin play a role in protein degradation in plants?
    • doi: 10.1042/BST0360843
    • Lannoo, N., Peumans, W. J., and Van Damme, E. J. M. (2008). Do F-box proteins with a C-terminal domain homologous with the tobacco lectin play a role in protein degradation in plants? Biochem. Soc. Trans. 36, 843-847. doi: 10.1042/BST0360843
    • (2008) Biochem. Soc. Trans , vol.36 , pp. 843-847
    • Lannoo, N.1    Peumans, W.J.2    van Damme, E.J.M.3
  • 67
    • 33751083838 scopus 로고    scopus 로고
    • Localization and in vitro binding studies suggest that the cytoplasmic/nuclear tobacco lectin can interact in situ with high-mannose and complex N-glycans
    • doi: 10.1016/j.febslet.2006.10.044
    • Lannoo, N., Peumans, W. J., Van Pamel, E., Alvarez, R., Xiong, T., Hause, G., et al. (2006). Localization and in vitro binding studies suggest that the cytoplasmic/nuclear tobacco lectin can interact in situ with high-mannose and complex N-glycans. FEBS Lett. 580, 6329-6337. doi: 10.1016/j.febslet.2006.10.044
    • (2006) FEBS Lett , vol.580 , pp. 6329-6337
    • Lannoo, N.1    Peumans, W.J.2    van Pamel, E.3    Alvarez, R.4    Xiong, T.5    Hause, G.6
  • 68
    • 77949294113 scopus 로고    scopus 로고
    • Nucleocytoplasmic plant lectins
    • doi: 10.1016/j.bbagen.2009.07.021
    • Lannoo, N., and Van Damme, E. J. (2010). Nucleocytoplasmic plant lectins. Biochem. Biophys. Acta 1800, 190-201. doi: 10.1016/j.bbagen.2009.07.021
    • (2010) Biochem. Biophys. Acta , vol.1800 , pp. 190-201
    • Lannoo, N.1    van Damme, E.J.2
  • 69
    • 34548038411 scopus 로고    scopus 로고
    • The jasmonate-induced expression of the Nicotiana tabacum leaf lectin
    • doi: 10.1093/pcp/ pcm090
    • Lannoo, N., Vandenborre, G., Miersch, O., Smagghe, G., Wasternack, C., Peumans, W. J., et al. (2007). The jasmonate-induced expression of the Nicotiana tabacum leaf lectin. Plant Cell Physiol. 48, 1207-1218. doi: 10.1093/pcp/ pcm090
    • (2007) Plant Cell Physiol , vol.48 , pp. 1207-1218
    • Lannoo, N.1    Vandenborre, G.2    Miersch, O.3    Smagghe, G.4    Wasternack, C.5    Peumans, W.J.6
  • 70
    • 84890856499 scopus 로고    scopus 로고
    • Molecular chaperone function of Arabidopsis thaliana phloem protein 2-A1 encodes a protein similar to phloem lectin
    • doi: 10.1016/j.bbrc.2013.11.034
    • Lee, J. R., Boltz, K. A., and Lee, S. Y. (2014). Molecular chaperone function of Arabidopsis thaliana phloem protein 2-A1 encodes a protein similar to phloem lectin. Biochem. Biophys. Res. Commun. 443, 18-21. doi: 10.1016/j.bbrc.2013.11.034
    • (2014) Biochem. Biophys. Res. Commun , vol.443 , pp. 18-21
    • Lee, J.R.1    Boltz, K.A.2    Lee, S.Y.3
  • 71
    • 0034938756 scopus 로고    scopus 로고
    • Leaf senescence in rice plants: Cloning and characterization of senescence up-regulated genes
    • doi: 10.1093/jexbot/52.358.1117
    • Lee, R. H., Wang, C. H., Huang, L. T., and Chen, S. C. (2001). Leaf senescence in rice plants: cloning and characterization of senescence up-regulated genes. J. Exp. Bot. 52, 1117-1121. doi: 10.1093/jexbot/52.358.1117
    • (2001) J. Exp. Bot , vol.52 , pp. 1117-1121
    • Lee, R.H.1    Wang, C.H.2    Huang, L.T.3    Chen, S.C.4
  • 72
    • 70449413848 scopus 로고    scopus 로고
    • A type I-secreted, sulfated peptide triggers XA21-mediated innate immunity
    • doi: 10.1126/science.1173438
    • Lee, S. W., Han, S. W., Sririyanum, M., Park, C. J., Seo, Y. S., and Ronald, P. C. (2009). A type I-secreted, sulfated peptide triggers XA21-mediated innate immunity. Science 326, 850-853. doi: 10.1126/science.1173438
    • (2009) Science , vol.326 , pp. 850-853
    • Lee, S.W.1    Han, S.W.2    Sririyanum, M.3    Park, C.J.4    Seo, Y.S.5    Ronald, P.C.6
  • 73
    • 84900008928 scopus 로고    scopus 로고
    • Over-expression of ArathEULS3 confers ABA sensitivity and drought tolerance in Arabidopsis
    • doi: 10.1007/s11240-014-0453-0
    • Li, D., Wang, X., Yuan, D., Zhang, L., Jiang, X., Tao, Z., et al. (2014). Over-expression of ArathEULS3 confers ABA sensitivity and drought tolerance in Arabidopsis. Plant Cell Tissue Organ Cult. 117, 431-442. doi: 10.1007/s11240-014-0453-0
    • (2014) Plant Cell Tissue Organ Cult , vol.117 , pp. 431-442
    • Li, D.1    Wang, X.2    Yuan, D.3    Zhang, L.4    Jiang, X.5    Tao, Z.6
  • 74
    • 70349452301 scopus 로고    scopus 로고
    • Specific ER quality control components required for biogenesis of the plant innate immune receptor EFR
    • doi: 10.1073/pnas.0905532106
    • Li, J., Zhao-Hui, C., Batoux, M., Nekrasov, V., Roux, M., Chinchilla, D., et al. (2009). Specific ER quality control components required for biogenesis of the plant innate immune receptor EFR. Proc. Natl. Acad. Sci. U.S.A. 106, 15973-15978. doi: 10.1073/pnas.0905532106
    • (2009) Proc. Natl. Acad. Sci. U.S.A , vol.106 , pp. 15973-15978
    • Li, J.1    Zhao-Hui, C.2    Batoux, M.3    Nekrasov, V.4    Roux, M.5    Chinchilla, D.6
  • 75
    • 0142240337 scopus 로고    scopus 로고
    • LysM domain receptor kinases regulating rhizobial Nod factor-induced infection
    • doi: 10.1126/science.1090074
    • Limpens, E., Franken, C., Smit, P., Willemse, J., Bisseling, T., and Geurts, R. (2003). LysM domain receptor kinases regulating rhizobial Nod factor-induced infection. Science 302, 630-633. doi: 10.1126/science.1090074
    • (2003) Science , vol.302 , pp. 630-633
    • Limpens, E.1    Franken, C.2    Smit, P.3    Willemse, J.4    Bisseling, T.5    Geurts, R.6
  • 76
    • 84866989809 scopus 로고    scopus 로고
    • Lysin motif-containing proteins LYP4 and LYP6 play dual roles in peptidoglycan and chitin perception in rice innate immunity
