메뉴 건너뛰기




Volumn 27, Issue 5, 2014, Pages 403-414

Alternative cell death mechanisms determine epidermal resistance in incompatible barley-ustilago interactions

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE 3; FUNGAL PROTEIN; HYDROGEN PEROXIDE; VEGETABLE PROTEIN;

EID: 84898629154     PISSN: 08940282     EISSN: None     Source Type: Journal    
DOI: 10.1094/MPMI-10-13-0317-R     Document Type: Article
Times cited : (24)

References (63)
  • 1
    • 33749989815 scopus 로고    scopus 로고
    • Multivesicular compartments proliferate in susceptible and resistant mla12-barley leaves in response to infection by the biotrophic powdery mildew fungus
    • An, Q., Ehlers, K., Kogel, K.-H., van Bel, A. J. E., and Hückelhoven, R. 2006. Multivesicular compartments proliferate in susceptible and resistant MLA12-barley leaves in response to infection by the biotrophic powdery mildew fungus. New Phytol. 172:563-576.
    • (2006) New Phytol. , vol.172 , pp. 563-576
    • An, Q.1    Ehlers, K.2    Kogel, K.-H.3    Van Bel, A.J.E.4    Hückelhoven, R.5
  • 2
    • 58549102305 scopus 로고    scopus 로고
    • Over-expression of the cell death regulator bax inhibitor-1 in barley confers reduced or enhanced susceptibility to distinct fungal pathogens
    • Babaeizad, V., Imani, J., Kogel, K.-H., Eichmann, R., and Hückelhoven, R. 2009. Over-expression of the cell death regulator BAX inhibitor-1 in barley confers reduced or enhanced susceptibility to distinct fungal pathogens. Theor. Appl. Genet. 118:455-463.
    • (2009) Theor. Appl. Genet. , vol.118 , pp. 455-463
    • Babaeizad, V.1    Imani, J.2    Kogel, K.-H.3    Eichmann, R.4    Hückelhoven, R.5
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principles of protein-dye binding
    • Bradford, M. 1976. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principles of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.1
  • 10
    • 19444370899 scopus 로고    scopus 로고
    • Visualization of autophagy in arabidopsis using the fluorescent dye monodansylcadaverine and a gfp-Atatg8e fusion protein
    • Contento, A. L., Xiong, Y., and Bassham, D. C. 2005. Visualization of autophagy in Arabidopsis using the fluorescent dye monodansylcadaverine and a GFP-AtATG8e fusion protein. Plant J. 42:598-608.
    • (2005) Plant J. , vol.42 , pp. 598-608
    • Contento, A.L.1    Xiong, Y.2    Bassham, D.C.3
  • 11
    • 0032497567 scopus 로고    scopus 로고
    • Caspases and programmed cell death in the hypersensitive response of plants to pathogens
    • Del Pozo, O., and Lam, E. 1998. Caspases and programmed cell death in the hypersensitive response of plants to pathogens. Curr. Biol. 8:1129-1132.
    • (1998) Curr. Biol. , vol.8 , pp. 1129-1132
    • Del Pozo, O.1    Lam, E.2
  • 12
    • 84877614712 scopus 로고    scopus 로고
    • Apoplastic immunity and its suppression by filamentous plant pathogens
    • Doehlemann, G., and Hemetsberger, C. 2013. Apoplastic immunity and its suppression by filamentous plant pathogens. New Phytol. 198:1001-1016.
    • (2013) New Phytol. , vol.198 , pp. 1001-1016
    • Doehlemann, G.1    Hemetsberger, C.2
  • 14
    • 1942504703 scopus 로고    scopus 로고
    • The barley apoptosis suppressor homologue bax inhibitor-1 compromises nonhost penetration resistance of barley to the inappropriate pathogen blumeria graminis f. Sp. Tritici
    • Eichmann, R., Holger, S., Kogel, K. H., and Hückelhoven, R. 2004. The barley apoptosis suppressor homologue Bax inhibitor-1 compromises nonhost penetration resistance of barley to the inappropriate pathogen Blumeria graminis f. sp. tritici. Mol. Plant-Microbe Interact. 17:484-490.
