메뉴 건너뛰기




Volumn 11, Issue 11, 2013, Pages 761-776

On the front line: Structural insights into plant-pathogen interactions

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHOTRANSFERASE;

EID: 84888007160     PISSN: 17401526     EISSN: 17401534     Source Type: Journal    
DOI: 10.1038/nrmicro3118     Document Type: Review
Times cited : (92)

References (161)
  • 1
    • 76749108117 scopus 로고    scopus 로고
    • Armed and dangerous
    • Pennisi, E. Armed and dangerous. Science 327, 804-805 (2010).
    • (2010) Science , vol.327 , pp. 804-805
    • Pennisi, E.1
  • 2
    • 84872158786 scopus 로고    scopus 로고
    • Planetary disasters: It could happen one night
    • Jones, N. Planetary disasters: It could happen one night. Nature 493, 154-156 (2013).
    • (2013) Nature , vol.493 , pp. 154-156
    • Jones, N.1
  • 4
    • 84871272212 scopus 로고    scopus 로고
    • Effector biology of plant-associated organisms: Concepts and perspectives
    • Win, J. et al. Effector biology of plant-associated organisms: concepts and perspectives. Cold Spring Harb. Symp. Quant. Biol. 77, 235-247 (2012)
    • (2012) Cold Spring Harb. Symp. Quant. Biol. , vol.77 , pp. 235-247
    • Win, J.1
  • 5
    • 77954763024 scopus 로고    scopus 로고
    • Plant immunity: Towards an integrated view of plant-pathogen interactions
    • 323-329 2006
    • Dodds, P. N. & Rathjen, J. P. Plant immunity: towards an integrated view of plant-pathogen interactions. Nature Rev. Genet. 11, 539-548 (2010).
    • (2010) Nature Rev. Genet. , vol.11 , pp. 539-548
    • Dodds, P.N.1    Rathjen, J.P.2
  • 6
    • 33751100626 scopus 로고    scopus 로고
    • The plant immune system
    • DOI 10.1038/nature05286, PII NATURE05286
    • Jones, J. D. & Dangl, J. L. The plant immune system. Nature 444, 323-329 (2006). (Pubitemid 44764102)
    • (2006) Nature , vol.444 , Issue.7117 , pp. 323-329
    • Jones, J.D.G.1    Dangl, J.L.2
  • 7
    • 79952302258 scopus 로고    scopus 로고
    • Of PAMPs and effectors: The blurred PTI-ETI dichotomy
    • Thomma, B. P., Nurnberger, T. & Joosten, M. H. Of PAMPs and effectors: the blurred PTI-ETI dichotomy. Plant Cell 23, 4-15 (2011).
    • (2011) Plant Cell , vol.23 , pp. 4-15
    • Thomma, B.P.1    Nurnberger, T.2    Joosten, M.H.3
  • 8
    • 66249135697 scopus 로고    scopus 로고
    • A renaissance of elicitors: Perception of microbe-associated molecular patterns and danger signals by pattern-recognition receptors
    • Boller, T. & Felix, G. A renaissance of elicitors: perception of microbe-associated molecular patterns and danger signals by pattern-recognition receptors. Annu. Rev. Plant Biol. 60, 379-406 (2009).
    • (2009) Annu. Rev. Plant Biol. , vol.60 , pp. 379-406
    • Boller, T.1    Felix, G.2
  • 9
    • 32944479048 scopus 로고    scopus 로고
    • Host-microbe interactions: Shaping the evolution of the plant immune response
    • DOI 10.1016/j.cell.2006.02.008, PII S0092867406001838
    • Chisholm, S. T., Coaker, G., Day, B. & Staskawicz, B. J. Host-microbe interactions: shaping the evolution of the plant immune response. Cell 124, 803-814 (2006). (Pubitemid 43261453)
    • (2006) Cell , vol.124 , Issue.4 , pp. 803-814
    • Chisholm, S.T.1    Coaker, G.2    Day, B.3    Staskawicz, B.J.4
  • 10
    • 3242663688 scopus 로고    scopus 로고
    • The Nep1-like proteins - A growing family of microbial elicitors of plant necrosis
    • DOI 10.1111/j.1364-3703.2004.00235.x
    • Pemberton, C. L. & Salmond, G. P. The Nep1-like proteins-a growing family of microbial elicitors of plant necrosis. Mol. Plant Pathol. 5, 353-359 (2004). (Pubitemid 38940771)
    • (2004) Molecular Plant Pathology , vol.5 , Issue.4 , pp. 353-359
    • Pemberton, C.L.1    Salmond, G.P.C.2
  • 11
    • 67649880530 scopus 로고    scopus 로고
    • A common toxin fold mediates microbial attack and plant defense
    • Ottmann, C. et al. A common toxin fold mediates microbial attack and plant defense. Proc. Natl Acad. Sci. USA 106, 10359-10364 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 10359-10364
    • Ottmann, C.1
  • 12
    • 33747595647 scopus 로고    scopus 로고
    • Nep1-like proteins from plant pathogens: Recruitment and diversification of the NPP1 domain across taxa
    • DOI 10.1016/j.phytochem.2005.12.008, PII S0031942205006758
    • Gijzen, M. & Nurnberger, T. Nep1-like proteins from plant pathogens: recruitment and diversification of the NPP1 domain across taxa. Phytochemistry 67, 1800-1807 (2006). (Pubitemid 44262364)
    • (2006) Phytochemistry , vol.67 , Issue.16 , pp. 1800-1807
    • Gijzen, M.1    Nurnberger, T.2
  • 14
    • 84860168324 scopus 로고    scopus 로고
    • Nontoxic Nep1-like proteins of the downy mildew pathogen Hyaloperonospora arabidopsidis: Repression of necrosis-inducing activity by a surface-exposed region
    • Cabral, A. et al. Nontoxic Nep1-like proteins of the downy mildew pathogen Hyaloperonospora arabidopsidis: repression of necrosis-inducing activity by a surface-exposed region. Mol. Plant Microbe Interact. 25, 697-708 (2012).
    • (2012) Mol. Plant Microbe Interact. , vol.25 , pp. 697-708
    • Cabral, A.1
  • 15
    • 33746225235 scopus 로고    scopus 로고
    • Synergistic interactions of the plant cell death pathways induced by Phytophthora infestans Nep1-like protein PiNPP1.1 and INF1 elicitin
    • DOI 10.1094/MPMI-19-0854
    • Kanneganti, T. D., Huitema, E., Cakir, C. & Kamoun, S. Synergistic interactions of the plant cell death pathways induced by Phytophthora infestans Nepl-like protein PiNPP1.1 and INF1 elicitin. Mol. Plant Microbe Interact. 19, 854-863 (2006). (Pubitemid 44098617)
    • (2006) Molecular Plant-Microbe Interactions , vol.19 , Issue.8 , pp. 854-863
    • Kanneganti, T.-D.1    Huitema, E.2    Cakir, C.3    Kamoun, S.4
  • 17
    • 70350400636 scopus 로고    scopus 로고
    • Molecular mechanism of pore formation by actinoporins
    • Kristan, K. C., Viero, G., Dalla Serra, M., Macek, P. & Anderluh, G. Molecular mechanism of pore formation by actinoporins. Toxicon 54, 1125-1134 (2009).
    • (2009) Toxicon , vol.54 , pp. 1125-1134
    • Kristan, K.C.1    Viero, G.2    Dalla, S.M.3    MacEk, P.4    Anderluh, G.5
  • 19
    • 80755156284 scopus 로고    scopus 로고
    • The crystal structure of necrosis-and ethylene-inducing protein 2 from the causal agent of cacao's Witches' Broom disease reveals key elements for its activity
    • Zaparoli, G. et al. The crystal structure of necrosis-and ethylene-inducing protein 2 from the causal agent of cacao's Witches' Broom disease reveals key elements for its activity. Biochemistry 50, 9901-9910 (2011).
    • (2011) Biochemistry , vol.50 , pp. 9901-9910
    • Zaparoli, G.1
  • 20
    • 33748334490 scopus 로고    scopus 로고
    • A catalogue of the effector secretome of plant pathogenic oomycetes
    • DOI 10.1146/annurev.phyto.44.070505.143436
    • Kamoun, S. A catalogue of the effector secretome of plant pathogenic oomycetes. Annu. Rev. Phytopathol. 44, 41-60 (2006). (Pubitemid 44435697)
    • (2006) Annual Review of Phytopathology , vol.44 , pp. 41-60
    • Kamoun, S.1
  • 21
    • 32544442145 scopus 로고    scopus 로고
    • Polygalacturonase inhibiting proteins: Players in plant innate immunity?
