메뉴 건너뛰기




Volumn 19, Issue 9, 2007, Pages 2898-2912

Crystal structures of flax rust avirulence proteins AvrL567-A and -D reveal details of the structural basis for flax disease resistance specificity

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CRYSTAL STRUCTURE; DISEASE CONTROL; GENES; PATHOGENS; PLANTS (BOTANY); POLYMORPHISM;

EID: 35748972958     PISSN: 10404651     EISSN: 1532298X     Source Type: Journal    
DOI: 10.1105/tpc.107.053611     Document Type: Article
Times cited : (128)

References (88)
  • 1
    • 11144353587 scopus 로고    scopus 로고
    • Complete genome sequence of the apicomplexan, Cryptosporidium parvum
    • Abrahamsen, M.S., et al. (2004). Complete genome sequence of the apicomplexan, Cryptosporidium parvum. Science 304: 441-445.
    • (2004) Science , vol.304 , pp. 441-445
    • Abrahamsen, M.S.1
  • 4
    • 0031127301 scopus 로고    scopus 로고
    • Inactivation of the flax rust resistance gene M associated with loss of a repeated unit within the leucine-rich repeat coding region
    • Anderson, P.A., Lawrence, G.J., Morrish, B.C., Ayliffe, M.A., Finnegan, E.J., and Ellis, J.G. (1997). Inactivation of the flax rust resistance gene M associated with loss of a repeated unit within the leucine-rich repeat coding region. Plant Cell 9: 641-651.
    • (1997) Plant Cell , vol.9 , pp. 641-651
    • Anderson, P.A.1    Lawrence, G.J.2    Morrish, B.C.3    Ayliffe, M.A.4    Finnegan, E.J.5    Ellis, J.G.6
  • 5
    • 20644441182 scopus 로고    scopus 로고
    • An ancestral oomycete locus contains late blight avirulence gene Avr3a, encoding a protein that is recognized in the host cytoplasm
    • Armstrong, M.R., et al. (2005). An ancestral oomycete locus contains late blight avirulence gene Avr3a, encoding a protein that is recognized in the host cytoplasm. Proc. Natl. Acad. Sci. USA 102: 7766-7771.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 7766-7771
    • Armstrong, M.R.1
  • 6
    • 0037423390 scopus 로고    scopus 로고
    • Initiation of RPS2-specified disease resistance in Arabidopsis is coupled to the AvrRpt2-directed elimination of RIN4
    • Axtell, M.J., and Staskawicz, B.J. (2003). Initiation of RPS2-specified disease resistance in Arabidopsis is coupled to the AvrRpt2-directed elimination of RIN4. Cell 112: 369-377.
    • (2003) Cell , vol.112 , pp. 369-377
    • Axtell, M.J.1    Staskawicz, B.J.2
  • 7
    • 3042762926 scopus 로고    scopus 로고
    • Plant disease resistance protein signaling: NBS-LRR proteins and their partners
    • Belkhadir, Y., Subramaniam, R., and Dangl, J.L. (2004). Plant disease resistance protein signaling: NBS-LRR proteins and their partners. Curr. Opin. Plant Biol. 7: 391-399.
    • (2004) Curr. Opin. Plant Biol , vol.7 , pp. 391-399
    • Belkhadir, Y.1    Subramaniam, R.2    Dangl, J.L.3
  • 9
    • 33645729843 scopus 로고    scopus 로고
    • Haustorially expressed secreted proteins from flax rust are highly enriched for avirulence elicitors
    • Catanzariti, A.M., Dodds, P.N., Lawrence, G.J., Ayliffe, M.A., and Ellis, J.G. (2006). Haustorially expressed secreted proteins from flax rust are highly enriched for avirulence elicitors. Plant Cell 18: 243-256.
    • (2006) Plant Cell , vol.18 , pp. 243-256
    • Catanzariti, A.M.1    Dodds, P.N.2    Lawrence, G.J.3    Ayliffe, M.A.4    Ellis, J.G.5
  • 10
    • 1942537173 scopus 로고    scopus 로고
    • Catanzariti, A.M., Soboleva, T.A., Jans, D.A., Board, P.G., and Baker, R.T. (2004). An efficient system for high-level expression and easy purification of authentic recombinant proteins. Protein Sci. 13: 1331-1339.
    • Catanzariti, A.M., Soboleva, T.A., Jans, D.A., Board, P.G., and Baker, R.T. (2004). An efficient system for high-level expression and easy purification of authentic recombinant proteins. Protein Sci. 13: 1331-1339.
  • 11
    • 0037093643 scopus 로고    scopus 로고
    • Docking unbound proteins using shape complementarity, desolvation, and electrostatics
    • Chen, R., and Weng, Z. (2002). Docking unbound proteins using shape complementarity, desolvation, and electrostatics. Proteins 47: 281-294.