    • (2004) Mol. Plant-Microbe Interact. , vol.17 , pp. 484-490
    • Eichmann, R.1    Holger, S.2    Kogel, K.H.3    Hückelhoven, R.4
  • 17
    • 0029978182 scopus 로고    scopus 로고
    • Sequential activation of ice-like and cpp32-like proteases during fas-mediated apoptosis
    • Enari, M., Talanian, R. V., Wong, W. W., and Nagata, S. 1996. Sequential activation of ICE-like and CPP32-like proteases during Fas-mediated apoptosis. Nature 380:723-726.
    • (1996) Nature , vol.380 , pp. 723-726
    • Enari, M.1    Talanian, R.V.2    Wong, W.W.3    Nagata, S.4
  • 18
    • 84870234936 scopus 로고    scopus 로고
    • Devdase activity is induced in potato leaves during phytophthora infestans infection
    • Fernández, M. B., Daleo, G. R., and Guevara, M. G. 2012. DEVDase activity is induced in potato leaves during Phytophthora infestans infection. Plant Physiol. Biochem. 61:197-203.
    • (2012) Plant Physiol. Biochem. , vol.61 , pp. 197-203
    • Fernández, M.B.1    Daleo, G.R.2    Guevara, M.G.3
  • 19
    • 1342305253 scopus 로고    scopus 로고
    • The role and regulation of programmed cell death in plant-pathogen interactions
    • Greenberg, J. T., and Yao, N. 2004. The role and regulation of programmed cell death in plant-pathogen interactions. Cell. Microbiol. 6:201-211.
    • (2004) Cell. Microbiol. , vol.6 , pp. 201-211
    • Greenberg, J.T.1    Yao, N.2
  • 20
    • 84866743040 scopus 로고    scopus 로고
    • The proteasome is responsible for caspase-3-like activity during xylem development
    • Han, J. J., Lin, W., Oda, Y., Cui, K. M., Fukuda, H., and He, X. Q. 2012. The proteasome is responsible for caspase-3-like activity during xylem development. Plant J. 72:129-141.
    • (2012) Plant J. , vol.72 , pp. 129-141
    • Han, J.J.1    Lin, W.2    Oda, Y.3    Cui, K.M.4    Fukuda, H.5    He, X.Q.6
  • 23
    • 0034484977 scopus 로고    scopus 로고
    • Hypersensitive response-related cell death
    • Heath, M. C. 2000. Hypersensitive response-related cell death. Plant Mol. Biol. 44:321-334.
    • (2000) Plant Mol. Biol. , vol.44 , pp. 321-334
    • Heath, M.C.1
  • 24
    • 84862497259 scopus 로고    scopus 로고
    • The ustilago maydis effector pep1 suppresses plant immunity by inhibition of host peroxidase activity
    • Published online
    • Hemetsberger, C., Herrberger, C., Zechmann, B., Hillmer, M., and Doehlemann, G. 2012. The Ustilago maydis effector Pep1 suppresses plant immunity by inhibition of host peroxidase activity. PloS Pathog. 8:e1002684. Published online.
    • (2012) PloS Pathog. , vol.8
    • Hemetsberger, C.1    Herrberger, C.2    Zechmann, B.3    Hillmer, M.4    Doehlemann, G.5
  • 25
    • 79960222617 scopus 로고    scopus 로고
    • Role of autophagy in disease resistance and hypersensitive response-Associated cell death
    • Hofius, D., Munch, D., Bressendorff, S., Mundy, J., and Petersen, M. 2011. Role of autophagy in disease resistance and hypersensitive response-Associated cell death. Cell Death Differ. 18:1257-1262.
    • (2011) Cell Death Differ. , vol.18 , pp. 1257-1262
    • Hofius, D.1    Munch, D.2    Bressendorff, S.3    Mundy, J.4    Petersen, M.5
  • 27
    • 3242806002 scopus 로고    scopus 로고
    • Bax inhibitor-1, an ancient cell death suppressor in animals and plants with prokaryotic relatives
    • Hückelhoven, R. 2004. BAX Inhibitor-1, an ancient cell death suppressor in animals and plants with prokaryotic relatives. Apoptosis 9:299-307.
    • (2004) Apoptosis , vol.9 , pp. 299-307
    • Hückelhoven, R.1
  • 28
    • 33751100626 scopus 로고    scopus 로고
    • The plant immune system
    • Jones, J. D., and Dangl, J. L. 2006. The plant immune system. Nature 444:323-329.
