메뉴 건너뛰기




Volumn 6, Issue 10, 2011, Pages 1469-1474

Revealing plant defense signaling getting more sophisticated with phosphoproteomics

Author keywords

Kinase; Phosphoproteomics; Plant pathogen interaction; Protein phosphorylation

Indexed keywords


EID: 80053581724     PISSN: 15592316     EISSN: 15592324     Source Type: Journal    
DOI: 10.4161/psb.6.10.17345     Document Type: Article
Times cited : (23)

References (39)
  • 1
    • 33644864894 scopus 로고    scopus 로고
    • Analysis of protein phosphorylation: Methods and strategies for studying kinases and substrates
    • PMID:16441346; DOI:10.1111/j.1365-313X.2005.02613.x
    • Peck SC. Analysis of protein phosphorylation: methods and strategies for studying kinases and substrates. Plant J 2006; 45:512-22 PMID:16441346; DOI:10.1111/j.1365-313X.2005.02613.x.
    • (2006) Plant J , vol.45 , pp. 512-522
    • Peck, S.C.1
  • 2
    • 63349084973 scopus 로고    scopus 로고
    • Advancements in plant proteomics using quantitative mass spectrometry
    • PMID:19049910; DOI:10.1016/j.jprot.2008.11.008
    • Oeljeklaus S, Meyer HE, Warscheid B. Advancements in plant proteomics using quantitative mass spectrometry. J Proteomics 2009; 72:545-54 PMID:19049910; DOI:10.1016/j.jprot.2008.11.008.
    • (2009) J Proteomics , vol.72 , pp. 545-554
    • Oeljeklaus, S.1    Meyer, H.E.2    Warscheid, B.3
  • 3
    • 23044511526 scopus 로고    scopus 로고
    • Proteomic and phosphoproteomic approaches to understanding plant-pathogen interactions
    • DOI:10.1016/j.pmpp.2005.03.00
    • Thurston G, Regan S, Rampitsch C, Xing T. Proteomic and phosphoproteomic approaches to understanding plant-pathogen interactions. Physiol Mol Plant Pathol 2005; 66:3-11 DOI:10.1016/j.pmpp.2005.03.004.
    • (2005) Physiol Mol Plant Pathol , vol.66 , pp. 3-11
    • Thurston, G.1    Regan, S.2    Rampitsch, C.3    Xing, T.4
  • 4
    • 0033565503 scopus 로고    scopus 로고
    • Immobilized gallium(III) affinity chromatography of phosphopeptides
    • PMID:10424175; DOI:10.1021/ac981409y
    • Posewitz MC, Tempst P. Immobilized gallium(III) affinity chromatography of phosphopeptides. Anal Chem 1999; 71:2883-92 PMID:10424175; DOI:10.1021/ac981409y.
    • (1999) Anal Chem , vol.71 , pp. 2883-2892
    • Posewitz, M.C.1    Tempst, P.2
  • 6
    • 77954247252 scopus 로고    scopus 로고
    • Large-scale comparative phosphoproteomics identifies conserved phosphorylation sites in plants
    • PMID:20466843; DOI:10.1104/pp.110.157347
    • Nakagami H, Sugiyama N, Mochida K, Daudi A, Yoshida Y, Toyoda T, et al. Large-scale comparative phosphoproteomics identifies conserved phosphorylation sites in plants. Plant Physiol 2010; 153:1161-74 PMID:20466843; DOI:10.1104/pp.110.157347.
    • (2010) Plant Physiol , vol.153 , pp. 1161-1174
    • Nakagami, H.1    Sugiyama, N.2    Mochida, K.3    Daudi, A.4    Yoshida, Y.5    Toyoda, T.6
  • 7
    • 43249124511 scopus 로고    scopus 로고
    • Large-scale phosphorylation mapping reveals the extent of tyrosine phosphorylation in Arabidopsis
    • PMID:18463617; DOI:10.1038/msb.2008.32
    • Sugiyama N, Nakagami H, Mochida K, Daudi A, Tomita M, Shirasu K, et al. Large-scale phosphorylation mapping reveals the extent of tyrosine phosphorylation in Arabidopsis. Mol Syst Biol 2008; 4:193-9 PMID:18463617; DOI:10.1038/msb.2008.32.