    • (2002) Proteins , vol.47 , pp. 281-294
    • Chen, R.1    Weng, Z.2
  • 12
    • 32944479048 scopus 로고    scopus 로고
    • Host-microbe interactions: Shaping the evolution of the plant immune response
    • Chisholm, S.T., Coaker, G., Day, B., and Staskawicz, B.J. (2006). Host-microbe interactions: Shaping the evolution of the plant immune response. Cell 124: 803-814.
    • (2006) Cell , vol.124 , pp. 803-814
    • Chisholm, S.T.1    Coaker, G.2    Day, B.3    Staskawicz, B.J.4
  • 13
    • 0031080669 scopus 로고    scopus 로고
    • A single gene encodes a selective toxin causal to the development of tan spot of wheat
    • Ciuffetti, L.M., Tuori, R.P., and Gaventa, J.M. (1997). A single gene encodes a selective toxin causal to the development of tan spot of wheat. Plant Cell 9: 135-144.
    • (1997) Plant Cell , vol.9 , pp. 135-144
    • Ciuffetti, L.M.1    Tuori, R.P.2    Gaventa, J.M.3
  • 14
    • 0035859020 scopus 로고    scopus 로고
    • Plant pathogens and integrated defence responses to infection
    • Dangl, J.L., and Jones, J.D. (2001). Plant pathogens and integrated defence responses to infection. Nature 411: 826-833.
    • (2001) Nature , vol.411 , pp. 826-833
    • Dangl, J.L.1    Jones, J.D.2
  • 15
    • 0037595606 scopus 로고    scopus 로고
    • Physical interaction between RRS1-R, a protein conferring resistance to bacterial wilt, and PopP2, a type III effector targeted to the plant nucleus
    • Deslandes, L., Olivier, J., Peeters, N., Feng, D.X., Khounlotham, M., Boucher, C., Somssich, I., Genin, S., and Marco, Y. (2003). Physical interaction between RRS1-R, a protein conferring resistance to bacterial wilt, and PopP2, a type III effector targeted to the plant nucleus. Proc. Natl. Acad. Sci. USA 100: 8024-8029.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 8024-8029
    • Deslandes, L.1    Olivier, J.2    Peeters, N.3    Feng, D.X.4    Khounlotham, M.5    Boucher, C.6    Somssich, I.7    Genin, S.8    Marco, Y.9
  • 16
    • 1542542334 scopus 로고    scopus 로고
    • The Melampsora lini AvrL567 avirulence genes are expressed in haustoria and their products are recognized inside plant cells
    • Dodds, P.N., Lawrence, G.J., Catanzariti, A.M., Ayliffe, M.A., and Ellis, J.G. (2004). The Melampsora lini AvrL567 avirulence genes are expressed in haustoria and their products are recognized inside plant cells. Plant Cell 16: 755-768.
    • (2004) Plant Cell , vol.16 , pp. 755-768
    • Dodds, P.N.1    Lawrence, G.J.2    Catanzariti, A.M.3    Ayliffe, M.A.4    Ellis, J.G.5
  • 17
    • 33745015480 scopus 로고    scopus 로고
    • Direct protein interaction underlies gene-for-gene specificity and coevolution of the flax resistance genes and flax rust avirulence genes
    • Dodds, P.N., Lawrence, G.J., Catanzariti, A.M., Teh, T., Wang, C.I., Ayliffe, M.A., Kobe, B., and Ellis, J.G. (2006). Direct protein interaction underlies gene-for-gene specificity and coevolution of the flax resistance genes and flax rust avirulence genes. Proc. Natl. Acad. Sci. USA 103: 8888-8893.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 8888-8893
    • Dodds, P.N.1    Lawrence, G.J.2    Catanzariti, A.M.3    Teh, T.4    Wang, C.I.5    Ayliffe, M.A.6    Kobe, B.7    Ellis, J.G.8
  • 18
    • 0035108614 scopus 로고    scopus 로고
    • Six amino acid changes confined to the leucine-rich repeat beta-strand/beta-turn motif determine the difference between the P and P2 rust resistance specificities in flax
    • Dodds, P.N., Lawrence, G.J., and Ellis, J.G. (2001a). Six amino acid changes confined to the leucine-rich repeat beta-strand/beta-turn motif determine the difference between the P and P2 rust resistance specificities in flax. Plant Cell 13: 163-178.
    • (2001) Plant Cell , vol.13 , pp. 163-178
    • Dodds, P.N.1    Lawrence, G.J.2    Ellis, J.G.3
  • 19
    • 0034784612 scopus 로고    scopus 로고
    • Contrasting modes of evolution acting on the complex N locus for rust resistance in flax
    • Dodds, P.N., Lawrence, G.J., and Ellis, J.G. (2001b). Contrasting modes of evolution acting on the complex N locus for rust resistance in flax. Plant J. 27: 439-453.
