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Volumn 6, Issue 9, 2008, Pages 1910-1926

Correction: Rice XB15, a protein phosphatase 2C, negatively regulates cell death and XA21-mediated innate immunity (Plos Biology (2008) 6, 9, (e231) DOI: 10.1371/journal.pbio.0060231);Rice XB15, a protein phosphatase 2C, negatively regulates cell death and XA21-mediated innate immunity

Author keywords

[No Author keywords available]

Indexed keywords

HYBRID PROTEIN; PHOSPHOPROTEIN PHOSPHATASE; PHOSPHOPROTEIN PHOSPHATASE 2C; PROTEIN XA21; PROTEIN XB15; UNCLASSIFIED DRUG; VEGETABLE PROTEIN; PROTEIN SERINE THREONINE KINASE; XA21 PROTEIN, ORYZA SATIVA;

EID: 54749114874     PISSN: 15449173     EISSN: 15457885     Source Type: Journal    
DOI: 10.1371/journal.pbio.0060282     Document Type: Erratum
Times cited : (172)

References (102)
  • 1
    • 26844558577 scopus 로고    scopus 로고
    • Sending the right signals: Regulating receptor kinase activity
    • Johnson KL, Ingram GC (2005) Sending the right signals: regulating receptor kinase activity. Curr Opin Plant Biol 8: 648-656.
    • (2005) Curr Opin Plant Biol , vol.8 , pp. 648-656
    • Johnson, K.L.1    Ingram, G.C.2
  • 2
    • 0029993727 scopus 로고    scopus 로고
    • Active and inactive protein kinases: Structural basis for regulation
    • Johnson LN, Noble ME, Owen DJ (1996) Active and inactive protein kinases: structural basis for regulation. Cell 85: 149-158.
    • (1996) Cell , vol.85 , pp. 149-158
    • Johnson, L.N.1    Noble, M.E.2    Owen, D.J.3
  • 3
    • 0033827884 scopus 로고    scopus 로고
    • Receptor kinase activation and signal transduction in plants: An emerging picture
    • Torii KU (2000) Receptor kinase activation and signal transduction in plants: an emerging picture. Curr Opin Plant Biol 3: 361-367.
    • (2000) Curr Opin Plant Biol , vol.3 , pp. 361-367
    • Torii, K.U.1
  • 4
    • 1642463788 scopus 로고    scopus 로고
    • Innate immunity in plants and animals: Striking similarities and obvious differences
    • Nurnberger T, Brunner F, Kemmerling B, 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
  • 5
    • 0036775463 scopus 로고    scopus 로고
    • IRAK-4 as the central TIR signaling mediator in innate immunity
    • Suzuki N, Suzuki S, Yeh WC (2002) IRAK-4 as the central TIR signaling mediator in innate immunity. Trends Immunol 23: 503-506.
    • (2002) Trends Immunol , vol.23 , pp. 503-506
    • Suzuki, N.1    Suzuki, S.2    Yeh, W.C.3
  • 6
    • 0036017858 scopus 로고    scopus 로고
    • Innate immunity in plants and animals: Emerging parallels between the recognition of general elicitors and pathogen-associated molecular patterns
    • Nurnberger T, Brunner F (2002) Innate immunity in plants and animals: emerging parallels between the recognition of general elicitors and pathogen-associated molecular patterns. Curr Opin Plant Biol 5: 318-324.
    • (2002) Curr Opin Plant Biol , vol.5 , pp. 318-324
    • Nurnberger, T.1    Brunner, F.2
  • 7
    • 3142724031 scopus 로고    scopus 로고
    • Toll-like receptor signalling
    • Akira S, Takeda K (2004) Toll-like receptor signalling. Nat Rev Immunol 4: 499-511.
    • (2004) Nat Rev Immunol , vol.4 , pp. 499-511
    • Akira, S.1    Takeda, K.2
  • 8
    • 2442642691 scopus 로고    scopus 로고
    • RIP1 is an essential mediator of Toll-like receptor 3-induced NF-kappa B activation
    • Meylan E, Burns K, Hofmann K, Blancheteau V, Martinon F, et al. (2004) RIP1 is an essential mediator of Toll-like receptor 3-induced NF-kappa B activation. Nat Immunol 5: 503-507.
    • (2004) Nat Immunol , vol.5 , pp. 503-507
    • Meylan, E.1    Burns, K.2    Hofmann, K.3    Blancheteau, V.4    Martinon, F.5
  • 9
    • 27144540463 scopus 로고    scopus 로고
    • Are innate immune signaling pathways in plants and animals conserved?
    • Ausubel FM (2005) Are innate immune signaling pathways in plants and animals conserved? Nat Immunol 6: 973-979.
    • (2005) Nat Immunol , vol.6 , pp. 973-979
    • Ausubel, F.M.1
  • 10
    • 33645776778 scopus 로고    scopus 로고
    • Plant and animal pathogen recognition receptors signal through non-RD kinases
    • doi:10.1371/journal. ppat.0020002
    • Dardick C, Ronald P (2006) Plant and animal pathogen recognition receptors signal through non-RD kinases. PLoS Pathog 2: e2. doi:10.1371/journal. ppat.0020002
    • (2006) PLoS Pathog , vol.2
    • Dardick, C.1    Ronald, P.2
  • 11
    • 0032560489 scopus 로고    scopus 로고
    • The Eleventh Datta Lecture. The structural basis for substrate recognition and control by protein kinases
    • Johnson LN, Lowe ED, Noble ME, Owen DJ (1998) The Eleventh Datta Lecture. The structural basis for substrate recognition and control by protein kinases. FEBS Lett 430: 1-11.
    • (1998) FEBS Lett , vol.430 , pp. 1-11
    • Johnson, L.N.1    Lowe, E.D.2    Noble, M.E.3    Owen, D.J.4
  • 12
    • 0035956425 scopus 로고    scopus 로고
    • Evolutionary perspective on innate immune recognition
    • Mushegian A, Medzhitov R (2001) Evolutionary perspective on innate immune recognition. J Cell Biol 155: 705-710.
    • (2001) J Cell Biol , vol.155 , pp. 705-710
    • Mushegian, A.1    Medzhitov, R.2
  • 13
    • 2442591728 scopus 로고    scopus 로고
    • Comparative analysis of the receptor-like kinase family in Arabidopsis and rice
    • Shiu SH, Karlowski WM, Pan R, Tzeng YH, Mayer KF, et al. (2004) Comparative analysis of the receptor-like kinase family in Arabidopsis and rice. Plant Cell 16: 1220-1234.
