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Volumn 9, Issue 3, 2011, Pages 200-211

Structural and functional analysis of a plant resistance protein TIR domain reveals interfaces for self-association, signaling, and autoregulation

Author keywords

[No Author keywords available]

Indexed keywords

INTERLEUKIN 1 RECEPTOR; LEUCINE RICH REPEAT KINASE 2; NUCLEOTIDE BINDING PROTEIN;

EID: 79952643473     PISSN: 19313128     EISSN: 19346069     Source Type: Journal    
DOI: 10.1016/j.chom.2011.02.009     Document Type: Article
Times cited : (282)

References (62)
  • 2
    • 77954257799 scopus 로고    scopus 로고
    • ConSurf 2010: Calculating evolutionary conservation in sequence and structure of proteins and nucleic acids
    • Ashkenazy, H., Erez, E., Martz, E., Pupko, T., and Ben-Tal, N. (2010). ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids. Nucleic Acids Res. Suppl. 38, W529-W533.
    • (2010) Nucleic Acids Res. Suppl. , vol.38
    • Ashkenazy, H.1    Erez, E.2    Martz, E.3    Pupko, T.4    Ben-Tal, N.5
  • 3
    • 0035964342 scopus 로고    scopus 로고
    • Electrostatics of nanosystems: Application to microtubules and the ribosome
    • Baker, N.A., Sept, D., Joseph, S., Holst, M.J., and McCammon, J.A. (2001). Electrostatics of nanosystems: application to microtubules and the ribosome. Proc. Natl. Acad. Sci. USA 98, 10037-10041.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 10037-10041
    • Baker, N.A.1    Sept, D.2    Joseph, S.3    Holst, M.J.4    McCammon, J.A.5
  • 4
    • 33845501864 scopus 로고    scopus 로고
    • Apoptosome: A platform for the activation of initiator caspases
    • DOI 10.1038/sj.cdd.4402028, PII 4402028
    • Bao, Q., and Shi, Y. (2007). Apoptosome: a platform for the activation of initiator caspases. Cell Death Differ. 14, 56-65. (Pubitemid 44911894)
    • (2007) Cell Death and Differentiation , vol.14 , Issue.1 , pp. 56-65
    • Bao, Q.1    Shi, Y.2
  • 5
    • 57749094835 scopus 로고    scopus 로고
    • RD19, an Arabidopsis cysteine protease required for RRS1-R-mediated resistance, is relocalized to the nucleus by the Ralstonia solanacearum PopP2 effector
    • DOI 10.1105/tpc.108.058685
    • Bernoux, M., Timmers, T., Jauneau, A., Briere, C., de Wit, P.J., Marco, Y., and Deslandes, L. (2008). RD19, an Arabidopsis cysteine protease required for RRS1-R-mediated resistance, is relocalized to the nucleus by the Ralstonia solanacearum PopP2 effector. Plant Cell 20, 2252-2264. (Pubitemid 352844523)
    • (2008) Plant Cell , vol.20 , Issue.8 , pp. 2252-2264
    • Bernoux, M.1    Timmers, T.2    Jauneau, A.3    Briere, C.4    De Wit, P.J.G.M.5    Marco, Y.6    Deslandesa, L.7
  • 6
    • 39349100844 scopus 로고    scopus 로고
    • Signalling of toll-like receptors
    • Brikos, C., and O'Neill, L.A. (2008). Signalling of toll-like receptors. Handb. Exp. Pharmacol. 2008, 21-50.