    • DOI 10.1016/j.tplants.2005.12.005, PII S1360138505003031
    • Federici, L., Di Matteo, A., Fernandez-Recio, J., Tsernoglou, D. & Cervone, F. Polygalacturonase inhibiting proteins: players in plant innate immunity? Trends Plant Sci. 11, 65-70 (2006). (Pubitemid 43238417)
    • (2006) Trends in Plant Science , vol.11 , Issue.2 , pp. 65-70
    • Federici, L.1    Di Matteo, A.2    Fernandez-Recio, J.3    Tsernoglou, D.4    Cervone, F.5
  • 22
    • 0034789069 scopus 로고    scopus 로고
    • The role of polygalacturonase-inhibiting proteins (PGIPS) in defense against pathogenic fungi
    • DOI 10.1146/annurev.phyto.39.1.313
    • De Lorenzo, G., D'Ovidio, R. & Cervone, F. The role of polygalacturonase-inhibiting proteins (PGIPs) in defense against pathogenic fungi. Annu. Rev. Phytopathol. 39, 313-335 (2001). (Pubitemid 32965188)
    • (2001) Annual Review of Phytopathology , vol.39 , pp. 313-335
    • De Lorenzo, G.1    D'Ovidio, R.2    Cervone, F.3
  • 23
    • 77952690864 scopus 로고    scopus 로고
    • A domain swap approach reveals a role of the plant wall-associated kinase 1 (WAK1) as a receptor of oligogalacturonides
    • Brutus, A., Sicilia, F., Macone, A., Cervone, F. & De Lorenzo, G. A domain swap approach reveals a role of the plant wall-associated kinase 1 (WAK1) as a receptor of oligogalacturonides. Proc. Natl Acad. Sci. USA 107, 9452-9457 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 9452-9457
    • Brutus, A.1    Sicilia, F.2    MacOne, A.3    Cervone, F.4    De Lorenzo, G.5
  • 25
    • 66149150616 scopus 로고    scopus 로고
    • Integration of evolutionary and desolvation energy analysis identifies functional sites in a plant immunity protein
    • Casasoli, M. et al. Integration of evolutionary and desolvation energy analysis identifies functional sites in a plant immunity protein. Proc. Natl Acad. Sci. USA 106, 7666-7671 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 7666-7671
    • Casasoli, M.1
  • 26
    • 0033522402 scopus 로고    scopus 로고
    • The specificity of polygalacturonase-inhibiting protein (PGIP): A single amino acid substitution in the solvent-exposed β-strand/β-turn region of the leucine-rich repeats (LRRs) confers a new recognition capability
    • DOI 10.1093/emboj/18.9.2352
    • Leckie, F. et al. The specificity of polygalacturonase-inhibiting protein (PGIP): a single amino acid substitution in the solvent-exposed ?-strand/?-turn region of the leucine-rich repeats (LRRs) confers a new recognition capability. EMBO J. 18, 2352-2363 (1999). (Pubitemid 29213269)
    • (1999) EMBO Journal , vol.18 , Issue.9 , pp. 2352-2363
    • Leckie, F.1    Mattei, B.2    Capodicasa, C.3    Hemmings, A.4    Nuss, L.5    Aracri, B.6    De Lorenzo, G.7    Cervone, F.8
  • 27
    • 80053585495 scopus 로고    scopus 로고
    • Structural resolution of the complex between a fungal polygalacturonase and a plant polygalacturonase-inhibiting protein by small-angle X-ray scattering
    • Benedetti, M. et al. Structural resolution of the complex between a fungal polygalacturonase and a plant polygalacturonase-inhibiting protein by small-angle X-ray scattering. Plant Physiol. 157, 599-607 (2011).
    • (2011) Plant Physiol. , vol.157 , pp. 599-607
    • Benedetti, M.1
  • 28
    • 84861665941 scopus 로고    scopus 로고
    • Chitin-induced dimerization activates a plant immune receptor
    • Liu, T. et al. Chitin-induced dimerization activates a plant immune receptor. Science 336, 1160-1164 (2012).
    • (2012) Science , vol.336 , pp. 1160-1164
    • Liu, T.1
  • 29
    • 84863097745 scopus 로고    scopus 로고
    • How plant lysin motif receptors get activated: Lessons learned from structural biology
    • Willmann, R. & Nurnberger, T. How plant lysin motif receptors get activated: Lessons learned from structural biology. Sci. Signal. 5, e28 (2012).
    • (2012) Sci. Signal. , vol.5
    • Willmann, R.1    Nurnberger, T.2
  • 30
    • 37649023555 scopus 로고    scopus 로고
    • CERK1, a LysM receptor kinase, is essential for chitin elicitor signaling in Arabidopsis
    • Miya, A. et al. CERK1, a LysM receptor kinase, is essential for chitin elicitor signaling in Arabidopsis. Proc. Natl Acad. Sci. USA 104, 19613-19618 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 19613-19618
    • Miya, A.1
  • 32
    • 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
    • Petutschnig, E. K., Jones, A. M., Serazetdinova, L., Lipka, U. & Lipka, V. 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 (2010).
    • (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
  • 33
    • 77449083235 scopus 로고    scopus 로고
    • Direct binding of a plant LysM receptor-like kinase, LysM RLK1/CERK1, to chitin in vitro
    • Iizasa, E., Mitsutomi, M. & Nagano, Y. Direct binding of a plant LysM receptor-like kinase, LysM RLK1/CERK1, to chitin in vitro. J. Biol. Chem. 285, 2996-3004 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 2996-3004
    • Iizasa, E.1    Mitsutomi, M.2    Nagano, Y.3
  • 34
    • 77955841193 scopus 로고    scopus 로고
    • Chitooligosaccharide sensing and downstream signaling: Contrasted outcomes in pathogenic and beneficial plant-microbe interactions
    • Hamel, L. P. & Beaudoin, N. Chitooligosaccharide sensing and downstream signaling: contrasted outcomes in pathogenic and beneficial plant-microbe interactions. Planta 232, 787-806 (2010).
    • (2010) Planta , vol.232 , pp. 787-806
    • Hamel, L.P.1    Beaudoin, N.2
  • 37
    • 0034640111 scopus 로고    scopus 로고
    • Eukaryotic fatty acylation drives plasma membrane targeting and enhances function of several type III effector proteins from Pseudomonas syringae
    • Nimchuk, Z. et al. Eukaryotic fatty acylation drives plasma membrane targeting and enhances function of several type III effector proteins from Pseudomonas syringae. Cell 101, 353-363 (2000).
    • (2000) Cell , vol.101 , pp. 353-363
    • Nimchuk, Z.1
  • 38
    • 0034927988 scopus 로고    scopus 로고
    • Eukaryotic features of the Xanthomonas type III effector AvrBs3: Protein domains involved in transcriptional activation and the interaction with nuclear import receptors from pepper
    • DOI 10.1046/j.0960-7412.2001.01046.x
    • Szurek, B., Marois, E., Bonas, U. & Van den Ackerveken, G. Eukaryotic features of the Xanthomonas type III effector AvrBs3: protein domains involved in transcriptional activation and the interaction with nuclear import receptors from pepper. Plant J. 26, 523-534 (2001). (Pubitemid 32665050)
    • (2001) Plant Journal , vol.26 , Issue.5 , pp. 523-534
    • Szurek, B.1    Marois, E.2    Bonas, U.3    Van Ackerveken, G.D.4
  • 39
    • 84855682453 scopus 로고    scopus 로고
    • Subcellular localization of the Hpa RxLR effector repertoire identifies a tonoplast-associated protein HaRxL17 that confers enhanced plant susceptibility
    • Caillaud, M. C. et al. Subcellular localization of the Hpa RxLR effector repertoire identifies a tonoplast-associated protein HaRxL17 that confers enhanced plant susceptibility. Plant J. 69, 252-265 (2012).
    • (2012) Plant J. , vol.69 , pp. 252-265
    • Caillaud, M.C.1
  • 40
    • 70350235037 scopus 로고    scopus 로고
    • From bacterial avirulence genes to effector functions via the hrp delivery system: An overview of 25 years of progress in our understanding of plant innate immunity
    • Mansfield, J. W. From bacterial avirulence genes to effector functions via the hrp delivery system: an overview of 25 years of progress in our understanding of plant innate immunity. Mol. Plant Pathol. 10, 721-734 (2009).
    • (2009) Mol. Plant Pathol. , vol.10 , pp. 721-734
    • Mansfield, J.W.1
  • 41
    • 83655167376 scopus 로고    scopus 로고
    • Structural analysis of Pseudomonas syringae AvrPtoB bound to host BAK1 reveals two similar kinase-interacting domains in a type III effector
    • Cheng, W. et al. Structural analysis of Pseudomonas syringae AvrPtoB bound to host BAK1 reveals two similar kinase-interacting domains in a type III effector. Cell Host Microbe 10, 616-626 (2011).
    • (2011) Cell Host Microbe , vol.10 , pp. 616-626
    • Cheng, W.1
  • 42
    • 61449086250 scopus 로고    scopus 로고
    • AvrPtoB targets the LysM receptor kinase CERK1 to promote bacterial virulence on plants
    • Gimenez-Ibanez, S. et al. AvrPtoB targets the LysM receptor kinase CERK1 to promote bacterial virulence on plants. Curr. Biol. 19, 423-429 (2009).