    • (2006) Nature , vol.444 , pp. 323-329
    • Jones, J.D.1    Dangl, J.L.2
  • 29
    • 84876840236 scopus 로고    scopus 로고
    • Cell death control: The interplay of apoptosis and autophagy in the pathogenicity of sclerotinia sclerotiorum
    • Published online
    • Kabbage, M., Williams, B., and Dickman, M. B. 2013. Cell death control: The interplay of apoptosis and autophagy in the pathogenicity of Sclerotinia sclerotiorum. PloS Pathog. 9:e1003287. Published online.
    • (2013) PloS Pathog. , vol.9
    • Kabbage, M.1    Williams, B.2    Dickman, M.B.3
  • 30
    • 0035834172 scopus 로고    scopus 로고
    • Mammalian bax-induced plant cell death can be down-regulated by overexpression of arabidopsis bax inhibitor-1 (atbi-1)
    • Kawai-Yamada, M., Jin, U., Yoshinaga, K., Hirata, A., and Uchimiya, H. 2001. Mammalian Bax-induced plant cell death can be down-regulated by overexpression of Arabidopsis Bax inhibitor-1 (AtBI-1). Proc. Natl. Acad. Sci. U.S.A. 98:12295-12300.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 12295-12300
    • Kawai-Yamada, M.1    Jin, U.2    Yoshinaga, K.3    Hirata, A.4    Uchimiya, H.5
  • 31
    • 0001017429 scopus 로고
    • Comparison of histological and physiological responses to phakopsora pachyrhizi in resistant and susceptible soybean
    • Keogh, R. C., Deverall, B. J., and McLeod, S. 1980. Comparison of histological and physiological responses to Phakopsora pachyrhizi in resistant and susceptible soybean. Trans. Br. Mycol. Sci. 74:329-333.
    • (1980) Trans. Br. Mycol. Sci. , vol.74 , pp. 329-333
    • Keogh, R.C.1    Deverall, B.J.2    McLeod, S.3
  • 32
    • 38949108670 scopus 로고    scopus 로고
    • Guidelines for the use and interpretation of assays for monitoring autophagy in higher eukaryotes
    • Klionsky, D. J., Abeliovich, H., Agostinis, P., Agrawal, D. K., Aliev, G., Askew, D. S., Baba, M., Baehrecke, E. H., Bahr, B. A., Ballabio, A., Bamber, B. A., Bassham, D. C., Bergamini, E., Bi, X., Biard-Piechaczyk, M., Blum, J. S., Bredesen, D. E., Brodsky, J. L., Brumell, J. H., Brunk, U. T., Bursch, W., Camougrand, N., Cebollero, E., Cecconi, F., Chen, Y., Chin, L. S., Choi, A., Chu, C. T., Chung, J., Clarke, P. G., Clark, R. S., Clarke, S. G., Clavé, C., Cleveland, J. L., Codogno, P., Colombo, M. I., Coto-Montes, A., Cregg, J. M., Cuervo, A. M., Debnath, J., Demarchi, F., Dennis, P. B., Dennis, P. A., Deretic, V., Devenish, R. J., Di Sano, F., Dice, J. F., Difiglia, M., Dinesh-Kumar, S., Distelhorst, C. W., Djavaheri-Mergny, M., Dorsey, F. C., Dröge, W., Dron, M., Dunn, W. A., Jr., Duszenko, M., Eissa, N. T., Elazar, Z., Esclatine, A., Eskelinen, E. L., Fésüs, L., Finley, K. D., Fuentes, J. M., Fueyo, J., Fujisaki, K., Galliot, B., Gao, F. B., Gewirtz, D. A., Gibson, S. B., Gohla, A., Goldberg, A. L., Gonzalez, R., González-Estévez, C., Gorski, S., Gottlieb, R. A., Häussinger, D., He, Y. W., Heidenreich, K., Hill, J. A., Høyer-Hansen, M., Hu, X., Huang, W. P., Iwasaki, A., Jää