    • doi: 10.1105/tpc.112.102475
    • Liu, B., Li, J. F., Ao, Y., Qu, J., Li, Z., Su, J., et al. (2012a). Lysin motif-containing proteins LYP4 and LYP6 play dual roles in peptidoglycan and chitin perception in rice innate immunity. Plant Cell 24, 3406-3419. doi: 10.1105/tpc.112.102475
    • (2012) Plant Cell , vol.24 , pp. 3406-3419
    • Liu, B.1    Li, J.F.2    Ao, Y.3    Qu, J.4    Li, Z.5    Su, J.6
  • 77
    • 84861665941 scopus 로고    scopus 로고
    • Chitin-induced dimerization activates a plant immune receptor
    • doi: 10.1126/science.1218867
    • Liu, T., Liu, Z., Song, C., Hu, Y., Han, Z., She, J., et al. (2012b). Chitin-induced dimerization activates a plant immune receptor. Science 336, 1160-1164. doi: 10.1126/science.1218867
    • (2012) Science , vol.336 , pp. 1160-1164
    • Liu, T.1    Liu, Z.2    Song, C.3    Hu, Y.4    Han, Z.5    She, J.6
  • 78
    • 84901059610 scopus 로고    scopus 로고
    • Endoplasmic reticulum-mediated protein quality control in Arabidopsis
    • doi: 10.3389/fpls.2014.00162
    • Liu, Y., and Li, J. (2014). Endoplasmic reticulum-mediated protein quality control in Arabidopsis. Front. Plant Sci. 5:162. doi: 10.3389/fpls.2014.00162
    • (2014) Front. Plant Sci , vol.5 , pp. 162
    • Liu, Y.1    Li, J.2
  • 79
    • 74249087507 scopus 로고    scopus 로고
    • Overexpression of a wheat jasmonate-regulated lectin increases pathogen resistance
    • doi: 10.1016/j.biochi.2009.11.008
    • Ma, Q. H., Tian, B., and Li, Y. L. (2010). Overexpression of a wheat jasmonate-regulated lectin increases pathogen resistance. Biochimie 92, 187-193. doi: 10.1016/j.biochi.2009.11.008
    • (2010) Biochimie , vol.92 , pp. 187-193
    • Ma, Q.H.1    Tian, B.2    Li, Y.L.3
  • 80
    • 84872767678 scopus 로고    scopus 로고
    • Jacalin domain in wheat jasmonate-regulated protein Ta-JA1 confers agglutinating activity and pathogen resistance
    • doi: 10.1016/j.biochi.2012.10.014
    • Ma, Q. H., Zhen, W. B., and Liu, Y. C. (2013). Jacalin domain in wheat jasmonate-regulated protein Ta-JA1 confers agglutinating activity and pathogen resistance. Biochimie 95, 359-365. doi: 10.1016/j.biochi.2012.10.014
    • (2013) Biochimie , vol.95 , pp. 359-365
    • Ma, Q.H.1    Zhen, W.B.2    Liu, Y.C.3
  • 81
    • 84899149746 scopus 로고    scopus 로고
    • Plant PRRs and the activation of innate immune signaling
    • doi: 10.1016/j.molcel.2014.03.028
    • Macho, A. P., and Zipfel, C. (2014). Plant PRRs and the activation of innate immune signaling. Mol. Cell 54, 263-272. doi: 10.1016/j.molcel.2014.03.028
    • (2014) Mol. Cell , vol.54 , pp. 263-272
    • Macho, A.P.1    Zipfel, C.2
  • 82
    • 0142104972 scopus 로고    scopus 로고
    • A receptor kinase gene of the LysM type is involved in legume perception of rhizobial signals
    • doi: 10.1038/nature02045
    • Madsen, E. B., Madsen, L. H., Radutoiu, S., Olbryt, M., Rakwalska, M., Szczyglowski, K., et al. (2003). A receptor kinase gene of the LysM type is involved in legume perception of rhizobial signals. Nature 425, 637-640. doi: 10.1038/nature02045
    • (2003) Nature , vol.425 , pp. 637-640
    • Madsen, E.B.1    Madsen, L.H.2    Radutoiu, S.3    Olbryt, M.4    Rakwalska, M.5    Szczyglowski, K.6
  • 83
    • 84901054390 scopus 로고    scopus 로고
    • The role of the cell wall in plant immunity
    • doi: 10.3389/fpls.2014.00178
    • Malinovsky, F. G., Fangel, J. U., and Willats, W. G. T. (2014). The role of the cell wall in plant immunity. Front. Plant Sci. 5:178. doi: 10.3389/fpls.2014.00178
    • (2014) Front. Plant Sci , vol.5 , pp. 178
    • Malinovsky, F.G.1    Fangel, J.U.2    Willats, W.G.T.3
  • 84
    • 33748129962 scopus 로고    scopus 로고
    • Plant stomata function in innate immunity against bacterial invasion
    • doi: 10.1016/j.cell.2006.06.054
    • Melotto, M., Underwood, W., Koczan, J., Nomura, K., and He, S. Y. (2006). Plant stomata function in innate immunity against bacterial invasion. Cell 126, 969-980. doi: 10.1016/j.cell.2006.06.054
    • (2006) Cell , vol.126 , pp. 969-980
    • Melotto, M.1    Underwood, W.2    Koczan, J.3    Nomura, K.4    He, S.Y.5
  • 85
    • 37649023555 scopus 로고    scopus 로고
    • CERK1, a LysM receptor kinase, is essential for chitin elicitor signaling in Arabidopsis
    • doi: 10.1073/pnas.0705147104
    • Miya, A., Albert, P., Shinya, T., Desaki, Y., Ichimura, K., Shirasu, K., et al. (2007). CERK1, a LysM receptor kinase, is essential for chitin elicitor signaling in Arabidopsis. Proc. Natl. Acad. Sci. U.S.A. 104, 19613-19618. doi: 10.1073/pnas.0705147104
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.104 , pp. 19613-19618
    • Miya, A.1    Albert, P.2    Shinya, T.3    Desaki, Y.4    Ichimura, K.5    Shirasu, K.6
  • 86
    • 33748703839 scopus 로고    scopus 로고
    • LysM domains of Medicago truncatula NFP protein involved in Nod factor perception. Glycosylation state, molecular modeling and docking of chitooligosaccharides and Nod factors
    • doi: 10.1093/glycob/cwl006
    • Mulder, L., Lefebvre, B., Cullimore, J., and Imberty, A. (2006). LysM domains of Medicago truncatula NFP protein involved in Nod factor perception. Glycosylation state, molecular modeling and docking of chitooligosaccharides and Nod factors. Glycobiology 16, 801-809. doi: 10.1093/glycob/cwl006
    • (2006) Glycobiology , vol.16 , pp. 801-809
    • Mulder, L.1    Lefebvre, B.2    Cullimore, J.3    Imberty, A.4
  • 87
    • 84878016523 scopus 로고    scopus 로고
    • Plant innate immunity: An updated insight into defense mechanism
    • doi: 10.1007/s12038-013-9302-2