    • (2008) Mol Syst Biol , vol.4 , pp. 193-199
    • Sugiyama, N.1    Nakagami, H.2    Mochida, K.3    Daudi, A.4    Tomita, M.5    Shirasu, K.6
  • 8
    • 0037186599 scopus 로고    scopus 로고
    • MAP kinase signalling cascade in Arabidopsis innate immunity
    • PMID:11875555; DOI:10.1038/415977a
    • Asai T, Tena G, Plotnikova J, Willmann MR, Chiu WL, Gómez-Gómez L, et al. MAP kinase signalling cascade in Arabidopsis innate immunity. Nature 2002; 415:977-83 PMID:11875555; DOI:10.1038/415977a.
    • (2002) Nature , vol.415 , pp. 977-983
    • Asai, T.1    Tena, G.2    Plotnikova, J.3    Willmann, M.R.4    Chiu, W.L.5    Gómez-Gómez, L.6
  • 9
    • 34547151023 scopus 로고    scopus 로고
    • A flagellin-induced complex of the receptor FLS2 and BAK1 initiates plant defence
    • PMID:17625569; DOI:10.1038/nature05999
    • Chinchilla D, Zipfel C, Robatzek S, Kemmerling B, Nürnberger T, Jones JDJ, et al. A flagellin-induced complex of the receptor FLS2 and BAK1 initiates plant defence. Nature 2007; 448:497-500 PMID:17625569; DOI:10.1038/nature05999.
    • (2007) Nature , vol.448 , pp. 497-500
    • Chinchilla, D.1    Zipfel, C.2    Robatzek, S.3    Kemmerling, B.4    Nürnberger, T.5    Jones, J.D.J.6
  • 10
    • 34548128405 scopus 로고    scopus 로고
    • Quantitative phosphoproteomic analysis of plasma membrane proteins reveals regulatory mechanisms of plant innate immune responses
    • PMID:17651370; DOI:10.1111/j.1365-313X.2007.03192.x
    • Nühse TS, Bottrill AR, Jones AME, Peck SC. Quantitative phosphoproteomic analysis of plasma membrane proteins reveals regulatory mechanisms of plant innate immune responses. Plant J 2007; 51:931-40 PMID:17651370; DOI:10.1111/j.1365-313X.2007.03192.x.
    • (2007) Plant J , vol.51 , pp. 931-940
    • Nühse, T.S.1    Bottrill, A.R.2    Jones, A.M.E.3    Peck, S.C.4
  • 11
    • 3042530074 scopus 로고    scopus 로고
    • The transcriptional innate immune response to flg22: Interplay and overlap with Avr genedependent defense responses and bacterial pathogenesis
    • PMID:15181213; DOI:10.1104/pp.103.036749
    • Navarro L, Zipfel C, Rowland O, Keller I, Robatzek S, Boller T, et al. The transcriptional innate immune response to flg22: Interplay and overlap with Avr genedependent defense responses and bacterial pathogenesis. Plant Physiol 2004; 135:1113-28 PMID:15181213; DOI:10.1104/pp.103.036749.
    • (2004) Plant Physiol , vol.135 , pp. 1113-1128
    • Navarro, L.1    Zipfel, C.2    Rowland, O.3    Keller, I.4    Robatzek, S.5    Boller, T.6
  • 12
    • 0037324536 scopus 로고    scopus 로고
    • Quantitative nature of Arabidopsis responses during compatible and incompatible interactions with the bacterial pathogen Pseudomonas syringae
    • PMID:12566575; DOI:10.1105/ tpc.007591
    • Tao Y, Xie Z, Chen W, Glazebrook J, Chang HS, Han B, et al. Quantitative nature of Arabidopsis responses during compatible and incompatible interactions with the bacterial pathogen Pseudomonas syringae. Plant Cell 2003; 15:317-30 PMID:12566575; DOI:10.1105/ tpc.007591.