    • (2009) Curr. Biol. , vol.19 , pp. 423-429
    • Gimenez-Ibanez, S.1
  • 43
    • 35848959483 scopus 로고    scopus 로고
    • The N-terminal region of Pseudomonas type III effector AvrPtoB elicits Pto-dependent immunity and has two distinct virulence determinants
    • DOI 10.1111/j.1365-313X.2007.03259.x
    • Xiao, F. et al. The N-terminal region of Pseudomonas type III effector AvrPtoB elicits Pto-dependent immunity and has two distinct virulence determinants. Plant J. 52, 595-614 (2007). (Pubitemid 350060585)
    • (2007) Plant Journal , vol.52 , Issue.4 , pp. 595-614
    • Xiao, F.1    He, P.2    Abramovitch, R.B.3    Dawson, J.E.4    Nicholson, L.K.5    Sheen, J.6    Martin, G.B.7
  • 44
    • 83655199961 scopus 로고    scopus 로고
    • A tomato LysM receptor-like kinase promotes immunity and its kinase activity is inhibited by AvrPtoB
    • Zeng, L., Velasquez, A. C., Munkvold, K. R., Zhang, J. & Martin, G. B. A tomato LysM receptor-like kinase promotes immunity and its kinase activity is inhibited by AvrPtoB. Plant J. 69, 92-103 (2012).
    • (2012) Plant J. , vol.69 , pp. 92-103
    • Zeng, L.1    Velasquez, A.C.2    Munkvold, K.R.3    Zhang, J.4    Martin, G.B.5
  • 45
    • 46749157912 scopus 로고    scopus 로고
    • Bacterial Effectors Target the Common Signaling Partner BAK1 to Disrupt Multiple MAMP Receptor-Signaling Complexes and Impede Plant Immunity
    • DOI 10.1016/j.chom.2008.05.017, PII S1931312808001893
    • Shan, L. et al. Bacterial effectors target the common signaling partner BAK1 to disrupt multiple MAMP receptor-signaling complexes and impede plant immunity. Cell Host Microbe 4, 17-27 (2008). (Pubitemid 351944052)
    • (2008) Cell Host and Microbe , vol.4 , Issue.1 , pp. 17-27
    • Shan, L.1    He, P.2    Li, J.3    Heese, A.4    Peck, S.C.5    Nurnberger, T.6    Martin, G.B.7    Sheen, J.8
  • 46
    • 33646134105 scopus 로고    scopus 로고
    • Specific bacterial suppressors of MAMP signaling upstream of MAPKKK in Arabidopsis innate immunity
    • He, P. et al. Specific bacterial suppressors of MAMP signaling upstream of MAPKKK in Arabidopsis innate immunity. Cell 125, 563-575 (2006).
    • (2006) Cell , vol.125 , pp. 563-575
    • He, P.1
  • 47
    • 30844458212 scopus 로고    scopus 로고
    • A bacterial inhibitor of host programmed cell death defenses is an E3 ubiquitin ligase
    • DOI 10.1126/science.1120131
    • Janjusevic, R., Abramovitch, R. B., Martin, G. B. & Stebbins, C. E. A bacterial inhibitor of host programmed cell death defenses is an E3 ubiquitin ligase. Science 311, 222-226 (2006). (Pubitemid 43108186)
    • (2006) Science , vol.311 , Issue.5758 , pp. 222-226
    • Janjusevic, R.1    Abramovitch, R.B.2    Martin, G.B.3    Stebbins, C.E.4
  • 48
    • 70349243161 scopus 로고    scopus 로고
    • Crystal structure of the complex between Pseudomonas effector AvrPtoB and the tomato Pto kinase reveals both a shared and a unique interface compared with AvrPto-Pto
    • Dong, J. et al. Crystal structure of the complex between Pseudomonas effector AvrPtoB and the tomato Pto kinase reveals both a shared and a unique interface compared with AvrPto-Pto. Plant Cell 21, 1846-1859 (2009).
    • (2009) Plant Cell , vol.21 , pp. 1846-1859
    • Dong, J.1
  • 49
    • 84863014802 scopus 로고    scopus 로고
    • Structural analysis of HopPmaL reveals the presence of a second adaptor domain common to the HopAB family of Pseudomonas syringae type III effectors
    • Singer, A. U. et al. Structural analysis of HopPmaL reveals the presence of a second adaptor domain common to the HopAB family of Pseudomonas syringae type III effectors. Biochemistry 51, 1-3 (2012).
    • (2012) Biochemistry , vol.51 , pp. 1-3
    • Singer, A.U.1
  • 50
    • 40149083472 scopus 로고    scopus 로고
    • Pseudomonas syringae effector AvrPto blocks innate immunity by targeting receptor kinases
    • Xiang, T. et al. Pseudomonas syringae effector AvrPto blocks innate immunity by targeting receptor kinases. Curr. Biol. 18, 74-80 (2008).
    • (2008) Curr. Biol. , vol.18 , pp. 74-80
    • Xiang, T.1
  • 52
    • 78650652060 scopus 로고    scopus 로고
    • BAK1 is not a target of the Pseudomonas syringae effector AvrPto
    • Xiang, T. et al. BAK1 is not a target of the Pseudomonas syringae effector AvrPto. Mol. Plant Microbe Interact. 24, 100-107 (2011).
    • (2011) Mol. Plant Microbe Interact. , vol.24 , pp. 100-107
    • Xiang, T.1
  • 53
    • 3142534455 scopus 로고    scopus 로고
    • The solution structure of type III effector protein AvrPto reveals conformational and dynamic features important for plant pathogenesis
    • DOI 10.1016/j.str.2004.04.017, PII S0969212604001704
    • Wulf, J., Pascuzzi, P. E., Fahmy, A., Martin, G. B. & Nicholson, L. K. The solution structure of type III effector protein AvrPto reveals conformational and dynamic features important for plant pathogenesis. Structure 12, 1257-1268 (2004). (Pubitemid 38900768)
    • (2004) Structure , vol.12 , Issue.7 , pp. 1257-1268
    • Wulf, J.1    Pascuzzi, P.E.2    Fahmy, A.3    Martin, G.B.4    Nicholson, L.K.5
  • 55
    • 84888016483 scopus 로고    scopus 로고
    • SmADP-RTs: Versatile virulence factors from bacterial pathogens of plants and mammals
    • Wirthmueller, L. & Banfield, M. J. mADP-RTs: versatile virulence factors from bacterial pathogens of plants and mammals. Front. Plant Sci. 3, 142 (2012).
    • (2012) Front. Plant Sci. , vol.3 , pp. 142
    • Wirthmueller, L.1    Banfield, M.J.2
  • 56
    • 84875222858 scopus 로고    scopus 로고
    • Pseudomonas HopU1 modulates plant immune receptor levels by blocking the interaction of their mRNAs with GRP7
    • Nicaise, V. et al. Pseudomonas HopU1 modulates plant immune receptor levels by blocking the interaction of their mRNAs with GRP7. EMBO J. 32, 701-712 (2013).
    • (2013) EMBO J. , vol.32 , pp. 701-712
    • Nicaise, V.1
  • 57
    • 83355169694 scopus 로고    scopus 로고
    • Structure function analysis of an ADP-ribosyltransferase type III effector and its RNA-binding target in plant immunity
    • Jeong, B. R. et al. Structure function analysis of an ADP-ribosyltransferase type III effector and its RNA-binding target in plant immunity. J. Biol. Chem. 286, 43272-43281 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 43272-43281
    • Jeong, B.R.1
  • 58
    • 36849007471 scopus 로고    scopus 로고
    • Auto-regulation of the circadian slave oscillator component AtGRP7 and regulation of its targets is impaired by a single RNA recognition motif point mutation
    • DOI 10.1111/j.1365-313X.2007.03302.x
    • Schoning, J. C. et al. Auto-regulation of the circadian slave oscillator component AtGRP7 and regulation of its targets is impaired by a single RNA recognition motif point mutation. Plant J. 52, 1119-1130 (2007). (Pubitemid 350231155)
    • (2007) Plant Journal , vol.52 , Issue.6 , pp. 1119-1130
    • Schoning, J.C.1    Streitner, C.2    Page, D.R.3    Hennig, S.4    Uchida, K.5    Wolf, E.6    Furuya, M.7    Staiger, D.8
  • 59
    • 4444333128 scopus 로고    scopus 로고
    • Crystal structures of the type III effector protein AvrPphF and its chaperone reveal residues required for plant pathogenesis
    • DOI 10.1016/j.str.2004.06.023, PII S0969212604002771
    • Singer, A. U. et al. Crystal structures of the type III effector protein AvrPphF and its chaperone reveal residues required for plant pathogenesis. Structure 12, 1669-1681 (2004). (Pubitemid 39200519)
    • (2004) Structure , vol.12 , Issue.9 , pp. 1669-1681
    • Singer, A.U.1    Desveaux, D.2    Betts, L.3    Chang, J.H.4    Nimchuk, Z.5    Grant, S.R.6    Dangl, J.L.7    Sondek, J.8
  • 60
    • 77955854952 scopus 로고    scopus 로고
    • A Pseudomonas syringae ADP-ribosyltransferase inhibits Arabidopsis mitogen-activated protein kinase kinases
    • Wang, Y. et al. A Pseudomonas syringae ADP-ribosyltransferase inhibits Arabidopsis mitogen-activated protein kinase kinases. Plant Cell 22, 2033-2044 (2010).