    • (2001) Plant J , vol.27 , pp. 439-453
    • Dodds, P.N.1    Lawrence, G.J.2    Ellis, J.G.3
  • 20
    • 0002963645 scopus 로고    scopus 로고
    • Genetic analysis and evolution of plant disease resistance genes
    • Molecular Plant Pathology, M. Dickinson and J. Beynon, eds Sheffield, UK: Sheffield Academic Press, pp
    • Dodds, P.N., Lawrence, G.J., Pryor, A., and Ellis, J.G. (2000). Genetic analysis and evolution of plant disease resistance genes. In Molecular Plant Pathology. Annual Plant Reviews, Vol. 4, M. Dickinson and J. Beynon, eds (Sheffield, UK: Sheffield Academic Press), pp. 88-107.
    • (2000) Annual Plant Reviews , vol.4 , pp. 88-107
    • Dodds, P.N.1    Lawrence, G.J.2    Pryor, A.3    Ellis, J.G.4
  • 21
    • 0031743421 scopus 로고    scopus 로고
    • Profile hidden Markov models
    • Eddy, S.R. (1998). Profile hidden Markov models. Bioinformatics 14: 755-763.
    • (1998) Bioinformatics , vol.14 , pp. 755-763
    • Eddy, S.R.1
  • 22
    • 0033799535 scopus 로고    scopus 로고
    • The generation of plant disease resistance gene specificities
    • Ellis, J., Dodds, P., and Pryor, T. (2000). The generation of plant disease resistance gene specificities. Trends Plant Sci. 5: 373-379.
    • (2000) Trends Plant Sci , vol.5 , pp. 373-379
    • Ellis, J.1    Dodds, P.2    Pryor, T.3
  • 23
    • 32544456877 scopus 로고    scopus 로고
    • The problem of how fungal and oomycete avirulence proteins enter plant cells
    • Ellis, J., Catanzariti, A.M., and Dodds, P. (2006). The problem of how fungal and oomycete avirulence proteins enter plant cells. Trends Plant Sci. 11: 61-63.
    • (2006) Trends Plant Sci , vol.11 , pp. 61-63
    • Ellis, J.1    Catanzariti, A.M.2    Dodds, P.3
  • 24
    • 0033101488 scopus 로고    scopus 로고
    • Identification of regions in alleles of the flax rust resistance gene L that determine differences in gene-for-gene specificity
    • Ellis, J.G., Lawrence, G.J., Luck, J.E., and Dodds, P.N. (1999). Identification of regions in alleles of the flax rust resistance gene L that determine differences in gene-for-gene specificity. Plant Cell 11: 495-506.
    • (1999) Plant Cell , vol.11 , pp. 495-506
    • Ellis, J.G.1    Lawrence, G.J.2    Luck, J.E.3    Dodds, P.N.4
  • 25
    • 33644876020 scopus 로고    scopus 로고
    • Pfam: Clans, web tools and services
    • Finn, R.D., et al. (2006). Pfam: Clans, web tools and services. Nucleic Acids Res. 34: D247-D251.
    • (2006) Nucleic Acids Res , vol.34
    • Finn, R.D.1
  • 26
    • 0347383758 scopus 로고    scopus 로고
    • Modeller: Generation and refinement of homology-based protein structure models
    • Fiser, A., and Sali, A. (2003). Modeller: Generation and refinement of homology-based protein structure models. Methods Enzymol. 374: 461-491.
    • (2003) Methods Enzymol , vol.374 , pp. 461-491
    • Fiser, A.1    Sali, A.2
  • 27
    • 0001119910 scopus 로고
    • Current status of the gene-for-gene concept
    • Flor, H. (1971). Current status of the gene-for-gene concept. Annu. Rev. Phytopathol. 9: 275-296.
    • (1971) Annu. Rev. Phytopathol , vol.9 , pp. 275-296
    • Flor, H.1
  • 28
    • 0003161894 scopus 로고
    • Seed-flax improvemnt. III. Flax rust
    • Flor, H.H. (1954). Seed-flax improvemnt. III. Flax rust. Adv. Agron. 6: 152-161.
    • (1954) Adv. Agron , vol.6 , pp. 152-161
    • Flor, H.H.1
  • 30
    • 33947331276 scopus 로고    scopus 로고
    • 2+ for crystallization and structure determination, using a conventional monochromatic X-ray source, of flax rust avirulence protein. Acta Crystallograph. Sect. F Struct. Biol. Cryst. Commun. Biol. Cryst. Commun. 63: 209-213.
    • 2+ for crystallization and structure determination, using a conventional monochromatic X-ray source, of flax rust avirulence protein. Acta Crystallograph. Sect. F Struct. Biol. Cryst. Commun. Biol. Cryst. Commun. 63: 209-213.
  • 31
    • 0031865006 scopus 로고    scopus 로고
    • Touring protein fold space with Dali/ FSSP
    • Holm, L., and Sander, C. (1998). Touring protein fold space with Dali/ FSSP. Nucleic Acids Res. 26: 316-319.
