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Volumn 27, Issue 6, 2015, Pages 1755-1770

Wheat stripe rust resistance protein WKS1 reduces the ability of the thylakoid-associated ascorbate peroxidase to detoxify reactive oxygen species

Author keywords

[No Author keywords available]

Indexed keywords

PUCCINIA STRIIFORMIS; TRITICUM AESTIVUM;

EID: 84936936058     PISSN: 10404651     EISSN: 1532298X     Source Type: Journal    
DOI: 10.1105/tpc.114.134296     Document Type: Article
Times cited : (115)

References (57)
  • 1
    • 84890558909 scopus 로고    scopus 로고
    • START ships lipids across interorganelle space
    • Alpy, F., and Tomasetto, C. (2014). START ships lipids across interorganelle space. Biochimie 96: 85-95.
    • (2014) Biochimie , vol.96 , pp. 85-95
    • Alpy, F.1    Tomasetto, C.2
  • 2
    • 33748291408 scopus 로고    scopus 로고
    • Phospholipase-dependent signalling during the AvrRpm1-and AvrRpt2-induced disease resistance responses in Arabidopsis thaliana
    • Andersson, M. X., Kourtchenko, O., Dangl, J. L., Mackey, D., and Ellerström, M. (2006). Phospholipase-dependent signalling during the AvrRpm1-and AvrRpt2-induced disease resistance responses in Arabidopsis thaliana. Plant J. 47: 947-959.
    • (2006) Plant J , vol.47 , pp. 947-959
    • Andersson, M.X.1    Kourtchenko, O.2    Dangl, J.L.3    McKey, D.4    Ellerström, M.5
  • 4
    • 64249153116 scopus 로고    scopus 로고
    • The chloroplast protein RPH1 plays a role in the immune response of Arabidopsis to Phytophthora brassicae
    • Belhaj, K., Lin, B., and Mauch, F. (2009). The chloroplast protein RPH1 plays a role in the immune response of Arabidopsis to Phytophthora brassicae. Plant J. 58: 287-298.
    • (2009) Plant J , vol.58 , pp. 287-298
    • Belhaj, K.1    Lin, B.2    Mauch, F.3
  • 5
    • 0026735576 scopus 로고
    • Elicitor-and wound-induced oxidative cross-linking of a proline-rich plant cell wall protein: A novel, rapid defense response
    • Bradley, D. J., Kjellbom, P., and Lamb, C. J. (1992). Elicitor-and wound-induced oxidative cross-linking of a proline-rich plant cell wall protein: a novel, rapid defense response. Cell 70: 21-30.
    • (1992) Cell , vol.70 , pp. 21-30
    • Bradley, D.J.1    Kjellbom, P.2    Lamb, C.J.3
  • 6
    • 49149122284 scopus 로고    scopus 로고
    • Agronomic and quality evaluation of common wheat near-isogenic lines carrying the leaf rust resistance gene Lr47
    • Brevis, J. C., Chicaiza, O., Khan, I. A., Jackson, L., Morris, C. F., and Dubcovsky, J. (2008). Agronomic and quality evaluation of common wheat near-isogenic lines carrying the leaf rust resistance gene Lr47. Crop Sci. 48: 1441-1451.
    • (2008) Crop Sci , vol.48 , pp. 1441-1451
    • Brevis, J.C.1    Chicaiza, O.2    Khan, I.A.3    Jackson, L.4    Morris, C.F.5    Dubcovsky, J.6
  • 9
    • 38849106202 scopus 로고    scopus 로고
    • Chloroplastic protein NRIP1 mediates innate immune receptor recognition of a viral effector
    • 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.
    • (2008) Cell , vol.132 , pp. 449-462
    • Caplan, J.L.1    Mamillapalli, P.2    Burch-Smith, T.M.3    Czymmek, K.4    Dinesh-Kumar, S.P.5
  • 11
    • 84857854776 scopus 로고    scopus 로고
    • The mammalian START domain protein family in lipid transport in health and disease
    • Clark, B. J. (2012). The mammalian START domain protein family in lipid transport in health and disease. J. Endocrinol. 212: 257-275.