    • (2008) Handb. Exp. Pharmacol. , vol.2008 , pp. 21-50
    • Brikos, C.1    O'Neill, L.A.2
  • 7
    • 38849106202 scopus 로고    scopus 로고
    • Chloroplastic Protein NRIP1 Mediates Innate Immune Receptor Recognition of a Viral Effector
    • DOI 10.1016/j.cell.2007.12.031, PII S0092867408000524
    • Caplan, J.L., Mamillapalli, P., Burch-Smith, T.M., Czymmek, K., and Dinesh-Kumar, S.P. (2008). Chloroplastic protein NRIP1 mediates innate immune receptor recognition of a viral effector. Cell 132, 449-462. (Pubitemid 351191994)
    • (2008) Cell , vol.132 , Issue.3 , pp. 449-462
    • Caplan, J.L.1    Mamillapalli, P.2    Burch-Smith, T.M.3    Czymmek, K.4    Dinesh-Kumar, S.P.5
  • 9
    • 75149175757 scopus 로고    scopus 로고
    • The crystal structure of a TIR domain from Arabidopsis thaliana reveals a conserved helical region unique to plants
    • Chan, S.L., Mukasa, T., Santelli, E., Low, L.Y., and Pascual, J. (2010). The crystal structure of a TIR domain from Arabidopsis thaliana reveals a conserved helical region unique to plants. Protein Sci. 19, 155-161.
    • (2010) Protein Sci. , vol.19 , pp. 155-161
    • Chan, S.L.1    Mukasa, T.2    Santelli, E.3    Low, L.Y.4    Pascual, J.5
  • 11
    • 32944479048 scopus 로고    scopus 로고
    • Host-microbe interactions: Shaping the evolution of the plant immune response
    • DOI 10.1016/j.cell.2006.02.008, PII S0092867406001838
    • Chisholm, S.T., Coaker, G., Day, B., and Staskawicz, B.J. (2006). Host-microbe interactions: shaping the evolution of the plant immune response. Cell 124, 803-814. (Pubitemid 43261453)
    • (2006) Cell , vol.124 , Issue.4 , pp. 803-814
    • Chisholm, S.T.1    Coaker, G.2    Day, B.3    Staskawicz, B.J.4
  • 12
    • 0037208360 scopus 로고    scopus 로고
    • An overview of the CCP4 project in protein crystallography: An example of a collaborative project
    • CPP4 (Collaborative Computational Project, Number 4)
    • CPP4 (Collaborative Computational Project, Number 4). (2003). An overview of the CCP4 project in protein crystallography: an example of a collaborative project. J. Synchrotron Radiat. 10, 23-25.
    • (2003) J. Synchrotron Radiat. , vol.10 , pp. 23-25
  • 13
    • 48449100887 scopus 로고    scopus 로고
    • KFC Server: Interactive forecasting of protein interaction hot spots
    • Darnell, S.J., LeGault, L., and Mitchell, J.C. (2008). KFC Server: interactive forecasting of protein interaction hot spots. Nucleic Acids Res. 36, W265-W269.
    • (2008) Nucleic Acids Res. , vol.36
    • Darnell, S.J.1    LeGault, L.2    Mitchell, J.C.3
  • 14
    • 0034687842 scopus 로고    scopus 로고
    • Structure-function analysis of the tobacco mosaic virus resistance gene N
    • Dinesh-Kumar, S.P., Tham, W.H., and Baker, B.J. (2000). Structure-function analysis of the tobacco mosaic virus resistance gene N. Proc. Natl. Acad. Sci. USA 97, 14789-14794.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 14789-14794
    • Dinesh-Kumar, S.P.1    Tham, W.H.2    Baker, B.J.3
  • 15
    • 77954763024 scopus 로고    scopus 로고
    • Plant immunity: Towards an integrated view of plant-pathogen interactions
    • Dodds, P.N., and Rathjen, J.P. (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
  • 16
    • 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
    • DOI 10.1105/tpc.13.1.163
    • Dodds, P.N., Lawrence, G.J., and Ellis, J.G. (2001). 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. (Pubitemid 32177041)
    • (2001) Plant Cell , vol.13 , Issue.1 , pp. 163-178
    • Dodds, P.N.1    Lawrence, G.J.2    Ellis, J.G.3
  • 17
    • 1542542334 scopus 로고    scopus 로고
    • The Melampsora lini AvrL567 avirulence genes are expressed in haustoria and their products are recognized inside plant cells
    • DOI 10.1105/tpc.020040
    • 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. (Pubitemid 38335284)
    • (2004) Plant Cell , vol.16 , Issue.3 , pp. 755-768
    • Dodds, P.N.1    Lawrence, G.J.2    Catanzariti, A.-M.3    Ayliffe, M.A.4    Ellis, J.G.5
  • 18
    • 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
  • 19
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: Multiple sequence alignment with high accuracy and high throughput
    • Edgar, R.C. (2004). MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res. 32, 1792-1797.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 20
    • 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
  • 21
  • 23
    • 1642311105 scopus 로고    scopus 로고
    • Tobacco transgenic for the flax rust resistance gene L expresses allele-specific activation of defense responses
    • Frost, D., Way, H., Howles, P., Luck, J., Manners, J., Hardham, A., Finnegan, J., and Ellis, J. (2004). Tobacco transgenic for the flax rust resistance gene L expresses allele-specific activation of defense responses. Mol. Plant Microbe Interact. 17, 224-232.