ttelä, M., Jackson, W. T., Jiang, X., Jin, S., Johansen, T., Jung, J. U., Kadowaki, M., Kang, C., Kelekar, A., Kessel, D. H., Kiel, J. A., Kim, H. P., Kimchi, A., Kinsella, T. J., Kiselyov, K., Kitamoto, K., Knecht, E., Komatsu, M., Kominami, E., Kondo, S., Kovács, A. L., Kroemer, G., Kuan, C. Y., Kumar, R., Kundu, M., Landry, J., Laporte, M., Le, W., Lei, H. Y., Lenardo, M. J., Levine, B., Lieberman, A., Lim, K. L., Lin, F. C., Liou, W., Liu, L. F., Lopez-Berestein, G., López-Otín, C., Lu, B., Macleod, K. F., Malorni, W., Martinet, W., Matsuoka, K., Mautner, J., Meijer, A. J., Meléndez, A., Michels, P., Miotto, G., Mistiaen, W. P., Mizushima, N., Mograbi, B., Monastyrska, I., Moore, M. N., Moreira, P. I., Moriyasu, Y., Motyl, T., Münz, C., Murphy, L. O., Naqvi, N. I., Neufeld, T. P., Nishino, I., Nixon, R. A., Noda, T., Nürnberg, B., Ogawa, M., Oleinick, N. L., Olsen, L. J., Ozpolat, B., Paglin, S., Palmer, G. E., Papassideri, I., Parkes, M., Perlmutter, D. H., Perry, G., Piacentini, M., Pinkas-Kramarski, R., Prescott, M., Proikas-Cezanne, T., Raben, N., Rami, A., Reggiori, F., Rohrer, B., Rubinsztein, D. C., Ryan, K. M., Sadoshima, J., Sakagami, H., Sakai, Y., Sandri, M., Sasakawa, C., Sass, M., Schneider, C., Seglen, P. O., Seleverstov, O., Settleman, J., Shacka, J. J., Shapiro, I. M., Sibirny, A., Silva-Zacarin, E. C., Simon, H. U., Simone, C., Simonsen, A., Smith, M. A., Spanel-Borowski, K., Srinivas, V., Steeves, M., Stenmark, H., Stromhaug, P. E., Subauste, C. S., Sugimoto, S., Sulzer, D., Suzuki, T., Swanson, M. S., Tabas, I., Takeshita, F., Talbot, N. J., Tallóczy, Z., Tanaka, K., Tanaka, K., Tanida, I., Taylor, G. S., Taylor, J. P., Terman, A., Tettamanti, G., Thompson, C. B., Thumm, M., Tolkovsky, A. M., Tooze, S. A., Truant, R., Tumanovska, L. V., Uchiyama, Y., Ueno, T., Uzcátegui, N. L., van der Klei, I., Vaquero, E. C., Vellai, T., Vogel, M. W., Wang, H. G., Webster, P., Wiley, J. W., Xi, Z., Xiao, G., Yahalom, J., Yang, J. M., Yap, G., Yin, X. M., Yoshimori, T., Yu, L., Yue, Z., Yuzaki, M., Zabirnyk, O., Zheng, X., Zhu, X., and Deter, R. L. 2008. Guidelines for the use and interpretation of assays for monitoring autophagy in higher eukaryotes. Autophagy 4:151-75.
    • (2008) Autophagy , vol.4 , pp. 151-175
    • Klionsky, D.J.1    Abeliovich, H.2    Agostinis, P.3    Agrawal, D.K.4    Aliev, G.5    Askew, D.S.6    Baba, M.7
  • 33
    • 25444522319 scopus 로고    scopus 로고
    • Vacuolar processing enzyme is essential for mycotoxin-induced cell death in arabidopsis thaliana
    • Kuroyanagi, M., Yamada, K., Hatsugai, N., Kondo, M., Nishimura, M., and Hara-Nishimura, I. 2005. Vacuolar processing enzyme is essential for mycotoxin-induced cell death in Arabidopsis thaliana. J. Biol. Chem. 280:32914-32920.
    • (2005) J. Biol. Chem. , vol.280 , pp. 32914-32920
    • Kuroyanagi, M.1    Yamada, K.2    Hatsugai, N.3    Kondo, M.4    Nishimura, M.5    Hara-Nishimura, I.6
  • 34
    • 84875738550 scopus 로고    scopus 로고
    • The rab gtpase rabg3b positively regulates autophagy and immunityassociated hypersensitive cell death in arabidopsis
    • Kwon, S. I., Cho, H. J., Kim, S. R., and Park, O. K. 2013. The Rab GTPase RabG3b positively regulates autophagy and immunityassociated hypersensitive cell death in Arabidopsis. Plant Physiol. 161:1722-1736.