    • (2004) Plant Cell , vol.16 , pp. 1220-1234
    • Shiu, S.H.1    Karlowski, W.M.2    Pan, R.3    Tzeng, Y.H.4    Mayer, K.F.5
  • 14
    • 33747872039 scopus 로고    scopus 로고
    • Functional analysis of receptor-like kinases in monocots and dicots
    • Morillo SA, Tax FE (2006) Functional analysis of receptor-like kinases in monocots and dicots. Curr Opin Plant Biol 9: 460-469.
    • (2006) Curr Opin Plant Biol , vol.9 , pp. 460-469
    • Morillo, S.A.1    Tax, F.E.2
  • 15
    • 0033634664 scopus 로고    scopus 로고
    • FLS2: An LRR receptor-like kinase involved in the perception of the bacterial elicitor flagellin in Arabidopsis
    • Gomez-Gomez L, Boller T (2000) FLS2: an LRR receptor-like kinase involved in the perception of the bacterial elicitor flagellin in Arabidopsis. Mol Cell 5: 1003-1011.
    • (2000) Mol Cell , vol.5 , pp. 1003-1011
    • Gomez-Gomez, L.1    Boller, T.2
  • 16
    • 33646525169 scopus 로고    scopus 로고
    • Perception of the bacterial PAMP EF-Tu by the receptor EFR restricts Agrobacterium-mediated transformation
    • Zipfel C, Kunze G, Chinchilla D, Caniard A, Jones JD, et al. (2006) Perception of the bacterial PAMP EF-Tu by the receptor EFR restricts Agrobacterium-mediated transformation. Cell 125: 749-760.
    • (2006) Cell , vol.125 , pp. 749-760
    • Zipfel, C.1    Kunze, G.2    Chinchilla, D.3    Caniard, A.4    Jones, J.D.5
  • 17
    • 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, et al. (2006) A B-lectin receptor kinase gene conferring rice blast resistance. Plant J 46: 794-804.
    • (2006) Plant J , vol.46 , pp. 794-804
    • Chen, X.1    Shang, J.2    Chen, D.3    Lei, C.4    Zou, Y.5
  • 18
    • 0007263597 scopus 로고
    • A receptor kinase-like protein encoded by the rice disease resistance gene, Xa21
    • Song WY, Wang GL, Chen LL, Kim HS, Pi LY, et al. (1995) A receptor kinase-like protein encoded by the rice disease resistance gene, Xa21. Science 270: 1804-1806.
    • (1995) Science , vol.270 , pp. 1804-1806
    • Song, W.Y.1    Wang, G.L.2    Chen, L.L.3    Kim, H.S.4    Pi, L.Y.5
  • 19
    • 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, et al. (2004) Xa26, a gene conferring resistance to Xanthomonas oryzae pv. oryzae in rice, encodes an LRR receptor kinase-like protein. Plant J 37: 517-527.
    • (2004) Plant J , vol.37 , pp. 517-527
    • Sun, X.1    Cao, Y.2    Yang, Z.3    Xu, C.4    Li, X.5
  • 20
    • 33845512033 scopus 로고    scopus 로고
    • From the Academy: Colloquium review. Unique characteristics of Xanthomonas oryzae pv. oryzae AvrXa21 and implications for plant innate immunity
    • Lee SW, Han SW, Bartley LE, Ronald PC (2006) From the Academy: Colloquium review. Unique characteristics of Xanthomonas oryzae pv. oryzae AvrXa21 and implications for plant innate immunity. Proc Natl Acad Sci U S A 103: 18395-18400.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 18395-18400
    • Lee, S.W.1    Han, S.W.2    Bartley, L.E.3    Ronald, P.C.4
  • 21
    • 0037066461 scopus 로고    scopus 로고
    • Recognition and rejection of self in plant reproduction
    • Nasrallah JB (2002) Recognition and rejection of self in plant reproduction. Science 296: 305-308.
    • (2002) Science , vol.296 , pp. 305-308
    • Nasrallah, J.B.1
  • 22
    • 0037469146 scopus 로고    scopus 로고
    • Activation loop phosphorylation and catalysis in protein kinases: Is there functional evidence for the autoinhibitor model?
    • Adams JA (2003) Activation loop phosphorylation and catalysis in protein kinases: is there functional evidence for the autoinhibitor model? Biochemistry 42: 601-607.
    • (2003) Biochemistry , vol.42 , pp. 601-607
    • Adams, J.A.1
  • 23
    • 0842346438 scopus 로고    scopus 로고
    • Specificity in signal transduction: From phosphotyrosine-SH2 domain interactions to complex cellular systems
    • Pawson T (2004) Specificity in signal transduction: from phosphotyrosine-SH2 domain interactions to complex cellular systems. Cell 116: 191-203.
    • (2004) Cell , vol.116 , pp. 191-203
    • Pawson, T.1
  • 24
    • 34548436187 scopus 로고    scopus 로고
    • The negative regulation of Toll-like receptor and associated pathways
    • Lang T, Mansell A (2007) The negative regulation of Toll-like receptor and associated pathways. Immunol Cell Biol 85: 425-434.
    • (2007) Immunol Cell Biol , vol.85 , pp. 425-434
    • Lang, T.1    Mansell, A.2
  • 26
    • 20644450804 scopus 로고    scopus 로고
    • Negative regulation of toll-like receptor-mediated immune responses
    • Liew FY, Xu D, Brint EK, O'Neill LA (2005) Negative regulation of toll-like receptor-mediated immune responses. Nat Rev Immunol 5: 446-458.
    • (2005) Nat Rev Immunol , vol.5 , pp. 446-458
    • Liew, F.Y.1    Xu, D.2    Brint, E.K.3    O'Neill, L.A.4
  • 27
    • 33847176551 scopus 로고    scopus 로고
    • MAPK phosphatases-regulating the immune response
    • Liu Y, Shepherd EG, Nelin LD (2007) MAPK phosphatases-regulating the immune response. Nat Rev Immunol 7: 202-212.
    • (2007) Nat Rev Immunol , vol.7 , pp. 202-212
    • Liu, Y.1    Shepherd, E.G.2    Nelin, L.D.3
  • 28
    • 2442602365 scopus 로고    scopus 로고
    • Plant PP2C phosphatases: Emerging functions in stress signaling
    • Schweighofer A, Hirt H, Meskiene I (2004) Plant PP2C phosphatases: emerging functions in stress signaling. Trends Plant Sci 9: 236-243.
    • (2004) Trends Plant Sci , vol.9 , pp. 236-243
    • Schweighofer, A.1    Hirt, H.2    Meskiene, I.3
  • 29
    • 34249665604 scopus 로고    scopus 로고
    • Regulation of innate immune response by MAP kinase phosphatase-1
    • Wang X, Liu Y (2007) Regulation of innate immune response by MAP kinase phosphatase-1. Cell Signal 19: 1372-1382.
