메뉴 건너뛰기




Volumn 162, Issue 3, 2013, Pages 1510-1528

Structural determinants at the interface of the ARC2 and leucine-rich repeat domains control the activation of the plant immune receptors Rx1 and Gpa2

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA; GLOBODERA PALLIDA; POTATO VIRUS X; SOLANUM TUBEROSUM;

EID: 84879724105     PISSN: 00320889     EISSN: 15322548     Source Type: Journal    
DOI: 10.1104/pp.113.218842     Document Type: Article
Times cited : (75)

References (73)
  • 1
    • 33847769886 scopus 로고    scopus 로고
    • Indirect activation of a plant nucleotide binding site-leucine-rich repeat protein by a bacterial protease
    • Ade J, DeYoung BJ, Golstein C, Innes RW (2007) Indirect activation of a plant nucleotide binding site-leucine-rich repeat protein by a bacterial protease. Proc Natl Acad Sci USA 104: 2531-2536.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 2531-2536
    • Ade, J.1    Deyoung, B.J.2    Golstein, C.3    Innes, R.W.4
  • 2
    • 28444488986 scopus 로고    scopus 로고
    • Update on the domain architectures of NLRs and R proteins
    • Albrecht M, Takken FLW (2006) Update on the domain architectures of NLRs and R proteins. Biochem Biophys Res Commun 339: 459-462.
    • (2006) Biochem Biophys Res Commun , vol.339 , pp. 459-462
    • Albrecht, M.1    Takken, F.L.W.2
  • 3
    • 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 DC (2002) Constitutive gain-of-function mutants in a nucleotide binding site-leucine rich repeat protein encoded at the Rx locus of potato. Plant J 32: 195-204.
    • (2002) Plant J , vol.32 , pp. 195-204
    • Bendahmane, A.1    Farnham, G.2    Moffett, P.3    Baulcombe, D.C.4
  • 4
    • 0034000967 scopus 로고    scopus 로고
    • Agrobacterium transient expression system as a tool for the isolation of disease resistance genes: Application to the Rx2 locus in potato
    • Bendahmane A, Querci M, Kanyuka K, Baulcombe DC (2000) Agrobacterium transient expression system as a tool for the isolation of disease resistance genes: application to the Rx2 locus in potato. Plant J 21: 73-81.
    • (2000) Plant J , vol.21 , pp. 73-81
    • Bendahmane, A.1    Querci, M.2    Kanyuka, K.3    Baulcombe, D.C.4
  • 5
    • 38549141229 scopus 로고    scopus 로고
    • Exploring the extremes of sequence/structure space with ensemble fold recognition in the program Phyre
    • Bennett-Lovsey RM, Herbert AD, Sternberg MJ, Kelley LA (2008) Exploring the extremes of sequence/structure space with ensemble fold recognition in the program Phyre. Proteins 70: 611-625.
    • (2008) Proteins , vol.70 , pp. 611-625
    • Bennett-Lovsey, R.M.1    Herbert, A.D.2    Sternberg, M.J.3    Kelley, L.A.4
  • 6
    • 79952643473 scopus 로고    scopus 로고
    • Structural and functional analysis of a plant resistance protein TIR domain reveals interfaces for selfassociation, signaling, and autoregulation
    • Bernoux M, Ve T, Williams S, Warren C, Hatters D, Valkov E, Zhang X, Ellis JG, Kobe B, Dodds PN (2011) Structural and functional analysis of a plant resistance protein TIR domain reveals interfaces for selfassociation, signaling, and autoregulation. Cell Host Microbe 9: 200-211.
    • (2011) Cell Host Microbe , vol.9 , pp. 200-211
    • Bernoux, M.1    Ve, T.2    Williams, S.3    Warren, C.4    Hatters, D.5    Valkov, E.6    Zhang, X.7    Ellis, J.G.8    Kobe, B.9    Dodds, P.N.10
  • 8
    • 79960505285 scopus 로고    scopus 로고
    • Cell death mediated by the Nterminal domains of a unique and highly conserved class of NB-LRR protein
    • Collier SM, Hamel LP, Moffett P (2011) Cell death mediated by the Nterminal domains of a unique and highly conserved class of NB-LRR protein. Mol Plant Microbe Interact 24: 918-931.