    • (2004) Mol. Plant Microbe Interact. , vol.17 , pp. 224-232
    • Frost, D.1    Way, H.2    Howles, P.3    Luck, J.4    Manners, J.5    Hardham, A.6    Finnegan, J.7    Ellis, J.8
  • 24
    • 0043123208 scopus 로고    scopus 로고
    • ESPript/ENDscript: Extracting and rendering sequence and 3D information from atomic structures of proteins
    • DOI 10.1093/nar/gkg556
    • Gouet, P., Robert, X., and Courcelle, E. (2003). ESPript/ENDscript: extracting and rendering sequence and 3D information from atomic structures of proteins. Nucleic Acids Res. 31, 3320-3323. (Pubitemid 37442149)
    • (2003) Nucleic Acids Research , vol.31 , Issue.13 , pp. 3320-3323
    • Gouet, P.1    Robert, X.2    Courcelle, E.3
  • 26
    • 17644366913 scopus 로고    scopus 로고
    • NOD-LRR proteins: Role in host-microbial interactions and inflammatory disease
    • Inohara, Chamaillard, McDonald, C., and Nunez, G. (2005). NOD-LRR proteins: role in host-microbial interactions and inflammatory disease. Annu. Rev. Biochem. 74, 355-383.
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 355-383
    • Inohara1    Chamaillard2    McDonald, C.3    Nunez, G.4
  • 27
    • 33751100626 scopus 로고    scopus 로고
    • The plant immune system
    • DOI 10.1038/nature05286, PII NATURE05286
    • Jones, J.D., and Dangl, J.L. (2006). The plant immune system. Nature 444, 323-329. (Pubitemid 44764102)
    • (2006) Nature , vol.444 , Issue.7117 , pp. 323-329
    • Jones, J.D.G.1    Dangl, J.L.2
  • 29
    • 3843055773 scopus 로고    scopus 로고
    • Crystal structure of the Toll/interleukin-1 receptor domain of human IL-1RAPL
    • Khan, J.A., Brint, E.K., O'Neill, L.A., and Tong, L. (2004). Crystal structure of the Toll/interleukin-1 receptor domain of human IL-1RAPL. J. Biol. Chem. 279, 31664-31670.
    • (2004) J. Biol. Chem. , vol.279 , pp. 31664-31670
    • Khan, J.A.1    Brint, E.K.2    O'Neill, L.A.3    Tong, L.4
  • 30
    • 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., and Wang, X. (2005). Formation of apoptosome is initiated by cytochrome c-induced dATP hydrolysis and subsequent nucleotide exchange on Apaf-1. Proc. Natl. Acad. Sci. USA 102, 17545-17550.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 17545-17550
    • Kim, H.E.1    Du, F.2    Fang, M.3    Wang, X.4
  • 32
    • 77956823972 scopus 로고    scopus 로고
    • Activation of an Arabidopsis resistance protein is specified by the in planta association of its leucine-rich repeat domain with the cognate oomycete effector
    • Krasileva, K.V., Dahlbeck, D., and Staskawicz, B.J. (2010). Activation of an Arabidopsis resistance protein is specified by the in planta association of its leucine-rich repeat domain with the cognate oomycete effector. Plant Cell 22, 1-15.