    • (1998) Nucleic Acids Res , vol.26 , pp. 316-319
    • Holm, L.1    Sander, C.2
  • 32
    • 19544374693 scopus 로고    scopus 로고
    • Autoactive alleles of the flax L6 rust resistance gene induce non-race-specific rust resistance associated with the hypersensitive response
    • Howles, P., Lawrence, G., Finnegan, J., McFadden, H., Ayliffe, M., Dodds, P., and Ellis, J. (2005). Autoactive alleles of the flax L6 rust resistance gene induce non-race-specific rust resistance associated with the hypersensitive response. Mol. Plant Microbe Interact. 18: 570-582.
    • (2005) Mol. Plant Microbe Interact , vol.18 , pp. 570-582
    • Howles, P.1    Lawrence, G.2    Finnegan, J.3    McFadden, H.4    Ayliffe, M.5    Dodds, P.6    Ellis, J.7
  • 33
    • 0038806568 scopus 로고    scopus 로고
    • Leucine-rich repeat-mediated intramolecular interactions in nematode recognition and cell death signaling by the tomato resistance protein Mi
    • Hwang, C.F., and Williamson, V.M. (2003). Leucine-rich repeat-mediated intramolecular interactions in nematode recognition and cell death signaling by the tomato resistance protein Mi. Plant J. 34: 585-593.
    • (2003) Plant J , vol.34 , pp. 585-593
    • Hwang, C.F.1    Williamson, V.M.2
  • 34
    • 34047094501 scopus 로고    scopus 로고
    • DP-Bind: A web server for sequence-based prediction of DNA-binding residues in DNA-binding proteins
    • Hwang, S., Gou, Z., and Kuznetsov, I.B. (2007). DP-Bind: A web server for sequence-based prediction of DNA-binding residues in DNA-binding proteins. Bioinformatics 23: 634-636.
    • (2007) Bioinformatics , vol.23 , pp. 634-636
    • Hwang, S.1    Gou, Z.2    Kuznetsov, I.B.3
  • 35
    • 84946655746 scopus 로고
    • A compendium on host genes in flax conferring resistance to flax rust
    • Islam, M.R., and Mayo, G.M. (1990). A compendium on host genes in flax conferring resistance to flax rust. Plant Breed. 104: 89-100.
    • (1990) Plant Breed , vol.104 , pp. 89-100
    • Islam, M.R.1    Mayo, G.M.2
  • 36
    • 30844458212 scopus 로고    scopus 로고
    • A bacterial inhibitor of host programmed cell death defenses is an E3 ubiquitin ligase
    • Janjusevic, R., Abramovitch, R.B., Martin, G.B., and Stebbins, C.E. (2006). A bacterial inhibitor of host programmed cell death defenses is an E3 ubiquitin ligase. Science 311: 222-226.
    • (2006) Science , vol.311 , pp. 222-226
    • Janjusevic, R.1    Abramovitch, R.B.2    Martin, G.B.3    Stebbins, C.E.4
  • 37
    • 0034254266 scopus 로고    scopus 로고
    • Direct interaction of resistance gene and avirulence gene products confers rice blast resistance
    • Jia, Y., McAdams, S.A., Bryan, G.T., Hershey, H.P., and Valent, B. (2000). Direct interaction of resistance gene and avirulence gene products confers rice blast resistance. EMBO J. 19: 4004-4014.
    • (2000) EMBO J , vol.19 , pp. 4004-4014
    • Jia, Y.1    McAdams, S.A.2    Bryan, G.T.3    Hershey, H.P.4    Valent, B.5
  • 38
    • 1042278906 scopus 로고    scopus 로고
    • Plant innate immunity - Direct and indirect recognition of general and specific pathogen-associated molecules
    • Jones, D.A., and Takemoto, D. (2004). Plant innate immunity - Direct and indirect recognition of general and specific pathogen-associated molecules. Curr. Opin. Immunol. 16: 48-62.
    • (2004) Curr. Opin. Immunol , vol.16 , pp. 48-62
    • Jones, D.A.1    Takemoto, D.2
  • 39
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W., and Sander, C. (1983). Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22: 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 40
    • 0036232188 scopus 로고    scopus 로고
    • Assessment of the ability to model proteins with leucine-rich repeats in light of the latest structural information
    • Kajava, A.V., and Kobe, B. (2002). Assessment of the ability to model proteins with leucine-rich repeats in light of the latest structural information. Protein Sci. 11: 1082-1090.
    • (2002) Protein Sci , vol.11 , pp. 1082-1090
    • Kajava, A.V.1    Kobe, B.2
  • 41
    • 0028911034 scopus 로고
    • A structural basis of the interactions between leucine-rich repeats and protein ligands
    • Kobe, B., and Deisenhofer, J. (1995). A structural basis of the interactions between leucine-rich repeats and protein ligands. Nature 374: 183-186.
    • (1995) Nature , vol.374 , pp. 183-186
    • Kobe, B.1    Deisenhofer, J.2
  • 42
    • 1542499131 scopus 로고    scopus 로고
    • Pentaprobe: A comprehensive sequence for the one-step detection of DNA-binding activities
    • Kwan, A.H., Czolij, R., Mackay, J.P., and Crossley, M. (2003). Pentaprobe: A comprehensive sequence for the one-step detection of DNA-binding activities. Nucleic Acids Res. 31: e124.
