메뉴 건너뛰기




Volumn , Issue , 2008, Pages 243-255

Resistance proteins: Scouts of the plant innate immune system

Author keywords

Disease resistance; Effector; NB LRR proteins; Nucleotide binding; Nucleus; PAMP

Indexed keywords


EID: 84900886120     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-1-4020-8780-6_4     Document Type: Chapter
Times cited : (7)

References (88)
  • 3
    • 0034284435 scopus 로고    scopus 로고
    • The BED finger, a novel DNA-binding domain in chromatin-boundary-element- binding proteins and transposases
    • Aravind, L. (2000). The BED finger, a novel DNA-binding domain in chromatin-boundary-element-binding proteins and transposases. Trends in Biochemical Sciences, 25, 421-423.
    • (2000) Trends in Biochemical Sciences , vol.25 , pp. 421-423
    • Aravind, L.1
  • 4
    • 27144540463 scopus 로고    scopus 로고
    • Are innate immune signaling pathways in plants and animals conserved
    • Ausubel, F. M. (2005). Are innate immune signaling pathways in plants and animals conserved. Nauret Immunoogyl, 6, 973-979.
    • (2005) Nauret Immunoogyl , vol.6 , pp. 973-979
    • Ausubel, F.M.1
  • 5
    • 0141566396 scopus 로고    scopus 로고
    • Genetic and molecular evidence that the Pseudomonas syringae type III effector protein AvrRpt2 is a cysteine protease
    • Axtell, M. J., Chisholm, S. T., Dahlbeck, D., & Staskawicz, B. J. (2003). Genetic and molecular evidence that the Pseudomonas syringae type III effector protein AvrRpt2 is a cysteine protease. Molecular Microbiology, 49, 1537-1546.
    • (2003) Molecular Microbiology , vol.49 , pp. 1537-1546
    • Axtell, M.J.1    Chisholm, S.T.2    Dahlbeck, D.3    Staskawicz, B.J.4
  • 7
    • 33846236461 scopus 로고    scopus 로고
    • Calcium blocks formation of apoptosome by preventing nucleotide exchange in Apaf-1
    • Bao, Q., Lu, W., Rabinowitz, J. D., & Shi, Y. (2007). Calcium blocks formation of apoptosome by preventing nucleotide exchange in Apaf-1. Molecular Cell, 25, 181-192.
    • (2007) Molecular Cell , vol.25 , pp. 181-192
    • Bao, Q.1    Lu, W.2    Rabinowitz, J.D.3    Shi, Y.4
  • 8
    • 0036775380 scopus 로고    scopus 로고
    • Constitutive gain-of-function mutants in a nucleotide binding site-leucine rich repeat protein encoded at the Rx locus of potato
    • Bendahmane, A., Farnham, G., Moffett, P., & Baulcombe, D. C. (2002). Constitutive gain-of-function mutants in a nucleotide binding site-leucine rich repeat protein encoded at the Rx locus of potato. Plant Journal, 32, 195-204.
    • (2002) Plant Journal , vol.32 , pp. 195-204
    • Bendahmane, A.1    Farnham, G.2    Moffett, P.3    Baulcombe, D.C.4
  • 9
    • 20444426395 scopus 로고    scopus 로고
    • RAR1 positively controls steady state levels of barley MLA resistance proteins and enables sufficient MLA6 accumulation for effective resistance
    • Bieri, S., Mauch, S., Shen, Q. H., Peart, J., Devoto, A., Casais, C., et al. (2004). RAR1 positively controls steady state levels of barley MLA resistance proteins and enables sufficient MLA6 accumulation for effective resistance. Plant Cell, 16, 3480-3495.
    • (2004) Plant Cell , vol.16 , pp. 3480-3495
    • Bieri, S.1    Mauch, S.2    Shen, Q.H.3    Peart, J.4    Devoto, A.5    Casais, C.6
  • 13
    • 33646894893 scopus 로고    scopus 로고
    • A B-lectin receptor kinase gene conferring rice blast resistance
    • Chen, X., Shang, J., Chen, D., Lei, C., Zou, Y., Zhai, W., et al. (2006). A B-lectin receptor kinase gene conferring rice blast resistance. Plant Journal, 46, 794-804.