    • (2012) J. Endocrinol , vol.212 , pp. 257-275
    • Clark, B.J.1
  • 12
    • 0000399720 scopus 로고
    • Thermolysin is a suitable protease for probing the surface of intact pea chloroplasts
    • Cline, K., Werner-Washburne, M., Andrews, J., and Keegstra, K. (1984). Thermolysin is a suitable protease for probing the surface of intact pea chloroplasts. Plant Physiol. 75: 675-678.
    • (1984) Plant Physiol , vol.75 , pp. 675-678
    • Cline, K.1    Werner-Washburne, M.2    Andrews, J.3    Keegstra, K.4
  • 13
    • 79960210750 scopus 로고    scopus 로고
    • Programmed cell death in the plant immune system
    • Coll, N. S., Epple, P., and Dangl, J. L. (2011). Programmed cell death in the plant immune system. Cell Death Differ. 18: 1247-1256.
    • (2011) Cell Death Differ , vol.18 , pp. 1247-1256
    • Coll, N.S.1    Epple, P.2    Dangl, J.L.3
  • 14
    • 0043011573 scopus 로고    scopus 로고
    • Thylakoid-bound ascorbate peroxidase mutant exhibits impaired electron transport and photosynthetic activity
    • Danna, C. H., Bartoli, C. G., Sacco, F., Ingala, L. R., Santa-María, G. E., Guiamet, J. J., and Ugalde, R. A. (2003). Thylakoid-bound ascorbate peroxidase mutant exhibits impaired electron transport and photosynthetic activity. Plant Physiol. 132: 2116-2125.
    • (2003) Plant Physiol , vol.132 , pp. 2116-2125
    • Danna, C.H.1    Bartoli, C.G.2    Sacco, F.3    Ingala, L.R.4    Santa-María, G.E.5    Guiamet, J.J.6    Ugalde, R.A.7
  • 16
    • 84890071599 scopus 로고    scopus 로고
    • Monodehydroascorbate reductase gene, regulated by the wheat PN-2013 miRNA, contributes to adult wheat plant resistance to stripe rust through ROS metabolism
    • Feng, H., Wang, X., Zhang, Q., Fu, Y., Feng, C., Wang, B., Huang, L., and Kang, Z. (2014). Monodehydroascorbate reductase gene, regulated by the wheat PN-2013 miRNA, contributes to adult wheat plant resistance to stripe rust through ROS metabolism. Biochim. Biophys. Acta 1839: 1-12.
    • (2014) Biochim. Biophys. Acta , vol.1839 , pp. 1-12
    • Feng, H.1    Wang, X.2    Zhang, Q.3    Fu, Y.4    Feng, C.5    Wang, B.6    Huang, L.7    Kang, Z.8
  • 17
    • 0035943588 scopus 로고    scopus 로고
    • The digalactosyldiacylglycerol (DGDG) synthase DGD1 is inserted into the outer envelope membrane of chloroplasts in a manner independent of the general import pathway and does not depend on direct interaction with monogalactosyldiacylglycerol synthase for DGDG biosynthesis
    • Froehlich, J. E., Benning, C., and Dörmann, P. (2001). The digalactosyldiacylglycerol (DGDG) synthase DGD1 is inserted into the outer envelope membrane of chloroplasts in a manner independent of the general import pathway and does not depend on direct interaction with monogalactosyldiacylglycerol synthase for DGDG biosynthesis. J. Biol. Chem. 276: 31806-31812.
    • (2001) J. Biol. Chem , vol.276 , pp. 31806-31812
    • Froehlich, J.E.1    Benning, C.2    Dörmann, P.3
  • 19
    • 0029909597 scopus 로고    scopus 로고
    • Programmed cell death: A way of life for plants
    • Greenberg, J. T. (1996). Programmed cell death: a way of life for plants. Proc. Natl. Acad. Sci. USA 93: 12094-12097.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12094-12097
    • Greenberg, J.T.1
  • 21
    • 84979598521 scopus 로고    scopus 로고
    • Phosphoinositide-signaling is one component of a robust plant defense response
    • Hung, C. Y., Aspesi, P., Jr., Hunter, M. R., Lomax, A. W., and Perera, I. Y. (2014). Phosphoinositide-signaling is one component of a robust plant defense response. Front. Plant Sci. 5: 267.