    • (2003) Nucleic Acids Res , vol.31
    • Kwan, A.H.1    Czolij, R.2    Mackay, J.P.3    Crossley, M.4
  • 43
    • 0035205750 scopus 로고    scopus 로고
    • Molecular secrets of bacterial type III effector proteins
    • Lahaye, T., and Bonas, U. (2001). Molecular secrets of bacterial type III effector proteins. Trends Plant Sci. 6: 479-485.
    • (2001) Trends Plant Sci , vol.6 , pp. 479-485
    • Lahaye, T.1    Bonas, U.2
  • 44
    • 23144448512 scopus 로고    scopus 로고
    • ConSurf 2005: The projection of evolutionary conservation scores of residues on protein structures
    • Landau, M., Mayrose, I., Rosenberg, Y., Glaser, F., Martz, E., Pupko, T., and Ben-Tal, N. (2005). ConSurf 2005: The projection of evolutionary conservation scores of residues on protein structures. Nucleic Acids Res. 33: W299-W302.
    • (2005) Nucleic Acids Res , vol.33
    • Landau, M.1    Mayrose, I.2    Rosenberg, Y.3    Glaser, F.4    Martz, E.5    Pupko, T.6    Ben-Tal, N.7
  • 45
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S., and Thornton, J.M. (1993). PROCHECK: A program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26: 283-291.
    • (1993) J. Appl. Crystallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 46
    • 22544441094 scopus 로고    scopus 로고
    • ProFunc: A server for predicting protein function from 3D structure
    • Laskowski, R.A., Watson, J.D., and Thornton, J.M. (2005). ProFunc: A server for predicting protein function from 3D structure. Nucleic Acids Res. 33: W89-W93.
    • (2005) Nucleic Acids Res , vol.33
    • Laskowski, R.A.1    Watson, J.D.2    Thornton, J.M.3
  • 47
    • 0029347064 scopus 로고
    • The L6 gene for flax rust resistance is related to the Arabidopsis bacterial resistance gene RPS2 and the tobacco viral resistance gene N
    • Lawrence, G.L., Finnegan, E.J., Ayliffe, M.A., and Ellis, J.G. (1995). The L6 gene for flax rust resistance is related to the Arabidopsis bacterial resistance gene RPS2 and the tobacco viral resistance gene N.. Plant Cell 7: 1195-1206.
    • (1995) Plant Cell , vol.7 , pp. 1195-1206
    • Lawrence, G.L.1    Finnegan, E.J.2    Ayliffe, M.A.3    Ellis, J.G.4
  • 49
    • 0035812849 scopus 로고    scopus 로고
    • Crystal structure of a Y-family DNA polymerase in action: A mechanism for error-prone and lesion-bypass replication
    • Ling, H., Boudsocq, F., Woodgate, R., and Yang, W. (2001). Crystal structure of a Y-family DNA polymerase in action: A mechanism for error-prone and lesion-bypass replication. Cell 107: 91-102.
    • (2001) Cell , vol.107 , pp. 91-102
    • Ling, H.1    Boudsocq, F.2    Woodgate, R.3    Yang, W.4
  • 50
    • 0033823644 scopus 로고    scopus 로고
    • Regions outside of the leucine-rich repeats of flax rust resistance proteins play a role in specificity determination
    • Luck, J.E., Lawrence, G.J., Dodds, P.N., Shepherd, K.W., and Ellis, J.G. (2000). Regions outside of the leucine-rich repeats of flax rust resistance proteins play a role in specificity determination. Plant Cell 12: 1367-1377.
    • (2000) Plant Cell , vol.12 , pp. 1367-1377
    • Luck, J.E.1    Lawrence, G.J.2    Dodds, P.N.3    Shepherd, K.W.4    Ellis, J.G.5
  • 51
    • 0035663413 scopus 로고    scopus 로고
    • Avirulence proteins of plant pathogens: Determinants of victory and defeat
    • Luderer, R., and Joosten, M.H. (2001). Avirulence proteins of plant pathogens: Determinants of victory and defeat. Mol. Plant Pathol. 6: 355-364.
    • (2001) Mol. Plant Pathol , vol.6 , pp. 355-364
    • Luderer, R.1    Joosten, M.H.2
  • 52
    • 0037423306 scopus 로고    scopus 로고
    • Arabidopsis RIN4 is a target of the type III virulence effector AvrRpt2 and modulates RPS2-mediated resistance
    • Mackey, D., Belkhadir, Y., Alonso, J.M., Ecker, J.R., and Dangl, J.L. (2003). Arabidopsis RIN4 is a target of the type III virulence effector AvrRpt2 and modulates RPS2-mediated resistance. Cell 112: 379-389.