    • (2003) Plant Cell , vol.15 , pp. 317-330
    • Tao, Y.1    Xie, Z.2    Chen, W.3    Glazebrook, J.4    Chang, H.S.5    Han, B.6
  • 13
    • 34547110110 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics of early elicitor signaling in Arabidopsis
    • PMID:17317660; DOI:10.1074/mcp.M600429-MCP200
    • Benschop JJ, Mohammed S, O'Flaherty M, Heck AJ, Slijper M, Menke FL. Quantitative phosphoproteomics of early elicitor signaling in Arabidopsis. Mol Cell Proteomics 2007; 6:1198-214 PMID:17317660; DOI:10.1074/mcp.M600429-MCP200.
    • (2007) Mol Cell Proteomics , vol.6 , pp. 1198-1214
    • Benschop, J.J.1    Mohammed, S.2    O'Flaherty, M.3    Heck, A.J.4    Slijper, M.5    Menke, F.L.6
  • 14
    • 4544291080 scopus 로고    scopus 로고
    • Phosphoproteomics of the Arabidopsis plasma membrane and a new phosphorylation site database
    • PMID:15308754; DOI:10.1105/tpc.104.023150
    • Nühse TS, Stansballe A, Jensen ON, Peck SC. Phosphoproteomics of the Arabidopsis plasma membrane and a new phosphorylation site database. Plant Cell 2004; 16:2394-405 PMID:15308754; DOI:10.1105/tpc.104.023150.
    • (2004) Plant Cell , vol.16 , pp. 2394-2405
    • Nühse, T.S.1    Stansballe, A.2    Jensen, O.N.3    Peck, S.C.4
  • 15
    • 34548459741 scopus 로고    scopus 로고
    • Using phosphoproteomics to reveal signalling dynamics in plants
    • de la Fuente van Bentem S, Hirt H, PMID:17765599; DOI:10.1016/j.tplants.2007.08.007
    • de la Fuente van Bentem S, Hirt H. Using phosphoproteomics to reveal signalling dynamics in plants. Trends Plant Sci 2007; 12:404-11 PMID:17765599; DOI:10.1016/j.tplants.2007.08.007.
    • (2007) Trends Plant Sci , vol.12 , pp. 404-411
  • 16
    • 11444263845 scopus 로고    scopus 로고
    • Largescale analysis of in vivo phosphorylated membrane proteins by immobilized metal ion affinity chromatography and mass spectrometry
    • PMID:14506206; DOI:10.1074/mcp.T300006-MCP200
    • Nühse TS, Stensballe A, Jensen ON, Peck SC. Largescale analysis of in vivo phosphorylated membrane proteins by immobilized metal ion affinity chromatography and mass spectrometry. Mol Cell Proteomics 2003; 2:1234-43 PMID:14506206; DOI:10.1074/mcp.T300006-MCP200.
    • (2003) Mol Cell Proteomics , vol.2 , pp. 1234-1243
    • Nühse, T.S.1    Stensballe, A.2    Jensen, O.N.3    Peck, S.C.4
  • 17
    • 0035886699 scopus 로고    scopus 로고
    • Calciumdependent protein kinase plays an essential role in the plant defense response
    • PMID:11597999; DOI:10.1093/emboj/20.20.5556
    • Romeis T, Ludwig AA, Martin R, Jones JDG. Calciumdependent protein kinase plays an essential role in the plant defense response. EMBO J 2001; 20:5556-67 PMID:11597999; DOI:10.1093/emboj/20.20.5556.