    • (2006) Plant Journal , vol.46 , pp. 794-804
    • Chen, X.1    Shang, J.2    Chen, D.3    Lei, C.4    Zou, Y.5    Zhai, W.6
  • 14
    • 32944479048 scopus 로고    scopus 로고
    • Host-microbe interactions: Shaping the evolution of the plant immune response
    • Chisholm, S. T., Coaker, G., Day, B., & 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
  • 15
    • 22544483556 scopus 로고    scopus 로고
    • Heat shock protein 90 and its co-chaperone protein phosphatase 5 interact with distinct regions of the tomato I-2 disease resistance protein
    • De La Fuente Van Bentem, S., Vossen, J. H., De Vries, K., Van Wees, S. C., Tameling, W. I. L., Dekker, H., et al. (2005). Heat shock protein 90 and its co-chaperone protein phosphatase 5 interact with distinct regions of the tomato I-2 disease resistance protein. Plant Journal, 43, 284-298.
    • (2005) Plant Journal , vol.43 , pp. 284-298
    • De La Fuente Van Bentem, S.1    Vossen, J.H.2    De Vries, K.3    Van Wees, S.C.4    Tameling, W.I.L.5    Dekker, H.6
  • 19
    • 0038032933 scopus 로고    scopus 로고
    • Plant meristems: A merry-go-round of signals
    • Doerner, P. (2003). Plant meristems: A merry-go-round of signals. Current Biology, 13, R368-R374.
    • (2003) Current Biology , vol.13
    • Doerner, P.1
  • 20
    • 35148843712 scopus 로고    scopus 로고
    • Flax rust resistance gene specificity is based on direct resistanceavirulence protein interactions
    • Ellis, J. G., Dodds, P. N., & Lawrence, G. J. (2007). Flax rust resistance gene specificity is based on direct resistanceavirulence protein interactions. Annual Review of Phytopathology, 45, 289-306.
    • (2007) Annual Review of Phytopathology , vol.45 , pp. 289-306
    • Ellis, J.G.1    Dodds, P.N.2    Lawrence, G.J.3
  • 21
    • 0034307755 scopus 로고    scopus 로고
    • Interplay of signaling pathways in plant disease resistance
    • Feys, B. J., & Parker, J. E. (2000). Interplay of signaling pathways in plant disease resistance. Trends in Genetics, 16, 449-455.
    • (2000) Trends in Genetics , vol.16 , pp. 449-455
    • Feys, B.J.1    Parker, J.E.2
  • 25
    • 33750097480 scopus 로고    scopus 로고
    • Subterfuge and manipulation: Type III effector proteins of phytopathogenic bacteria
    • Grant, S. R., Fisher, E. J., Chang, J. H., Mole, B. M., & Dangl, J. L. (2006). Subterfuge and Manipulation: Type III Effector Proteins of Phytopathogenic Bacteria. Annual Review of Microbiology, 60, 425-449.
    • (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
  • 26
    • 23244450437 scopus 로고    scopus 로고
    • Antagonistic control of disease resistance protein stability in the plant immune system
    • Holt 3rd, B. F., Belkhadir, Y., & Dangl, J. L. (2005). Antagonistic control of disease resistance protein stability in the plant immune system. Science, 309, 929-932.
    • (2005) Science , vol.309 , pp. 929-932
    • Holt III, B.F.1    Belkhadir, Y.2    Dangl, J.L.3
  • 27
    • 0036085807 scopus 로고    scopus 로고
    • An evolutionarily conserved mediator of plant disease resistance gene function is required for normal Arabidopsis development
    • Holt 3rd, B. F., Boyes, D. C., Ellerstrom, M., Siefers, N., Wiig, A., Kauffman, S., et al. (2002). An evolutionarily conserved mediator of plant disease resistance gene function is required for normal Arabidopsis development. Developmental Cell, 2, 807-817.
    • (2002) Developmental Cell , vol.2 , pp. 807-817
    • Holt III, B.F.1    Boyes, D.C.2    Ellerstrom, M.3    Siefers, N.4    Wiig, A.5    Kauffman, S.6
  • 28
    • 19544374693 scopus 로고    scopus 로고
    • Autoactive alleles of the flax L6 rust resistance gene induce non-racespecific rust resistance associated with the hypersensitive response
    • Howles, P., Lawrence, G., Finnegan, J., McFadden, H., Ayliffe, M., Dodds, P., et al. (2005). Autoactive alleles of the flax L6 rust resistance gene induce non-racespecific rust resistance associated with the hypersensitive response. Molecular Plant-Microbe Interactions, 18, 570-582.
    • (2005) Molecular Plant-microbe Interactions , vol.18 , pp. 570-582
    • Howles, P.1    Lawrence, G.2    Finnegan, J.3    McFadden, H.4    Ayliffe, M.5    Dodds, P.6
  • 29
    • 0242556837 scopus 로고    scopus 로고
    • Cytosolic HSP90 associates with and modulates the Arabidopsis RPM1 disease resistance protein
    • Hubert, D. A., Tornero, P., Belkhadir, Y., Krishna, P., Takahashi, A., Shirasu, K., et al. (2003). Cytosolic HSP90 associates with and modulates the Arabidopsis RPM1 disease resistance protein. EMBO Journal, 22, 5679-5689.