    • (2011) Mol Plant Microbe Interact , vol.24 , pp. 918-931
    • Collier, S.M.1    Hamel, L.P.2    Moffett, P.3
  • 9
    • 0034039342 scopus 로고    scopus 로고
    • Members of the Arabidopsis HRT/RPP8 family of resistance genes confer resistance to both viral and oomycete pathogens
    • Cooley MB, Pathirana S, Wu HJ, Kachroo P, Klessig DF (2000) Members of the Arabidopsis HRT/RPP8 family of resistance genes confer resistance to both viral and oomycete pathogens. Plant Cell 12: 663-676.
    • (2000) Plant Cell , vol.12 , pp. 663-676
    • Cooley, M.B.1    Pathirana, S.2    Wu, H.J.3    Kachroo, P.4    Klessig, D.F.5
  • 11
    • 59649103157 scopus 로고    scopus 로고
    • Wheel of life, wheel of death: A mechanistic insight into signaling by STAND proteins
    • Danot O, Marquenet E, Vidal-Ingigliardi D, Richet E (2009) Wheel of life, wheel of death: a mechanistic insight into signaling by STAND proteins. Structure 17: 172-182
    • (2009) Structure , vol.17 , pp. 172-182
    • Danot, O.1    Marquenet, E.2    Vidal-Ingigliardi, D.3    Richet, E.4
  • 13
    • 77954763024 scopus 로고    scopus 로고
    • Plant immunity: Towards an integrated view of plant-pathogen interactions
    • Dodds PN, Rathjen JP (2010) Plant immunity: towards an integrated view of plant-pathogen interactions. Nat Rev Genet 11: 539-548.
    • (2010) Nat Rev Genet , vol.11 , pp. 539-548
    • Dodds, P.N.1    Rathjen, J.P.2
  • 14
    • 0037442962 scopus 로고    scopus 로고
    • HADDOCK: A proteinprotein docking approach based on biochemical or biophysical information
    • Dominguez C, Boelens R, Bonvin AM (2003) HADDOCK: a proteinprotein docking approach based on biochemical or biophysical information. J Am Chem Soc 125: 1731-1737.
    • (2003) J Am Chem Soc , vol.125 , pp. 1731-1737
    • Dominguez, C.1    Boelens, R.2    Bonvin, A.M.3
  • 15
    • 24044538903 scopus 로고    scopus 로고
    • IUPred: Web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content
    • Dosztányi Z, Csizmok V, Tompa P, Simon I (2005) IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content. Bioinformatics 21: 3433-3434.
    • (2005) Bioinformatics , vol.21 , pp. 3433-3434
    • Dosztányi, Z.1    Csizmok, V.2    Tompa, P.3    Simon, I.4
  • 16
    • 33845495805 scopus 로고    scopus 로고
    • Artificial evolution extends the spectrum of viruses that are targeted by a disease-resistance gene from potato
    • Farnham G, Baulcombe DC (2006) Artificial evolution extends the spectrum of viruses that are targeted by a disease-resistance gene from potato. Proc Natl Acad Sci USA 103: 18828-18833.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 18828-18833
    • Farnham, G.1    Baulcombe, D.C.2
  • 17
    • 18844414326 scopus 로고    scopus 로고
    • High accuracy prediction of beta-turns and their types using propensities and multiple alignments
    • Fuchs PF, Alix AJ (2005) High accuracy prediction of beta-turns and their types using propensities and multiple alignments. Proteins 59: 828-839.
    • (2005) Proteins , vol.59 , pp. 828-839
    • Fuchs, P.F.1    Alix, A.J.2
  • 18
    • 0029884694 scopus 로고    scopus 로고
    • GOR method for predicting protein secondary structure from amino acid sequence
    • Garnier J, Gibrat JF, Robson B (1996) GOR method for predicting protein secondary structure from amino acid sequence. Methods Enzymol 266: 540-553.