    • (2013) Plant Physiol. , vol.161 , pp. 1722-1736
    • Kwon, S.I.1    Cho, H.J.2    Kim, S.R.3    Park, O.K.4
  • 35
    • 14744299759 scopus 로고    scopus 로고
    • Vacuolar proteases livening up programmed cell death
    • Lam, E. 2005. Vacuolar proteases livening up programmed cell death. Trends Cell Biol. 15:124-127.
    • (2005) Trends Cell Biol. , vol.15 , pp. 124-127
    • Lam, E.1
  • 37
    • 19344368318 scopus 로고    scopus 로고
    • Autophagy regulates programmed cell death during the plant innate immune response
    • Liu, Y., Schiff, M., Czymmek, K., Talloczy, Z., Levine, B., and Dinesh-Kumar, S. P. 2005. Autophagy regulates programmed cell death during the plant innate immune response. Cell 121:567-577.
    • (2005) Cell , vol.121 , pp. 567-577
    • Liu, Y.1    Schiff, M.2    Czymmek, K.3    Talloczy, Z.4    Levine, B.5    Dinesh-Kumar, S.P.6
  • 38
    • 84861666869 scopus 로고    scopus 로고
    • Programmed cell death in c. Elegans, mammals and plants
    • Lord, C. E. N., and Gunawardena, A. H. L. A. N. 2012. Programmed cell death in C. elegans, mammals and plants. Eur. J. Cell Biol. 91:603-613.
    • (2012) Eur. J. Cell Biol. , vol.91 , pp. 603-613
    • Lord, C.E.N.1    Gunawardena, A.H.L.A.N.2
  • 39
    • 34548188741 scopus 로고    scopus 로고
    • Self-eating and self-killing: Crosstalk between autophagy and apoptosis
    • Maiuri, M. C., Zalckvar, E., Kimchi, A., and Kroemer, G. 2007. Self-eating and self-killing: Crosstalk between autophagy and apoptosis. Nat. Rev. Mol. Cell. Biol. 9:741-52.
    • (2007) Nat. Rev. Mol. Cell. Biol. , vol.9 , pp. 741-752
    • Maiuri, M.C.1    Zalckvar, E.2    Kimchi, A.3    Kroemer, G.4
  • 40
    • 34548321733 scopus 로고    scopus 로고
    • 2 detoxification is required for virulence
    • 2 detoxification is required for virulence. Plant Cell 19:2293-2309.
    • (2007) Plant Cell , vol.19 , pp. 2293-2309
    • Molina, L.1    Kahmann, R.2
  • 42
    • 0036581160 scopus 로고    scopus 로고
    • Relative expression software tool (rest©) for group-wise comparison and statistical analysis of relative expression results in real-Time pcr
    • Pfaffl, M. W., Horgan, G. W., and Dempfle, L. 2002. Relative expression software tool (REST©) for group-wise comparison and statistical analysis of relative expression results in real-Time PCR. Nucleic Acids Res. 30:1-10.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 1-10
    • Pfaffl, M.W.1    Horgan, G.W.2    Dempfle, L.3
  • 43
    • 84859075052 scopus 로고    scopus 로고
    • The mutualistic fungus piriformospora indica colonizes arabidopsis roots by inducing an endoplasmic reticulum stress-Triggered caspase-dependent cell death
    • Qiang, X., Zechmann, B., Reitz, M. U., Kogel, K. H., and Schäfer, P. 2012. The mutualistic fungus Piriformospora indica colonizes Arabidopsis roots by inducing an endoplasmic reticulum stress-Triggered caspase-dependent cell death. Plant Cell 24:794-809.
    • (2012) Plant Cell , vol.24 , pp. 794-809
    • Qiang, X.1    Zechmann, B.2    Reitz, M.U.3    Kogel, K.H.4    Schäfer, P.5
  • 44
    • 43149104751 scopus 로고    scopus 로고
    • Programmed cell death in plants: Distinguishing between different modes
    • Reape, T. J., Molony, E. M., and McCabe, P. F. 2008. Programmed cell death in plants: Distinguishing between different modes. J. Exp. Bot. 59:435-444.