    • (2010) Plant Cell , vol.22 , pp. 2033-2044
    • Wang, Y.1
  • 61
    • 76649108592 scopus 로고    scopus 로고
    • The type III effector HopF2Pto targets Arabidopsis RIN4 protein to promote Pseudomonas syringae virulence
    • Wilton, M. et al. The type III effector HopF2Pto targets Arabidopsis RIN4 protein to promote Pseudomonas syringae virulence. Proc. Natl Acad. Sci. USA 107, 2349-2354 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 2349-2354
    • Wilton, M.1
  • 62
    • 57649100731 scopus 로고    scopus 로고
    • Plant pattern-recognition receptor FLS2 is directed for degradation by the bacterial ubiquitin ligase AvrPtoB
    • Gohre, V. et al. Plant pattern-recognition receptor FLS2 is directed for degradation by the bacterial ubiquitin ligase AvrPtoB. Curr. Biol. 18, 1824-1832 (2008).
    • (2008) Curr. Biol. , vol.18 , pp. 1824-1832
    • Gohre, V.1
  • 63
    • 77954583000 scopus 로고    scopus 로고
    • Receptor-like cytoplasmic kinases integrate signaling from multiple plant immune receptors and are targeted by a Pseudomonas syringae effector
    • Zhang, J. et al. Receptor-like cytoplasmic kinases integrate signaling from multiple plant immune receptors and are targeted by a Pseudomonas syringae effector. Cell Host Microbe 7, 290-301 (2010).
    • (2010) Cell Host Microbe , vol.7 , pp. 290-301
    • Zhang, J.1
  • 65
    • 0037205231 scopus 로고    scopus 로고
    • A Yersinia effector and a Pseudomonas avirulence protein define a family of cysteine proteases functioning in bacterial pathogenesis
    • DOI 10.1016/S0092-8674(02)00766-3
    • Shao, F., Merritt, P. M., Bao, Z., Innes, R. W. & Dixon, J. E. A Yersinia effector and a Pseudomonas avirulence protein define a family of cysteine proteases functioning in bacterial pathogenesis. Cell 109, 575-588 (2002). (Pubitemid 34628721)
    • (2002) Cell , vol.109 , Issue.5 , pp. 575-588
    • Shao, F.1    Merritt, P.M.2    Bao, Z.3    Innes, R.W.4    Dixon, J.E.5
  • 66
    • 76249083550 scopus 로고    scopus 로고
    • A receptor-like cytoplasmic kinase, BIK1, associates with a flagellin receptor complex to initiate plant innate immunity
    • Lu, D. et al. A receptor-like cytoplasmic kinase, BIK1, associates with a flagellin receptor complex to initiate plant innate immunity. Proc. Natl Acad. Sci. USA 107, 496-501 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 496-501
    • Lu, D.1
  • 68
    • 84862556859 scopus 로고    scopus 로고
    • Activation of a plant nucleotide binding-leucine rich repeat disease resistance protein by a modified self protein
    • DeYoung, B. J., Qi, D., Kim, S. H., Burke, T. P. & Innes, R. W. Activation of a plant nucleotide binding-leucine rich repeat disease resistance protein by a modified self protein. Cell. Microbiol. 14, 1071-1084 (2012).
    • (2012) Cell. Microbiol , vol.14 , pp. 1071-1084
    • Deyoung, B.J.1    Qi, D.2    Kim, S.H.3    Burke, T.P.4    Innes, R.W.5
  • 69
    • 0042322616 scopus 로고    scopus 로고
    • Cleavage of Arabidopsis PBS1 by a bacterial type III effector
    • DOI 10.1126/science.1085671
    • Shao, F. et al. Cleavage of Arabidopsis PBS1 by a bacterial type III effector. Science 301, 1230-1233 (2003). (Pubitemid 37052210)
    • (2003) Science , vol.301 , Issue.5637 , pp. 1230-1233
    • Shao, F.1    Golstein, C.2    Ade, J.3    Stoutemyer, M.4    Dixon, J.E.5    Innes, R.W.6
  • 70
    • 84875074459 scopus 로고    scopus 로고
    • A pathogen type III effector with a novel E3 ubiquitin ligase architecture
    • Singer, A. U. et al. A pathogen type III effector with a novel E3 ubiquitin ligase architecture. PLoS Pathog. 9, e1003121 (2013). This is an excellent example of how structural biology can promote elucidation of the molecular functions of plant pathogen effectors.
    • (2013) PLoS Pathog , vol.9
    • Singer, A.U.1
  • 71
    • 57149105701 scopus 로고    scopus 로고
    • Structure of the Shigella T3SS effector IpaH defines a new class of E3 ubiquitin ligases
    • Singer, A. U. et al. Structure of the Shigella T3SS effector IpaH defines a new class of E3 ubiquitin ligases. Nature Struct. Mol. Biol. 15, 1293-1301 (2008).
    • (2008) Nature Struct. Mol. Biol. , vol.15 , pp. 1293-1301
    • Singer, A.U.1
  • 72
    • 63849280748 scopus 로고    scopus 로고
    • A family of Salmonella virulence factors functions as a distinct class of autoregulated E3 ubiquitin ligases
    • Quezada, C. M., Hicks, S. W., Galan, J. E. & Stebbins, C. E. A family of Salmonella virulence factors functions as a distinct class of autoregulated E3 ubiquitin ligases. Proc. Natl Acad. Sci. USA 106, 4864-4869 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 4864-4869
    • Quezada, C.M.1    Hicks, S.W.2    Galan, J.E.3    Stebbins, C.E.4
  • 73
    • 57749115920 scopus 로고    scopus 로고
    • XopD SUMO protease affects host transcription, promotes pathogen growth, and delays symptom development in Xanthomonas-infected tomato leaves
    • Kim, J. G. et al. XopD SUMO protease affects host transcription, promotes pathogen growth, and delays symptom development in Xanthomonas-infected tomato leaves. Plant Cell 20, 1915-1929 (2008).
    • (2008) Plant Cell , vol.20 , pp. 1915-1929
    • Kim, J.G.1
  • 75
    • 84873890584 scopus 로고    scopus 로고
    • Xanthomonas type III effector XopD sesumoylates tomato transcription factor SlERF4 to suppress ethylene responses and promote pathogen growth
    • Kim, J. G., Stork, W. & Mudgett, M. B. Xanthomonas type III effector XopD sesumoylates tomato transcription factor SlERF4 to suppress ethylene responses and promote pathogen growth. Cell Host Microbe 13, 143-154 (2013).
    • (2013) Cell Host Microbe , vol.13 , pp. 143-154
    • Kim, J.G.1    Stork, W.2    Mudgett, M.B.3
  • 76
    • 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. & Dangl, J. L. Subterfuge and manipulation: type III effector proteins of phytopathogenic bacteria. Annu. Rev. Microbiol. 60, 425-449 (2006). (Pubitemid 44627956)
    • (2006) Annual Review of Microbiology , 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
  • 77
    • 20444369525 scopus 로고    scopus 로고
    • Two Pseudomonas syringae type III effectors inhibit RIN4-regulated basal defense in Arabidopsis
    • DOI 10.1016/j.cell.2005.03.025, PII S0092867405002977
    • Kim, M. G. et al. Two Pseudomonas syringae type III effectors inhibit RIN4-regulated basal defense in Arabidopsis. Cell 121, 749-759 (2005). (Pubitemid 40797597)
    • (2005) Cell , vol.121 , Issue.5 , pp. 749-759
    • Kim, M.G.1    Da Cunha, L.2    McFall, A.J.3    Belkhadir, Y.4    DebRoy, S.5    Dangl, J.L.6    Mackey, D.7
  • 78
    • 67649959828 scopus 로고    scopus 로고
    • RIN4 functions with plasma membrane H+ATPases to regulate stomatal apertures during pathogen attack
    • Liu, J. et al. RIN4 functions with plasma membrane H+ATPases to regulate stomatal apertures during pathogen attack. PLoS Biol. 7, e1000139 (2009).
    • (2009) PLoS Biol. , vol.7
    • Liu, J.1
  • 79
    • 82755195642 scopus 로고    scopus 로고
    • Separable fragments and membrane tethering of Arabidopsis RIN4 regulate its suppression of PAMP-triggered immunity
    • Afzal, A. J., da Cunha, L. & Mackey, D. Separable fragments and membrane tethering of Arabidopsis RIN4 regulate its suppression of PAMP-triggered immunity. Plant Cell 23, 3798-3811 (2011).