    • (2007) Cell Signal , vol.19 , pp. 1372-1382
    • Wang, X.1    Liu, Y.2
  • 30
    • 0024397415 scopus 로고
    • The structure and regulation of protein phosphatases
    • Cohen P (1989) The structure and regulation of protein phosphatases. Annu Rev Biochem 58: 453-508.
    • (1989) Annu Rev Biochem , vol.58 , pp. 453-508
    • Cohen, P.1
  • 31
    • 0031193654 scopus 로고    scopus 로고
    • Interaction of the maize and Arabidopsis kinase interaction domains with a subset of receptor-like protein kinases: Implications for transmembrane signaling in plants
    • Braun DM, Stone JM, Walker JC (1997) Interaction of the maize and Arabidopsis kinase interaction domains with a subset of receptor-like protein kinases: implications for transmembrane signaling in plants. Plant J 12: 83-95.
    • (1997) Plant J , vol.12 , pp. 83-95
    • Braun, D.M.1    Stone, J.M.2    Walker, J.C.3
  • 32
    • 33947198632 scopus 로고    scopus 로고
    • Phosphoprotein and phosphopeptide interactions with the FHA domain from Arabidopsis kinase-associated protein phosphatase
    • Ding Z, Wang H, Liang X, Morris ER, Gallazzi F, et al. (2007) Phosphoprotein and phosphopeptide interactions with the FHA domain from Arabidopsis kinase-associated protein phosphatase. Biochemistry 46: 2684-2696.
    • (2007) Biochemistry , vol.46 , pp. 2684-2696
    • Ding, Z.1    Wang, H.2    Liang, X.3    Morris, E.R.4    Gallazzi, F.5
  • 33
    • 0035006480 scopus 로고    scopus 로고
    • Both the extracellular leucine-rich repeat domain and the kinase activity of FSL2 are required for flagellin binding and signaling in Arabidopsis
    • Gomez-Gomez L, Bauer Z, Boller T (2001) Both the extracellular leucine-rich repeat domain and the kinase activity of FSL2 are required for flagellin binding and signaling in Arabidopsis. Plant Cell 13: 1155-1163.
    • (2001) Plant Cell , vol.13 , pp. 1155-1163
    • Gomez-Gomez, L.1    Bauer, Z.2    Boller, T.3
  • 34
    • 0036644983 scopus 로고    scopus 로고
    • The Arabidopsis kinase-associated protein phosphatase controls internalization of the somatic embryogenesis receptor kinase 1
    • Shah K, Russinova E, Gadella TW Jr., Willemse J, De Vries SC (2002) The Arabidopsis kinase-associated protein phosphatase controls internalization of the somatic embryogenesis receptor kinase 1. Genes Dev 16: 1707-1720.
    • (2002) Genes Dev , vol.16 , pp. 1707-1720
    • Shah, K.1    Russinova, E.2    Gadella Jr., T.W.3    Willemse, J.4    De Vries, S.C.5
  • 35
    • 0001096266 scopus 로고    scopus 로고
    • Control of meristem development by CLAVATA1 receptor kinase and kinase-associated protein phosphatase interactions
    • Stone JM, Trotochaud AE, Walker JC, Clark SE (1998) Control of meristem development by CLAVATA1 receptor kinase and kinase-associated protein phosphatase interactions. Plant Physiol 117: 1217-1225.
    • (1998) Plant Physiol , vol.117 , pp. 1217-1225
    • Stone, J.M.1    Trotochaud, A.E.2    Walker, J.C.3    Clark, S.E.4
  • 36
    • 0030930384 scopus 로고    scopus 로고
    • A possible role for kinase-associated protein phosphatase in the Arabidopsis CLAVATA1 signaling pathway
    • Williams RW, Wilson JM, Meyerowitz EM (1997) A possible role for kinase-associated protein phosphatase in the Arabidopsis CLAVATA1 signaling pathway. Proc Natl Acad Sci U S A 94: 10467-10472.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 10467-10472
    • Williams, R.W.1    Wilson, J.M.2    Meyerowitz, E.M.3
  • 37
    • 0028075896 scopus 로고
    • Interaction of a protein phosphatase with an Arabidopsis serine-threonine receptor kinase
    • Stone JM, Collinge MA, Smith RD, Horn MA, Walker JC (1994) Interaction of a protein phosphatase with an Arabidopsis serine-threonine receptor kinase. Science 266: 793-795.
    • (1994) Science , vol.266 , pp. 793-795
    • Stone, J.M.1    Collinge, M.A.2    Smith, R.D.3    Horn, M.A.4    Walker, J.C.5
  • 38
    • 0033101715 scopus 로고    scopus 로고
    • The CLAVATA1 receptor-like kinase requires CLAVATA3 for its assembly into a signaling complex that includes KAPP and a Rho-related protein
    • Trotochaud AE, Hao T, Wu G, Yang Z, Clark SE (1999) The CLAVATA1 receptor-like kinase requires CLAVATA3 for its assembly into a signaling complex that includes KAPP and a Rho-related protein. Plant Cell 11: 393-406.
    • (1999) Plant Cell , vol.11 , pp. 393-406
    • Trotochaud, A.E.1    Hao, T.2    Wu, G.3    Yang, Z.4    Clark, S.E.5
  • 39
    • 0033150292 scopus 로고    scopus 로고
    • Expression of a gibberellin-induced leucine-rich repeat receptor-like protein kinase in deepwater rice and its interaction with kinase-associated protein phosphatase
    • van der Knaap E, Song WY, Ruan DL, Sauter M, Ronald PC, et al. (1999) Expression of a gibberellin-induced leucine-rich repeat receptor-like protein kinase in deepwater rice and its interaction with kinase-associated protein phosphatase. Plant Physiol 120: 559-570.
    • (1999) Plant Physiol , vol.120 , pp. 559-570
    • van der Knaap, E.1    Song, W.Y.2    Ruan, D.L.3    Sauter, M.4    Ronald, P.C.5
  • 40
    • 0026677213 scopus 로고
    • Genetic and physical analysis of the rice bacterial blight disease resistance locus, Xa21
    • Ronald PC, Albano B, Tabien R, Abenes L, Wu KS, et al. (1992) Genetic and physical analysis of the rice bacterial blight disease resistance locus, Xa21. Mol Gen Genet 236: 113-120.
    • (1992) Mol Gen Genet , vol.236 , pp. 113-120
    • Ronald, P.C.1    Albano, B.2    Tabien, R.3    Abenes, L.4    Wu, K.S.5
  • 41
    • 63549104452 scopus 로고    scopus 로고
    • Xb10 encodes a WRKY transcription factor that mediates XA21 resistance
    • Peng Y, Bartley LE, Chen X, Dardick C, Chern M, et al. (2008) Xb10 encodes a WRKY transcription factor that mediates XA21 resistance. Mol Plant 1: 446-458.