    • (1996) Methods Enzymol , vol.266 , pp. 540-553
    • Garnier, J.1    Gibrat, J.F.2    Robson, B.3
  • 19
    • 0029595442 scopus 로고
    • SOPMA: Significant improvements in protein secondary structure prediction by consensus prediction from multiple alignments
    • Geourjon C, Deléage G (1995) SOPMA: significant improvements in protein secondary structure prediction by consensus prediction from multiple alignments. Comput Appl Biosci 11: 681-684.
    • (1995) Comput Appl Biosci , vol.11 , pp. 681-684
    • Geourjon, C.1    Deléage, G.2
  • 20
    • 0037388110 scopus 로고    scopus 로고
    • Self-association and conformational properties of RAG1: Implications for formation of the V(D)J recombinase
    • Godderz LJ, Rahman NS, Risinger GM, Arbuckle JL, Rodgers KK (2003) Self-association and conformational properties of RAG1: implications for formation of the V(D)J recombinase. Nucleic Acids Res 31: 2014-2023.
    • (2003) Nucleic Acids Res , vol.31 , pp. 2014-2023
    • Godderz, L.J.1    Rahman, N.S.2    Risinger, G.M.3    Arbuckle, J.L.4    Rodgers, K.K.5
  • 21
    • 1342305253 scopus 로고    scopus 로고
    • The role and regulation of programmed cell death in plant-pathogen interactions
    • Greenberg JT, Yao N (2004) The role and regulation of programmed cell death in plant-pathogen interactions. Cell Microbiol 6: 201-211.
    • (2004) Cell Microbiol , vol.6 , pp. 201-211
    • Greenberg, J.T.1    Yao, N.2
  • 22
    • 0035119502 scopus 로고    scopus 로고
    • The MLA6 coiled-coil, NBS-LRR protein confers AvrMla6-dependent resistance specificity to Blumeria graminis f. sp. hordei in barley and wheat
    • Halterman D, Zhou F, Wei F, Wise RP, Schulze-Lefert P (2001) The MLA6 coiled-coil, NBS-LRR protein confers AvrMla6-dependent resistance specificity to Blumeria graminis f. sp. hordei in barley and wheat. Plant J 25: 335-348.
    • (2001) Plant J , vol.25 , pp. 335-348
    • Halterman, D.1    Zhou, F.2    Wei, F.3    Wise, R.P.4    Schulze-Lefert, P.5
  • 23
    • 0032509354 scopus 로고    scopus 로고
    • WD-40 repeat region regulates Apaf-1 self-association and procaspase-9 activation
    • Hu Y, Ding L, Spencer DM, Núñez G (1998) WD-40 repeat region regulates Apaf-1 self-association and procaspase-9 activation. J Biol Chem 273: 33489-33494.
    • (1998) J Biol Chem , vol.273 , pp. 33489-33494
    • Hu, Y.1    Ding, L.2    Spencer, D.M.3    Núñez, G.4
  • 25
    • 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 CF, Williamson VM (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
  • 26
    • 43449100066 scopus 로고    scopus 로고
    • Allosteric and electrostatic protein-protein interactions regulate the assembly of the heterohexameric Tim9-Tim10 complex
    • Ivanova E, Lu H (2008) Allosteric and electrostatic protein-protein interactions regulate the assembly of the heterohexameric Tim9-Tim10 complex. J Mol Biol 379: 609-616.
    • (2008) J Mol Biol , vol.379 , pp. 609-616
    • Ivanova, E.1    Lu, H.2
  • 27
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on positionspecific scoring matrices
    • Jones DT (1999) Protein secondary structure prediction based on positionspecific scoring matrices. J Mol Biol 292: 195-202.
    • (1999) J Mol Biol , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 28
    • 33751100626 scopus 로고    scopus 로고
    • The plant immune system
    • Jones JD, Dangl JL (2006) The plant immune system. Nature 444: 323-329.
    • (2006) Nature , vol.444 , pp. 323-329
    • Jones, J.D.1    Dangl, J.L.2
  • 29
    • 0037372098 scopus 로고    scopus 로고
    • Prediction of b-turns in proteins from multiple alignment using neural network
    • Kaur H, Raghava GP (2003) Prediction of b-turns in proteins from multiple alignment using neural network. Protein Sci 12: 627-634.