    • (2014) Front. Plant Sci , vol.5 , pp. 267
    • Hung, C.Y.1    Aspesi, P.2    Hunter, M.R.3    Lomax, A.W.4    Perera, I.Y.5
  • 23
    • 0028171293 scopus 로고
    • H2O2 from the oxidative burst orchestrates the plant hypersensitive disease resistance response
    • Levine, A., Tenhaken, R., Dixon, R., and Lamb, C. (1994). H2O2 from the oxidative burst orchestrates the plant hypersensitive disease resistance response. Cell 79: 583-593.
    • (1994) Cell , vol.79 , pp. 583-593
    • Levine, A.1    Tenhaken, R.2    Dixon, R.3    Lamb, C.4
  • 24
    • 80052262460 scopus 로고    scopus 로고
    • Wheat flowering repressor VRN2 and promoter CO2 compete for interactions with NUCLEAR FACTOR-Y complexes
    • Li, C., Distelfeld, A., Comis, A., and Dubcovsky, J. (2011). Wheat flowering repressor VRN2 and promoter CO2 compete for interactions with NUCLEAR FACTOR-Y complexes. Plant J. 67: 763-773.
    • (2011) Plant J , vol.67 , pp. 763-773
    • Li, C.1    Distelfeld, A.2    Comis, A.3    Dubcovsky, J.4
  • 25
    • 17144366160 scopus 로고    scopus 로고
    • A highly conserved binding site in vesicle-associated membrane protein-associated protein (VAP) for the FFAT motif of lipid-binding proteins
    • Loewen, C. J. R., and Levine, T. P. (2005). A highly conserved binding site in vesicle-associated membrane protein-associated protein (VAP) for the FFAT motif of lipid-binding proteins. J. Biol. Chem. 280: 14097-14104.
    • (2005) J. Biol. Chem , vol.280 , pp. 14097-14104
    • Loewen, C.J.R.1    Levine, T.P.2
  • 26
    • 79953752182 scopus 로고    scopus 로고
    • Durable resistance to the wheat rusts: Integrating systems biology and traditional phenotype-based research methods to guide the deployment of resistance genes
    • Lowe, I., Cantu, D., and Dubcovsky, J. (2011). Durable resistance to the wheat rusts: integrating systems biology and traditional phenotype-based research methods to guide the deployment of resistance genes. Euphytica 179: 69-79.
    • (2011) Euphytica , vol.179 , pp. 69-79
    • Lowe, I.1    Cantu, D.2    Dubcovsky, J.3
  • 28
    • 76749113360 scopus 로고    scopus 로고
    • Arabidopsis chloroplastic ascorbate peroxidase isoenzymes play a dual role in photoprotection and gene regulation under photooxidative stress
    • Maruta, T., Tanouchi, A., Tamoi, M., Yabuta, Y., Yoshimura, K., Ishikawa, T., and Shigeoka, S. (2010). Arabidopsis chloroplastic ascorbate peroxidase isoenzymes play a dual role in photoprotection and gene regulation under photooxidative stress. Plant Cell Physiol. 51: 190-200.
    • (2010) Plant Cell Physiol , vol.51 , pp. 190-200
    • Maruta, T.1    Tanouchi, A.2    Tamoi, M.3    Yabuta, Y.4    Yoshimura, K.5    Ishikawa, T.6    Shigeoka, S.7
  • 30
    • 84881435452 scopus 로고    scopus 로고
    • Impacts of resistance gene genetics, function, and evolution on a durable future
    • Michelmore, R. W., Christopoulou, M., and Caldwell, K. S. (2013). Impacts of resistance gene genetics, function, and evolution on a durable future. Annu. Rev. Phytopathol. 51: 291-319.
    • (2013) Annu. Rev. Phytopathol , vol.51 , pp. 291-319
    • Michelmore, R.W.1    Christopoulou, M.2    Caldwell, K.S.3
  • 31
    • 84884910720 scopus 로고    scopus 로고
    • Multiple fates of non-mature lumenal proteins in thylakoids
    • Midorikawa, T., and Inoue, K. (2013). Multiple fates of non-mature lumenal proteins in thylakoids. Plant J. 76: 73-86.
    • (2013) Plant J , vol.76 , pp. 73-86
    • Midorikawa, T.1    Inoue, K.2
  • 33
    • 77951009331 scopus 로고    scopus 로고
    • Osmotic stress-induced phosphoinositide and inositol phosphate signalling in plants
    • Munnik, T., and Vermeer, J. E. M. (2010). Osmotic stress-induced phosphoinositide and inositol phosphate signalling in plants. Plant Cell Environ. 33: 655-669.