    • (2008) Mol Plant , vol.1 , pp. 446-458
    • Peng, Y.1    Bartley, L.E.2    Chen, X.3    Dardick, C.4    Chern, M.5
  • 42
    • 33947504480 scopus 로고    scopus 로고
    • Rice XA21 binding protein 3 is a ubiquitin ligase required for full Xa21-mediated disease resistance
    • Wang YS, Pi LY, Chen X, Chakrabarty PK, Jiang J, et al. (2006) Rice XA21 binding protein 3 is a ubiquitin ligase required for full Xa21-mediated disease resistance. Plant Cell 18: 3635-3646.
    • (2006) Plant Cell , vol.18 , pp. 3635-3646
    • Wang, Y.S.1    Pi, L.Y.2    Chen, X.3    Chakrabarty, P.K.4    Jiang, J.5
  • 43
    • 0037036381 scopus 로고    scopus 로고
    • Biochemical characterization of the kinase domain of the rice disease resistance receptor-like kinase XA21
    • Liu GZ, Pi LY, Walker JC, Ronald PC, Song WY (2002) Biochemical characterization of the kinase domain of the rice disease resistance receptor-like kinase XA21. J Biol Chem 277: 20264-20269.
    • (2002) J Biol Chem , vol.277 , pp. 20264-20269
    • Liu, G.Z.1    Pi, L.Y.2    Walker, J.C.3    Ronald, P.C.4    Song, W.Y.5
  • 44
    • 33644872221 scopus 로고    scopus 로고
    • The autophosphorylated Ser686, Thr688, and Ser689 residues in the intracellular juxtamembrane domain of XA21 are implicated in stability control of rice receptor-like kinase
    • Xu WH, Wang YS, Liu GZ, Chen X, Tinjuangjun P, et al. (2006) The autophosphorylated Ser686, Thr688, and Ser689 residues in the intracellular juxtamembrane domain of XA21 are implicated in stability control of rice receptor-like kinase. Plant J 45: 740-751.
    • (2006) Plant J , vol.45 , pp. 740-751
    • Xu, W.H.1    Wang, Y.S.2    Liu, G.Z.3    Chen, X.4    Tinjuangjun, P.5
  • 45
    • 0030296869 scopus 로고    scopus 로고
    • Molecular mechanisms of the protein serine/threonine phosphatases
    • Barford D (1996) Molecular mechanisms of the protein serine/threonine phosphatases. Trends Biochem Sci 21: 407-412.
    • (1996) Trends Biochem Sci , vol.21 , pp. 407-412
    • Barford, D.1
  • 46
    • 0030465532 scopus 로고    scopus 로고
    • Crystal structure of the protein serine/threonine phosphatase 2C at 2.0 A resolution
    • Das AK, Helps NR, Cohen PT, Barford D (1996) Crystal structure of the protein serine/threonine phosphatase 2C at 2.0 A resolution. Embo J 15: 6798-6809.
    • (1996) Embo J , vol.15 , pp. 6798-6809
    • Das, A.K.1    Helps, N.R.2    Cohen, P.T.3    Barford, D.4
  • 47
    • 0037314247 scopus 로고    scopus 로고
    • POLTERGEIST encodes a protein phosphatase 2C that regulates CLAVATA pathways controlling stem cell identity at Arabidopsis shoot and flower meristems
    • Yu LP, Miller AK, Clark SE (2003) POLTERGEIST encodes a protein phosphatase 2C that regulates CLAVATA pathways controlling stem cell identity at Arabidopsis shoot and flower meristems. Curr Biol 13: 179-188.
    • (2003) Curr Biol , vol.13 , pp. 179-188
    • Yu, L.P.1    Miller, A.K.2    Clark, S.E.3
  • 48
    • 24144456964 scopus 로고    scopus 로고
    • POL and related phosphatases are dosage-sensitive regulators of meristem and organ development in Arabidopsis
    • Song SK, Clark SE (2005) POL and related phosphatases are dosage-sensitive regulators of meristem and organ development in Arabidopsis. Dev Biol 285: 272-284.
    • (2005) Dev Biol , vol.285 , pp. 272-284
    • Song, S.K.1    Clark, S.E.2
  • 49
    • 0034107779 scopus 로고    scopus 로고
    • POLTERGEIST functions to regulate meristem development downstream of the CLAVATA loci
    • Yu LP, Simon EJ, Trotochaud AE, Clark SE (2000) POLTERGEIST functions to regulate meristem development downstream of the CLAVATA loci. Development 127: 1661-1670.
    • (2000) Development , vol.127 , pp. 1661-1670
    • Yu, L.P.1    Simon, E.J.2    Trotochaud, A.E.3    Clark, S.E.4
  • 50
    • 33846054841 scopus 로고    scopus 로고
    • POL and PLL1 phosphatases are CLAVATA1 signaling intermediates required for Arabidopsis shoot and floral stem cells
    • Song SK, Lee MM, Clark SE (2006) POL and PLL1 phosphatases are CLAVATA1 signaling intermediates required for Arabidopsis shoot and floral stem cells. Development 133: 4691-4698.
    • (2006) Development , vol.133 , pp. 4691-4698
    • Song, S.K.1    Lee, M.M.2    Clark, S.E.3
  • 51
    • 1842430185 scopus 로고    scopus 로고
    • Improved tandem affinity purification tag and methods for isolation of protein heterocomplexes from plants
    • Rohila JS, Chen M, Cerny R, Fromm ME (2004) Improved tandem affinity purification tag and methods for isolation of protein heterocomplexes from plants. Plant J 38: 172-181.
    • (2004) Plant J , vol.38 , pp. 172-181
    • Rohila, J.S.1    Chen, M.2    Cerny, R.3    Fromm, M.E.4
  • 52
    • 33646831324 scopus 로고    scopus 로고
    • Protein-protein interactions of tandem affinity purification-tagged protein kinases in rice
    • Rohila JS, Chen M, Chen S, Chen J, Cerny R, et al. (2006) Protein-protein interactions of tandem affinity purification-tagged protein kinases in rice. Plant J 46: 1-13.
    • (2006) Plant J , vol.46 , pp. 1-13
    • Rohila, J.S.1    Chen, M.2    Chen, S.3    Chen, J.4    Cerny, R.5
  • 53
    • 27144453303 scopus 로고    scopus 로고
    • Rice NRR, a negative regulator of disease resistance, interacts with Arabidopsis NPR1 and rice NH1
    • Chern M, Canlas PE, Fitzgerald HA, Ronald PC (2005) Rice NRR, a negative regulator of disease resistance, interacts with Arabidopsis NPR1 and rice NH1. Plant J 43: 623-635.