    • (2010) Plant Cell , vol.22 , pp. 1-15
    • Krasileva, K.V.1    Dahlbeck, D.2    Staskawicz, B.J.3
  • 33
    • 50249136103 scopus 로고    scopus 로고
    • Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7
    • Langer, G., Cohen, S.X., Lamzin, V.S., and Perrakis, A. (2008). Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7. Nat. Protoc. 3, 1171-1179.
    • (2008) Nat. Protoc. , vol.3 , pp. 1171-1179
    • Langer, G.1    Cohen, S.X.2    Lamzin, V.S.3    Perrakis, A.4
  • 34
    • 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
  • 35
    • 68149175128 scopus 로고    scopus 로고
    • STANDing strong, resistance proteins instigators of plant defence
    • Lukasik, E., and Takken, F.L. (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.2
  • 39
    • 33745455354 scopus 로고    scopus 로고
    • Elicitor-mediated oligomerization of the tobacco N disease resistance protein
    • DOI 10.1105/tpc.105.037234
    • Mestre, P., and Baulcombe, D.C. (2006). Elicitor-mediated oligomerization of the tobacco N disease resistance protein. Plant Cell 18, 491-501. (Pubitemid 43951308)
    • (2006) Plant Cell , vol.18 , Issue.2 , pp. 491-501
    • Mestre, P.1    Baulcombe, D.C.2
  • 40
    • 70350356853 scopus 로고    scopus 로고
    • Activating immunity: Lessons from the TLRs and NLRs
    • Monie, T.P., Bryant, C.E., and Gay, N.J. (2009). Activating immunity: lessons from the TLRs and NLRs. Trends Biochem. Sci. 34, 553-561.
    • (2009) Trends Biochem. Sci. , vol.34 , pp. 553-561
    • Monie, T.P.1    Bryant, C.E.2    Gay, N.J.3
  • 41
    • 45549086115 scopus 로고    scopus 로고
    • The crystal structure of the human toll-like receptor 10 cytoplasmic domain reveals a putative signaling dimer
    • Nyman, T., Stenmark, P., Flodin, S., Johansson, I., Hammarstrom, M., and Nordlund, P. (2008). The crystal structure of the human toll-like receptor 10 cytoplasmic domain reveals a putative signaling dimer. J. Biol. Chem. 283, 11861-11865.
    • (2008) J. Biol. Chem. , vol.283 , pp. 11861-11865
    • Nyman, T.1    Stenmark, P.2    Flodin, S.3    Johansson, I.4    Hammarstrom, M.5    Nordlund, P.6
  • 43
    • 58349093535 scopus 로고    scopus 로고
    • The leucine-rich repeat domain in plant innate immunity: A wealth of possibilities
    • Padmanabhan, M., Cournoyer, P., and Dinesh-Kumar, S.P. (2009). The leucine-rich repeat domain in plant innate immunity: a wealth of possibilities. Cell. Microbiol. 11, 191-198.
    • (2009) Cell. Microbiol. , vol.11 , pp. 191-198
    • Padmanabhan, M.1    Cournoyer, P.2    Dinesh-Kumar, S.P.3
  • 44
    • 36849045915 scopus 로고    scopus 로고
    • The inflammasome: A danger sensing complex triggering innate immunity
    • Petrilli, V., Dostert, C., Muruve, D.A., and Tschopp, J. (2007). The inflammasome: a danger sensing complex triggering innate immunity. Curr. Opin. Immunol. 19, 615-622.
    • (2007) Curr. Opin. Immunol. , vol.19 , pp. 615-622
    • Petrilli, V.1    Dostert, C.2    Muruve, D.A.3    Tschopp, J.4
  • 45
    • 77951881456 scopus 로고    scopus 로고
    • Crystal structure of the Caenorhabditis elegans apoptosome reveals an octameric assembly of CED-4
    • Qi, S., Pang, Y., Hu, Q., Liu, Q., Li, H., Zhou, Y., He, T., Liang, Q., Liu, Y., Yuan, X., et al. (2010). Crystal structure of the Caenorhabditis elegans apoptosome reveals an octameric assembly of CED-4. Cell 141, 446-457.