    • (2003) Cell , vol.112 , pp. 379-389
    • Mackey, D.1    Belkhadir, Y.2    Alonso, J.M.3    Ecker, J.R.4    Dangl, J.L.5
  • 54
    • 32544447423 scopus 로고    scopus 로고
    • Localization of Ptr ToxA produced by Pyrenophora tritici-repentis reveals protein import into wheat mesophyll cells
    • Manning, V.A., and Ciuffetti, L.M. (2005). Localization of Ptr ToxA produced by Pyrenophora tritici-repentis reveals protein import into wheat mesophyll cells. Plant Cell 17: 3203-3212.
    • (2005) Plant Cell , vol.17 , pp. 3203-3212
    • Manning, V.A.1    Ciuffetti, L.M.2
  • 57
    • 0037009437 scopus 로고    scopus 로고
    • Interaction between domains of a plant NBS-LRR protein in disease resistance-related cell death
    • Moffett, P., Farnham, G., Peart, J., and Baulcombe, D.C. (2002). Interaction between domains of a plant NBS-LRR protein in disease resistance-related cell death. EMBO J. 21: 4511-4519.
    • (2002) EMBO J , vol.21 , pp. 4511-4519
    • Moffett, P.1    Farnham, G.2    Peart, J.3    Baulcombe, D.C.4
  • 58
    • 0347383760 scopus 로고    scopus 로고
    • ARP/wARP and automatic interpretation of protein electron density maps
    • Morris, R.J., Perrakis, A., and Lamzin, V.S. (2003). ARP/wARP and automatic interpretation of protein electron density maps. Methods Enzymol. 374: 229-244.
    • (2003) Methods Enzymol , vol.374 , pp. 229-244
    • Morris, R.J.1    Perrakis, A.2    Lamzin, V.S.3
  • 60
    • 1842526090 scopus 로고    scopus 로고
    • ProMate: A structure based prediction program to identify the location of protein-protein binding sites
    • Neuvirth, H., Raz, R., and Schreiber, G. (2004). ProMate: A structure based prediction program to identify the location of protein-protein binding sites. J. Mol. Biol. 338: 181-199.
    • (2004) J. Mol. Biol , vol.338 , pp. 181-199
    • Neuvirth, H.1    Raz, R.2    Schreiber, G.3
  • 61
    • 84986486656 scopus 로고
    • A rapid finite difference algorithm, using successive over-relaxation to solve the Poisson-Boltzmann equation
    • Nicholls, A., and Honig, B. (1991). A rapid finite difference algorithm, using successive over-relaxation to solve the Poisson-Boltzmann equation. J. Comput. Chem. 12: 435-445.
    • (1991) J. Comput. Chem , vol.12 , pp. 435-445
    • Nicholls, A.1    Honig, B.2
  • 62
    • 1642463788 scopus 로고    scopus 로고
    • Innate immunity in plants and animals: Striking similarities and obvious differences
    • Nurnberger, T., Brunner, F., Kemmerling, B., and Piater, L. (2004). Innate immunity in plants and animals: Striking similarities and obvious differences. Immunol. Rev. 198: 249-266.
    • (2004) Immunol. Rev , vol.198 , pp. 249-266
    • Nurnberger, T.1    Brunner, F.2    Kemmerling, B.3    Piater, L.4
  • 63
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997). Processing of x-ray diffraction data collected in oscillation mode. Methods Enzymol. 276: 307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 64
    • 11844292002 scopus 로고    scopus 로고
    • Inference of protein function from protein structure
    • Pal, D., and Eisenberg, D. (2005). Inference of protein function from protein structure. Structure 13: 121-130.
    • (2005) Structure , vol.13 , pp. 121-130
    • Pal, D.1    Eisenberg, D.2
  • 66
    • 33747473700 scopus 로고    scopus 로고
    • Distinct domains in the ARC region of the potato resistance protein Rx mediate LRR binding and inhibition of activation
    • Rairdan, G.J., and Moffett, P. (2006). Distinct domains in the ARC region of the potato resistance protein Rx mediate LRR binding and inhibition of activation. Plant Cell 18: 2082-2093.
    • (2006) Plant Cell , vol.18 , pp. 2082-2093
    • Rairdan, G.J.1    Moffett, P.2
  • 68
    • 20544475699 scopus 로고    scopus 로고
    • Cladosporium Avr2 inhibits tomato Rcr3 protease required for Cf-2-dependent disease resistance
    • Rooney, H.C., Van't Klooster, J.W., van der Hoorn, R.A., Joosten, M.H., Jones, J.D., and de Wit, P.J. (2005). Cladosporium Avr2 inhibits tomato Rcr3 protease required for Cf-2-dependent disease resistance. Science. 308: 1783-1786.
    • (2005) Science , vol.308 , pp. 1783-1786
    • Rooney, H.C.1    Van't Klooster, J.W.2    van der Hoorn, R.A.3    Joosten, M.H.4    Jones, J.D.5    de Wit, P.J.6
  • 69
    • 33645977173 scopus 로고    scopus 로고
    • Structure of Ptr ToxA: An RGD-containing host-selective toxin from Pyrenophora tritici-repentis
    • Sarma, G.N., Manning, V.A., Ciuffetti, L.M., and Karplus, P.A. (2005). Structure of Ptr ToxA: An RGD-containing host-selective toxin from Pyrenophora tritici-repentis. Plant Cell 17: 3190-3202.