    • Muthamilarasan, M., and Prasad, M. (2013). Plant innate immunity: an updated insight into defense mechanism. J. Biosci. 38, 433-449. doi: 10.1007/s12038-013-9302-2
    • (2013) J. Biosci , vol.38 , pp. 433-449
    • Muthamilarasan, M.1    Prasad, M.2
  • 88
    • 48849112921 scopus 로고    scopus 로고
    • Antagonistic jacalin-related lectins regulate the size of ER body-type β-glucosidase complexes in Arabidopsis thaliana
    • doi: 10.1093/pcp/pcn075
    • Nagano, A. J., Fukao, Y., Fujiwara, M., Nishimura, M., and Hara-Nishimura, I. (2008). Antagonistic jacalin-related lectins regulate the size of ER body-type β-glucosidase complexes in Arabidopsis thaliana. Plant Cell Physiol. 49, 969-980. doi: 10.1093/pcp/pcn075
    • (2008) Plant Cell Physiol , vol.49 , pp. 969-980
    • Nagano, A.J.1    Fukao, Y.2    Fujiwara, M.3    Nishimura, M.4    Hara-Nishimura, I.5
  • 89
    • 0347052749 scopus 로고    scopus 로고
    • Characterization of four lectin-like receptor kinases expressed in roots of Medicago truncatula structure, location, regulation of expression, and potential role in the symbiosis with Sinorhizobium meliloti
    • doi: 10.1104/pp.103.027680
    • Navarro-Gochicoa, M. T., Camut, S., Timmers, A. C. J., Niebel, A., Herye, C., Boutet, E., et al. (2003). Characterization of four lectin-like receptor kinases expressed in roots of Medicago truncatula structure, location, regulation of expression, and potential role in the symbiosis with Sinorhizobium meliloti. Plant Physiol. 133, 1893-1910. doi: 10.1104/pp.103.027680
    • (2003) Plant Physiol , vol.133 , pp. 1893-1910
    • Navarro-Gochicoa, M.T.1    Camut, S.2    Timmers, A.C.J.3    Niebel, A.4    Herye, C.5    Boutet, E.6
  • 90
    • 84885852278 scopus 로고    scopus 로고
    • MAMP (microbeassociated molecular pattern) triggered immunity in plants
    • doi: 10.3389/fpls.2013.00139
    • Newman, M.-A., Sundelin, T., Nielsen, J. T., and Erbs, G. (2013). MAMP (microbeassociated molecular pattern) triggered immunity in plants. Front. Plant Sci. 4:139. doi: 10.3389/fpls.2013.00139
    • (2013) Front. Plant Sci , vol.4 , pp. 139
    • Newman, M.-A.1    Sundelin, T.2    Nielsen, J.T.3    Erbs, G.4
  • 91
    • 84877051926 scopus 로고    scopus 로고
    • Cell wall integrity signaling and innate immunity in plants
    • doi: 10.3389/fpls.2012.00280
    • Nühse, T. S. (2012). Cell wall integrity signaling and innate immunity in plants. Front. Plant Sci. 3:280. doi: 10.3389/fpls.2012.00280
    • (2012) Front. Plant Sci , vol.3 , pp. 280
    • Nühse, T.S.1
  • 92
    • 84899812833 scopus 로고    scopus 로고
    • The Arabidopsis LYSIN MOTIF-CONTAINING RECEPTOR-LIKE KINASE 3 regulates the cross talk between immunity and abscisic acid responses
    • doi: 10.1104/pp.113.233759
    • Paparella, C., Savatin, D. V., Marti, L., De Lorenzo, G., and Ferrari, S. (2014). The Arabidopsis LYSIN MOTIF-CONTAINING RECEPTOR-LIKE KINASE 3 regulates the cross talk between immunity and abscisic acid responses. Plant Physiol. 165, 262-276. doi: 10.1104/pp.113.233759
    • (2014) Plant Physiol , vol.165 , pp. 262-276
    • Paparella, C.1    Savatin, D.V.2    Marti, L.3    de Lorenzo, G.4    Ferrari, S.5
  • 93
    • 84863299558 scopus 로고    scopus 로고
    • Cleavage and nuclear localization of the rice XA21 immune receptor
    • doi: 10.1038/ncomms1932
    • Park, C. J., and Ronald, P. C. (2012). Cleavage and nuclear localization of the rice XA21 immune receptor. Nat. Commun. 3:920. doi: 10.1038/ncomms1932
    • (2012) Nat. Commun , vol.3 , pp. 920
    • Park, C.J.1    Ronald, P.C.2
  • 94
    • 77956550061 scopus 로고    scopus 로고
    • The lysin motif receptor-like kinase (LysM-RLK) CERK1 is a major chitin-binding protein in Arabidopsis thaliana and subject to chitin-induced phosphorylation
    • doi: 10.1074/jbc.M110.116657
    • Petutschnig, E. K., Jones, A. M., Serazetdinova, L., Lipka, U., and Lipka, V. (2010). The lysin motif receptor-like kinase (LysM-RLK) CERK1 is a major chitin-binding protein in Arabidopsis thaliana and subject to chitin-induced phosphorylation. J. Biol. Chem. 285, 28902-28911. doi: 10.1074/jbc.M110.116657
    • (2010) J. Biol. Chem , vol.285 , pp. 28902-28911
    • Petutschnig, E.K.1    Jones, A.M.2    Serazetdinova, L.3    Lipka, U.4    Lipka, V.5
  • 95
    • 0029379651 scopus 로고
    • Lectins as plant defense proteins
    • doi: 10.1104/pp.109.2.347
    • Peumans, W. J., and Van Damme, E. J. M. (1995). Lectins as plant defense proteins. Plant Physiol. 109, 347-352. doi: 10.1104/pp.109.2.347
    • (1995) Plant Physiol , vol.109 , pp. 347-352
    • Peumans, W.J.1    van Damme, E.J.M.2
  • 96
    • 27144496578 scopus 로고    scopus 로고
    • Hfr-2, a wheat cytolytic toxin-like gene, is up-regulated by virulent Hessian fly larval feeding
    • doi: 10.1111/j.1364- 3703.2005.00289.x
    • Puthoff, D. P., Sardesai, N., Subramanyam, S., Nemacheck, J. A., and Williams, C. E. (2005). Hfr-2, a wheat cytolytic toxin-like gene, is up-regulated by virulent Hessian fly larval feeding. Mol. Plant Pathol. 6, 411-423. doi: 10.1111/j.1364- 3703.2005.00289.x
    • (2005) Mol. Plant Pathol , vol.6 , pp. 411-423
    • Puthoff, D.P.1    Sardesai, N.2    Subramanyam, S.3    Nemacheck, J.A.4    Williams, C.E.5
  • 97
    • 0041828686 scopus 로고    scopus 로고
    • Identification of a lectin gene induced in rice in response to Magnaporthe grisea infection
    • Qin, Q. M., Zhang, Q., Zhao, W. S., Wang, Y. Y., and Peng, Y. L. (2003). Identification of a lectin gene induced in rice in response to Magnaporthe grisea infection. Acta Bot. Sin. 45, 76-81.