    • (2008) J. Exp. Bot. , vol.59 , pp. 435-444
    • Reape, T.J.1    Molony, E.M.2    McCabe, P.F.3
  • 45
    • 84858012913 scopus 로고    scopus 로고
    • No, ros, and cell death associated with caspase-like activity increase in stress-induced microspore embryogenesis of barley
    • Rodríguez-Serrano, M., Bárány, I., Prem, D., Coronado, M. J., Risueño, M. C., and Testillano, P. S. 2012. NO, ROS, and cell death associated with caspase-like activity increase in stress-induced microspore embryogenesis of barley. J. Exp. Bot. 63:2007-2024.
    • (2012) J. Exp. Bot. , vol.63 , pp. 2024
    • Rodríguez-Serrano, M.1    Bárány, I.2    Prem, D.3    Coronado, M.J.4    Risueño, M.C.5    Testillano, P.S.6
  • 48
    • 79955677000 scopus 로고    scopus 로고
    • Autophagic cell death: Loch ness monster or endangered species?
    • Shen, H. M., and Codogno, P. 2011. Autophagic cell death: Loch Ness monster or endangered species? Autophagy 7:457-465.
    • (2011) Autophagy , vol.7 , pp. 457-465
    • Shen, H.M.1    Codogno, P.2
  • 49
    • 79952302258 scopus 로고    scopus 로고
    • Of pamps and effectors: The blurred pti-eti dichotomy
    • Thomma, B. P., Nürnberger, T., and Joosten, M. H. 2011. Of PAMPs and effectors: The blurred PTI-ETI dichotomy. Plant Cell 23:4-15.
    • (2011) Plant Cell , vol.23 , pp. 4-15
    • Thomma, B.P.1    Nürnberger, T.2    Joosten, M.H.3
  • 51
    • 0033638182 scopus 로고    scopus 로고
    • Identification of aracaspases and metacaspases: Two ancient families of caspase-like proteins, one of which plays a key role in malt lymphoma
    • Uren, A. G., O'Rourke, K., Aravind, L., Pisabarro, M. T., Seshagiri, S., Koonin, E. V., and Dixit, V. M. 2000. Identification of aracaspases and Metacaspases: Two ancient families of caspase-like proteins, one of which plays a key role in MALT lymphoma. Mol. Cell 6:961-967.
    • (2000) Mol. Cell , vol.6 , pp. 961-967
    • Uren, A.G.1    O'Rourke, K.2    Aravind, L.3    Pisabarro, M.T.4    Seshagiri, S.5    Koonin, E.V.6    Dixit, V.M.7
  • 52
    • 78650334203 scopus 로고    scopus 로고
    • Systemic virus-induced gene silencing allows functional characterization of maize genes during biotrophic interaction with ustilago maydis
    • van der Linde, K., Kastner, C., Kumlehn, J., Kahmann, R., and Doehlemann, G. 2011. Systemic virus-induced gene silencing allows functional characterization of maize genes during biotrophic interaction with Ustilago maydis. New Phytol. 189:471-483.
    • (2011) New Phytol. , vol.189 , pp. 471-483
    • Van Der Linde, K.1    Kastner, C.2    Kumlehn, J.3    Kahmann, R.4    Doehlemann, G.5
  • 53
    • 80054099703 scopus 로고    scopus 로고
    • Classes of programmed cell death in plants, compared to those in animals
    • van Doorn, W. G. 2011. Classes of programmed cell death in plants, compared to those in animals. J. Exp. Bot. 62:4749-4761.
    • (2011) J. Exp. Bot. , vol.62 , pp. 4749-4761
    • Van Doorn, W.G.1
  • 55
    • 84866637318 scopus 로고    scopus 로고
    • Wheat bax inhibitor-1 contributes to wheat resistance to puccinia striiformis
    • Wang, X., Tang, C., Huang, X., Li, F., Chen, X., Zhang, G., Sun, Y., Han, D., and Kang, Z. 2012. Wheat BAX inhibitor-1 contributes to wheat resistance to Puccinia striiformis. J. Exp. Bot. 63:4571-4584.