    • (2005) Plant Cell , vol.17 , pp. 3190-3202
    • Sarma, G.N.1    Manning, V.A.2    Ciuffetti, L.M.3    Karplus, P.A.4
  • 70
    • 0037074015 scopus 로고    scopus 로고
    • Structure of internalin, a major invasion protein of Listeria monocytogenes, in complex with its human receptor E-cadherin
    • Schubert, W.D., Urbanke, C., Ziehm, T., Beier, V., Machner, M.P., Domann, E., Wehland, J., Chakraborty, T., and Heinz, D.W. (2002). Structure of internalin, a major invasion protein of Listeria monocytogenes, in complex with its human receptor E-cadherin. Cell 111: 825-836.
    • (2002) Cell , vol.111 , pp. 825-836
    • Schubert, W.D.1    Urbanke, C.2    Ziehm, T.3    Beier, V.4    Machner, M.P.5    Domann, E.6    Wehland, J.7    Chakraborty, T.8    Heinz, D.W.9
  • 71
    • 0042322616 scopus 로고    scopus 로고
    • Cleavage of Arabidopsis PBS1 by a bacterial type III effector
    • Shao, F., Golstein, C., Ade, J., Stoutemyer, M., Dixon, J.E., and Innes, R.W. (2003). Cleavage of Arabidopsis PBS1 by a bacterial type III effector. Science 301: 1230-1233.
    • (2003) Science , vol.301 , pp. 1230-1233
    • Shao, F.1    Golstein, C.2    Ade, J.3    Stoutemyer, M.4    Dixon, J.E.5    Innes, R.W.6
  • 73
    • 0242669338 scopus 로고    scopus 로고
    • Recognition specificity and RAR1/SGT1 dependence in barley Mla disease resistance genes to the powdery mildew fungus
    • Shen, Q.H., Zhou, F., Bieri, S., Haizel, T., Shirasu, K., and Schulze-Lefert, P. (2003). Recognition specificity and RAR1/SGT1 dependence in barley Mla disease resistance genes to the powdery mildew fungus. Plant Cell 15: 732-744.
    • (2003) Plant Cell , vol.15 , pp. 732-744
    • Shen, Q.H.1    Zhou, F.2    Bieri, S.3    Haizel, T.4    Shirasu, K.5    Schulze-Lefert, P.6
  • 74
    • 0031715982 scopus 로고    scopus 로고
    • Protein structure alignment by incremental combinatorial extension (CE) of the optimal path
    • Shindyalov, I.N., and Bourne, P.E. (1998). Protein structure alignment by incremental combinatorial extension (CE) of the optimal path. Protein Eng. 11: 739-747.
    • (1998) Protein Eng , vol.11 , pp. 739-747
    • Shindyalov, I.N.1    Bourne, P.E.2
  • 76
    • 33746989767 scopus 로고    scopus 로고
    • Resistance proteins: Molecular switches of plant defence
    • Takken, F.L., Albrecht, M., and Tameling, W.I. (2006). Resistance proteins: Molecular switches of plant defence. Curr. Opin. Plant Biol. 9: 383-390.
    • (2006) Curr. Opin. Plant Biol , vol.9 , pp. 383-390
    • Takken, F.L.1    Albrecht, M.2    Tameling, W.I.3
  • 78
    • 0036848846 scopus 로고    scopus 로고
    • Automated structure solution, density modifi-cation and model building
    • Terwilliger, T.C. (2002). Automated structure solution, density modifi-cation and model building. Acta Crystallogr. D Biol. Crystallogr. 58: 1937-1940.
    • (2002) Acta Crystallogr. D Biol. Crystallogr , vol.58 , pp. 1937-1940
    • Terwilliger, T.C.1
  • 80
    • 17444373556 scopus 로고    scopus 로고
    • PreDs: A server for predicting dsDNA-binding site on protein molecular surfaces
    • Tsuchiya, Y., Kinoshita, K., and Nakamura, H. (2005). PreDs: A server for predicting dsDNA-binding site on protein molecular surfaces. Bioinformatics 21: 1721-1723.
    • (2005) Bioinformatics , vol.21 , pp. 1721-1723
    • Tsuchiya, Y.1    Kinoshita, K.2    Nakamura, H.3
  • 81
    • 35748978069 scopus 로고
    • Weiterentwicklung eines Programms fur Molekulgraphik und Elektrondichte-Manipulation und seine Anwendung auf verschiedene Protein-Strukturaufklarungen. PhD dissertation Muenchen, Germany: Technische Universitat
    • Turk, D. (1992). Weiterentwicklung eines Programms fur Molekulgraphik und Elektrondichte-Manipulation und seine Anwendung auf verschiedene Protein-Strukturaufklarungen. PhD dissertation (Muenchen, Germany: Technische Universitat).