    • (2003) Acta Bot. Sin , vol.45 , pp. 76-81
    • Qin, Q.M.1    Zhang, Q.2    Zhao, W.S.3    Wang, Y.Y.4    Peng, Y.L.5
  • 98
    • 84856285927 scopus 로고    scopus 로고
    • A dual regulatory role of Arabidopsis calreticulin-2 in plant innate immunity
    • doi: 10.1111/j.1365-313X.2011.04807.x
    • Qiu, Y., Xi, J., Du, L., Roje, S., and Poovaiah, B. W. (2012). A dual regulatory role of Arabidopsis calreticulin-2 in plant innate immunity. Plant J. 69, 489-500. doi: 10.1111/j.1365-313X.2011.04807.x
    • (2012) Plant J , vol.69 , pp. 489-500
    • Qiu, Y.1    Xi, J.2    Du, L.3    Roje, S.4    Poovaiah, B.W.5
  • 99
    • 0142041483 scopus 로고    scopus 로고
    • Plant recognition of symbiotic bacteria requires two LysM receptor-like kinases
    • doi: 10.1038/ nature02039
    • Radutoiu, S., Madsen, L. H., Madsen, E. B., Felle, H. H., Umehara, Y., Gronlund, M., et al. (2003). Plant recognition of symbiotic bacteria requires two LysM receptor-like kinases. Nature 425, 585-592. doi: 10.1038/ nature02039
    • (2003) Nature , vol.425 , pp. 585-592
    • Radutoiu, S.1    Madsen, L.H.2    Madsen, E.B.3    Felle, H.H.4    Umehara, Y.5    Gronlund, M.6
  • 100
    • 84902285093 scopus 로고    scopus 로고
    • A sunflower lectin with antifungal properties and putative medical mycology applications
    • doi: 10.1007/s00284- 014-0558-z
    • Regente, M., Taveira, G. B., Pinedo, M., Elizalde, M. M., Ticchi, A. J., Diz, M. S. S., et al. (2014). A sunflower lectin with antifungal properties and putative medical mycology applications. Curr. Microbiol. 69, 88-95. doi: 10.1007/s00284- 014-0558-z
    • (2014) Curr. Microbiol , vol.69 , pp. 88-95
    • Regente, M.1    Taveira, G.B.2    Pinedo, M.3    Elizalde, M.M.4    Ticchi, A.J.5    Diz, M.S.S.6
  • 101
    • 0021015566 scopus 로고
    • Adenine binding sites of the lectin from lima beans (Phaseolus lunatus)
    • Roberts, D. D., and Goldstein, I. J. (1983). Adenine binding sites of the lectin from lima beans (Phaseolus lunatus). J. Biol. Chem. 258, 13820-13824.
    • (1983) J. Biol. Chem , vol.258 , pp. 13820-13824
    • Roberts, D.D.1    Goldstein, I.J.2
  • 102
    • 2942683505 scopus 로고    scopus 로고
    • The receptor for the fungal elicitor ethylene-inducing xylanase is a member of a resistance-like gene family in tomato
    • doi: 10.1105/tpc.022475
    • Ron, M., and Avni, A. (2004). The receptor for the fungal elicitor ethylene-inducing xylanase is a member of a resistance-like gene family in tomato. Plant Cell 16, 1604-1615. doi: 10.1105/tpc.022475
    • (2004) Plant Cell , vol.16 , pp. 1604-1615
    • Ron, M.1    Avni, A.2
  • 103
    • 0347926350 scopus 로고    scopus 로고
    • Identification of an essential component of the elicitation active site of the EIX protein elicitor
    • doi: 10.1046/j.1365-313X.2002.01490.x
    • Rotblat, B., Enshell-Seijffers, D., Gershoni, J. M., Schuster, S., and Avni, A. (2002). Identification of an essential component of the elicitation active site of the EIX protein elicitor. Plant J. 32, 1049-1055. doi: 10.1046/j.1365-313X.2002.01490.x
    • (2002) Plant J , vol.32 , pp. 1049-1055
    • Rotblat, B.1    Enshell-Seijffers, D.2    Gershoni, J.M.3    Schuster, S.4    Avni, A.5
  • 104
    • 0034615558 scopus 로고    scopus 로고
    • The systemin signaling pathway: Differential activation of plant defensive genes
    • doi: 10.1016/S0167- 4838(99)00269-1
    • Ryan, C. A. (2000). The systemin signaling pathway: differential activation of plant defensive genes. Biochim. Biophys. Acta 1477, 112-121. doi: 10.1016/S0167- 4838(99)00269-1
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 112-121
    • Ryan, C.A.1
  • 105
    • 0037047060 scopus 로고    scopus 로고
    • The systemin receptor SR160 from Lycop- ersicon peruvianum is a member of the LRR receptor kinase family
    • doi: 10.1073/pnas.132266499
    • Scheer, J. M., and Ryan, C. A. Jr. (2002). The systemin receptor SR160 from Lycop- ersicon peruvianum is a member of the LRR receptor kinase family. Proc. Natl. Acad. Sci. U.S.A. 99, 9585-9590. doi: 10.1073/pnas.132266499
    • (2002) Proc. Natl. Acad. Sci. U.S.A , vol.99 , pp. 9585-9590
    • Scheer, J.M.1    Ryan Jr., C.A.2
  • 107
    • 77951219239 scopus 로고    scopus 로고
    • Rapid heteromerization and phosphorylation of ligand-activated plant transmembrane receptors and their associated kinase BAK1
    • doi: 10.1074/jbc.M109.096842
    • Schulze, B., Mentzel, T., Jehle, A. K., Mueller, K., Beeler, S., Boller, T., et al. (2010). Rapid heteromerization and phosphorylation of ligand-activated plant transmembrane receptors and their associated kinase BAK1. J. Biol. Chem. 285, 9444-9451. doi: 10.1074/jbc.M109.096842
    • (2010) J. Biol. Chem , vol.285 , pp. 9444-9451
    • Schulze, B.1    Mentzel, T.2    Jehle, A.K.3    Mueller, K.4    Beeler, S.5    Boller, T.6
  • 108
    • 79952707705 scopus 로고    scopus 로고
    • Internalization of Sambucus nigra agglutinins I and II in insect midgut cells
    • doi: 10.1002/ arch.20405
    • Shahidi-Noghabi, S., Van Damme, E. J. M., De Vos, W. H., and Smagghe, G. (2011). Internalization of Sambucus nigra agglutinins I and II in insect midgut cells. Arch. Insect Biochem. Physiol. 76, 211-222. doi: 10.1002/ arch.20405
    • (2011) Arch. Insect Biochem. Physiol , vol.76 , pp. 211-222
    • Shahidi-Noghabi, S.1    van Damme, E.J.M.2    de Vos, W.H.3    Smagghe, G.4
  • 109
    • 56249104174 scopus 로고    scopus 로고
    • Carbohydrate-binding activity of the type-2 ribosome-inactivating protein SNA-I from elderberry (Sambucus nigra) is a determining factor for its insectici- dal activity
    • doi: 10.1016/j.phytochem.2008.09.012
    • Shahidi-Noghabi, S., Van Damme, E. J. M., and Smagghe, G. (2008). Carbohydrate-binding activity of the type-2 ribosome-inactivating protein SNA-I from elderberry (Sambucus nigra) is a determining factor for its insectici- dal activity. Phytochemistry 69, 2972-2978. doi: 10.1016/j.phytochem.2008.09.012
    • (2008) Phytochemistry , vol.69 , pp. 2972-2978