    • (2010) Cell , vol.141 , pp. 446-457
    • Qi, S.1    Pang, Y.2    Hu, Q.3    Liu, Q.4    Li, H.5    Zhou, Y.6    He, T.7    Liang, Q.8    Liu, Y.9    Yuan, X.10
  • 46
    • 70449625436 scopus 로고    scopus 로고
    • In the trenches of plant pathogen recognition: Role of NB-LRR proteins
    • Rafiqi, M., Bernoux, M., Ellis, J.G., and Dodds, P.N. (2009). In the trenches of plant pathogen recognition: role of NB-LRR proteins. Semin. Cell Dev. Biol. 20, 1017-1024.
    • (2009) Semin. Cell Dev. Biol. , vol.20 , pp. 1017-1024
    • Rafiqi, M.1    Bernoux, M.2    Ellis, J.G.3    Dodds, P.N.4
  • 47
    • 33747473700 scopus 로고    scopus 로고
    • Distinct domains in the ARC region of the potato resistance protein Rx mediate LRR binding and inhibition of activation
    • DOI 10.1105/tpc.106.042747
    • 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. (Pubitemid 44260198)
    • (2006) Plant Cell , vol.18 , Issue.8 , pp. 2082-2093
    • Rairdan, G.J.1    Moffett, P.2
  • 48
    • 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, G.J., Collier, S.M., Sacco, M.A., Baldwin, T.T., Boettrich, T., and 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
  • 49
    • 0242669338 scopus 로고    scopus 로고
    • Recognition specificity and RAR1/SGT1 dependence in barley Mla disease resistance genes to the powdery mildew fungus
    • DOI 10.1105/tpc.009258
    • 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. (Pubitemid 36339585)
    • (2003) Plant Cell , vol.15 , Issue.3 , pp. 732-744
    • Shen, Q.-H.1    Zhou, F.2    Bieri, S.3    Haizel, T.4    Shirasu, K.5    Schulze-Lefert, P.6
  • 50
    • 59749083228 scopus 로고    scopus 로고
    • The TIR domain of TIR-NB-LRR resistance proteins is a signaling domain involved in cell death induction
    • Swiderski, M.R., Birker, D., and Jones, J.D. (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
  • 51
    • 69949088965 scopus 로고    scopus 로고
    • Innate immune sensing and activation of cell surface Toll-like receptors
    • Tapping, R.I. (2009). Innate immune sensing and activation of cell surface Toll-like receptors. Semin. Immunol. 21, 175-184.
    • (2009) Semin. Immunol. , vol.21 , pp. 175-184
    • Tapping, R.I.1
  • 52
    • 77954294794 scopus 로고    scopus 로고
    • HotPoint: Hot spot prediction server for protein interfaces
    • Tuncbag, N., Keskin, O., and Gursoy, A. (2010). HotPoint: hot spot prediction server for protein interfaces. Nucleic Acids Res. Suppl. 38, W402-W406.
    • (2010) Nucleic Acids Res. Suppl. , vol.38
    • Tuncbag, N.1    Keskin, O.2    Gursoy, A.3
  • 53
    • 0032422882 scopus 로고    scopus 로고
    • Plant disease-resistance proteins and the gene-for-gene concept
    • Van der Biezen, E.A., and Jones, J.D. (1998). Plant disease-resistance proteins and the gene-for-gene concept. Trends Biochem. Sci. 23, 454-456.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 454-456
    • Van Der Biezen, E.A.1    Jones, J.D.2
  • 54
    • 45549084403 scopus 로고    scopus 로고
    • Structure-function analysis of the NB-ARC domain of plant disease resistance proteins
    • van Ooijen, G., Mayr, G., Kasiem, M.M., Albrecht, M., Cornelissen, B.J., and Takken, F.L. (2008). Structure-function analysis of the NB-ARC domain of plant disease resistance proteins. J. Exp. Bot. 59, 1383-1397.