    • (2001) EMBO J , vol.20 , pp. 5556-5567
    • Romeis, T.1    Ludwig, A.A.2    Martin, R.3    Jones, J.D.G.4
  • 18
    • 0000405774 scopus 로고    scopus 로고
    • Regulation of plant defense response to fungal pathogens: Two types of protein kinases in the reversible phosphorylation of the host plasma membrane H+-ATPase
    • PMID:12239392
    • Xing T, Higgins VJ, Blumwald E. Regulation of plant defense response to fungal pathogens: two types of protein kinases in the reversible phosphorylation of the host plasma membrane H+-ATPase. Plant Cell 1996; 8:555-64 PMID:12239392.
    • (1996) Plant Cell , vol.8 , pp. 555-564
    • Xing, T.1    Higgins, V.J.2    Blumwald, E.3
  • 19
    • 34547225068 scopus 로고    scopus 로고
    • Cytoskeleton and cell wall function in penetration resistance
    • PMID:17627866; DOI:10.1016/j.pbi.2007.05.001
    • Hardham AR, Jones DR, Takemoto D. Cytoskeleton and cell wall function in penetration resistance. Curr Opin Plant Biol 2007; 10:342-8 PMID:17627866; DOI:10.1016/j.pbi.2007.05.001.
    • (2007) Curr Opin Plant Biol , vol.10 , pp. 342-348
    • Hardham, A.R.1    Jones, D.R.2    Takemoto, D.3
  • 20
    • 27944454718 scopus 로고    scopus 로고
    • Pre- and postinvasion defenses both contribute to nonhost resistance in Arabidopsis
    • PMID:16293760; DOI:10.1126/science.1119409
    • Lipka V, Dittgen J, Bednarek P, Bhat R, Wiermer M, Stein M, et al. Pre- and postinvasion defenses both contribute to nonhost resistance in Arabidopsis. Science 2005; 310:1180-3 PMID:16293760; DOI:10.1126/science.1119409.
    • (2005) Science , vol.310 , pp. 1180-1183
    • Lipka, V.1    Dittgen, J.2    Bednarek, P.3    Bhat, R.4    Wiermer, M.5    Stein, M.6
  • 21
    • 48149106793 scopus 로고    scopus 로고
    • Arabidopsis MAPKs: A complex signalling network involved in multiple biological processes
    • PMID:18570633; DOI:10.1042/BJ20080625
    • Colcombet J, Hirt H. Arabidopsis MAPKs: a complex signalling network involved in multiple biological processes. Biochem J 2008; 413:217-26 PMID:18570633; DOI:10.1042/BJ20080625.
    • (2008) Biochem J , vol.413 , pp. 217-226
    • Colcombet, J.1    Hirt, H.2
  • 22
    • 27644573819 scopus 로고    scopus 로고
    • High throughput identification of potential Arabidopsis mitogen-activated protein kinases substrates
    • PMID:16009969; DOI:10.1074/mcp.M500007-MCP200
    • Feilner T, Hultschig C, Lee J, Meyer S, Immink RGH, Koenig A, et al. High throughput identification of potential Arabidopsis mitogen-activated protein kinases substrates. Mol Cell Proteomics 2005; 4:1558-68 PMID:16009969; DOI:10.1074/mcp.M500007-MCP200.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 1558-1568
    • Feilner, T.1    Hultschig, C.2    Lee, J.3    Meyer, S.4    Immink, R.G.H.5    Koenig, A.6
  • 23
    • 78650979357 scopus 로고    scopus 로고
    • MASCP Gator: An aggregation portal for the visualization of Arabidopsis proteomics data
    • PMID:21075962; DOI:10.1104/pp.110.168195
    • Joshi HJ, Hirsch-Hoffmann M, Baerenfaller K, Gruissem W, Baginsky S, Schmidt R, et al. MASCP Gator: an aggregation portal for the visualization of Arabidopsis proteomics data. Plant Physiol 2011; 155:259-70 PMID:21075962; DOI:10.1104/pp.110.168195.