    • (2005) Plant J , vol.43 , pp. 623-635
    • Chern, M.1    Canlas, P.E.2    Fitzgerald, H.A.3    Ronald, P.C.4
  • 54
    • 0034885293 scopus 로고    scopus 로고
    • Evidence for a disease-resistance pathway in rice similar to the NPR1-mediated signaling pathway in Arabidopsis
    • Chern MS, Fitzgerald HA, Yadav RC, Canlas PE, Dong X, et al. (2001) Evidence for a disease-resistance pathway in rice similar to the NPR1-mediated signaling pathway in Arabidopsis. Plant J 27: 101-113.
    • (2001) Plant J , vol.27 , pp. 101-113
    • Chern, M.S.1    Fitzgerald, H.A.2    Yadav, R.C.3    Canlas, P.E.4    Dong, X.5
  • 55
    • 0041419305 scopus 로고    scopus 로고
    • Target site specificity of the Tos17 retrotransposon shows a preference for insertion within genes and against insertion in retrotransposon-rich regions of the genome
    • Miyao A, Tanaka K, Murata K, Sawaki H, Takeda S, et al. (2003) Target site specificity of the Tos17 retrotransposon shows a preference for insertion within genes and against insertion in retrotransposon-rich regions of the genome. Plant Cell 15: 1771-1780.
    • (2003) Plant Cell , vol.15 , pp. 1771-1780
    • Miyao, A.1    Tanaka, K.2    Murata, K.3    Sawaki, H.4    Takeda, S.5
  • 56
    • 0033203409 scopus 로고    scopus 로고
    • Short communication: Developmental control of Xa21-mediated disease resistance in rice
    • Century KS, Lagman RA, Adkisson M, Morlan J, Tobias R, et al. (1999) Short communication: developmental control of Xa21-mediated disease resistance in rice. Plant J 20: 231-236.
    • (1999) Plant J , vol.20 , pp. 231-236
    • Century, K.S.1    Lagman, R.A.2    Adkisson, M.3    Morlan, J.4    Tobias, R.5
  • 57
    • 1842787809 scopus 로고    scopus 로고
    • Expression of plant protein phosphatase 2C interferes with nuclear import of the Agrobacterium T-complex protein VirD2
    • Tao Y, Rao PK, Bhattacharjee S, Gelvin SB (2004) Expression of plant protein phosphatase 2C interferes with nuclear import of the Agrobacterium T-complex protein VirD2. Proc Natl Acad Sci U S A 101: 5164-5169.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 5164-5169
    • Tao, Y.1    Rao, P.K.2    Bhattacharjee, S.3    Gelvin, S.B.4
  • 58
    • 34250155598 scopus 로고    scopus 로고
    • Tandem affinity purification of functional TAP-tagged proteins from human cells
    • Gregan J, Riedel CG, Petronczki M, Cipak L, Rumpf C, et al. (2007) Tandem affinity purification of functional TAP-tagged proteins from human cells. Nat Protoc 2: 1145-1151.
    • (2007) Nat Protoc , vol.2 , pp. 1145-1151
    • Gregan, J.1    Riedel, C.G.2    Petronczki, M.3    Cipak, L.4    Rumpf, C.5
  • 59
    • 33947730844 scopus 로고    scopus 로고
    • Identifying functional modules in the physical interactome of Saccharomyces cerevisiae
    • Pu S, Vlasblom J, Emili A, Greenblatt J, Wodak SJ (2007) Identifying functional modules in the physical interactome of Saccharomyces cerevisiae. Proteomics 7: 944-960.
    • (2007) Proteomics , vol.7 , pp. 944-960
    • Pu, S.1    Vlasblom, J.2    Emili, A.3    Greenblatt, J.4    Wodak, S.J.5
  • 60
    • 33646861792 scopus 로고    scopus 로고
    • MultiLoc: Prediction of protein subcellular localization using N-terminal targeting sequences, sequence motifs and amino acid composition
    • Hoglund A, Donnes P, Blum T, Adolph HW, Kohlbacher O (2006) MultiLoc: prediction of protein subcellular localization using N-terminal targeting sequences, sequence motifs and amino acid composition. Bioinformatics 22: 1158-1165.
    • (2006) Bioinformatics , vol.22 , pp. 1158-1165
    • Hoglund, A.1    Donnes, P.2    Blum, T.3    Adolph, H.W.4    Kohlbacher, O.5
  • 61
    • 0032972509 scopus 로고    scopus 로고
    • PSORT: A program for detecting sorting signals in proteins and predicting their subcellular localization
    • Nakai K, Horton P (1999) PSORT: a program for detecting sorting signals in proteins and predicting their subcellular localization. Trends Biochem Sci 24: 34-36.
    • (1999) Trends Biochem Sci , vol.24 , pp. 34-36
    • Nakai, K.1    Horton, P.2
  • 62
    • 0032030760 scopus 로고    scopus 로고
    • Soluble, highly fluorescent variants of green fluorescent protein (GFP) for use in higher plants
    • Davis SJ, Vierstra RD (1998) Soluble, highly fluorescent variants of green fluorescent protein (GFP) for use in higher plants. Plant Mol Biol 36: 521-528.
    • (1998) Plant Mol Biol , vol.36 , pp. 521-528
    • Davis, S.J.1    Vierstra, R.D.2
  • 63
    • 33847213280 scopus 로고    scopus 로고
    • Bart R, Chern M, Park C-J, Bartley L, Ronald PC (2006) A novel system for gene silencing using siRNAs in rice leaf and stem-derived protoplasts. Methodology Plant Methods 2: 13.
    • Bart R, Chern M, Park C-J, Bartley L, Ronald PC (2006) A novel system for gene silencing using siRNAs in rice leaf and stem-derived protoplasts. Methodology Plant Methods 2: 13.
  • 64
    • 1642564546 scopus 로고    scopus 로고
    • Pathogenesis-related protein 10 isolated from hot pepper functions as a ribonuclease in an antiviral pathway
    • Park CJ, Kim KJ, Shin R, Park JM, Shin YC, et al. (2004) Pathogenesis-related protein 10 isolated from hot pepper functions as a ribonuclease in an antiviral pathway. Plant J 37: 186-198.
    • (2004) Plant J , vol.37 , pp. 186-198
    • Park, C.J.1    Kim, K.J.2    Shin, R.3    Park, J.M.4    Shin, Y.C.5
  • 65
    • 10744232403 scopus 로고    scopus 로고
    • The Arabidopsis dynamin-like proteins ADL1C and ADL1E play a critical role in mitochondrial morphogenesis
    • Jin JB, Bae H, Kim SJ, Jin YH, Goh CH, et al. (2003) The Arabidopsis dynamin-like proteins ADL1C and ADL1E play a critical role in mitochondrial morphogenesis. Plant Cell 15: 2357-2369.