    • (2003) Protein Sci , vol.12 , pp. 627-634
    • Kaur, H.1    Raghava, G.P.2
  • 30
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the web: A case study using the Phyre server
    • Kelley LA, Sternberg MJ (2009) Protein structure prediction on the web: a case study using the Phyre server. Nat Protoc 4: 363-371.
    • (2009) Nat Protoc , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 31
    • 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 DD, Koonin EV, 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. J Mol Biol 343: 1-28.
    • (2004) J Mol Biol , vol.343 , pp. 1-28
    • Leipe, D.D.1    Koonin, E.V.2    Aravind, L.3
  • 32
    • 1242316239 scopus 로고    scopus 로고
    • Tandem and segmental gene duplication and recombination in the evolution of plant disease resistance gene
    • Leister D (2004) Tandem and segmental gene duplication and recombination in the evolution of plant disease resistance gene. Trends Genet 20: 116-122.
    • (2004) Trends Genet , vol.20 , pp. 116-122
    • Leister, D.1
  • 33
    • 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 RT, Dahlbeck D, Day B, Li Y, Chesnokova O, Staskawicz BJ (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
  • 35
    • 68149175128 scopus 로고    scopus 로고
    • STANDing strong, resistance proteins instigators of plant defence
    • Lukasik E, Takken FLW (2009) STANDing strong, resistance proteins instigators of plant defence. Curr Opin Plant Biol 12: 427-436.
    • (2009) Curr Opin Plant Biol , vol.12 , pp. 427-436
    • Lukasik, E.1    Takken, F.L.W.2
  • 37
    • 80051967147 scopus 로고    scopus 로고
    • NLR functions in plant and animal immune systems: So far and yet so close
    • Maekawa T, Kufer TA, Schulze-Lefert P (2011b) NLR functions in plant and animal immune systems: so far and yet so close. Nat Immunol 12: 817-826.
    • (2011) Nat Immunol , vol.12 , pp. 817-826
    • Maekawa, T.1    Kufer, T.A.2    Schulze-Lefert, P.3
  • 41
    • 0036288851 scopus 로고    scopus 로고
    • Characterization and prediction of linker sequences of multi-domain proteins by a neural network
    • Miyazaki S, Kuroda Y, Yokoyama S (2002) Characterization and prediction of linker sequences of multi-domain proteins by a neural network. J Struct Funct Genomics 2: 37-51.
    • (2002) J Struct Funct Genomics , vol.2 , pp. 37-51
    • Miyazaki, S.1    Kuroda, Y.2    Yokoyama, S.3
  • 42
    • 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 DC (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
  • 45
    • 17444397116 scopus 로고    scopus 로고
    • Porter: A new, accurate server for protein secondary structure prediction
    • Pollastri G, McLysaght A (2005) Porter: a new, accurate server for protein secondary structure prediction. Bioinformatics 21: 1719-1720.
    • (2005) Bioinformatics , vol.21 , pp. 1719-1720
    • Pollastri, G.1    McLysaght, A.2
  • 46
  • 47
    • 84859346744 scopus 로고    scopus 로고
    • Structure-function analysis of the coiled-coil and leucine-rich repeat domains of the RPS5 disease resistance protein
    • Qi D, DeYoung BJ, Innes RW (2012) Structure-function analysis of the coiled-coil and leucine-rich repeat domains of the RPS5 disease resistance protein. Plant Physiol 158: 1819-1832.
    • (2012) Plant Physiol , vol.158 , pp. 1819-1832
    • Qi, D.1    Deyoung, B.J.2    Innes, R.W.3
  • 48
    • 34247115054 scopus 로고    scopus 로고
    • Brothers in arms? Common and contrasting themes in pathogen perception by plant NB-LRR and animal NACHTLRR proteins
    • Rairdan G, Moffett P (2007) Brothers in arms? Common and contrasting themes in pathogen perception by plant NB-LRR and animal NACHTLRR proteins. Microbes Infect 9: 677-686.