    • (2003) EMBO Journal , vol.22 , pp. 5679-5689
    • Hubert, D.A.1    Tornero, P.2    Belkhadir, Y.3    Krishna, P.4    Takahashi, A.5    Shirasu, K.6
  • 30
    • 0033823537 scopus 로고    scopus 로고
    • Evidence for a role of the N terminus and leucine-rich repeat region of the Mi gene product in regulation of localized cell death
    • Hwang, C. F., Bhakta, A. V., Truesdell, G. M., Pudlo, W. M., & Williamson, V. M. (2000). Evidence for a role of the N terminus and leucine-rich repeat region of the Mi gene product in regulation of localized cell death. Plant Cell, 12, 1319-1329.
    • (2000) Plant Cell , vol.12 , pp. 1319-1329
    • Hwang, C.F.1    Bhakta, A.V.2    Truesdell, G.M.3    Pudlo, W.M.4    Williamson, V.M.5
  • 31
    • 33751100626 scopus 로고    scopus 로고
    • The plant immune system
    • Jones, J. D. G., & Dangl, J. L. (2006). The plant immune system. Nature, 444, 323-329.
    • (2006) Nature , vol.444 , pp. 323-329
    • Jones, J.D.G.1    Dangl, J.L.2
  • 32
    • 0032695338 scopus 로고    scopus 로고
    • The tomato-Cladosporium fulvum interaction: A versatile experimental system to study plant-pathogen interactions
    • Joosten, M. H. A. J., & De Wit, P. J. G. M. (1999). The tomato-Cladosporium fulvum interaction: A versatile experimental system to study plant-pathogen interactions. Annual Review of Phytopathology, 37, 355-367.
    • (1999) Annual Review of Phytopathology , vol.37 , pp. 355-367
    • Joosten, M.H.A.J.1    De Wit, P.J.G.M.2
  • 33
    • 0032478536 scopus 로고    scopus 로고
    • Structural diversity of leucine-rich repeat proteins
    • Kajava, A. V. (1998). Structural diversity of leucine-rich repeat proteins. Journal of Molecular Biology, 277, 519-527.
    • (1998) Journal of Molecular Biology , vol.277 , pp. 519-527
    • Kajava, A.V.1
  • 34
    • 27644505459 scopus 로고    scopus 로고
    • Formation of apoptosome is initiated by cytochrome c-induced dATP hydrolysis and subsequent nucleotide exchange on Apaf-1
    • Kim, H. E., Du, F., Fang, M., & Wang, X. (2005). Formation of apoptosome is initiated by cytochrome c-induced dATP hydrolysis and subsequent nucleotide exchange on Apaf-1. Proceedings of the National Academy of Sciences of the United States of America, 102, 17545-17550.
    • (2005) Proceedings of the National Academy of Sciences of the United States of America , vol.102 , pp. 17545-17550
    • Kim, H.E.1    Du, F.2    Fang, M.3    Wang, X.4
  • 35
    • 0028080261 scopus 로고
    • The leucine-rich repeat: A versatile binding motif
    • Kobe, B., & Deisenhofer, J. (1994). The leucine-rich repeat: A versatile binding motif. Trends in Biochemical Sciences, 19, 415-421.
    • (1994) Trends in Biochemical Sciences , vol.19 , pp. 415-421
    • Kobe, B.1    Deisenhofer, J.2
  • 36
    • 4644247731 scopus 로고    scopus 로고
    • STAND, a class of P-loop NTPases including animal and plant regulators of programmed cell death: Multiple, complex domain architectures, unusual phyletic patterns, and evolution by horizontal gene transfer
    • Leipe, D. D., Koonin, E. V., & Aravind, L. (2004). STAND, a class of P-loop NTPases including animal and plant regulators of programmed cell death: Multiple, complex domain architectures, unusual phyletic patterns, and evolution by horizontal gene transfer. Journal of Molecular Biology, 343, 1-28.
    • (2004) Journal of Molecular Biology , vol.343 , pp. 1-28
    • Leipe, D.D.1    Koonin, E.V.2    Aravind, L.3
  • 37
    • 21044458960 scopus 로고    scopus 로고
    • Molecular genetic evidence for the role of SGT1 in the intramolecular complementation of Bs2 protein activity in Nicotiana benthamiana
    • Leister, R. T., Dahlbeck, D., Day, B., Li, Y., Chesnokova, O., & Staskawicz, B. J. (2005). Molecular genetic evidence for the role of SGT1 in the intramolecular complementation of Bs2 protein activity in Nicotiana benthamiana. Plant Cell, 17, 1268-1278.