    • (2011) Plant Cell , vol.23 , pp. 3798-3811
    • Afzal, A.J.1    Da Cunha, L.2    MacKey, D.3
  • 80
    • 70349656645 scopus 로고    scopus 로고
    • Proteolysis of a negative regulator of innate immunity is dependent on resistance genes in tomato and Nicotiana benthamiana and induced by multiple bacterial effectors
    • Luo, Y., Caldwell, K. S., Wroblewski, T., Wright, M. E. & Michelmore, R. W. Proteolysis of a negative regulator of innate immunity is dependent on resistance genes in tomato and Nicotiana benthamiana and induced by multiple bacterial effectors. Plant Cell 21, 2458-2472 (2009).
    • (2009) Plant Cell , vol.21 , pp. 2458-2472
    • Luo, Y.1    Caldwell, K.S.2    Wroblewski, T.3    Wright, M.E.4    Michelmore, R.W.5
  • 81
    • 76649108592 scopus 로고    scopus 로고
    • The type III effector HopF2Pto targets Arabidopsis RIN4 protein to promote Pseudomonas syringae virulence
    • Wilton, M. et al. The type III effector HopF2Pto targets Arabidopsis RIN4 protein to promote Pseudomonas syringae virulence. Proc. Natl Acad. Sci. USA 107, 2349-2354 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 2349-2354
    • Wilton, M.1
  • 82
    • 0037155687 scopus 로고    scopus 로고
    • RIN4 interacts with Pseudomonas syringae type III effector molecules and is required for RPM1-mediated resistance in Arabidopsis
    • DOI 10.1016/S0092-8674(02)00661-X
    • Mackey, D., Holt, B. F., 3rd, Wiig, A. & Dangl, J. L. RIN4 interacts with Pseudomonas syringae type III effector molecules and is required for RPM1-mediated resistance in Arabidopsis. Cell 108, 743-754 (2002). (Pubitemid 34327527)
    • (2002) Cell , vol.108 , Issue.6 , pp. 743-754
    • Mackey, D.1    Holt III, B.F.2    Wiig, A.3    Dangl, J.L.4
  • 83
    • 0141566396 scopus 로고    scopus 로고
    • Genetic and molecular evidence that the Pseudomonas syringae type III effector protein AvrRpt2 is a cysteine protease
    • DOI 10.1046/j.1365-2958.2003.03666.x
    • Axtell, M. J., Chisholm, S. T., Dahlbeck, D. & Staskawicz, B. J. Genetic and molecular evidence that the Pseudomonas syringae type III effector protein AvrRpt2 is a cysteine protease. Mol. Microbiol. 49, 1537-1546 (2003). (Pubitemid 37153514)
    • (2003) Molecular Microbiology , vol.49 , Issue.6 , pp. 1537-1546
    • Axtell, M.J.1    Chisholm, S.T.2    Dahlbeck, D.3    Staskawicz, B.J.4
  • 84
    • 0037423390 scopus 로고    scopus 로고
    • Initiation of RPS2-specified disease resistance in Arabidopsis is coupled to the AvrRpt2-directed elimination of RIN4
    • DOI 10.1016/S0092-8674(03)00036-9
    • Axtell, M. J. & Staskawicz, B. J. Initiation of RPS2-specified disease resistance in Arabidopsis is coupled to the AvrRpt2-directed elimination of RIN4. Cell 112, 369-377 (2003). (Pubitemid 36183656)
    • (2003) Cell , vol.112 , Issue.3 , pp. 369-377
    • Axtell, M.J.1    Staskawicz, B.J.2
  • 85
    • 0037423306 scopus 로고    scopus 로고
    • Arabidopsis RIN4 is a target of the type III virulence effector AvrRpt2 and modulates RPS2-mediated resistance
    • DOI 10.1016/S0092-8674(03)00040-0
    • Mackey, D., Belkhadir, Y., Alonso, J. M., Ecker, J. R. & Dangl, J. L. Arabidopsis RIN4 is a target of the type III virulence effector AvrRpt2 and modulates RPS2-mediated resistance. Cell 112, 379-389 (2003). (Pubitemid 36183657)
    • (2003) Cell , vol.112 , Issue.3 , pp. 379-389
    • Mackey, D.1    Belkhadir, Y.2    Alonso, J.M.3    Ecker, J.R.4    Dangl, J.L.5
  • 87
    • 79951636212 scopus 로고    scopus 로고
    • A receptor-like cytoplasmic kinase phosphorylates the host target RIN4, leading to the activation of a plant innate immune receptor
    • Liu, J., Elmore, J. M., Lin, Z. J. & Coaker, G. A receptor-like cytoplasmic kinase phosphorylates the host target RIN4, leading to the activation of a plant innate immune receptor. Cell Host Microbe 9, 137-146 (2011).
    • (2011) Cell Host Microbe , vol.9 , pp. 137-146
    • Liu, J.1    Elmore, J.M.2    Lin, Z.J.3    Coaker, G.4
  • 89
    • 34047233602 scopus 로고    scopus 로고
    • Type III effector activation via nucleotide binding, phosphorylation, and host target interaction
    • Desveaux, D. et al. Type III effector activation via nucleotide binding, phosphorylation, and host target interaction. PLoS Pathog. 3, e48 (2007).
    • (2007) PLoS Pathog , vol.3
    • Desveaux, D.1
  • 90
    • 18144399349 scopus 로고    scopus 로고
    • The Pseudomonas syringae effector AvrRpt2 cleaves its C-terminally acylated target, RIN4, from Arabidopsis membranes to block RPM1 activation
    • Kim, H. S. et al. The Pseudomonas syringae effector AvrRpt2 cleaves its C-terminally acylated target, RIN4, from Arabidopsis membranes to block RPM1 activation. Proc. Natl Acad. Sci. USA 102, 6496-6501 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 6496-6501
    • Kim, H.S.1
  • 91
    • 84860541901 scopus 로고    scopus 로고
    • A Xanthomonas uridine 5?-monophosphate transferase inhibits plant immune kinases
    • Feng, F. et al. A Xanthomonas uridine 5?-monophosphate transferase inhibits plant immune kinases. Nature 485, 114-118 (2012).
    • (2012) Nature , vol.485 , pp. 114-118
    • Feng, F.1
  • 92
    • 67149136177 scopus 로고    scopus 로고
    • Fido a novel AMPylation domain common to fic, doc, and AvrB
    • Kinch, L. N., Yarbrough, M. L., Orth, K. & Grishin, N. V. Fido, a novel AMPylation domain common to fic, doc, and AvrB. PLoS ONE 4, e5818 (2009).
    • (2009) PLoS ONE , vol.4
    • Kinch, L.N.1    Yarbrough, M.L.2    Orth, K.3    Grishin, N.V.4
  • 93
    • 63649139064 scopus 로고    scopus 로고
    • The fic domain: Regulation of cell signaling by adenylylation
    • Worby, C. A. et al. The fic domain: regulation of cell signaling by adenylylation. Mol. Cell 34, 93-103 (2009).
    • (2009) Mol. Cell , vol.34 , pp. 93-103
    • Worby, C.A.1
  • 94
    • 58149400542 scopus 로고    scopus 로고
    • AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding and downstream signaling
    • Yarbrough, M. L. et al. AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding and downstream signaling. Science 323, 269-272 (2009).
    • (2009) Science , vol.323 , pp. 269-272
    • Yarbrough, M.L.1
  • 95
    • 0037205227 scopus 로고    scopus 로고
    • Two distinct Pseudomonas effector proteins interact with the Pto kinase and activate plant immunity
    • DOI 10.1016/S0092-8674(02)00743-2
    • Kim, Y. J., Lin, N. C. & Martin, G. B. Two distinct Pseudomonas effector proteins interact with the Pto kinase and activate plant immunity. Cell 109, 589-598 (2002). (Pubitemid 34628722)
    • (2002) Cell , vol.109 , Issue.5 , pp. 589-598
    • Kim, Y.J.1    Lin, N.-C.2    Martin, G.B.3
  • 96
    • 84875079085 scopus 로고    scopus 로고
    • The tomato Prf complex is a molecular trap for bacterial effectors based on pto transphosphorylation
    • Ntoukakis, V. et al. The tomato Prf complex is a molecular trap for bacterial effectors based on pto transphosphorylation. PLoS Pathog. 9, e1003123 (2013).
    • (2013) PLoS Pathog , vol.9
    • Ntoukakis, V.1
  • 97
    • 34447542796 scopus 로고    scopus 로고
    • A bacterial E3 ubiquitin ligase targets a host protein kinase to disrupt plant immunity
    • DOI 10.1038/nature05966, PII NATURE05966
    • Rosebrock, T. R. et al. A bacterial E3 ubiquitin ligase targets a host protein kinase to disrupt plant immunity. Nature 448, 370-374 (2007). (Pubitemid 47080344)
    • (2007) Nature , vol.448 , Issue.7151 , pp. 370-374
    • Rosebrock, T.R.1    Zeng, L.2    Brady, J.J.3    Abramovitch, R.B.4    Xiao, F.5    Martin, G.B.6
  • 98
    • 65649140096 scopus 로고    scopus 로고
    • Host inhibition of a bacterial virulence effector triggers immunity to infection
    • Ntoukakis, V. et al. Host inhibition of a bacterial virulence effector triggers immunity to infection. Science 324, 784-787 (2009).