    • (2011) Plant Physiol , vol.155 , pp. 259-270
    • Joshi, H.J.1    Hirsch-Hoffmann, M.2    Baerenfaller, K.3    Gruissem, W.4    Baginsky, S.5    Schmidt, R.6
  • 24
    • 0042232498 scopus 로고    scopus 로고
    • MALDI-Qq-TOF-MS and transient gene expression analysis indicated co-enhancement of β-1,3-glucanase and endochitinase by tMEK2 and the involvement of divergent pathways
    • DOI:10.1016/S0885-5765(03)00062-6
    • Xing T, Rampitsch C, Miki BL, Mauthe W, Stebbing JA, Malik K, et al. MALDI-Qq-TOF-MS and transient gene expression analysis indicated co-enhancement of β-1,3-glucanase and endochitinase by tMEK2 and the involvement of divergent pathways. Physiol Mol Plant Pathol 2003; 62:209-17 DOI:10.1016/S0885-5765(03)00062-6.
    • (2003) Physiol Mol Plant Pathol , vol.62 , pp. 209-217
    • Xing, T.1    Rampitsch, C.2    Miki, B.L.3    Mauthe, W.4    Stebbing, J.A.5    Malik, K.6
  • 25
    • 0037870267 scopus 로고    scopus 로고
    • Nucleoside diphosphate kinases in mammalian signal transduction systems: Recent development and perspective
    • PMID:12848340; DOI:10.1023/A:1023489722460
    • Kimura N, Shimada N, Ishijima Y, Fukuda M, Takagi Y, Ishikawa N. Nucleoside diphosphate kinases in mammalian signal transduction systems: recent development and perspective. J Bioenerg Biomembr 2003; 35:41-7 PMID:12848340; DOI:10.1023/A:1023489722460.
    • (2003) J Bioenerg Biomembr , vol.35 , pp. 41-47
    • Kimura, N.1    Shimada, N.2    Ishijima, Y.3    Fukuda, M.4    Takagi, Y.5    Ishikawa, N.6
  • 26
    • 67349211435 scopus 로고    scopus 로고
    • TAB2, a nucleoside diphosphate protein kinase, is a component of the tMEK2 disease resistance pathway in tomato
    • DOI:10.1016/j.pmpp.2008.11.003
    • Xing T, Rampitsch C, Sun S, Romanowski A, Conroy C, Stebbing J, et al. TAB2, a nucleoside diphosphate protein kinase, is a component of the tMEK2 disease resistance pathway in tomato. Physiol Mol Plant Pathol 2008; 73:33-9 DOI:10.1016/j.pmpp.2008.11.003.
    • (2008) Physiol Mol Plant Pathol , vol.73 , pp. 33-39
    • Xing, T.1    Rampitsch, C.2    Sun, S.3    Romanowski, A.4    Conroy, C.5    Stebbing, J.6
  • 27
    • 66149126624 scopus 로고    scopus 로고
    • Primary metabolism and plant defense-fuel for the fire
    • PMID:19348567; DOI:10.1094/MPMI-22-5-0487
    • Bolton MD. Primary metabolism and plant defense-fuel for the fire. Mol Plant Microbe Interact 2009; 22:487-97 PMID:19348567; DOI:10.1094/MPMI-22-5-0487.
    • (2009) Mol Plant Microbe Interact , vol.22 , pp. 487-497
    • Bolton, M.D.1
  • 28
    • 77955860256 scopus 로고    scopus 로고
    • Yeast two-hybrid screening of MAP kinase cascade identifies cytosolic glutamine synthetase 1b as a tMEK2 interactive protein in wheat
    • DOI:10.1080/07060660909507615
    • Fan T, Gao Y, Al-Shammari A, Wang XJ, Xing T. Yeast two-hybrid screening of MAP kinase cascade identifies cytosolic glutamine synthetase 1b as a tMEK2 interactive protein in wheat. Can J Plant Pathol 2009; 31:407-14 DOI:10.1080/07060660909507615.