    • (2005) Plant Cell , vol.17 , pp. 1268-1278
    • Leister, R.T.1    Dahlbeck, D.2    Day, B.3    Li, Y.4    Chesnokova, O.5    Staskawicz, B.J.6
  • 38
    • 0347087451 scopus 로고    scopus 로고
    • Molecular chaperone Hsp90 associates with resistance protein N and its signaling proteins SGT1 and Rar1 to modulate an innate immune response in plants
    • Liu, Y., Burch-Smith, T., Schiff, M., Feng, S., & Dinesh-Kumar, S. P. (2004). Molecular chaperone Hsp90 associates with resistance protein N and its signaling proteins SGT1 and Rar1 to modulate an innate immune response in plants. Journal of Biological Chemistry, 279, 2101-2108.
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 2101-2108
    • Liu, Y.1    Burch-Smith, T.2    Schiff, M.3    Feng, S.4    Dinesh-Kumar, S.P.5
  • 39
    • 0035984050 scopus 로고    scopus 로고
    • Role of SCF ubiquitin-ligase and the COP9 signalosome in the N gene-mediated resistance response to tobacco mosaic virus
    • Liu, Y., Schiff, M., Serino, G., Deng, X. W., & Dinesh-Kumar, S. P. (2002). Role of SCF Ubiquitin-Ligase and the COP9 Signalosome in the N Gene-Mediated Resistance Response to Tobacco mosaic virus. Plant Cell, 14, 1483-1496.
    • (2002) Plant Cell , vol.14 , pp. 1483-1496
    • Liu, Y.1    Schiff, M.2    Serino, G.3    Deng, X.W.4    Dinesh-Kumar, S.P.5
  • 40
    • 0037155687 scopus 로고    scopus 로고
    • RIN4 interacts with Pseudomonas syringae type III effector molecules and is required for RPM1-mediated resistance in Arabidopsis
    • Mackey, D., Holt, B. F., Wiig, A., & Dangl, J. L. (2002). RIN4 interacts with Pseudomonas syringae type III effector molecules and is required for RPM1-mediated resistance in Arabidopsis. Cell, 108, 743-754.
    • (2002) Cell , vol.108 , pp. 743-754
    • Mackey, D.1    Holt, B.F.2    Wiig, A.3    Dangl, J.L.4
  • 41
    • 0142057020 scopus 로고    scopus 로고
    • Understanding the functions of plant disease resistance proteins
    • Martin, G. B., Bogdanove, A. J., & Sessa, G. (2003). Understanding the functions of plant disease resistance proteins. Annual Review of Plant Biology, 54, 23-61.
    • (2003) Annual Review of Plant Biology , vol.54 , pp. 23-61
    • Martin, G.B.1    Bogdanove, A.J.2    Sessa, G.3
  • 43
    • 33845899112 scopus 로고    scopus 로고
    • Composition of the plant nuclear envelope: Theme and variations
    • Meier, I. (2007). Composition of the plant nuclear envelope: Theme and variations. Journal of Experimental Botany, 58, 27-34.
    • (2007) Journal of Experimental Botany , vol.58 , pp. 27-34
    • Meier, I.1
  • 44
    • 0346728564 scopus 로고    scopus 로고
    • Nucleo-cytoplasmic partitioning of proteins in plants: Implications for the regulation of environmental and developmental signalling
    • Merkle, T. (2003). Nucleo-cytoplasmic partitioning of proteins in plants: Implications for the regulation of environmental and developmental signalling. Current Genetics, 44, 231-260.
    • (2003) Current Genetics , vol.44 , pp. 231-260
    • Merkle, T.1
  • 45
    • 33745455354 scopus 로고    scopus 로고
    • Elicitor-mediated oligomerization of the tobacco N disease resistance protein
    • Mestre, P., & Baulcombe, D. C. (2006). Elicitor-mediated oligomerization of the tobacco N disease resistance protein. Plant Cell, 18, 491-501.
    • (2006) Plant Cell , vol.18 , pp. 491-501
    • Mestre, P.1    Baulcombe, D.C.2
  • 46
    • 0033231602 scopus 로고    scopus 로고
    • Plant disease resistance genes encode members of an ancient and diverse protein family within the nucleotide-binding superfamily
    • Meyers, B. C., Dickerman, A. W., Michelmore, R. W., Sivaramakrishnan, S., Sobral, B. W., & Young, N. D. (1999). Plant disease resistance genes encode members of an ancient and diverse protein family within the nucleotide-binding superfamily. Plant Journal, 20, 317-332.