    • (2008) J. Exp. Bot. , vol.59 , pp. 1383-1397
    • Van Ooijen, G.1    Mayr, G.2    Kasiem, M.M.3    Albrecht, M.4    Cornelissen, B.J.5    Takken, F.L.6
  • 55
    • 79951480917 scopus 로고    scopus 로고
    • Crystallization, X-ray diffraction analysis, and preliminary structure determination of the TIR domain from the flax resistance protein L6
    • Ve, T., Williams, S., Valkov, E., Ellis, J.G., Dodds, P.N., and Kobe, B. (2011). Crystallization, X-ray diffraction analysis, and preliminary structure determination of the TIR domain from the flax resistance protein L6. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 67, 237-240.
    • (2011) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. , vol.67 , pp. 237-240
    • Ve, T.1    Williams, S.2    Valkov, E.3    Ellis, J.G.4    Dodds, P.N.5    Kobe, B.6
  • 57
    • 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
    • DOI 10.1111/j.1365-313X.2006.02834.x
    • Weaver, L.M., Swiderski, M.R., Li, Y., and 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 J. 47, 829-840. (Pubitemid 44326433)
    • (2006) Plant Journal , vol.47 , Issue.6 , pp. 829-840
    • Michael, W.L.1    Swiderski, M.R.2    Li, Y.3    Jones, J.D.G.4
  • 58
    • 0030571043 scopus 로고    scopus 로고
    • Size-exclusion chromatography with on-line light-scattering, absorbance, and refractive index detectors for studying proteins and their interactions
    • Wen, J., Arakawa, T., and Philo, J.S. (1996). Size-exclusion chromatography with on-line light-scattering, absorbance, and refractive index detectors for studying proteins and their interactions. Anal. Biochem. 240, 155-166.
    • (1996) Anal. Biochem. , vol.240 , pp. 155-166
    • Wen, J.1    Arakawa, T.2    Philo, J.S.3
  • 59
    • 0027931646 scopus 로고
    • The product of the tobacco mosaic virus resistance gene N: Similarity to toll and the interleukin-1 receptor
    • DOI 10.1016/0092-8674(94)90283-6
    • Whitham, S., Dinesh-Kumar, S.P., Choi, D., Hehl, R., Corr, C., and Baker, B. (1994). The product of the tobacco mosaic virus resistance gene N: similarity to toll and the interleukin-1 receptor. Cell 78, 1101-1115. (Pubitemid 24292336)
    • (1994) Cell , vol.78 , Issue.6 , pp. 1101-1115
    • Whitham, S.1    Dinesh-Kumar, S.P.2    Choi, D.3    Hehl, R.4    Corr, C.5    Baker, B.6
  • 60
    • 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., and Tong, L. (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    Tong, L.7
  • 61
    • 27644483812 scopus 로고    scopus 로고
    • A structure of the human apoptosome at 12.8 A resolution provides insights into this cell death platform
    • DOI 10.1016/j.str.2005.09.006, PII S0969212605003497
    • Yu, X., Acehan, D., Menetret, J.F., Booth, C.R., Ludtke, S.J., Riedl, S.J., Shi, Y., Wang, X., and Akey, C.W. (2005). A structure of the human apoptosome at 12.8 A resolution provides insights into this cell death platform. Structure 13, 1725-1735. (Pubitemid 41571836)
    • (2005) Structure , vol.13 , Issue.11 , pp. 1725-1735
    • Yu, X.1    Acehan, D.2    Menetret, J.-F.3    Booth, C.R.4    Ludtke, S.J.5    Riedl, S.J.6    Shi, Y.7    Wang, X.8    Akey, C.W.9
  • 62
    • 77952652352 scopus 로고    scopus 로고
    • Structure of an apoptosome-procaspase-9 CARD complex
    • Yuan, S., Yu, X., Topf, M., Ludtke, S.J., Wang, X., and Akey, C.W. (2010). Structure of an apoptosome-procaspase-9 CARD complex. Structure 18, 571-583.
    • (2010) Structure , vol.18 , pp. 571-583
    • Yuan, S.1    Yu, X.2    Topf, M.3    Ludtke, S.J.4    Wang, X.5    Akey, C.W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.