    • (2007) Microbes Infect , vol.9 , pp. 677-686
    • Rairdan, G.1    Moffett, P.2
  • 49
    • 48249140729 scopus 로고    scopus 로고
    • The coiled-coil and nucleotide binding domains of the potato Rx disease resistance protein function in pathogen recognition and signaling
    • Rairdan GJ, Collier SM, Sacco MA, Baldwin TT, Boettrich T, Moffett P (2008) The coiled-coil and nucleotide binding domains of the potato Rx disease resistance protein function in pathogen recognition and signaling. Plant Cell 20: 739-751.
    • (2008) Plant Cell , vol.20 , pp. 739-751
    • Rairdan, G.J.1    Collier, S.M.2    Sacco, M.A.3    Baldwin, T.T.4    Boettrich, T.5    Moffett, P.6
  • 50
    • 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 GJ, 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
  • 51
    • 80051534863 scopus 로고    scopus 로고
    • Crystal structure of fulllength Apaf-1: How the death signal is relayed in the mitochondrial pathway of apoptosis
    • Reubold TF, Wohlgemuth S, Eschenburg S (2011) Crystal structure of fulllength Apaf-1: how the death signal is relayed in the mitochondrial pathway of apoptosis. Structure 19: 1074-1083.
    • (2011) Structure , vol.19 , pp. 1074-1083
    • Reubold, T.F.1    Wohlgemuth, S.2    Eschenburg, S.3
  • 52
    • 17244368276 scopus 로고    scopus 로고
    • Structure of the apoptotic protease-activating factor 1 bound to ADP
    • Riedl SJ, Li WY, Chao Y, Schwarzenbacher R, Shi YG (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.Y.2    Chao, Y.3    Schwarzenbacher, R.4    Shi, Y.G.5
  • 54
    • 34347407697 scopus 로고    scopus 로고
    • A RanGAP protein physically interacts with the NB-LRR protein Rx, and is required for Rx-mediated viral resistance
    • Sacco MA, 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 J 52: 82-93.
    • (2007) Plant J , vol.52 , pp. 82-93
    • Sacco, M.A.1    Mansoor, S.2    Moffett, P.3
  • 55
    • 0032568655 scopus 로고    scopus 로고
    • SMART, a simple modular architecture research tool: Identification of signaling domains
    • Schultz J, Milpetz F, Bork P, Ponting CP (1998) SMART, a simple modular architecture research tool: identification of signaling domains. Proc Natl Acad Sci USA 95: 5857-5864.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 5857-5864
    • Schultz, J.1    Milpetz, F.2    Bork, P.3    Ponting, C.P.4
  • 57
    • 0034039797 scopus 로고    scopus 로고
    • Electrostatic aspects of proteinprotein interactions
    • Sheinerman FB, Norel R, Honig B (2000) Electrostatic aspects of proteinprotein interactions. Curr Opin Struct Biol 10: 153-159.
    • (2000) Curr Opin Struct Biol , vol.10 , pp. 153-159
    • Sheinerman, F.B.1    Norel, R.2    Honig, B.3
  • 58
    • 0027477526 scopus 로고
    • Structural analysis based on statespace modeling
    • Stultz CM, White JV, Smith TF (1993) Structural analysis based on statespace modeling. Protein Sci 2: 305-314.
    • (1993) Protein Sci , vol.2 , pp. 305-314
    • Stultz, C.M.1    White, J.V.2    Smith, T.F.3
  • 59
    • 59749083228 scopus 로고    scopus 로고
    • The TIR domain of TIR-NB-LRR resistance proteins is a signaling domain involved in cell death induction
    • Swiderski MR, Birker D, Jones JD (2009) The TIR domain of TIR-NB-LRR resistance proteins is a signaling domain involved in cell death induction. Mol Plant Microbe Interact 22: 157-165.
    • (2009) Mol Plant Microbe Interact , vol.22 , pp. 157-165
    • Swiderski, M.R.1    Birker, D.2    Jones, J.D.3
  • 61
    • 65649140098 scopus 로고    scopus 로고
    • To nibble at plant resistance proteins
    • Takken FLW, Tameling WIL (2009) To nibble at plant resistance proteins. Science 324: 744-746.