    • Shahidi-Noghabi, S.1    van Damme, E.J.M.2    Smagghe, G.3
  • 110
    • 62149087073 scopus 로고    scopus 로고
    • Expression of Sambucus nigra agglutinin (SNA-I') from elderberry bark in transgenic tobacco plants results in enhanced resistance to different insect species
    • doi: 10.1007/s11248-008-9215-2
    • Shahidi-Noghabi, S., Van Damme, E. J. M., and Smagghe, G. (2009). Expression of Sambucus nigra agglutinin (SNA-I') from elderberry bark in transgenic tobacco plants results in enhanced resistance to different insect species. Transgenic Res. 18, 249-259. doi: 10.1007/s11248-008-9215-2
    • (2009) Transgenic Res , vol.18 , pp. 249-259
    • Shahidi-Noghabi, S.1    van Damme, E.J.M.2    Smagghe, G.3
  • 111
    • 84903814915 scopus 로고    scopus 로고
    • Comparative analysis of carbohydrate binding properties of Sambucus nigra lectins and ribosome-inactivating proteins
    • doi: 10.1007/s10719-014-9527-952
    • Shang, C., and Van Damme, E. J. M. (2014). Comparative analysis of carbohydrate binding properties of Sambucus nigra lectins and ribosome-inactivating proteins. Glycoconj. J. 31, 345-354. doi: 10.1007/s10719-014-9527-952
    • (2014) Glycoconj. J , vol.31 , pp. 345-354
    • Shang, C.1    van Damme, E.J.M.2
  • 112
    • 34047262038 scopus 로고    scopus 로고
    • S locus genes and the evolution of self-fertility in Arabidopsis thaliana
    • doi: 10.1105/tpc.106.048199
    • Sherman-Broyles, S., Boggs, N., Farkas, A., Liu, P., Vrebalov, J., Nasrallah, M. E., et al. (2007). S locus genes and the evolution of self-fertility in Arabidopsis thaliana. Plant Cell 19, 94-106. doi: 10.1105/tpc.106.048199
    • (2007) Plant Cell , vol.19 , pp. 94-106
    • Sherman-Broyles, S.1    Boggs, N.2    Farkas, A.3    Liu, P.4    Vrebalov, J.5    Nasrallah, M.E.6
  • 113
    • 78649609189 scopus 로고    scopus 로고
    • Two LysM receptor molecules, CEBiP and OsCERK1, cooperatively regulate chitin elicitor signaling in rice
    • doi: 10.1111/j.1365- 313X.2010.04324.x
    • Shimizu, T., Nakano, T., Takamizawa, D., Desaki, Y., Ishii-Minami, N., Nishizawa, Y., et al. (2010). Two LysM receptor molecules, CEBiP and OsCERK1, cooperatively regulate chitin elicitor signaling in rice. Plant J. 64, 204-214. doi: 10.1111/j.1365- 313X.2010.04324.x
    • (2010) Plant J , vol.64 , pp. 204-214
    • Shimizu, T.1    Nakano, T.2    Takamizawa, D.3    Desaki, Y.4    Ishii-Minami, N.5    Nishizawa, Y.6
  • 114
    • 84867491576 scopus 로고    scopus 로고
    • Functional characterization of CEBiP and CERK1 homologs in Arabidopsis and rice reveals the presence of different chitin receptor systems in plants
    • doi: 10.1093/pcp/pcs113
    • Shinya, T., Motoyama, N., Ikeda, A., Wada, M., Kamiya, K., Hayafune, M., et al. (2012). Functional characterization of CEBiP and CERK1 homologs in Arabidopsis and rice reveals the presence of different chitin receptor systems in plants. Plant Cell Physiol. 53, 1696-1706. doi: 10.1093/pcp/pcs113
    • (2012) Plant Cell Physiol , vol.53 , pp. 1696-1706
    • Shinya, T.1    Motoyama, N.2    Ikeda, A.3    Wada, M.4    Kamiya, K.5    Hayafune, M.6
  • 115
    • 84860206331 scopus 로고    scopus 로고
    • The lectin-receptor kinase-VI.2 is required for priming and positively regulates Arabidopsis pattern-triggered immunity
    • doi: 10.1105/tpc.112.095778
    • Singh, P., Kuo, Y. C., Mishra, S., Tsai, C. H., Chien, C. C., Chen, C. W., et al. (2012). The lectin-receptor kinase-VI.2 is required for priming and positively regulates Arabidopsis pattern-triggered immunity. Plant Cell 24, 1256-1270. doi: 10.1105/tpc.112.095778
    • (2012) Plant Cell , vol.24 , pp. 1256-1270
    • Singh, P.1    Kuo, Y.C.2    Mishra, S.3    Tsai, C.H.4    Chien, C.C.5    Chen, C.W.6
  • 116
    • 84887968915 scopus 로고    scopus 로고
    • Lectin receptor kinases in plant innate immunity
    • doi: 10.3389/fpls.2013.00124
    • Singh, P., and Zimmerli, L. (2013). Lectin receptor kinases in plant innate immunity. Front. Plant Sci. 4:124. doi: 10.3389/fpls.2013.00124
    • (2013) Front. Plant Sci , vol.4 , pp. 124
    • Singh, P.1    Zimmerli, L.2
  • 117
    • 84891794813 scopus 로고    scopus 로고
    • Sensitvity to Flg22 is modulated by ligand-induced degradation and de novo synthesis of the endogenous flagellin-receptor FLAGELLIN-SENSING2
    • doi: 10.1104/pp.113.229179
    • Smith, J. M., Salamango, D. J., Leslie, M. E., Collins, C. A., and Heese, A. (2014). Sensitvity to Flg22 is modulated by ligand-induced degradation and de novo synthesis of the endogenous flagellin-receptor FLAGELLIN-SENSING2. Plant Physiol. 164, 440-454. doi: 10.1104/pp.113.229179
    • (2014) Plant Physiol , vol.164 , pp. 440-454
    • Smith, J.M.1    Salamango, D.J.2    Leslie, M.E.3    Collins, C.A.4    Heese, A.5
  • 118
    • 84888329704 scopus 로고    scopus 로고
    • Association of jacalin-related lectins with wheat responses to stresses revealed by transcriptional profiling
    • doi: 10.1007/s11103-013-0121-5
    • Song, M., Xu, W., Xiang, Y., Jia, H., Zhang, L., and Ma, Z. (2014). Association of jacalin-related lectins with wheat responses to stresses revealed by transcriptional profiling. Plant Mol. Biol. 84, 95-110. doi: 10.1007/s11103-013-0121-5
    • (2014) Plant Mol. Biol , vol.84 , pp. 95-110
    • Song, M.1    Xu, W.2    Xiang, Y.3    Jia, H.4    Zhang, L.5    Ma, Z.6
  • 119
    • 84863472557 scopus 로고    scopus 로고
    • Arabidopsis F-box protein containing a Nictaba-related lectin domain inter- acts with N-acetyllactosamine structures
    • doi: 10.1016/j.fob.2012.06.002
    • Stefanowicz, K., Lannoo, N., Proost, P., and Van Damme, E. J. M. (2012). Arabidopsis F-box protein containing a Nictaba-related lectin domain inter- acts with N-acetyllactosamine structures. FEBS Open Bio 2, 151-158. doi: 10.1016/j.fob.2012.06.002
    • (2012) FEBS Open Bio , vol.2 , pp. 151-158
    • Stefanowicz, K.1    Lannoo, N.2    Proost, P.3    van Damme, E.J.M.4
  • 120
    • 33747229123 scopus 로고    scopus 로고