    • (2009) Can J Plant Pathol , vol.31 , pp. 407-414
    • Fan, T.1    Gao, Y.2    Al-Shammari, A.3    Wang, X.J.4    Xing, T.5
  • 29
    • 0033763413 scopus 로고    scopus 로고
    • Post-translational regulation of cytosolic glutamine synthetase by reversible phosphorylation and 14-3-3 protein interaction
    • PMID:11069692; DOI:10.1046/j.1365-313x.2000.00863.x
    • Finnemann J, Schjoerring JK. Post-translational regulation of cytosolic glutamine synthetase by reversible phosphorylation and 14-3-3 protein interaction. Plant J 2000; 24:171-81 PMID:11069692; DOI:10.1046/j.1365-313x.2000.00863.x.
    • (2000) Plant J , vol.24 , pp. 171-181
    • Finnemann, J.1    Schjoerring, J.K.2
  • 30
    • 65249121277 scopus 로고    scopus 로고
    • The importance of cytosolic glutamine synthetase in nitrogen assimilation and recycling
    • PMID:19422547; DOI:10.1111/j.1469-8137.2009.02823.x
    • Bernard SM, Habash DZ. The importance of cytosolic glutamine synthetase in nitrogen assimilation and recycling. New Phytol 2009; 182:608-20 PMID:19422547; DOI:10.1111/j.1469-8137.2009.02823.x.
    • (2009) New Phytol , vol.182 , pp. 608-620
    • Bernard, S.M.1    Habash, D.Z.2
  • 31
    • 0042572083 scopus 로고    scopus 로고
    • Early phosphorylation events in biotic stress
    • PMID:12873527; DOI:10.1016/S1369-5266(03)00056-6
    • Peck SC. Early phosphorylation events in biotic stress. Curr Opin Plant Biol 2003; 6:334-8 PMID:12873527; DOI:10.1016/S1369-5266(03)00056-6.
    • (2003) Curr Opin Plant Biol , vol.6 , pp. 334-338
    • Peck, S.C.1
  • 32
    • 33747126774 scopus 로고    scopus 로고
    • Analysis of the subcellular localization, function and proteolytic control of the Arabidopsis cyclin-dependent kinase inhibitor ICK1/KRP11
    • PMID:16766674; DOI:10.1104/pp.106.081406
    • Jakoby MJ, Wein C, Pusch S, Kuijt SJH, Merkle T, Dissmeyer N, et al. Analysis of the subcellular localization, function and proteolytic control of the Arabidopsis cyclin-dependent kinase inhibitor ICK1/KRP11. Plant Physiol 2006; 141:1293-305 PMID:16766674; DOI:10.1104/pp.106.081406.
    • (2006) Plant Physiol , vol.141 , pp. 1293-1305
    • Jakoby, M.J.1    Wein, C.2    Pusch, S.3    Kuijt, S.J.H.4    Merkle, T.5    Dissmeyer, N.6
  • 33
    • 0035984056 scopus 로고    scopus 로고
    • Protein-protein interactions between sucrose transporters of different affinities colocalized in the same enucleate sieve element
    • PMID:12119375; DOI:10.1105/ tpc.002428
    • Reinders A, Schulze W, Kühn C, Barker L, Schulz A, Ward JM, et al. Protein-protein interactions between sucrose transporters of different affinities colocalized in the same enucleate sieve element. Plant Cell 2002; 14:1567-77 PMID:12119375; DOI:10.1105/ tpc.002428.
    • (2002) Plant Cell , vol.14 , pp. 1567-1577
    • Reinders, A.1    Schulze, W.2    Kühn, C.3    Barker, L.4    Schulz, A.5    Ward, J.M.6
  • 34
    • 61749088967 scopus 로고    scopus 로고
    • Interactions between membrane-bound cellulose synthases involved in the synthesis of the secondary cell wall
    • PMID:19258017; DOI:10.1016/j.febslet. 2009.02.035
    • Timmers J, Vernhettes S, Desprez T, Vincken J, Visser R, Trindade L. Interactions between membrane-bound cellulose synthases involved in the synthesis of the secondary cell wall. FEBS Lett 2009; 583:978-82 PMID:19258017; DOI:10.1016/j.febslet. 2009.02.035.