    • (2010) Plant Cell Environ , vol.33 , pp. 655-669
    • Munnik, T.1    Vermeer, J.E.M.2
  • 34
    • 34547677722 scopus 로고    scopus 로고
    • Development of series of gateway binary vectors, pGWBs, for realizing efficient construction of fusion genes for plant transformation
    • Nakagawa, T., Kurose, T., Hino, T., Tanaka, K., Kawamukai, M., Niwa, Y., Toyooka, K., Matsuoka, K., Jinbo, T., and Kimura, T. (2007). Development of series of gateway binary vectors, pGWBs, for realizing efficient construction of fusion genes for plant transformation. J. Biosci. Bioeng. 104: 34-41.
    • (2007) J. Biosci. Bioeng , vol.104 , pp. 34-41
    • Nakagawa, T.1    Kurose, T.2    Hino, T.3    Tanaka, K.4    Kawamukai, M.5    Niwa, Y.6    Toyooka, K.7    Matsuoka, K.8    Jinbo, T.9    Kimura, T.10
  • 35
    • 0036984378 scopus 로고    scopus 로고
    • Engineering deoxynivalenol metabolism in wheat through the expression of a fungal trichothecene acetyltransferase gene
    • Okubara, P. A., Blechl, A. E., McCormick, S. P., Alexander, N. J., Dill-Macky, R., and Hohn, T. M. (2002). Engineering deoxynivalenol metabolism in wheat through the expression of a fungal trichothecene acetyltransferase gene. Theor. Appl. Genet. 106: 74-83.
    • (2002) Theor. Appl. Genet , vol.106 , pp. 74-83
    • Okubara, P.A.1    Blechl, A.E.2    McCormick, S.P.3    Alexander, N.J.4    Dill-Macky, R.5    Hohn, T.M.6
  • 36
    • 0842285694 scopus 로고    scopus 로고
    • Phosphatidic acid induces leaf cell death in Arabidopsis by activating the Rhorelated small G protein GTPase-mediated pathway of reactive oxygen species generation
    • Park, J., Gu, Y., Lee, Y., Yang, Z., and Lee, Y. (2004). Phosphatidic acid induces leaf cell death in Arabidopsis by activating the Rhorelated small G protein GTPase-mediated pathway of reactive oxygen species generation. Plant Physiol. 134: 129-136.
    • (2004) Plant Physiol , vol.134 , pp. 129-136
    • Park, J.1    Gu, Y.2    Lee, Y.3    Yang, Z.4    Lee, Y.5
  • 37
    • 33644844932 scopus 로고    scopus 로고
    • Ascorbic acid deficiency activates cell death and disease resistance responses in Arabidopsis
    • Pavet, V., Olmos, E., Kiddle, G., Mowla, S., Kumar, S., Antoniw, J., Alvarez, M. E., and Foyer, C. H. (2005). Ascorbic acid deficiency activates cell death and disease resistance responses in Arabidopsis. Plant Physiol. 139: 1291-1303.
    • (2005) Plant Physiol , vol.139 , pp. 1291-1303
    • Pavet, V.1    Olmos, E.2    Kiddle, G.3    Mowla, S.4    Kumar, S.5    Antoniw, J.6    Alvarez, M.E.7    Foyer, C.H.8
  • 38
    • 33746368041 scopus 로고    scopus 로고
    • Evidence for an ER to Golgi to chloroplast protein transport pathway
    • Radhamony, R. N., and Theg, S. M. (2006). Evidence for an ER to Golgi to chloroplast protein transport pathway. Trends Cell Biol. 16: 385-387.
    • (2006) Trends Cell Biol , vol.16 , pp. 385-387
    • Radhamony, R.N.1    Theg, S.M.2
  • 39
    • 79951767425 scopus 로고    scopus 로고
    • Phosphatidic acid production in chitosan-elicited tomato cells, via both phospholipase D and phospholipase C/diacylglycerol kinase, requires nitric oxide
    • Raho, N., Ramirez, L., Lanteri, M. L., Gonorazky, G., Lamattina, L., ten Have, A., and Laxalt, A. M. (2011). Phosphatidic acid production in chitosan-elicited tomato cells, via both phospholipase D and phospholipase C/diacylglycerol kinase, requires nitric oxide. J. Plant Physiol. 168: 534-539.