    • (2009) Science , vol.324 , pp. 744-746
    • Takken, F.L.W.1    Tameling, W.I.L.2
  • 62
    • 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 WIL, Baulcombe DC (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: 1682-1694.
    • (2007) Plant Cell , vol.19 , pp. 1682-1694
    • Tameling, W.I.L.1    Baulcombe, D.C.2
  • 64
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22: 4673-4680
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 65
    • 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 EA, Jones JDG (1998) The NB-ARC domain: a novel signalling motif shared by plant resistance gene products and regulators of cell death in animals. Curr Biol 8: R226-R227.
    • (1998) Curr Biol , vol.8
    • van der Biezen, E.A.1    Jones, J.D.G.2
  • 66
    • 0034063376 scopus 로고    scopus 로고
    • Agroinfiltration is a versatile tool that facilitates comparative analyses of Avr9/Cf-9-induced and Avr4/Cf-4-induced necrosis
    • Van der Hoorn RAL, Laurent F, Roth R, DeWit PJ (2000) Agroinfiltration is a versatile tool that facilitates comparative analyses of Avr9/Cf-9-induced and Avr4/Cf-4-induced necrosis. Mol Plant Microbe Interact 13: 439-446
    • (2000) Mol Plant Microbe Interact , vol.13 , pp. 439-446
    • Van der Hoorn, R.A.L.1    Laurent, F.2    Roth, R.3    Dewit, P.J.4
  • 69
    • 68149089161 scopus 로고    scopus 로고
    • Transcomplementation, but not physical association of the CC-NB-ARC and LRR domains of tomato R protein Mi-1.2 is altered by mutations in the ARC2 subdomain
    • van Ooijen G, Mayr G, Albrecht M, Cornelissen BJC, Takken FLW(2008) Transcomplementation, but not physical association of the CC-NB-ARC and LRR domains of tomato R protein Mi-1.2 is altered by mutations in the ARC2 subdomain. Mol Plant 1: 401-410.
    • (2008) Mol Plant , vol.1 , pp. 401-410
    • van Ooijen, G.1    Mayr, G.2    Albrecht, M.3    Cornelissen, B.J.C.4    Takken, F.L.W.5
  • 70
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • Ward JJ, Sodhi JS, McGuffin LJ, Buxton BF, Jones DT (2004) Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J Mol Biol 337: 635-645.
    • (2004) J Mol Biol , vol.337 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 71
    • 0032170811 scopus 로고    scopus 로고
    • A mutation within the leucine-rich repeat domain of the Arabidopsis disease resistance gene RPS5 partially suppresses multiple bacterial and downy mildew resistance genes
    • Warren RF, Henk A, Mowery P, Holub E, Innes RW (1998) A mutation within the leucine-rich repeat domain of the Arabidopsis disease resistance gene RPS5 partially suppresses multiple bacterial and downy mildew resistance genes. Plant Cell 10: 1439-1452.
    • (1998) Plant Cell , vol.10 , pp. 1439-1452
    • Warren, R.F.1    Henk, A.2    Mowery, P.3    Holub, E.4    Innes, R.W.5
  • 72
    • 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 JJ, Lee ES, Gu LC, Liu Q, He JQ, Wu JW, Kokel D, Li HL, Hao Q, 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.J.2    Lee, E.S.3    Gu, L.C.4    Liu, Q.5    He, J.Q.6    Wu, J.W.7    Kokel, D.8    Li, H.L.9    Hao, Q.10
  • 73
    • 0030745646 scopus 로고    scopus 로고
    • Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome cdependent activation of caspase-3
    • Zou H, Henzel WJ, Liu X, Lutschg A, Wang X (1997) Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome cdependent activation of caspase-3. Cell 90: 405-413
    • (1997) Cell , vol.90 , pp. 405-413
    • Zou, H.1    Henzel, W.J.2    Liu, X.3    Lutschg, A.4    Wang, X.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.