    • (1999) Plant Journal , vol.20 , pp. 317-332
    • Meyers, B.C.1    Dickerman, A.W.2    Michelmore, R.W.3    Sivaramakrishnan, S.4    Sobral, B.W.5    Young, N.D.6
  • 47
    • 0037390933 scopus 로고    scopus 로고
    • Genome-wide analysis of NBS-LRR-encoding genes in Arabidopsis
    • Meyers, B. C., Kozik, A., Griego, A., Kuang, H., & Michelmore, R. W. (2003). Genome-wide analysis of NBS-LRR-encoding genes in Arabidopsis. Plant Cell, 15, 809-834.
    • (2003) Plant Cell , vol.15 , pp. 809-834
    • Meyers, B.C.1    Kozik, A.2    Griego, A.3    Kuang, H.4    Michelmore, R.W.5
  • 48
    • 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., & Baulcombe, D. C. (2002). Interaction between domains of a plant NBS-LRR protein in disease resistance-related cell death. EMBO Journal, 21, 4511-4519.
    • (2002) EMBO Journal , vol.21 , pp. 4511-4519
    • Moffett, P.1    Farnham, G.2    Peart, J.3    Baulcombe, D.C.4
  • 50
    • 33750988221 scopus 로고    scopus 로고
    • The tomato NBARC-LRR protein Prf interacts with Pto kinase in vivo to regulate specific plant immunity
    • Mucyn, T. S., Clemente, A., Andriotis, V. M. E., Balmuth, A. L., Mucyn Oldroyd, G. E. D., Staskawicz, B. J., et al. (2006). The tomato NBARC-LRR protein Prf Interacts with Pto kinase in vivo to regulate specific plant immunity. Plant Cell, 18(10), 2792-806.
    • (2006) Plant Cell , vol.18 , Issue.10 , pp. 2792-2806
    • Mucyn, T.S.1    Clemente, A.2    Andriotis, V.M.E.3    Balmuth, A.L.4    Mucyn Oldroyd, G.E.D.5    Staskawicz, B.J.6
  • 51
    • 33750316409 scopus 로고    scopus 로고
    • Receptor protein kinases-pattern recognition receptors in plant immunity
    • Nürnberger, T., & Kemmerling, B. (2006). Receptor protein kinases-pattern recognition receptors in plant immunity. Trends in Plant Scencei, 11, 519-522.
    • (2006) Trends in Plant Scencei , vol.11 , pp. 519-522
    • Nürnberger, T.1    Kemmerling, B.2
  • 52
    • 20544446717 scopus 로고    scopus 로고
    • An importin alpha homolog, MOS6, plays an important role in plant innate immunity
    • Palma, K., Zhang, Y., & Li, X. (2005). An importin alpha homolog, MOS6, plays an important role in plant innate immunity. Current Biology, 15, 1129-1135.
    • (2005) Current Biology , vol.15 , pp. 1129-1135
    • Palma, K.1    Zhang, Y.2    Li, X.3
  • 53
    • 0343352530 scopus 로고    scopus 로고
    • Divergent evolution of plant NBS-LRR resistance gene homologues in dicot and cereal genomes
    • Pan, Q., Wendel, J., & Fluhr, R. (2000). Divergent evolution of plant NBS-LRR resistance gene homologues in dicot and cereal genomes. Journal of Molecular Evolution, 50, 203-213.
    • (2000) Journal of Molecular Evolution , vol.50 , pp. 203-213
    • Pan, Q.1    Wendel, J.2    Fluhr, R.3
  • 54
    • 0036017872 scopus 로고    scopus 로고
    • Plant RanGAPs are localized at the nuclear envelope in interphase and associated with microtubules in mitotic cells
    • Pay, A., Resch, K., Frohnmeyer, H., Fejes, E., Nagy, F., & Nick, P. (2002). Plant RanGAPs are localized at the nuclear envelope in interphase and associated with microtubules in mitotic cells. Plant Journal, 30, 699-709.
    • (2002) Plant Journal , vol.30 , pp. 699-709
    • Pay, A.1    Resch, K.2    Frohnmeyer, H.3    Fejes, E.4    Nagy, F.5    Nick, P.6
  • 55
    • 20144382377 scopus 로고    scopus 로고
    • NRG1, a CC-NB-LRR protein, together with N, a TIR-NB-LRR protein, mediates resistance against tobacco mosaic virus
    • Peart, J. R., Mestre, P., Lu, R., Malcuit, I., & Baulcombe, D. C. (2005). NRG1, a CC-NB-LRR Protein, together with N, a TIR-NB-LRR Protein, Mediates Resistance against Tobacco Mosaic Virus. Current Biology, 15, 968-973.