    • (2009) FEBS Lett , vol.583 , pp. 978-982
    • Timmers, J.1    Vernhettes, S.2    Desprez, T.3    Vincken, J.4    Visser, R.5    Trindade, L.6
  • 35
    • 77952406753 scopus 로고    scopus 로고
    • QIKS-Quantitative identification of kinase substrates
    • PMID:20217869; DOI:10.1002/pmic.200900749
    • Morandell S, Grosstessner-Hain K, Roitinger E, Hudecz O, Lindhorst T, Teis D, et al. QIKS-Quantitative identification of kinase substrates. Proteomics 2010; 10:2015-25 PMID:20217869; DOI:10.1002/pmic.200900749.
    • (2010) Proteomics , vol.10 , pp. 2015-2025
    • Morandell, S.1    Grosstessner-Hain, K.2    Roitinger, E.3    Hudecz, O.4    Lindhorst, T.5    Teis, D.6
  • 36
    • 0037343103 scopus 로고    scopus 로고
    • Laser capture microdissection, a tool for the global expression in specific plant cell types: Identification of genes expressed differentially in epidermal cells or vascular tissue in maize
    • DOI:10.1105/tpc.008102
    • Nakazono M, Qiu F, Borusk LA, Schnable PS. Laser capture microdissection, a tool for the global expression in specific plant cell types: identification of genes expressed differentially in epidermal cells or vascular tissue in maize. Plant Cell 2003; 15:583-96 DOI:10.1105/tpc.008102.
    • (2003) Plant Cell , vol.15 , pp. 583-596
    • Nakazono, M.1    Qiu, F.2    Borusk, L.A.3    Schnable, P.S.4
  • 37
    • 34247234601 scopus 로고    scopus 로고
    • The rice kinase database: Phylogenomic database for the rice kinome
    • PMID:17172291; DOI:10.1104/pp.106.087270
    • Dardick C, Chen J, Richter T, Ouyang S, Ronald P. The rice kinase database: phylogenomic database for the rice kinome. Plant Physiol 2007; 143:579-86 PMID:17172291; DOI:10.1104/pp.106.087270.
    • (2007) Plant Physiol , vol.143 , pp. 579-586
    • Dardick, C.1    Chen, J.2    Richter, T.3    Ouyang, S.4    Ronald, P.5
  • 38
    • 36049046122 scopus 로고    scopus 로고
    • An immunoaffinity tandem mass spectrometry (iMALDI) assay for detection of Francisella tularensis
    • PMID:18022413; DOI:10.1016/j.aca.2007.10.025
    • Jiang J, Parker CE, Fuller JR, Kawula TH, Borchers CH. An immunoaffinity tandem mass spectrometry (iMALDI) assay for detection of Francisella tularensis. Anal Chim Acta 2007; 605:70-9 PMID:18022413; DOI:10.1016/j.aca.2007.10.025.
    • (2007) Anal Chim Acta , vol.605 , pp. 70-79
    • Jiang, J.1    Parker, C.E.2    Fuller, J.R.3    Kawula, T.H.4    Borchers, C.H.5
  • 39
    • 77956878144 scopus 로고    scopus 로고
    • Towards the development of an immuno MALDI (iMALDI) mass spectrometry assay for the diagnosis of hypertension
    • PMID:20199871; DOI:10.1016/j. jasms.2010.01.024
    • Reid JD, Holmes DT, Mason DR, Shah B, Borchers CH. Towards the development of an immuno MALDI (iMALDI) mass spectrometry assay for the diagnosis of hypertension. J Am Soc Mass Spectrom 2010; 21:1680-6 PMID:20199871; DOI:10.1016/j. jasms.2010.01.024.
    • (2010) J Am Soc Mass Spectrom , vol.21 , pp. 1680-1686
    • Reid, J.D.1    Holmes, D.T.2    Mason, D.R.3    Shah, B.4    Borchers, C.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.