    • (2009) Science , vol.324 , pp. 784-787
    • Ntoukakis, V.1
  • 99
    • 42049121663 scopus 로고    scopus 로고
    • Plant pathogenic bacterial type III effectors subdue host responses
    • Zhou, J. M. & Chai, J. Plant pathogenic bacterial type III effectors subdue host responses. Curr. Opin. Microbiol. 11, 179-185 (2008).
    • (2008) Curr. Opin. Microbiol , vol.11 , pp. 179-185
    • Zhou, J.M.1    Chai, J.2
  • 100
    • 57749111993 scopus 로고    scopus 로고
    • From guard to decoy: A new model for perception of plant pathogen effectors
    • DOI 10.1105/tpc.108.060194
    • van der Hoorn, R. A. & Kamoun, S. From guard to decoy: a new model for perception of plant pathogen effectors. Plant Cell 20, 2009-2017 (2008). (Pubitemid 352844506)
    • (2008) Plant Cell , vol.20 , Issue.8 , pp. 2009-2017
    • Van Der Hoorn, R.A.L.1    Kamoun, S.2
  • 101
    • 72449183266 scopus 로고    scopus 로고
    • A locus conferring resistance to Colletotrichum higginsianum is shared by four geographically distinct Arabidopsis accessions
    • Birker, D. et al. A locus conferring resistance to Colletotrichum higginsianum is shared by four geographically distinct Arabidopsis accessions. Plant J. 60, 602-613 (2009).
    • (2009) Plant J. , vol.60 , pp. 602-613
    • Birker, D.1
  • 102
    • 84874222682 scopus 로고    scopus 로고
    • Interfamily transfer of dual NB-LRR genes confers resistance to multiple pathogens
    • Narusaka, M. et al. Interfamily transfer of dual NB-LRR genes confers resistance to multiple pathogens. PLoS ONE 8, e55954 (2013).
    • (2013) PLoS ONE , vol.8
    • Narusaka, M.1
  • 103
    • 70349881464 scopus 로고    scopus 로고
    • RRS1 and RPS4 provide a dual resistance-gene system against fungal and bacterial pathogens
    • Narusaka, M. et al. RRS1 and RPS4 provide a dual resistance-gene system against fungal and bacterial pathogens. Plant J. 60, 218-226 (2009).
    • (2009) Plant J. , vol.60 , pp. 218-226
    • Narusaka, M.1
  • 104
    • 84867063299 scopus 로고    scopus 로고
    • Distinct regions of the Pseudomonas syringae coiled-coil effector AvrRps4 are required for activation of immunity
    • Sohn, K. H., Hughes, R. K., Piquerez, S. J., Jones, J. D. & Banfield, M. J. Distinct regions of the Pseudomonas syringae coiled-coil effector AvrRps4 are required for activation of immunity. Proc. Natl Acad. Sci. USA 109, 16371-16376 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 16371-16376
    • Sohn, K.H.1    Hughes, R.K.2    Piquerez, S.J.3    Jones, J.D.4    Banfield, M.J.5
  • 105
    • 62149108660 scopus 로고    scopus 로고
    • The Pseudomonas syringae effector protein, AvrRPS4, requires in planta processing and the KRVY domain to function
    • Sohn, K. H., Zhang, Y. & Jones, J. D. The Pseudomonas syringae effector protein, AvrRPS4, requires in planta processing and the KRVY domain to function. Plant J. 57, 1079-1091 (2009).
    • (2009) Plant J. , vol.57 , pp. 1079-1091
    • Sohn, K.H.1    Zhang, Y.2    Jones, J.D.3
  • 106
    • 83255188814 scopus 로고    scopus 로고
    • Pathogen effectors target Arabidopsis EDS1 and alter its interactions with immune regulators
    • Bhattacharjee, S., Halane, M. K., Kim, S. H. & Gassmann, W. Pathogen effectors target Arabidopsis EDS1 and alter its interactions with immune regulators. Science 334, 1405-1408 (2011).
    • (2011) Science , vol.334 , pp. 1405-1408
    • Bhattacharjee, S.1    Halane, M.K.2    Kim, S.H.3    Gassmann, W.4
  • 107
    • 83255164814 scopus 로고    scopus 로고
    • Arabidopsis EDS1 connects pathogen effector recognition to cell compartment-specific immune responses
    • Heidrich, K. et al. Arabidopsis EDS1 connects pathogen effector recognition to cell compartment-specific immune responses. Science 334, 1401-1404 (2011).
    • (2011) Science , vol.334 , pp. 1401-1404
    • Heidrich, K.1
  • 108
    • 77956126894 scopus 로고    scopus 로고
    • Xanthomonas AvrBs3 family-type III effectors: Discovery and function
    • Boch, J. & Bonas, U. Xanthomonas AvrBs3 family-type III effectors: discovery and function. Annu. Rev. Phytopathol. 48, 419-436 (2010).
    • (2010) Annu. Rev. Phytopathol. , vol.48 , pp. 419-436
    • Boch, J.1    Bonas, U.2
  • 109
    • 35548942766 scopus 로고    scopus 로고
    • A bacterial effector acts as a plant transcription factor and induces a cell size regulator
    • DOI 10.1126/science.1144956
    • Kay, S., Hahn, S., Marois, E., Hause, G. & Bonas, U. A. Bacterial effector acts as a plant transcription factor and induces a cell size regulator. Science 318, 648-651 (2007). (Pubitemid 350014839)
    • (2007) Science , vol.318 , Issue.5850 , pp. 648-651
    • Kay, S.1    Hahn, S.2    Marois, E.3    Hause, G.4    Bonas, U.5
  • 110
    • 35548939950 scopus 로고    scopus 로고
    • Plant pathogen recognition mediated by promoter activation of the pepper Bs3 resistance gene
    • DOI 10.1126/science.1144958
    • Romer, P. et al. Plant pathogen recognition mediated by promoter activation of the pepper Bs3 resistance gene. Science 318, 645-648 (2007). (Pubitemid 350014838)
    • (2007) Science , vol.318 , Issue.5850 , pp. 645-648
    • Romer, P.1    Hahn, S.2    Jordan, T.3    Strauss, T.4    Bonas, U.5    Lahaye, T.6
  • 111
    • 72149110399 scopus 로고    scopus 로고
    • Breaking the code of DNA binding specificity of TAL-type III effectors
    • Boch, J. et al. Breaking the code of DNA binding specificity of TAL-type III effectors. Science 326, 1509-1512 (2009).
    • (2009) Science , vol.326 , pp. 1509-1512
    • Boch, J.1
  • 112
    • 72149090954 scopus 로고    scopus 로고
    • A simple cipher governs DNA recognition by TAL effectors
    • Moscou, M. J. & Bogdanove, A. J. A simple cipher governs DNA recognition by TAL effectors. Science 326, 1501 (2009).
    • (2009) Science , vol.326 , pp. 1501
    • Moscou, M.J.1    Bogdanove, A.J.2
  • 113
    • 80053343092 scopus 로고    scopus 로고
    • TAL effectors: Customizable proteins for DNA targeting
    • Bogdanove, A. J. & Voytas, D. F. TAL effectors: customizable proteins for DNA targeting. Science 333, 1843-1846 (2011).
    • (2011) Science , vol.333 , pp. 1843-1846
    • Bogdanove, A.J.1    Voytas, D.F.2
  • 114
    • 78650739853 scopus 로고    scopus 로고
    • Regulation of selected genome loci using de novo-engineered transcription activator-like effector (TALE)-type transcription factors
    • Morbitzer, R., Römer, P., Boch, J. & Lahaye, T. Regulation of selected genome loci using de novo-engineered transcription activator-like effector (TALE)-type transcription factors. Proc. Natl Acad. Sci. USA 107, 21617-21622 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 21617-21622
    • Morbitzer, R.1    Römer, P.2    Boch, J.3    Lahaye, T.4
  • 115
    • 78349276063 scopus 로고    scopus 로고
    • The repeat domain of the type III effector protein PthA shows a TPR-like structure and undergoes conformational changes upon DNA interaction
    • Murakami, M. T. et al. The repeat domain of the type III effector protein PthA shows a TPR-like structure and undergoes conformational changes upon DNA interaction. Proteins 78, 3386-3395 (2010).
    • (2010) Proteins , vol.78 , pp. 3386-3395
    • Murakami, M.T.1
  • 116
    • 84857032466 scopus 로고    scopus 로고
    • Structural basis for sequence-specific recognition of DNA by TAL effectors
    • Deng, D. et al. Structural basis for sequence-specific recognition of DNA by TAL effectors. Science 335, 720-723 (2012).