    • (2005) Current Biology , vol.15 , pp. 968-973
    • Peart, J.R.1    Mestre, P.2    Lu, R.3    Malcuit, I.4    Baulcombe, D.C.5
  • 56
    • 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., & 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
  • 57
    • 34247115054 scopus 로고    scopus 로고
    • Brothers in arms? Common and contrasting themes in pathogen perception by plant NB-LRR and animal NACHT-LRR proteins
    • Rairdan, G., & Moffett, P. (2007). Brothers in arms? Common and contrasting themes in pathogen perception by plant NB-LRR and animal NACHT-LRR proteins. Microbes and Infection, 9, 677-686.
    • (2007) Microbes and Infection , vol.9 , pp. 677-686
    • Rairdan, G.1    Moffett, P.2
  • 58
    • 17244368276 scopus 로고    scopus 로고
    • Structure of the apoptotic protease-activating factor 1 bound to ADP
    • Riedl, S. J., Li, W., Chao, Y., Schwarzenbacher, R., & Shi, Y. (2005). Structure of the apoptotic protease-activating factor 1 bound to ADP. Nature, 434, 926-933.
    • (2005) Nature , vol.434 , pp. 926-933
    • Riedl, S.J.1    Li, W.2    Chao, Y.3    Schwarzenbacher, R.4    Shi, Y.5
  • 59
    • 0036491745 scopus 로고    scopus 로고
    • An approximately 400 kDa membrane-associated complex that contains one molecule of the resistance protein Cf-4
    • Rivas, S., Mucyn, T., Van Den Burg, H. A., Vervoort, J., & Jones, J. D. G. (2002a). An approximately 400 kDa membrane-associated complex that contains one molecule of the resistance protein Cf-4. Plant Journal, 29, 783-796.
    • (2002) Plant Journal , vol.29 , pp. 783-796
    • Rivas, S.1    Mucyn, T.2    Van Den Burg, H.A.3    Vervoort, J.4    Jones, J.D.G.5
  • 60
    • 0036221525 scopus 로고    scopus 로고
    • The Cf-9 disease resistance protein is present in an approximately 420-kilodalton heteromultimeric membrane-associated complex at one molecule per complex
    • Rivas, S., Romeis, T., & Jones, J. D. G. (2002b). The Cf-9 disease resistance protein is present in an approximately 420-kilodalton heteromultimeric membrane-associated complex at one molecule per complex. Plant Cell, 14, 689-702.
    • (2002) Plant Cell , vol.14 , pp. 689-702
    • Rivas, S.1    Romeis, T.2    Jones, J.D.G.3
  • 61
    • 24944497655 scopus 로고    scopus 로고
    • Molecular interactions between tomato and the leaf mold pathogen Cladosporium fulvum
    • Rivas, S., & Thomas, C. M. (2005). Molecular interactions between tomato and the leaf mold pathogen Cladosporium fulvum. Annual Review of Phytopathology, 43, 395-436.
    • (2005) Annual Review of Phytopathology , vol.43 , pp. 395-436
    • Rivas, S.1    Thomas, C.M.2
  • 62
    • 2942683505 scopus 로고    scopus 로고
    • The receptor for the fungal elicitor ethylene-inducing xylanase is a member of a resistancelike gene family in tomato
    • Ron, M., & Avni, A. (2004). The receptor for the fungal elicitor ethylene-inducing xylanase is a member of a resistancelike gene family in tomato. Plant Cell, 16, 1604-1615.
    • (2004) Plant Cell , vol.16 , pp. 1604-1615
    • Ron, M.1    Avni, A.2
  • 64
    • 34347407697 scopus 로고    scopus 로고
    • A RanGAP protein physically interacts with the NB-LRR protein Rx and is required for Rx-mediated viral resistance
    • DOI 10.111/j.1365-313x.2007.03213.x
    • Sacco, M., Mansoor, S., & Moffett, P. (2007). A RanGAP protein physically interacts with the NB-LRR protein Rx and is required for Rx-mediated viral resistance. Plant Journal, DOI 10.111/j.1365-313x.2007.03213.x.
    • (2007) Plant Journal
    • Sacco, M.1    Mansoor, S.2    Moffett, P.3
  • 65
    • 34250159521 scopus 로고    scopus 로고
    • Purification of the M flax-rust resistance protein expressed in Pichia pastoris
    • Schmidt, S. A., Williams, S. J., Wang, C. I., Sornaraj, P., James, B., Kobe, B., et al. (2007). Purification of the M flax-rust resistance protein expressed in Pichia pastoris. Plant Journal, 50, 1107-1117.
    • (2007) Plant Journal , vol.50 , pp. 1107-1117
    • Schmidt, S.A.1    Williams, S.J.2    Wang, C.I.3    Sornaraj, P.4    James, B.5    Kobe, B.6
  • 66
    • 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., & 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
  • 67
    • 33847254952 scopus 로고    scopus 로고
    • Nuclear activity of MLA immune receptors links isolate-specific and basal disease-resistance responses
    • Shen, Q. H., Saijo, Y., Mauch, S., Biskup, C., Bieri, S., Keller, B., et al. (2007). Nuclear activity of MLA immune receptors links isolate-specific and basal disease-resistance responses. Science, 315, 1098-1103.