    • (1992)
    • Turk, D.1
  • 82
    • 33745184517 scopus 로고    scopus 로고
    • Direct interaction between the tobacco mosaic virus helicase domain and the ATP-bound resistance protein, N factor during the hypersensitive response in tobacco plants
    • Ueda, H., Yamaguchi, Y., and Sano, H. (2006). Direct interaction between the tobacco mosaic virus helicase domain and the ATP-bound resistance protein, N factor during the hypersensitive response in tobacco plants. Plant Mol. Biol. 61: 31-45.
    • (2006) Plant Mol. Biol , vol.61 , pp. 31-45
    • Ueda, H.1    Yamaguchi, Y.2    Sano, H.3
  • 83
    • 0032922193 scopus 로고    scopus 로고
    • SFCHECK: A unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model
    • Vaguine, A.A., Richelle, J., and Wodak, S.J. (1999). SFCHECK: A unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model. Acta Crystallogr. D Biol. Crystallogr. 55: 191-205.
    • (1999) Acta Crystallogr. D Biol. Crystallogr , vol.55 , pp. 191-205
    • Vaguine, A.A.1    Richelle, J.2    Wodak, S.J.3
  • 84
    • 0042848482 scopus 로고    scopus 로고
    • Natural disulfide bond-disrupted mutants of AVR4 of the tomato pathogen Cladosporium fulvum are sensitive to proteolysis, circumvent Cf-4-mediated resistance, but retain their chitin binding ability
    • van den Burg, H.A., Westerink, N., Francoijs, K.J., Roth, R., Woestenenk, E., Boeren, S., de Wit, P.J., Joosten, M.H., and Vervoort, J. (2003). Natural disulfide bond-disrupted mutants of AVR4 of the tomato pathogen Cladosporium fulvum are sensitive to proteolysis, circumvent Cf-4-mediated resistance, but retain their chitin binding ability. J. Biol. Chem. 278: 27340-27346.
    • (2003) J. Biol. Chem , vol.278 , pp. 27340-27346
    • van den Burg, H.A.1    Westerink, N.2    Francoijs, K.J.3    Roth, R.4    Woestenenk, E.5    Boeren, S.6    de Wit, P.J.7    Joosten, M.H.8    Vervoort, J.9
  • 85
    • 0035957232 scopus 로고    scopus 로고
    • Disulfide bond structure of the AVR9 elicitor of the fungal tomato pathogen Cladosporium fulvum: Evidence for a cystine knot
    • van den Hooven, H.W., van den Burg, H.A., Vossen, P., Boeren, S., de Wit, P.J., and Vervoort, J. (2001). Disulfide bond structure of the AVR9 elicitor of the fungal tomato pathogen Cladosporium fulvum: Evidence for a cystine knot. Biochemistry 40: 3458-3466.
    • (2001) Biochemistry , vol.40 , pp. 3458-3466
    • van den Hooven, H.W.1    van den Burg, H.A.2    Vossen, P.3    Boeren, S.4    de Wit, P.J.5    Vervoort, J.6
  • 86
    • 0242664724 scopus 로고    scopus 로고
    • Solution structure of the plant disease resistance-triggering protein NIP1 from the fungus Rhynchosporium secalis shows a novel beta-sheet fold
    • van't Slot,K.A., van den Burg,H.A., Kloks, C.P.,Hilbers,C.W., Knogge, W., and Papavoine, C.H. (2003). Solution structure of the plant disease resistance-triggering protein NIP1 from the fungus Rhynchosporium secalis shows a novel beta-sheet fold. J. Biol. Chem. 278: 45730-45736.
    • (2003) J. Biol. Chem , vol.278 , pp. 45730-45736
    • van't Slot, K.A.1    van den Burg, H.A.2    Kloks, C.P.3    Hilbers, C.W.4    Knogge, W.5    Papavoine, C.H.6
  • 87
    • 3142534455 scopus 로고    scopus 로고
    • The solution structure of type III effector protein AvrP to reveals conformational and dynamic features important for plant pathogenesis
    • Wulf, J., Pascuzzi, P.E., Fahmy, A., Martin, G.B., and Nicholson, L.K. (2004). The solution structure of type III effector protein AvrP to reveals conformational and dynamic features important for plant pathogenesis. Structure 12: 1257-1268.
    • (2004) Structure , vol.12 , pp. 1257-1268
    • Wulf, J.1    Pascuzzi, P.E.2    Fahmy, A.3    Martin, G.B.4    Nicholson, L.K.5
  • 88
    • 0347719364 scopus 로고    scopus 로고
    • The crystal structure of Pseudomonas avirulence protein AvrPphB: A papain-like fold with a distinct substrate-binding site
    • Zhu, M., Shao, F., Innes, R.W., Dixon, J.E., and Xu, Z. (2004). The crystal structure of Pseudomonas avirulence protein AvrPphB: A papain-like fold with a distinct substrate-binding site. Proc. Natl. Acad. Sci. USA 101: 302-307.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 302-307
    • Zhu, M.1    Shao, F.2    Innes, R.W.3    Dixon, J.E.4    Xu, Z.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.