    • (2012) Science , vol.335 , pp. 720-723
    • Deng, D.1
  • 118
    • 84857029597 scopus 로고    scopus 로고
    • The crystal structure of TAL effector PthXo1 bound to its DNA Target
    • Mak, A. N.-S., Bradley, P., Cernadas, R. A., Bogdanove, A. J. & Stoddard, B. L. The crystal structure of TAL effector PthXo1 bound to its DNA Target. Science 335, 716-719 (2012)
    • (2012) Science , vol.335 , pp. 716-719
    • Mak, A.N.-S.1    Bradley, P.2    Cernadas, R.A.3    Bogdanove, A.J.4    Stoddard, B.L.5
  • 119
    • 84868106504 scopus 로고    scopus 로고
    • Specific DNA-RNA hybrid recognition by TAL effectors
    • Yin, P. et al. Specific DNA-RNA hybrid recognition by TAL effectors. Cell Rep. 2, 707-713 (2012).
    • (2012) Cell Rep. , vol.2 , pp. 707-713
    • Yin, P.1
  • 120
    • 84867095660 scopus 로고    scopus 로고
    • Recognition of methylated DNA by TAL effectors
    • Deng, D. et al. Recognition of methylated DNA by TAL effectors. Cell Res. 22, 1502-1504 (2012).
    • (2012) Cell Res. , vol.22 , pp. 1502-1504
    • Deng, D.1
  • 121
    • 84870583046 scopus 로고    scopus 로고
    • Crystal structure of a TALE protein reveals an extended N-terminal DNA binding region
    • Gao, H., Wu, X., Chai, J. & Han, Z. Crystal structure of a TALE protein reveals an extended N-terminal DNA binding region. Cell Res. 22, 1716-1720 (2012).
    • (2012) Cell Res. , vol.22 , pp. 1716-1720
    • Gao, H.1    Wu, X.2    Chai, J.3    Han, Z.4
  • 123
    • 77953184858 scopus 로고    scopus 로고
    • Translocation of Magnaporthe oryzae effectors into rice cells and their subsequent cell-to-cell movement
    • Khang, C. H. et al. Translocation of Magnaporthe oryzae effectors into rice cells and their subsequent cell-to-cell movement. Plant Cell 22, 1388-1403 (2010).
    • (2010) Plant Cell , vol.22 , pp. 1388-1403
    • Khang, C.H.1
  • 124
    • 65649149779 scopus 로고    scopus 로고
    • Terrific protein traffic: The mystery of effector protein delivery by filamentous plant pathogens
    • Panstruga, R. & Dodds, P. N. Terrific protein traffic: the mystery of effector protein delivery by filamentous plant pathogens. Science 324, 748-750 (2009).
    • (2009) Science , vol.324 , pp. 748-750
    • Panstruga, R.1    Dodds, P.N.2
  • 125
    • 80052276859 scopus 로고    scopus 로고
    • Showdown at the RXLR motif: Serious differences of opinion in how effector proteins from filamentous eukaryotic pathogens enter plant cells
    • Ellis, J. G. & Dodds, P. N. Showdown at the RXLR motif: Serious differences of opinion in how effector proteins from filamentous eukaryotic pathogens enter plant cells. Proc. Natl Acad. Sci. USA 108, 14381-14382 (2011)
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 14381-14382
    • Ellis, J.G.1    Dodds, P.N.2
  • 126
    • 84877107553 scopus 로고    scopus 로고
    • Microbe-independent entry of oomycete RxLR effectors and fungal RxLR-like effectors into plant and animal cells is specific and reproducible
    • Tyler, B. M. et al. Microbe-independent entry of oomycete RxLR effectors and fungal RxLR-like effectors into plant and animal cells is specific and reproducible. Mol. Plant Microbe Interact. 26, 611-616 (2013).
    • (2013) Mol. Plant Microbe Interact. , vol.26 , pp. 611-616
    • Tyler, B.M.1
  • 127
    • 84875972308 scopus 로고    scopus 로고
    • In vitro translocation experiments with RxLR-reporter fusion proteins of Avr1b from Phytophthora sojae and AVR3a from Phytophthora infestans fail to demonstrate specific autonomous uptake in plant and animal cells
    • Wawra, S. et al. In vitro translocation experiments with RxLR-reporter fusion proteins of Avr1b from Phytophthora sojae and AVR3a from Phytophthora infestans fail to demonstrate specific autonomous uptake in plant and animal cells. Mol. Plant Microbe Interact. 26, 528-536 (2013).
    • (2013) Mol. Plant Microbe Interact. , vol.26 , pp. 528-536
    • Wawra, S.1
  • 128
    • 80052281811 scopus 로고    scopus 로고
    • Structures of Phytophthora RXLR effector proteins: A conserved but adaptable fold underpins functional diversity
    • Boutemy, L. S. et al. Structures of Phytophthora RXLR effector proteins: a conserved but adaptable fold underpins functional diversity. J. Biol. Chem. 286, 35834-35842 (2011)
    • (2011) J. Biol. Chem. , vol.286 , pp. 35834-35842
    • Boutemy, L.S.1
  • 129
    • 80052302918 scopus 로고    scopus 로고
    • Phosphatidylinositol monophosphate-binding interface in the oomycete RXLR effector AVR3a is required for its stability in host cells to modulate plant immunity
    • Yaeno, T. et al. Phosphatidylinositol monophosphate-binding interface in the oomycete RXLR effector AVR3a is required for its stability in host cells to modulate plant immunity. Proc. Natl Acad. Sci. USA 108, 14682-14687 (2011)
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 14682-14687
    • Yaeno, T.1
  • 130
    • 84874088579 scopus 로고    scopus 로고
    • Structural basis for interactions of the Phytophthora sojae RxLR effector Avh5 with phosphatidylinositol 3-phosphate and for host cell entry
    • Sun, F. et al. Structural basis for interactions of the Phytophthora sojae RxLR effector Avh5 with phosphatidylinositol 3-phosphate and for host cell entry. Mol. Plant Microbe Interact. 26, 330-344 (2013).
    • (2013) Mol. Plant Microbe Interact. , vol.26 , pp. 330-344
    • Sun, F.1
  • 131
    • 33749264793 scopus 로고    scopus 로고
    • The C-terminal half of Phytophthora infestans RXLR effector AVR3a is sufficient to trigger R3a-mediated hypersensitivity and suppress INF1-induced cell death in Nicotiana benthamiana
    • DOI 10.1111/j.1365-313X.2006.02866.x
    • Bos, J. I. B. et al. The C-terminal half of Phytophthora infestans RXLR effector AVR3a is sufficient to trigger R3a-mediated hypersensitivity and suppress INF1-induced cell death in Nicotiana benthamiana. Plant J. 48, 165-176 (2006). (Pubitemid 44484859)
    • (2006) Plant Journal , vol.48 , Issue.2 , pp. 165-176
    • Bos, J.I.B.1    Kanneganti, T.-D.2    Young, C.3    Cakir, C.4    Huitema, E.5    Win, J.6    Armstrong, M.R.7    Birch, P.R.J.8    Kamoun, S.9
  • 133
    • 80051993849 scopus 로고    scopus 로고
    • Hyaloperonospora arabidopsidis ATR1 effector is a repeat protein with distributed recognition surfaces
    • Chou, S. et al. Hyaloperonospora arabidopsidis ATR1 effector is a repeat protein with distributed recognition surfaces. Proc. Natl Acad. Sci. USA 108, 13323-13328 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 13323-13328
    • Chou, S.1
  • 134
    • 84855258469 scopus 로고    scopus 로고
    • Structural elucidation and functional characterization of the Hyaloperonospora arabidopsidis effector protein ATR13
    • Leonelli, L. et al. Structural elucidation and functional characterization of the Hyaloperonospora arabidopsidis effector protein ATR13. PLoS Pathog. 7, e1002428 (2011).
    • (2011) PLoS Pathog , vol.7
    • Leonelli, L.1
  • 135
    • 84857479035 scopus 로고    scopus 로고
    • Sequence divergent RXLR effectors share a structural fold conserved across plant pathogenic oomycete species
    • Win, J. et al. Sequence divergent RXLR effectors share a structural fold conserved across plant pathogenic oomycete species. PLoS Pathog. 8, e1002400 (2012).
    • (2012) PLoS Pathog , vol.8
    • Win, J.1
  • 137
    • 35748972958 scopus 로고    scopus 로고
    • Crystal structures of flax rust avirulence proteins AvrL567-A and-D reveal details of the structural basis for flax disease resistance specificity
    • Wang, C. I. et al. Crystal structures of flax rust avirulence proteins AvrL567-A and-D reveal details of the structural basis for flax disease resistance specificity. Plant Cell 19, 2898-2912 (2007).
    • (2007) Plant Cell , vol.19 , pp. 2898-2912
    • Wang, C.I.1
  • 138
    • 84879556031 scopus 로고    scopus 로고
    • Solution structure of the Magnaporthe oryzae avirulence protein AvrPiz-t
    • Zhang, Z. M. et al. Solution structure of the Magnaporthe oryzae avirulence protein AvrPiz-t. J. Biomol. NMR 55, 219-223 (2013).