    • (2007) Science , vol.315 , pp. 1098-1103
    • Shen, Q.H.1    Saijo, Y.2    Mauch, S.3    Biskup, C.4    Bieri, S.5    Keller, B.6
  • 68
    • 33646947047 scopus 로고    scopus 로고
    • Point mutations with positive selection were a major force during the evolution of a receptor-kinase resistance gene family of rice
    • Sun, X., Cao, Y., & Wang, S. (2006). Point mutations with positive selection were a major force during the evolution of a receptor-kinase resistance gene family of rice. Plant Physiology, 140, 998-1008.
    • (2006) Plant Physiology , vol.140 , pp. 998-1008
    • Sun, X.1    Cao, Y.2    Wang, S.3
  • 69
    • 1342333402 scopus 로고    scopus 로고
    • Xa26, a gene conferring resistance to Xanthomonas oryzae pv. oryzae. in rice, encodes an LRR receptor kinase-like protein
    • Sun, X., Cao, Y., Yang, Z., Xu, C., Li, X., Wang, S., et al. (2004). Xa26, a gene conferring resistance to Xanthomonas oryzae pv. oryzae. in rice, encodes an LRR receptor kinase-like protein. Plant Journal, 37, 517-527.
    • (2004) Plant Journal , vol.37 , pp. 517-527
    • Sun, X.1    Cao, Y.2    Yang, Z.3    Xu, C.4    Li, X.5    Wang, S.6
  • 70
    • 0035013980 scopus 로고    scopus 로고
    • Recombination between paralogues at the rp1 rust resistance locus in maize
    • Sun, Q., Collins, N. C., Ayliffe, M., Smith, S. M., Drake, J., Pryor, T., et al. (2001). Recombination between paralogues at the rp1 rust resistance locus in maize. Genetics, 158, 423-438.
    • (2001) Genetics , vol.158 , pp. 423-438
    • Sun, Q.1    Collins, N.C.2    Ayliffe, M.3    Smith, S.M.4    Drake, J.5    Pryor, T.6
  • 73
    • 34347378219 scopus 로고    scopus 로고
    • Physical association of the NB-LRR resistance protein Rx with a Ran GTPase-activating protein is required for extreme resistance to potato virus X
    • Tameling, W. I. L., & Baulcombe, D. C. (2007). Physical association of the NB-LRR resistance protein Rx with a Ran GTPase-activating protein is required for extreme resistance to potato virus X. Plant Cell, 19, 1682-694.
    • (2007) Plant Cell , vol.19 , pp. 1682-1694
    • Tameling, W.I.L.1    Baulcombe, D.C.2
  • 74
    • 0036844825 scopus 로고    scopus 로고
    • The tomato R gene products I-2 and Mi-1 are functional ATP binding proteins with ATPase activity
    • Tameling, W. I. L., Elzinga, S. D., Darmin, P. S., Vossen, J. H., Takken, F. L. W., Haring, M. A., et al. (2002). The tomato R gene products I-2 and Mi-1 are functional ATP binding proteins with ATPase activity. Plant Cell, 14, 2929-2939.
    • (2002) Plant Cell , vol.14 , pp. 2929-2939
    • Tameling, W.I.L.1    Elzinga, S.D.2    Darmin, P.S.3    Vossen, J.H.4    Takken, F.L.W.5    Haring, M.A.6
  • 75
  • 77
    • 0037324536 scopus 로고    scopus 로고
    • Quantitative nature of Arabidopsis responses during compatible and incompatible interactions with the bacterial pathogen Pseudomonas syringae
    • Tao, Y., Xie, Z., Chen, W., Glazebrook, J., Chang, H. S., Han, B., et al. (2003). Quantitative nature of Arabidopsis responses during compatible and incompatible interactions with the bacterial pathogen Pseudomonas syringae. Plant Cell, 15, 317-330.
    • (2003) Plant Cell , vol.15 , pp. 317-330
    • Tao, Y.1    Xie, Z.2    Chen, W.3    Glazebrook, J.4    Chang, H.S.5    Han, B.6
  • 78
    • 33344476398 scopus 로고    scopus 로고
    • CATERPILLERs, pyrin and hereditary immunological disorders. Natures review
    • Ting, J. P., Kastner, D. L., & Hoffman, H. M. (2006). CATERPILLERs, pyrin and hereditary immunological disorders. Natures Review. Immunology, 6, 183-195.