    • (2011) J. Plant Physiol , vol.168 , pp. 534-539
    • Raho, N.1    Ramirez, L.2    Lanteri, M.L.3    Gonorazky, G.4    Lamattina, L.5    ten Have, A.6    Laxalt, A.M.7
  • 40
    • 58149235147 scopus 로고    scopus 로고
    • Highly efficient Agrobacterium-mediated transformation of wheat via in planta inoculation
    • H. D. Jones and P. R. Shewry, eds (New York: Humana Press)
    • Risacher, T., Craze, M., Bowden, S., Paul, W., and Barsby, T. (2009). Highly efficient Agrobacterium-mediated transformation of wheat via in planta inoculation. In Methods in Molecular Biology: Transgenic Wheat, Barley and Oats, H. D. Jones and P. R. Shewry, eds (New York: Humana Press), pp. 115-124.
    • (2009) In Methods in Molecular Biology: Transgenic Wheat, Barley and Oats , pp. 115-124
    • Risacher, T.1    Craze, M.2    Bowden, S.3    Paul, W.4    Barsby, T.5
  • 41
    • 33646831324 scopus 로고    scopus 로고
    • Protein-protein interactions of tandem affinity purification-tagged protein kinases in rice
    • Rohila, J. S., 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
  • 42
    • 0344718457 scopus 로고    scopus 로고
    • Mapping of the leaf rust resistance gene Lr3 on chromosome 6B of Sinvalocho MA wheat
    • Sacco, F., Suarez, E. Y., and Naranjo, T. (1998). Mapping of the leaf rust resistance gene Lr3 on chromosome 6B of Sinvalocho MA wheat. Genome 41: 686-690.
    • (1998) Genome , vol.41 , pp. 686-690
    • Sacco, F.1    Suarez, E.Y.2    Naranjo, T.3
  • 43
    • 4844226474 scopus 로고    scopus 로고
    • START lipid/sterol-binding domains are amplified in plants and are predominantly associated with homeodomain transcription factors
    • Schrick, K., Nguyen, D., Karlowski, W. M., and Mayer, K. F. X. (2004). START lipid/sterol-binding domains are amplified in plants and are predominantly associated with homeodomain transcription factors. Genome Biol. 5: R41.
    • (2004) Genome Biol , vol.5
    • Schrick, K.1    Nguyen, D.2    Karlowski, W.M.3    Mayer, K.F.X.4
  • 45
    • 84871749722 scopus 로고    scopus 로고
    • The chloroplast protein import system: From algae to trees
    • Shi, L. X., and Theg, S. M. (2013). The chloroplast protein import system: From algae to trees. Biochim. Biophys. Acta 1833: 314-331.
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 314-331
    • Shi, L.X.1    Theg, S.M.2
  • 47
    • 84856170491 scopus 로고    scopus 로고
    • How do plants achieve immunity? Defence without specialized immune cells
    • Spoel, S. H., and Dong, X. (2012). How do plants achieve immunity? Defence without specialized immune cells. Nat. Rev. Immunol. 12: 89-100.
    • (2012) Nat. Rev. Immunol , vol.12 , pp. 89-100
    • Spoel, S.H.1    Dong, X.2
  • 48
    • 0033601180 scopus 로고    scopus 로고
    • Tic40, a new "old" subunit of the chloroplast protein import translocon
    • Stahl, T., Glockmann, C., Soll, J., and Heins, L. (1999). Tic40, a new "old" subunit of the chloroplast protein import translocon. J. Biol. Chem. 274: 37467-37472.
    • (1999) J. Biol. Chem , vol.274 , pp. 37467-37472
    • Stahl, T.1    Glockmann, C.2    Soll, J.3    Heins, L.4
  • 49
    • 84888396486 scopus 로고    scopus 로고
    • Alternative splicing at the intersection of biological timing, development, and stress responses
    • Staiger, D., and Brown, J. W. S. (2013). Alternative splicing at the intersection of biological timing, development, and stress responses. Plant Cell 25: 3640-3656.