    • (2013) J. Biomol. NMR , vol.55 , pp. 219-223
    • Zhang, Z.M.1
  • 140
    • 73949112504 scopus 로고    scopus 로고
    • The AvrM effector from flax rust has a structured C-terminal domain and interacts directly with the M resistance protein
    • Catanzariti, A. M. et al. The AvrM effector from flax rust has a structured C-terminal domain and interacts directly with the M resistance protein. Mol. Plant Microbe Interact. 23, 49-57 (2010).
    • (2010) Mol. Plant Microbe Interact , vol.23 , pp. 49-57
    • Catanzariti, A.M.1
  • 141
    • 77956823972 scopus 로고    scopus 로고
    • Activation of an Arabidopsis resistance protein is specified by the in planta association of its leucine-rich repeat domain with the cognate oomycete effector
    • Krasileva, K. V., Dahlbeck, D. & Staskawicz, B. J. Activation of an Arabidopsis resistance protein is specified by the in planta association of its leucine-rich repeat domain with the cognate oomycete effector. Plant Cell 22, 2444-2458 (2010).
    • (2010) Plant Cell , vol.22 , pp. 2444-2458
    • Krasileva, K.V.1    Dahlbeck, D.2    Staskawicz, B.J.3
  • 143
    • 70349585670 scopus 로고    scopus 로고
    • NB-LRRs work a bait and switch" on pathogens
    • Collier, S. M. & Moffett, P. NB-LRRs work a "bait and switch" on pathogens. Trends Plant Sci. 14, 521-529 (2009).
    • (2009) Trends Plant Sci. , vol.14 , pp. 521-529
    • Collier, S.M.1    Moffett, P.2
  • 144
    • 80051967147 scopus 로고    scopus 로고
    • NLR functions in plant and animal immune systems: So far and yet so close
    • Maekawa, T., Kufer, T. A. & Schulze-Lefert, P. NLR functions in plant and animal immune systems: so far and yet so close. Nature Immunol. 12, 817-826 (2011).
    • (2011) Nature Immunol. , vol.12 , pp. 817-826
    • Maekawa, T.1    Kufer, T.A.2    Schulze-Lefert, P.3
  • 145
    • 79952642803 scopus 로고    scopus 로고
    • Coiled-coil domain-dependent homodimerization of intracellular barley immune receptors defines a minimal functional module for triggering cell death
    • Maekawa, T. et al. Coiled-coil domain-dependent homodimerization of intracellular barley immune receptors defines a minimal functional module for triggering cell death. Cell Host Microbe 9, 187-199 (2011).
    • (2011) Cell Host Microbe , vol.9 , pp. 187-199
    • Maekawa, T.1
  • 146
    • 33847254952 scopus 로고    scopus 로고
    • Nuclear activity of MLA immune receptors links isolate-specific and basal disease-resistance responses
    • Shen, Q. H. et al. Nuclear activity of MLA immune receptors links isolate-specific and basal disease-resistance responses. Science 315, 1098-1103 (2007).
    • (2007) Science , vol.315 , pp. 1098-1103
    • Shen, Q.H.1
  • 147
    • 75149175757 scopus 로고    scopus 로고
    • The crystal structure of a TIR domain from Arabidopsis thaliana reveals a conserved helical region unique to plants
    • Chan, S. L., Mukasa, T., Santelli, E., Low, L. Y. & Pascual, J. The crystal structure of a TIR domain from Arabidopsis thaliana reveals a conserved helical region unique to plants. Protein Sci. 19, 155-161 (2010).
    • (2010) Protein Sci. , vol.19 , pp. 155-161
    • Chan, S.L.1    Mukasa, T.2    Santelli, E.3    Low, L.Y.4    Pascual, J.5
  • 148
    • 79952643473 scopus 로고    scopus 로고
    • Structural and functional analysis of a plant resistance protein TIR domain reveals interfaces for self-association, signaling, and autoregulation
    • Bernoux, M. et al. Structural and functional analysis of a plant resistance protein TIR domain reveals interfaces for self-association, signaling, and autoregulation. Cell Host Microbe 9, 200-211 (2011).
    • (2011) Cell Host Microbe , vol.9 , pp. 200-211
    • Bernoux, M.1
  • 149
    • 77956823972 scopus 로고    scopus 로고
    • Activation of an Arabidopsis resistance protein Is specified by the in planta association of its leucine-rich repeat domain with the cognate oomycete effector
    • Krasileva, K. V., Dahlbeck, D. & Staskawicz, B. J. Activation of an Arabidopsis resistance protein Is specified by the in planta association of its leucine-rich repeat domain with the cognate oomycete effector. Plant Cell 22, 2444-2458 (2010).
    • (2010) Plant Cell , vol.22 , pp. 2444-2458
    • Krasileva, K.V.1    Dahlbeck, D.2    Staskawicz, B.J.3
  • 150
    • 33745455354 scopus 로고    scopus 로고
    • Elicitor-mediated oligomerization of the tobacco N disease resistance protein
    • DOI 10.1105/tpc.105.037234
    • Mestre, P. & Baulcombe, D. C. Elicitor-mediated oligomerization of the tobacco N disease resistance protein. Plant Cell 18, 491-501 (2006). (Pubitemid 43951308)
    • (2006) Plant Cell , vol.18 , Issue.2 , pp. 491-501
    • Mestre, P.1    Baulcombe, D.C.2
  • 151
    • 27144540463 scopus 로고    scopus 로고
    • Are innate immune signaling pathways in plants and animals conserved?
    • DOI 10.1038/ni1253, PII N1253
    • Ausubel, F. M. Are innate immune signaling pathways in plants and animals conserved? Nature Immunol. 6, 973-979 (2005). (Pubitemid 41486181)
    • (2005) Nature Immunology , vol.6 , Issue.10 , pp. 973-979
    • Ausubel, F.M.1
  • 152
    • 84856170491 scopus 로고    scopus 로고
    • How do plants achieve immunity? Defence without specialized immune cells
    • Spoel, S. H. & Dong, X. How do plants achieve immunity? Defence without specialized immune cells. Nature Rev. Immunol. 12, 89-100 (2012).
    • (2012) Nature Rev. Immunol. , vol.12 , pp. 89-100
    • Spoel, S.H.1    Dong, X.2
  • 153
    • 84870514425 scopus 로고    scopus 로고
    • Plants and pathogens: Putting infection strategies and defence mechanisms on the map
    • Faulkner, C. & Robatzek, S. Plants and pathogens: putting infection strategies and defence mechanisms on the map. Curr. Opin. Plant Biol. 15, 699-707 (2012).
    • (2012) Curr. Opin. Plant Biol. , vol.15 , pp. 699-707
    • Faulkner, C.1    Robatzek, S.2
  • 154
    • 84864520212 scopus 로고    scopus 로고
    • Plant pattern recognition receptor complexes at the plasma membrane
    • Monaghan, J. & Zipfel, C. Plant pattern recognition receptor complexes at the plasma membrane. Curr. Opin. Plant Biol. 15, 349-357 (2012).
    • (2012) Curr. Opin. Plant Biol. , vol.15 , pp. 349-357
    • Monaghan, J.1    Zipfel, C.2
  • 156
    • 79960210750 scopus 로고    scopus 로고
    • Programmed cell death in the plant immune system
    • Coll, N. S., Epple, P. & Dangl, J. L. Programmed cell death in the plant immune system. Cell Death Differ. 18, 1247-1256 (2011).
    • (2011) Cell Death Differ. , vol.18 , pp. 1247-1256
    • Coll, N.S.1    Epple, P.2    Dangl, J.L.3
  • 158
    • 84865781586 scopus 로고    scopus 로고
    • Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis
    • Plechanovova, A., Jaffray, E. G., Tatham, M. H., Naismith, J. H. & Hay, R. T. Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis. Nature 489, 115-120 (2012).
    • (2012) Nature , vol.489 , pp. 115-120
    • Plechanovova, A.1    Jaffray, E.G.2    Tatham, M.H.3    Naismith, J.H.4    Hay, R.T.5
  • 159
    • 57649155916 scopus 로고    scopus 로고
    • Doc of prophage P1 is inhibited by its antitoxin partner Phd through fold complementation
    • Garcia-Pino, A. et al. Doc of prophage P1 is inhibited by its antitoxin partner Phd through fold complementation. J. Biol. Chem. 283, 30821-30827 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 30821-30827
    • Garcia-Pino, A.1
  • 160
    • 84880280093 scopus 로고    scopus 로고
    • Crystal structure of NLRC4 reveals its autoinhibition mechanism
    • Hu, Z. et al. Crystal structure of NLRC4 reveals its autoinhibition mechanism. Science 341, 172-175 (2013).
    • (2013) Science , vol.341 , pp. 172-175
    • Hu, Z.1
  • 161
    • 84881529325 scopus 로고    scopus 로고
    • Fungal effector Ecp6 outcompetes host immune receptor for chitin binding through intrachain LysM dimerization
    • Sanchez-Vallet, A. et al. Fungal effector Ecp6 outcompetes host immune receptor for chitin binding through intrachain LysM dimerization. eLife 2, e00790 (2013).
    • (2013) ELife , vol.2
    • Sanchez-Vallet, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.