    • (2006) Immunology , vol.6 , pp. 183-195
    • Ting, J.P.1    Kastner, D.L.2    Hoffman, H.M.3
  • 79
  • 80
    • 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., & 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 Molecular Biology, 61, 31-45.
    • (2006) Plant Molecular Biology , vol.61 , pp. 31-45
    • Ueda, H.1    Yamaguchi, Y.2    Sano, H.3
  • 81
    • 4444340698 scopus 로고    scopus 로고
    • WRKY transcription factors: From DNA binding towards biological function
    • Ulker, B., & Somssich, I. E. (2004). WRKY transcription factors: From DNA binding towards biological function. Current Opinion in Plant Biology, 7, 491-498.
    • (2004) Current Opinion in Plant Biology , vol.7 , pp. 491-498
    • Ulker, B.1    Somssich, I.E.2
  • 82
    • 0032568168 scopus 로고    scopus 로고
    • The NB-ARC domain: A novel signalling motif shared by plant resistance gene products and regulators of cell death in animals
    • Van Der Biezen, E. A., & Jones, J. D. G. (1998). The NB-ARC domain: A novel signalling motif shared by plant resistance gene products and regulators of cell death in animals. Current Biology, 8, R226-227.
    • (1998) Current Biology , vol.8
    • Van Der Biezen, E.A.1    Jones, J.D.G.2
  • 83
    • 0043068000 scopus 로고    scopus 로고
    • Rapid migration in gel filtration of the Cf-4 and Cf-9 resistance proteins is an intrinsic property of Cf proteins and not because of their association with high-molecular-weight proteins
    • Van Der Hoorn, R. A., Rivas, S., Wulff, B. B., Jones, J. D., & Joosten, M. H. (2003). Rapid migration in gel filtration of the Cf-4 and Cf-9 resistance proteins is an intrinsic property of Cf proteins and not because of their association with high-molecular-weight proteins. Plant Journal, 35, 305-315.
    • (2003) Plant Journal , vol.35 , pp. 305-315
    • Van Der Hoorn, R.A.1    Rivas, S.2    Wulff, B.B.3    Jones, J.D.4    Joosten, M.H.5
  • 85
    • 33748304125 scopus 로고    scopus 로고
    • The Arabidopsis thaliana TIR-NB-LRR R-protein, RPP1A; protein localization and constitutive activation of defence by truncated alleles in tobacco and Arabidopsis
    • Weaver, M. L., Swiderski, M. R., Li, Y., & Jones, J. D. (2006). The Arabidopsis thaliana TIR-NB-LRR R-protein, RPP1A; protein localization and constitutive activation of defence by truncated alleles in tobacco and Arabidopsis. Plant Journal, 47, 829-840.
    • (2006) Plant Journal , vol.47 , pp. 829-840
    • Weaver, M.L.1    Swiderski, M.R.2    Li, Y.3    Jones, J.D.4
  • 86
    • 0034597766 scopus 로고    scopus 로고
    • Structural basis for signal transduction by the Toll/interleukin-1 receptor domains
    • Xu, Y., Tao, X., Shen, B., Horng, T., Medzhitov, R., Manley, J. L., et al. (2000). Structural basis for signal transduction by the Toll/interleukin-1 receptor domains. Nature, 408, 111-115.
    • (2000) Nature , vol.408 , pp. 111-115
    • Xu, Y.1    Tao, X.2    Shen, B.3    Horng, T.4    Medzhitov, R.5    Manley, J.L.6
  • 87
    • 26844485563 scopus 로고    scopus 로고
    • Structure of the CED-4-CED-9 complex provides insights into programmed cell death in Caenorhabditis elegans
    • Yan, N., Chai, J., Lee, E. S., Gu, L., Liu, Q., He, J., et al. (2005). Structure of the CED-4-CED-9 complex provides insights into programmed cell death in Caenorhabditis elegans. Nature, 437, 831-837.
    • (2005) Nature , vol.437 , pp. 831-837
    • Yan, N.1    Chai, J.2    Lee, E.S.3    Gu, L.4    Liu, Q.5    He, J.6
  • 88
    • 6444233160 scopus 로고    scopus 로고
    • Expression of RPS4 in tobacco induces an AvrRps4-independent HR that requires EDS1, SGT1 and HSP90
    • Zhang, Y., Dorey, S., Swiderski, M., & Jones, J. D. (2004). Expression of RPS4 in tobacco induces an AvrRps4-independent HR that requires EDS1, SGT1 and HSP90. Plant Journal, 40, 213-224.
    • (2004) Plant Journal , vol.40 , pp. 213-224
    • Zhang, Y.1    Dorey, S.2    Swiderski, M.3    Jones, J.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.