    • Ribosome-inactivating proteins: Progress and problems
    • doi: 10.1007/s00018-006-6078-7
    • Stirpe, F., and Battelli, M. G. (2006). Ribosome-inactivating proteins: progress and problems. Cell. Mol. Life Sci. 63, 1850-1866. doi: 10.1007/s00018-006-6078-7
    • (2006) Cell. Mol. Life Sci , vol.63 , pp. 1850-1866
    • Stirpe, F.1    Battelli, M.G.2
  • 121
    • 0037182899 scopus 로고    scopus 로고
    • A plant receptor-like kinase required for both bacterial and fungal symbiosis
    • doi: 10.1038/nature00841
    • Stracke, S., Kistner, C., Yoshida, S., Mulder, L., Sato, S., Kaneko, T., et al. (2002). A plant receptor-like kinase required for both bacterial and fungal symbiosis. Nature 417, 959-962. doi: 10.1038/nature00841
    • (2002) Nature , vol.417 , pp. 959-962
    • Stracke, S.1    Kistner, C.2    Yoshida, S.3    Mulder, L.4    Sato, S.5    Kaneko, T.6
  • 122
    • 51549108188 scopus 로고    scopus 로고
    • Functional characterization of HFR1, a high-mannose N-glycan-specific wheat lectin induced by Hessian fly larvae
    • doi: 10.1104/pp.108.116145
    • Subramanyam, S., Smith, D. F., Clemens, J. C., Webb, M. A., Sardesai, N., and Williams, C. E. (2008). Functional characterization of HFR1, a high-mannose N-glycan-specific wheat lectin induced by Hessian fly larvae. Plant Physiol. 147, 1412-1426. doi: 10.1104/pp.108.116145
    • (2008) Plant Physiol , vol.147 , pp. 1412-1426
    • Subramanyam, S.1    Smith, D.F.2    Clemens, J.C.3    Webb, M.A.4    Sardesai, N.5    Williams, C.E.6
  • 123
    • 1342333402 scopus 로고    scopus 로고
    • Xa26, a gene conferring resistance to Xanthomonas oryzae pv. oryzae in rice, encodes an LRR receptor kinase-like protein
    • doi: 10.1046/j.1365-313X.2003. 01976.x
    • Sun, X., Cao, Y., Yang, Z., Xu, C., Li, X., Wang, S., et al. (2004). Xa26, a gene conferring resistance to Xanthomonas oryzae pv. oryzae in rice, encodes an LRR receptor kinase-like protein. Plant J. 37, 517-527. doi: 10.1046/j.1365-313X.2003. 01976.x
    • (2004) Plant J , vol.37 , pp. 517-527
    • Sun, X.1    Cao, Y.2    Yang, Z.3    Xu, C.4    Li, X.5    Wang, S.6
  • 124
    • 84875528603 scopus 로고    scopus 로고
    • GsSRK, a G-type lectin S-receptor-like serine/threonine protein kinase, is a positive regulator of plant tolerance to salt stress
    • doi: 10.1016/j.jplph.2012.11.017
    • Sun, X.-L., Yu, Q.-Y., Tang, L.-L., Ji, W., Bai, X., Cai, H., et al. (2013). GsSRK, a G-type lectin S-receptor-like serine/threonine protein kinase, is a positive regulator of plant tolerance to salt stress. J. Plant Physiol. 170, 505-515. doi: 10.1016/j.jplph.2012.11.017
    • (2013) J. Plant Physiol , vol.170 , pp. 505-515
    • Sun, X.-L.1    Yu, Q.-Y.2    Tang, L.-L.3    Ji, W.4    Bai, X.5    Cai, H.6
  • 125
    • 1042268311 scopus 로고    scopus 로고
    • Expression and interaction analysis of Arabidopsis Skp1-related genes
    • doi: 10.1093/pcp/pch009
    • Takahashi, N., Kuroda, H., Kuromori, T., Hirayama, T., Seki, M., Shinozaki, K., et al. (2004). Expression and interaction analysis of Arabidopsis Skp1-related genes. Plant Cell Physiol. 45, 83-91. doi: 10.1093/pcp/pch009
    • (2004) Plant Cell Physiol , vol.45 , pp. 83-91
    • Takahashi, N.1    Kuroda, H.2    Kuromori, T.3    Hirayama, T.4    Seki, M.5    Shinozaki, K.6
  • 126
    • 84873496181 scopus 로고    scopus 로고
    • Role of LysM receptors in chitin-triggered plant innate immunity
    • doi: 10.4161/psb.22598
    • Tanaka, K., Nguyen, C. T., Liang, Y., Cao, Y., and Stacey, G. (2013). Role of LysM receptors in chitin-triggered plant innate immunity. Plant Signal. Behav. 8:e22598. doi: 10.4161/psb.22598
    • (2013) Plant Signal. Behav , vol.8
    • Tanaka, K.1    Nguyen, C.T.2    Liang, Y.3    Cao, Y.4    Stacey, G.5
  • 127
    • 79958251812 scopus 로고    scopus 로고
    • Diverging functions among calreticulin isoforms in higher plants
    • doi: 10.4161/psb.6.6.15339
    • Thelin, L., Mutwil, M., Sommarin, M., and Persson, S. (2011). Diverging functions among calreticulin isoforms in higher plants. Plant Signal. Behav. 6, 905-910. doi: 10.4161/psb.6.6.15339
    • (2011) Plant Signal. Behav , vol.6 , pp. 905-910
    • Thelin, L.1    Mutwil, M.2    Sommarin, M.3    Persson, S.4
  • 128
    • 79952302258 scopus 로고    scopus 로고
    • Of PAMPs and effec- tors: The blurred PTI-ETI dichotomy
    • doi: 10.1105/tpc.110.082602
    • Thomma, B. P., Nurnberger, T., and Joosten, M. H. (2011). Of PAMPs and effec- tors: the blurred PTI-ETI dichotomy. Plant Cell 23, 4-15. doi: 10.1105/tpc.110.082602
    • (2011) Plant Cell , vol.23 , pp. 4-15
    • Thomma, B.P.1    Nurnberger, T.2    Joosten, M.H.3
  • 129
    • 84901011750 scopus 로고    scopus 로고
    • ER-mediated control for abundance, quality, and signaling of transmembrane immune receptors in plants
    • doi: 10.3389/fpls.2014.00065
    • Tintor, N., and Saijo, Y. (2014). ER-mediated control for abundance, quality, and signaling of transmembrane immune receptors in plants. Front. Plant Sci. 5:65. doi: 10.3389/fpls.2014.00065
    • (2014) Front. Plant Sci , vol.5 , pp. 65
    • Tintor, N.1    Saijo, Y.2
  • 130
    • 84885028241 scopus 로고    scopus 로고
    • Knights in action: Lectin receptor-like kinases in plant development and stress responses
    • doi: 10.1093/mp/sst033
    • Vaid, N., Macovei, A., and Tuteja, N. (2013). Knights in action: lectin receptor-like kinases in plant development and stress responses. Mol. Plant 6, 1405-1418. doi: 10.1093/mp/sst033
    • (2013) Mol. Plant , vol.6 , pp. 1405-1418
    • Vaid, N.1    Macovei, A.2    Tuteja, N.3
  • 131
    • 84867593747 scopus 로고    scopus 로고
    • Genome-wide analysis of lectin receptor-like kinase family from Arabidopsis and rice
    • doi: 10.1007/s11103-012-9952-8
    • Vaid, N., Pandey, P. K., and Tuteja, N. (2012). Genome-wide analysis of lectin receptor-like kinase family from Arabidopsis and rice. Plant Mol. Biol. 80, 365-388. doi: 10.1007/s11103-012-9952-8
    • (2012) Plant Mol. Biol , vol.80 , pp. 365-388