    • (2003) Plant Cell , vol.15 , pp. 2357-2369
    • Jin, J.B.1    Bae, H.2    Kim, S.J.3    Jin, Y.H.4    Goh, C.H.5
  • 66
    • 34548011031 scopus 로고    scopus 로고
    • Review of innate and specific immunity in plants and animals
    • Iriti M, Faoro F (2007) Review of innate and specific immunity in plants and animals. Mycopathologia 164: 57-64.
    • (2007) Mycopathologia , vol.164 , pp. 57-64
    • Iriti, M.1    Faoro, F.2
  • 67
    • 0036439235 scopus 로고    scopus 로고
    • Receptor kinase signaling in plant development
    • Becraft PW (2002) Receptor kinase signaling in plant development. Annu Rev Cell Dev Biol 18: 163-192.
    • (2002) Annu Rev Cell Dev Biol , vol.18 , pp. 163-192
    • Becraft, P.W.1
  • 68
    • 0842310394 scopus 로고    scopus 로고
    • The structural basis for autoinhibition of FLT3 by the juxtamembrane domain
    • Griffith J, Black J, Faerman C, Swenson L, Wynn M, et al. (2004) The structural basis for autoinhibition of FLT3 by the juxtamembrane domain. Mol Cell 13: 169-178.
    • (2004) Mol Cell , vol.13 , pp. 169-178
    • Griffith, J.1    Black, J.2    Faerman, C.3    Swenson, L.4    Wynn, M.5
  • 69
    • 0031924794 scopus 로고    scopus 로고
    • SHP-1 binds and negatively modulates the c-Kit receptor by interaction with tyrosine 569 in the c-Kit juxtamembrane domain
    • Kozlowski M, Larose L, Lee F, Le DM, Rottapel R, et al. (1998) SHP-1 binds and negatively modulates the c-Kit receptor by interaction with tyrosine 569 in the c-Kit juxtamembrane domain. Mol Cell Biol 18: 2089-2099.
    • (1998) Mol Cell Biol , vol.18 , pp. 2089-2099
    • Kozlowski, M.1    Larose, L.2    Lee, F.3    Le, D.M.4    Rottapel, R.5
  • 70
    • 0030014452 scopus 로고    scopus 로고
    • Signalling by the W/Kit receptor tyrosine kinase is negatively regulated in vivo by the protein tyrosine phosphatase Shp1
    • Paulson RF, Vesely S, Siminovitch KA, Bernstein A (1996) Signalling by the W/Kit receptor tyrosine kinase is negatively regulated in vivo by the protein tyrosine phosphatase Shp1. Nat Genet 13: 309-315.
    • (1996) Nat Genet , vol.13 , pp. 309-315
    • Paulson, R.F.1    Vesely, S.2    Siminovitch, K.A.3    Bernstein, A.4
  • 71
    • 0035929146 scopus 로고    scopus 로고
    • Structural basis for autoinhibition of the Ephb2 receptor tyrosine kinase by the unphosphorylated juxtamembrane region
    • Wybenga-Groot LE, Baskin B, Ong SH, Tong J, Pawson T, et al. (2001) Structural basis for autoinhibition of the Ephb2 receptor tyrosine kinase by the unphosphorylated juxtamembrane region. Cell 106: 745-757.
    • (2001) Cell , vol.106 , pp. 745-757
    • Wybenga-Groot, L.E.1    Baskin, B.2    Ong, S.H.3    Tong, J.4    Pawson, T.5
  • 72
    • 33646544352 scopus 로고    scopus 로고
    • Subcellular localization and functions of the barley stem rust resistance receptor-like serine/threonine-specific protein kinase Rpg1
    • Nirmala J, Brueggeman R, Maier C, Clay C, Rostoks N, et al. (2006) Subcellular localization and functions of the barley stem rust resistance receptor-like serine/threonine-specific protein kinase Rpg1. Proc Natl Acad Sci U S A 103: 7518-7523.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 7518-7523
    • Nirmala, J.1    Brueggeman, R.2    Maier, C.3    Clay, C.4    Rostoks, N.5
  • 73
    • 34548433354 scopus 로고    scopus 로고
    • Receptor-like protein kinase HvLysMR1 of barley (Hordeum vulgare L.) is induced during leaf senescence and heavy metal stress
    • Ouelhadj A, Kaminski M, Mittag M, Humbeck K (2007) Receptor-like protein kinase HvLysMR1 of barley (Hordeum vulgare L.) is induced during leaf senescence and heavy metal stress. J Exp Bot 58: 1381-1396.
    • (2007) J Exp Bot , vol.58 , pp. 1381-1396
    • Ouelhadj, A.1    Kaminski, M.2    Mittag, M.3    Humbeck, K.4
  • 74
    • 0034657116 scopus 로고    scopus 로고
    • Thr38 and Ser198 are Pto autophosphorylation sites required for the AvrPto-Pto-mediated hypersensitive response
    • Sessa G, D'Ascenzo M, Martin GB (2000) Thr38 and Ser198 are Pto autophosphorylation sites required for the AvrPto-Pto-mediated hypersensitive response. Embo J 19: 2257-2269.
    • (2000) Embo J , vol.19 , pp. 2257-2269
    • Sessa, G.1    D'Ascenzo, M.2    Martin, G.B.3
  • 75
    • 23944457745 scopus 로고    scopus 로고
    • Identification and functional analysis of in vivo phosphorylation sites of the Arabidopsis BRASSINOSTEROID-INSENSITIVE1 receptor kinase
    • Wang X, Goshe MB, Soderblom EJ, Phinney BS, Kuchar JA, et al. (2005) Identification and functional analysis of in vivo phosphorylation sites of the Arabidopsis BRASSINOSTEROID-INSENSITIVE1 receptor kinase. Plant Cell 17: 1685-1703.
    • (2005) Plant Cell , vol.17 , pp. 1685-1703
    • Wang, X.1    Goshe, M.B.2    Soderblom, E.J.3    Phinney, B.S.4    Kuchar, J.A.5
  • 76
    • 15744398710 scopus 로고    scopus 로고
    • Regulation of plant symbiosis receptor kinase through serine and threonine phosphorylation
    • Yoshida S, Parniske M (2005) Regulation of plant symbiosis receptor kinase through serine and threonine phosphorylation. J Biol Chem 280: 9203-9209.