    • (2012) J. Exp. Bot. , vol.63 , pp. 4571-4584
    • Wang, X.1    Tang, C.2    Huang, X.3    Li, F.4    Chen, X.5    Zhang, G.6    Sun, Y.7    Han, D.8    Kang, Z.9
  • 56
    • 17644412048 scopus 로고    scopus 로고
    • Two arabidopsis metacaspases atmcp1b and atmcp2b are arginine/lysine- specific cysteine proteases and activate apoptosis-like cell death in yeast
    • Watanabe, N., and Lam, E. 2005. Two Arabidopsis metacaspases AtMCP1b and AtMCP2b are arginine/lysine-specific cysteine proteases and activate apoptosis-like cell death in yeast. J. Biol. Chem. 280:14691-14699.
    • (2005) J. Biol. Chem. , vol.280 , pp. 14691-14699
    • Watanabe, N.1    Lam, E.2
  • 57
    • 68949100235 scopus 로고    scopus 로고
    • Bax inhibitor-1, a conserved cell death suppressor, is a key molecular switch downstream from a variety of biotic and abiotic stress signals in plants
    • Watanabe, N., and Lam, E. 2009. Bax Inhibitor-1, a conserved cell death suppressor, is a key molecular switch downstream from a variety of biotic and abiotic stress signals in plants. Int. J. Mol. Sci. 10:3149-3167.
    • (2009) Int. J. Mol. Sci. , vol.10 , pp. 3149-3167
    • Watanabe, N.1    Lam, E.2
  • 58
    • 79959847069 scopus 로고    scopus 로고
    • Tipping the balance: Sclerotinia sclerotiorum secreted oxalic acid suppresses host defenses by manipulating the host redox environment
    • Published online
    • Williams, B., Kabbage, M., Kim, H. J., Britt, R., and Dickman, M. B. 2011. Tipping the balance: Sclerotinia sclerotiorum secreted oxalic acid suppresses host defenses by manipulating the host redox environment. PloS Pathog. 7:e1002107. Published online.
    • (2011) PloS Pathog. , vol.7
    • Williams, B.1    Kabbage, M.2    Kim, H.J.3    Britt, R.4    Dickman, M.B.5
  • 59
    • 4644303690 scopus 로고    scopus 로고
    • Death proteases come alive
    • Woltering, E. J. 2004. Death proteases come alive. Trends Plant Sci. 9:469-472.
    • (2004) Trends Plant Sci. , vol.9 , pp. 469-472
    • Woltering, E.J.1
  • 61
    • 70849127320 scopus 로고    scopus 로고
    • Autophagy negatively regulates cell death by controlling npr1-dependent salicylic acid signaling during senescence and the innate immune response in arabidopsis
    • Yoshimoto, K., Jikumaru, Y., Kamiya, Y., Kusano, M., Consonni, C., Panstruga, R., Ohsumi, Y., and Shirasu, K. 2009. Autophagy negatively regulates cell death by controlling NPR1-dependent salicylic acid signaling during senescence and the innate immune response in Arabidopsis. Plant Cell 21:2914-2927.
    • (2009) Plant Cell , vol.21 , pp. 2914-2927
    • Yoshimoto, K.1    Jikumaru, Y.2    Kamiya, Y.3    Kusano, M.4    Consonni, C.5    Panstruga, R.6    Ohsumi, Y.7    Shirasu, K.8
  • 62
    • 68249141795 scopus 로고    scopus 로고
    • Real-Time detection of caspase-3-like protease activation in vivo using fluorescence resonance energy transfer during plant programmed cell death induced by ultraviolet c overexposure
    • Zhang, L., Xu, Q., Xing, D., Gao, C., and Xiong, H. 2009. Real-Time detection of caspase-3-like protease activation in vivo using fluorescence resonance energy transfer during plant programmed cell death induced by ultraviolet C overexposure. Plant Physiol. 150:1773-1783.
    • (2009) Plant Physiol. , vol.150 , pp. 1773-1783
    • Zhang, L.1    Xu, Q.2    Xing, D.3    Gao, C.4    Xiong, H.5
  • 63
    • 0017226658 scopus 로고
    • A new fluorogenic substrate for chymotrypsin
    • Zimmerman, M., Yurewicz, E., and Patel, G. 1976. A new fluorogenic substrate for chymotrypsin. Anal. Biochem. 70:258-262.
    • (1976) Anal. Biochem. , vol.70 , pp. 258-262
    • Zimmerman, M.1    Yurewicz, E.2    Patel, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.