    • Vaid, N.1    Pandey, P.K.2    Tuteja, N.3
  • 133
    • 0034815870 scopus 로고    scopus 로고
    • Ribosome-inactivating proteins: A family of plant proteins that do more than inactivate ribosomes
    • doi: 10.1080/07352689.2001.10131826
    • Van Damme, E. J. M., Hao, Q., Chen, Y., Barre, A., Vandenbussche, F., Desmyter, S., et al. (2001). Ribosome-inactivating proteins: a family of plant proteins that do more than inactivate ribosomes. Crit. Rev. Plant Sci. 20,395-465. doi: 10.1080/07352689.2001.10131826
    • (2001) Crit. Rev. Plant Sci , vol.20 , pp. 395-465
    • van Damme, E.J.M.1    Hao, Q.2    Chen, Y.3    Barre, A.4    Vandenbussche, F.5    Desmyter, S.6
  • 134
    • 57149085053 scopus 로고    scopus 로고
    • Plant lectins
    • doi: 10.1016/S0065-2296(08)00403-5
    • Van Damme, E. J. M., Lannoo, N., and Peumans, W. J. (2008). Plant lectins. Adv. Bot. Res. 48,107-209. doi: 10.1016/S0065-2296(08)00403-5
    • (2008) Adv. Bot. Res , vol.48 , pp. 107-209
    • van Damme, E.J.M.1    Lannoo, N.2    Peumans, W.J.3
  • 135
    • 77649246717 scopus 로고    scopus 로고
    • Nicotiana tabacum agglutinin is active against Lepidopteran pest insects
    • doi: 10.1093/jxb/ erp365
    • Vandenborre, G., Groten, K., Smagghe, G., Lannoo, N., Baldwin, I. T., and Van Damme, E. J. M. (2010). Nicotiana tabacum agglutinin is active against Lepidopteran pest insects. J. Exp. Bot. 61, 1003-1014. doi: 10.1093/jxb/ erp365
    • (2010) J. Exp. Bot , vol.61 , pp. 1003-1014
    • Vandenborre, G.1    Groten, K.2    Smagghe, G.3    Lannoo, N.4    Baldwin, I.T.5    van Damme, E.J.M.6
  • 136
    • 79960736310 scopus 로고    scopus 로고
    • Plant lectins as defense proteins against phytophagous insects
    • doi: 10.1016/j.phytochem.2011.02.024
    • Vandenborre, G., Smagghe, G., and Van Damme, E. J. M. (2011). Plant lectins as defense proteins against phytophagous insects. Phytochemistry 72, 1538-1550. doi: 10.1016/j.phytochem.2011.02.024
    • (2011) Phytochemistry , vol.72 , pp. 1538-1550
    • Vandenborre, G.1    Smagghe, G.2    van Damme, E.J.M.3
  • 137
    • 2142811538 scopus 로고    scopus 로고
    • Analysis of the in planta antiviral activity of elderberry ribosome-inactivating proteins
    • doi: 10.1111/j.1432-1033.2004.04059.x
    • Vandenbussche, F., Desmyter, S., Ciani, M., Proost, P., Peumans, W. J., and Van Damme, E. J. M. (2004a). Analysis of the in planta antiviral activity of elderberry ribosome-inactivating proteins. Eur. J. Biochem. 271, 1508-1515. doi: 10.1111/j.1432-1033.2004.04059.x
    • (2004) Eur. J. Biochem , vol.271 , pp. 1508-1515
    • Vandenbussche, F.1    Desmyter, S.2    Ciani, M.3    Proost, P.4    Peumans, W.J.5    van Damme, E.J.M.6
  • 138
    • 11844289024 scopus 로고    scopus 로고
    • The type-1 and type-2 ribosome-inactivating proteins from Iris confer transgenic tobacco plants local but not systemic protection against viruses
    • doi: 10.1007/s00425-004- 1334-2
    • Vandenbussche, F., Peumans, W. J., Desmyter, S., Proost, P., Ciani, M., and Van Damme, E. J. M. (2004b). The type-1 and type-2 ribosome-inactivating proteins from Iris confer transgenic tobacco plants local but not systemic protection against viruses. Planta 220, 211-221. doi: 10.1007/s00425-004- 1334-2
    • (2004) Planta , vol.220 , pp. 211-221
    • Vandenbussche, F.1    Peumans, W.J.2    Desmyter, S.3    Proost, P.4    Ciani, M.5    van Damme, E.J.M.6
  • 139
    • 80054076082 scopus 로고    scopus 로고
    • Lectin activity of the nucleocytoplasmic EUL protein from Arabidopsis thaliana
    • doi: 10.1016/j.bbrc.2011.09.031
    • Van Hove, J., Fouquaert, E., Smith, D. F., Proost, P., and Van Damme, E. J. M. (2011). Lectin activity of the nucleocytoplasmic EUL protein from Arabidopsis thaliana. Biochem. Biophys. Res. Commun. 414, 101-105. doi: 10.1016/j.bbrc.2011.09.031
    • (2011) Biochem. Biophys. Res. Commun , vol.414 , pp. 101-105
    • van Hove, J.1    Fouquaert, E.2    Smith, D.F.3    Proost, P.4    van Damme, E.J.M.5
  • 140
    • 84865837379 scopus 로고    scopus 로고
    • LYK4, a lysine motif receptor-like kinase, is important for chitin signaling and plant innate immunity in Arabidopsis
    • doi: 10.1104/pp.112.201699
    • Wan, J., Tanaka, K., Zhang, X. C., Son, G. H., Brechenmacher, L., Nguyen, T. H., et al. (2012). LYK4, a lysine motif receptor-like kinase, is important for chitin signaling and plant innate immunity in Arabidopsis. Plant Physiol. 160, 396-406. doi: 10.1104/pp.112.201699
    • (2012) Plant Physiol , vol.160 , pp. 396-406
    • Wan, J.1    Tanaka, K.2    Zhang, X.C.3    Son, G.H.4    Brechenmacher, L.5    Nguyen, T.H.6
  • 141
    • 11144328286 scopus 로고    scopus 로고
    • Toxicity of two type II ribosome-inactivating proteins (cinnamomin and ricin) to domestic silkworm larvae
    • doi: 10.1002/arch.20024
    • Wei, G. Q., Liu, R. S., Wang, Q., and Liu, W. Y. (2004). Toxicity of two type II ribosome-inactivating proteins (cinnamomin and ricin) to domestic silkworm larvae. Arch. Insect Biochem. Physiol. 57, 160-165. doi: 10.1002/arch.20024
    • (2004) Arch. Insect Biochem. Physiol , vol.57 , pp. 160-165
    • Wei, G.Q.1    Liu, R.S.2    Wang, Q.3    Liu, W.Y.4
  • 142
    • 0035990058 scopus 로고    scopus 로고
    • A lectin-like wheat gene responds systemically to attempted feeding by avirulent first-instar Hessian fly larvae
    • doi: 10.1023/A:1016200619766
    • Williams, C. E., Collier, C. C., Nemacheck, J. A., Liang, C., and Cambron, S. E. (2002). A lectin-like wheat gene responds systemically to attempted feeding by avirulent first-instar Hessian fly larvae. J. Chem. Ecol. 28, 1411-1428. doi: 10.1023/A:1016200619766
    • (2002) J. Chem. Ecol , vol.28 , pp. 1411-1428
    • Williams, C.E.1    Collier, C.C.2    Nemacheck, J.A.3    Liang, C.4    Cambron, S.E.5
  • 143
    • 33645080188 scopus 로고    scopus 로고
    • Beyond lectins: The calnexin/calreticulin chaperone sys- tem of the endoplasmic reticulum
    • doi: 10.1242/jcs.02856