    • (2005) J Biol Chem , vol.280 , pp. 9203-9209
    • Yoshida, S.1    Parniske, M.2
  • 77
    • 0032499739 scopus 로고    scopus 로고
    • Identification of a family of zinc transporter genes from Arabidopsis that respond to zinc deficiency
    • Grotz N, Fox T, Connolly E, Park W, Guerinot ML, et al. (1998) Identification of a family of zinc transporter genes from Arabidopsis that respond to zinc deficiency. Proc Natl Acad Sci U S A 95: 7220-7224.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 7220-7224
    • Grotz, N.1    Fox, T.2    Connolly, E.3    Park, W.4    Guerinot, M.L.5
  • 78
    • 0000551443 scopus 로고    scopus 로고
    • An Arabidopsis GSK3/shaggy-like gene that complements yeast salt stress-sensitive mutants is induced by NaCl and abscisic acid
    • Piao HL, Pih KT, Lim JH, Kang SG, Jin JB, et al. (1999) An Arabidopsis GSK3/shaggy-like gene that complements yeast salt stress-sensitive mutants is induced by NaCl and abscisic acid. Plant Physiol 119: 1527-1534.
    • (1999) Plant Physiol , vol.119 , pp. 1527-1534
    • Piao, H.L.1    Pih, K.T.2    Lim, J.H.3    Kang, S.G.4    Jin, J.B.5
  • 79
    • 0033102221 scopus 로고    scopus 로고
    • Overexpression of a novel Arabidopsis gene related to putative zinc-transporter genes from animals can lead to enhanced zinc resistance and accumulation
    • van der Zaal BJ, Neuteboom LW, Pinas JE, Chardonnens AN, Schat H, et al. (1999) Overexpression of a novel Arabidopsis gene related to putative zinc-transporter genes from animals can lead to enhanced zinc resistance and accumulation. Plant Physiol 119: 1047-1055.
    • (1999) Plant Physiol , vol.119 , pp. 1047-1055
    • van der Zaal, B.J.1    Neuteboom, L.W.2    Pinas, J.E.3    Chardonnens, A.N.4    Schat, H.5
  • 80
    • 0020196646 scopus 로고
    • Disease lesion mimics in maize. I. Effect of genetic background, temperature, developmental age, and wounding on necrotic spot formation with Les1
    • Hoisington DA, Neuffer MG, Walbot V (1982) Disease lesion mimics in maize. I. Effect of genetic background, temperature, developmental age, and wounding on necrotic spot formation with Les1. Dev Biol 93: 381-388.
    • (1982) Dev Biol , vol.93 , pp. 381-388
    • Hoisington, D.A.1    Neuffer, M.G.2    Walbot, V.3
  • 81
    • 0027648727 scopus 로고
    • Arabidopsis mutants compromised for the control of cellular damage during pathogenesis and aging
    • Greenberg JT, Ausubel FM (1993) Arabidopsis mutants compromised for the control of cellular damage during pathogenesis and aging. Plant J 4: 327-341.
    • (1993) Plant J , vol.4 , pp. 327-341
    • Greenberg, J.T.1    Ausubel, F.M.2
  • 82
    • 0028337519 scopus 로고
    • Programmed cell death in plants: A pathogen-triggered response activated coordinately with multiple defense functions
    • Greenberg JT, Guo A, Klessig DF, Ausubel FM (1994) Programmed cell death in plants: a pathogen-triggered response activated coordinately with multiple defense functions. Cell 77: 551-563.
    • (1994) Cell , vol.77 , pp. 551-563
    • Greenberg, J.T.1    Guo, A.2    Klessig, D.F.3    Ausubel, F.M.4
  • 83
    • 33750133993 scopus 로고    scopus 로고
    • Differential expression of defense/stress-related marker proteins in leaves of a unique rice blast lesion mimic mutant (blm)
    • Jung YH, Rakwal R, Agrawal GK, Shibato J, Kim JA, et al. (2006) Differential expression of defense/stress-related marker proteins in leaves of a unique rice blast lesion mimic mutant (blm). J Proteome Res 5: 2586-2598.
    • (2006) J Proteome Res , vol.5 , pp. 2586-2598
    • Jung, Y.H.1    Rakwal, R.2    Agrawal, G.K.3    Shibato, J.4    Kim, J.A.5
  • 84
    • 34547234985 scopus 로고    scopus 로고
    • Proteome analysis and characterization of phenotypes of lesion mimic mutant spotted leaf 6 in rice
    • Kang SG, Matin MN, Bae H, Natarajan S (2007) Proteome analysis and characterization of phenotypes of lesion mimic mutant spotted leaf 6 in rice. Proteomics 7: 2447-2458.
    • (2007) Proteomics , vol.7 , pp. 2447-2458
    • Kang, S.G.1    Matin, M.N.2    Bae, H.3    Natarajan, S.4
  • 85
    • 0033103420 scopus 로고    scopus 로고
    • Lesion mimic mutants of rice with alterations in early signaling events of defense
    • Takahashi A, Kawasaki T, Henmi K, Shi IK, Kodama O, et al. (1999) Lesion mimic mutants of rice with alterations in early signaling events of defense. Plant J 17: 535-545.
    • (1999) Plant J , vol.17 , pp. 535-545
    • Takahashi, A.1    Kawasaki, T.2    Henmi, K.3    Shi, I.K.4    Kodama, O.5
  • 86
    • 0027322860 scopus 로고
    • The mlo resistance alleles to powdery mildew infection in barley trigger a developmentally controlled defence mimic phenotype
    • Wolter M, Hollricher K, Salamini F, Schulze-Lefert P (1993) The mlo resistance alleles to powdery mildew infection in barley trigger a developmentally controlled defence mimic phenotype. Mol Gen Genet 239: 122-128.
    • (1993) Mol Gen Genet , vol.239 , pp. 122-128
    • Wolter, M.1    Hollricher, K.2    Salamini, F.3    Schulze-Lefert, P.4
  • 87
    • 0037593489 scopus 로고    scopus 로고
    • Lesion mimic mutants: Keys for deciphering cell death and defense pathways in plants?
    • Lorrain S, Vailleau F, Balague C, Roby D (2003) Lesion mimic mutants: keys for deciphering cell death and defense pathways in plants? Trends Plant Sci 8: 263-271.
    • (2003) Trends Plant Sci , vol.8 , pp. 263-271
    • Lorrain, S.1    Vailleau, F.2    Balague, C.3    Roby, D.4
  • 88
    • 0037084038 scopus 로고    scopus 로고
    • Knockout of Arabidopsis accelerated-cell-death11 encoding a sphingosine transfer protein causes activation of programmed cell death and defense
    • Brodersen P, Petersen M, Pike HM, Olszak B, Skov S, et al. (2002) Knockout of Arabidopsis accelerated-cell-death11 encoding a sphingosine transfer protein causes activation of programmed cell death and defense. Genes Dev 16: 490-502.