    • (2013) Plant Cell , vol.25 , pp. 3640-3656
    • Staiger, D.1    Brown, J.W.S.2
  • 51
    • 33644796704 scopus 로고    scopus 로고
    • Regulation of plant defense responses in Arabidopsis by EDR2, a PH and START domain-containing protein
    • Tang, D., Ade, J., Frye, C. A., and Innes, R. W. (2005). Regulation of plant defense responses in Arabidopsis by EDR2, a PH and START domain-containing protein. Plant J. 44: 245-257.
    • (2005) Plant J , vol.44 , pp. 245-257
    • Tang, D.1    Ade, J.2    Frye, C.A.3    Innes, R.W.4
  • 52
    • 79955461974 scopus 로고    scopus 로고
    • Molecular, cellular, and physiological responses to phosphatidic acid formation in plants
    • Testerink, C., and Munnik, T. (2011). Molecular, cellular, and physiological responses to phosphatidic acid formation in plants. J. Exp. Bot. 62: 2349-2361.
    • (2011) J. Exp. Bot , vol.62 , pp. 2349-2361
    • Testerink, C.1    Munnik, T.2
  • 53
    • 77952089074 scopus 로고    scopus 로고
    • ROS in biotic interactions
    • Torres, M. A. (2010). ROS in biotic interactions. Physiol. Plant. 138: 414-429.
    • (2010) Physiol. Plant , vol.138 , pp. 414-429
    • Torres, M.A.1
  • 54
    • 36349010952 scopus 로고    scopus 로고
    • A novel serine/proline-rich domain in combination with a transmembrane domain is required for the insertion of AtTic40 into the inner envelope membrane of chloroplasts
    • Tripp, J., Inoue, K., Keegstra, K., and Froehlich, J. E. (2007). A novel serine/proline-rich domain in combination with a transmembrane domain is required for the insertion of AtTic40 into the inner envelope membrane of chloroplasts. Plant J. 52: 824-838.
    • (2007) Plant J , vol.52 , pp. 824-838
    • Tripp, J.1    Inoue, K.2    Keegstra, K.3    Froehlich, J.E.4
  • 55
    • 34548219040 scopus 로고    scopus 로고
    • EDR2 negatively regulates salicylic acid-based defenses and cell death during powdery mildew infections of Arabidopsis thaliana
    • Vorwerk, S., Schiff, C., Santamaria, M., Koh, S., Nishimura, M., Vogel, J., Somerville, C., and Somerville, S. (2007). EDR2 negatively regulates salicylic acid-based defenses and cell death during powdery mildew infections of Arabidopsis thaliana. BMC Plant Biol. 7: 35.
    • (2007) BMC Plant Biol , vol.7 , pp. 35
    • Vorwerk, S.1    Schiff, C.2    Santamaria, M.3    Koh, S.4    Nishimura, M.5    Vogel, J.6    Somerville, C.7    Somerville, S.8
  • 56
    • 46549089201 scopus 로고    scopus 로고
    • Histochemical studies on the accumulation of reactive oxygen species (O2-and H2O2) in the incompatible and compatible interaction of wheat-Puccinia striiformis f
    • Wang, C. F., Huang, L. L., Buchenauer, H., Han, Q. M., Zhang, H. C., and Kang, Z. S. (2007). Histochemical studies on the accumulation of reactive oxygen species (O2-and H2O2) in the incompatible and compatible interaction of wheat-Puccinia striiformis f. sp. tritici. Physiol. Mol. Plant Pathol. 71: 230-239.
    • (2007) Sp. tritici. Physiol. Mol. Plant Pathol , vol.71 , pp. 230-239
    • Wang, C.F.1    Huang, L.L.2    Buchenauer, H.3    Han, Q.M.4    Zhang, H.C.5    Kang, Z.S.6
  • 57
    • 84883422180 scopus 로고    scopus 로고
    • A comparative approach expands the protein-protein interaction node of the immune receptor XA21 in wheat and rice
    • Yang, B., Ruan, R., Cantu, D., Wang, X., Ji, W., Ronald, P. C., and Dubcovsky, J. (2013). A comparative approach expands the protein-protein interaction node of the immune receptor XA21 in wheat and rice. Genome 56: 315-326.
    • (2013) Genome , vol.56 , pp. 315-326
    • Yang, B.1    Ruan, R.2    Cantu, D.3    Wang, X.4    Ji, W.5    Ronald, P.C.6    Dubcovsky, J.7


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