    • Williams, D. B. (2006). Beyond lectins: the calnexin/calreticulin chaperone sys- tem of the endoplasmic reticulum. J. Cell Sci. 119, 615-623. doi: 10.1242/jcs.02856
    • (2006) J. Cell Sci , vol.119 , pp. 615-623
    • Williams, D.B.1
  • 144
    • 83755195019 scopus 로고    scopus 로고
    • Arabidopsis lysine-motif proteins LYM1 LYM3 CERK1 mediate bacterial peptidoglycan sensing and immunity to bacterial infection
    • doi: 10.1073/pnas.1112862108
    • Willmann, R., Lajunen, H. M., Erbs, G., Newman, M. A., Kolb, D., Tsuda, K., et al. (2011). Arabidopsis lysine-motif proteins LYM1 LYM3 CERK1 mediate bacterial peptidoglycan sensing and immunity to bacterial infection. Proc. Natl. Acad. Sci. U.S.A. 108, 19824-19829. doi: 10.1073/pnas.1112862108
    • (2011) Proc. Natl. Acad. Sci. U.S.A , vol.108 , pp. 19824-19829
    • Willmann, R.1    Lajunen, H.M.2    Erbs, G.3    Newman, M.A.4    Kolb, D.5    Tsuda, K.6
  • 145
    • 84888007160 scopus 로고    scopus 로고
    • On the front line: Struc- tural insights into plant-pathogen interactions
    • doi: 10.1038/nrmicro3118
    • Wirthmueller, L., Maqbool, A., and Banfield, M. J. (2013). On the front line: struc- tural insights into plant-pathogen interactions. Nat. Rev. Microbiol. 11, 761-776. doi: 10.1038/nrmicro3118
    • (2013) Nat. Rev. Microbiol , vol.11 , pp. 761-776
    • Wirthmueller, L.1    Maqbool, A.2    Banfield, M.J.3
  • 146
    • 33746384018 scopus 로고    scopus 로고
    • Transgenic cotton, expressing Amaranthus caudatus agglutinin, confers enhanced resistance to aphids
    • doi: 10.1111/j.1439-0523.2006.01247.x
    • Wu, J., Luo, X., Guo, H., Xiao, J., and Tian, Y. (2006). Transgenic cotton, expressing Amaranthus caudatus agglutinin, confers enhanced resistance to aphids. Plant Breed.125, 390-394. doi: 10.1111/j.1439-0523.2006.01247.x
    • (2006) Plant Breed , vol.125 , pp. 390-394
    • Wu, J.1    Luo, X.2    Guo, H.3    Xiao, J.4    Tian, Y.5
  • 147
    • 82255163278 scopus 로고    scopus 로고
    • A jacalin- related lectin-like gene in wheat is a component of the plant defence system
    • doi: 10.1093/jxb/err226
    • Xiang, Y., Song, M., Wei, Z., Tong, J., Zhang, L., Xiao, L., et al. (2011). A jacalin- related lectin-like gene in wheat is a component of the plant defence system. J. Exp. Bot. 62, 5471-5483. doi: 10.1093/jxb/err226
    • (2011) J. Exp. Bot , vol.62 , pp. 5471-5483
    • Xiang, Y.1    Song, M.2    Wei, Z.3    Tong, J.4    Zhang, L.5    Xiao, L.6
  • 148
    • 79961194243 scopus 로고    scopus 로고
    • Transgenic potato overexpressing the Amaranthus caudatus agglutinin gene to confer aphid resistance
    • doi: 10.2135/cropsci2010.11.0650
    • Xin, Y., Xiangrong, Z., Mingju, Z., Wenchao, G., Yingchuan, T., Qizhong, X., et al. (2011). Transgenic potato overexpressing the Amaranthus caudatus agglutinin gene to confer aphid resistance. Crop Sci. 51, 2119-2124. doi: 10.2135/cropsci2010.11.0650
    • (2011) Crop Sci , vol.51 , pp. 2119-2124
    • Xin, Y.1    Xiangrong, Z.2    Mingju, Z.3    Wenchao, G.4    Yingchuan, T.5    Qizhong, X.6
  • 149
    • 84859034258 scopus 로고    scopus 로고
    • Lectin-mediated resistance impairs plant virus infection at the cellular level
    • doi: 10.1105/tpc.111.093658
    • Yamaji, Y., Maejima, K., Ozeki, J., Komatsu, K., Shiraishi, T., Okano, Y., et al. (2012). Lectin-mediated resistance impairs plant virus infection at the cellular level. Plant Cell 24, 778-793. doi: 10.1105/tpc.111.093658
    • (2012) Plant Cell , vol.24 , pp. 778-793
    • Yamaji, Y.1    Maejima, K.2    Ozeki, J.3    Komatsu, K.4    Shiraishi, T.5    Okano, Y.6
  • 150
    • 0038082174 scopus 로고    scopus 로고
    • Vernalization- induced flowering in wheat is mediated by a lectin-like gene VER2
    • Yong, W. D., Xu, Y. Y., Xu, W. Z., Wang, X., Li, N., Wu, J. S., et al. (2003). Vernalization- induced flowering in wheat is mediated by a lectin-like gene VER2. Planta 217, 261-270.
    • (2003) Planta , vol.217 , pp. 261-270
    • Yong, W.D.1    Xu, Y.Y.2    Xu, W.Z.3    Wang, X.4    Li, N.5    Wu, J.S.6
  • 151
    • 78651303570 scopus 로고    scopus 로고
    • Harpin-induced expression and transgenic overexpression of the phloem protein gene AtPP2-A1 in Arabidopsis repress phloem feeding of the green peach aphid Myzus persicae
    • doi: 10.1186/1471- 2229-11-11
    • Zhang, C., Shi, H., Chen, L., Wang, X., Lu, B., Zhang, S., et al. (2011). Harpin-induced expression and transgenic overexpression of the phloem protein gene AtPP2-A1 in Arabidopsis repress phloem feeding of the green peach aphid Myzus persicae. BMC Plant Biol. 11:11. doi: 10.1186/1471- 2229-11-11
    • (2011) BMC Plant Biol , vol.11 , pp. 11
    • Zhang, C.1    Shi, H.2    Chen, L.3    Wang, X.4    Lu, B.5    Zhang, S.6
  • 152
    • 33646525169 scopus 로고    scopus 로고
    • Perception of the bacterial PAMP EF-Tu by the receptor EFR restricts Agrobacterium-mediated transformation
    • doi: 10.1016/j.cell.2006.03.037
    • Zipfel, C., Kunze, G., Chinchilla, D., Caniard, A., Jones, J. D., Boller, T., et al. (2006). Perception of the bacterial PAMP EF-Tu by the receptor EFR restricts Agrobacterium-mediated transformation. Cell 125,749-760. doi: 10.1016/j.cell.2006.03.037
    • (2006) Cell , vol.125 , pp. 749-760
    • Zipfel, C.1    Kunze, G.2    Chinchilla, D.3    Caniard, A.4    Jones, J.D.5    Boller, T.6
  • 153
    • 0034072442 scopus 로고    scopus 로고
    • Isolation and characterization of a jacalin-related mannose-binding lectin from salt-stressed rice (Oryza sativa) plants
    • doi: 10.1007/s004250050705
    • Zhang, W., Peumans, W. J., Barre, A., Astoul, C. H., Rovira, P., Rougé, P., et al. (2000). Isolation and characterization of a jacalin-related mannose-binding lectin from salt-stressed rice (Oryza sativa) plants. Planta 210, 970-978. doi: 10.1007/s004250050705
    • (2000) Planta , vol.210 , pp. 970-978
    • Zhang, W.1    Peumans, W.J.2    Barre, A.3    Astoul, C.H.4    Rovira, P.5    Rougé, P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.