    • (2002) Genes Dev , vol.16 , pp. 490-502
    • Brodersen, P.1    Petersen, M.2    Pike, H.M.3    Olszak, B.4    Skov, S.5
  • 89
    • 0035859054 scopus 로고    scopus 로고
    • Programmed cell death, mitochondria and the plant hypersensitive response
    • Lam E, Kato N, Lawton M (2001) Programmed cell death, mitochondria and the plant hypersensitive response. Nature 411: 848-853.
    • (2001) Nature , vol.411 , pp. 848-853
    • Lam, E.1    Kato, N.2    Lawton, M.3
  • 90
    • 0037809234 scopus 로고    scopus 로고
    • Regulation of the interleukin-1-induced signaling pathways by a novel member of the protein phosphatase 2C family (PP2Cepsilon)
    • Li MG, Katsura K, Nomiyama H, Komaki K, Ninomiya-Tsuji J, et al. (2003) Regulation of the interleukin-1-induced signaling pathways by a novel member of the protein phosphatase 2C family (PP2Cepsilon). J Biol Chem 278: 12013-12021.
    • (2003) J Biol Chem , vol.278 , pp. 12013-12021
    • Li, M.G.1    Katsura, K.2    Nomiyama, H.3    Komaki, K.4    Ninomiya-Tsuji, J.5
  • 91
    • 0032509295 scopus 로고    scopus 로고
    • Defective LPS signaling in C3H/HeJ and C57BL/10ScCr mice: Mutations in Tlr4 gene
    • Poltorak A, He X, Smirnova I, Liu MY, Van Huffel C, et al. (1998) Defective LPS signaling in C3H/HeJ and C57BL/10ScCr mice: mutations in Tlr4 gene. Science 282: 2085-2088.
    • (1998) Science , vol.282 , pp. 2085-2088
    • Poltorak, A.1    He, X.2    Smirnova, I.3    Liu, M.Y.4    Van Huffel, C.5
  • 92
    • 33947721445 scopus 로고    scopus 로고
    • Structure, interactions, and dynamics of the RING domain from human TRAF6
    • Mercier P, Lewis MJ, Hau DD, Saltibus LF, Xiao W, et al. (2007) Structure, interactions, and dynamics of the RING domain from human TRAF6. Protein Sci 16: 602-614.
    • (2007) Protein Sci , vol.16 , pp. 602-614
    • Mercier, P.1    Lewis, M.J.2    Hau, D.D.3    Saltibus, L.F.4    Xiao, W.5
  • 93
    • 33745542086 scopus 로고    scopus 로고
    • Role of MAP kinase-dependent apoptotic pathway in innate immune responses and viral infection
    • Sumbayev VV, Yasinska IM (2006) Role of MAP kinase-dependent apoptotic pathway in innate immune responses and viral infection. Scand J Immunol 63: 391-400.
    • (2006) Scand J Immunol , vol.63 , pp. 391-400
    • Sumbayev, V.V.1    Yasinska, I.M.2
  • 94
    • 0035913278 scopus 로고    scopus 로고
    • TAK1 is a ubiquitin-dependent kinase of MKK and IKK
    • Wang C, Deng L, Hong M, Akkaraju GR, Inoue J, et al. (2001) TAK1 is a ubiquitin-dependent kinase of MKK and IKK. Nature 412: 346-351.
    • (2001) Nature , vol.412 , pp. 346-351
    • Wang, C.1    Deng, L.2    Hong, M.3    Akkaraju, G.R.4    Inoue, J.5
  • 95
    • 34447557009 scopus 로고    scopus 로고
    • Innate immunogenetics: A tool for exploring new frontiers of host defence
    • Bochud PY, Bochud M, Telenti A, Calandra T (2007) Innate immunogenetics: a tool for exploring new frontiers of host defence. Lancet Infect Dis 7: 531-542.
    • (2007) Lancet Infect Dis , vol.7 , pp. 531-542
    • Bochud, P.Y.1    Bochud, M.2    Telenti, A.3    Calandra, T.4
  • 96
    • 33845404635 scopus 로고    scopus 로고
    • Vesicle trafficking in plant immune responses
    • Robatzek S (2007) Vesicle trafficking in plant immune responses. Cell Microbiol 9: 1-8.
    • (2007) Cell Microbiol , vol.9 , pp. 1-8
    • Robatzek, S.1
  • 97
    • 0037186599 scopus 로고    scopus 로고
    • MAP kinase signalling cascade in Arabidopsis innate immunity
    • Asai T, Tena G, Plotnikova J, Willmann MR, Chiu WL, et al. (2002) MAP kinase signalling cascade in Arabidopsis innate immunity. Nature 415: 977-983.
    • (2002) Nature , vol.415 , pp. 977-983
    • Asai, T.1    Tena, G.2    Plotnikova, J.3    Willmann, M.R.4    Chiu, W.L.5
  • 98
    • 0036618235 scopus 로고    scopus 로고
    • Flagellin perception: A paradigm for innate immunity
    • Gomez-Gomez L, Boller T (2002) Flagellin perception: a paradigm for innate immunity. Trends Plant Sci 7: 251-256.
    • (2002) Trends Plant Sci , vol.7 , pp. 251-256
    • Gomez-Gomez, L.1    Boller, T.2
  • 99
    • 0032076826 scopus 로고    scopus 로고
    • Xa21D encodes a receptor-like molecule with a leucine-rich repeat domain that determines race-specific recognition and is subject to adaptive evolution
    • Wang GL, Ruan DL, Song WY, Sideris S, Chen L, et al. (1998) Xa21D encodes a receptor-like molecule with a leucine-rich repeat domain that determines race-specific recognition and is subject to adaptive evolution. Plant Cell 10: 765-779.
    • (1998) Plant Cell , vol.10 , pp. 765-779
    • Wang, G.L.1    Ruan, D.L.2    Song, W.Y.3    Sideris, S.4    Chen, L.5
  • 100
    • 0031238679 scopus 로고    scopus 로고
    • The molecular basis of disease resistance in rice
    • Ronald PC (1997) The molecular basis of disease resistance in rice. Plant Mol Biol 35: 179-186.
    • (1997) Plant Mol Biol , vol.35 , pp. 179-186
    • Ronald, P.C.1
  • 101
    • 0033978737 scopus 로고    scopus 로고
    • A genomic approach of the hepatitis C virus generates a protein interaction map
    • Flajolet M, Rotondo G, Daviet L, Bergametti F, Inchauspe G, et al. (2000) A genomic approach of the hepatitis C virus generates a protein interaction map. Gene 242: 369-379.
    • (2000) Gene , vol.242 , pp. 369-379
    • Flajolet, M.1    Rotondo, G.2    Daviet, L.3    Bergametti, F.4    Inchauspe, G.5


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