메뉴 건너뛰기




Volumn 5, Issue FEB, 2014, Pages

Endoplasmic reticulum KDEL-tailed cysteine endopeptidase 1 of Arabidopsis (AtCEP1) is involved in pathogen defense

Author keywords

Cell wall; Haustorium; Plant immunity; Programmed cell death; Sporulation

Indexed keywords


EID: 84901056338     PISSN: None     EISSN: 1664462X     Source Type: Journal    
DOI: 10.3389/fpls.2014.00058     Document Type: Article
Times cited : (36)

References (57)
  • 1
    • 39449119290 scopus 로고    scopus 로고
    • Do plant cells secrete exosomes derived from multivesicular bodies?
    • doi: 10.4161/psb.2.1.3596
    • An, Q., van Bel, A. J., and Hückelhoven, R. (2007). Do plant cells secrete exosomes derived from multivesicular bodies? Plant Signal. Behav. 2, 4-7. doi: 10.4161/psb.2.1.3596
    • (2007) Plant Signal. Behav. , vol.2 , pp. 4-7
    • An, Q.1    van Bel, A.J.2    Hückelhoven, R.3
  • 2
    • 0030931105 scopus 로고    scopus 로고
    • Proteinase A, a storage-globulin-degrading endopeptidase of vetch (Vicia sativa L.) seeds, is not involved in early steps of storage protein mobilization
    • doi: 10.1111/j.1432-1033.1997.00304.x
    • Becker, C., Senyuk, V. I., Shutov, A. D., Nong, V. H., Fischer, J., Horstmann, C., et al. (1997). Proteinase A, a storage-globulin-degrading endopeptidase of vetch (Vicia sativa L.) seeds, is not involved in early steps of storage protein mobilization. Eur. J. Biochem. 248, 304-312. doi: 10.1111/j.1432-1033.1997.00304.x
    • (1997) Eur. J. Biochem. , vol.248 , pp. 304-312
    • Becker, C.1    Senyuk, V.I.2    Shutov, A.D.3    Nong, V.H.4    Fischer, J.5    Horstmann, C.6
  • 3
    • 0001193725 scopus 로고    scopus 로고
    • Programmed cell death during plant growth and development
    • doi: 10.1038/sj.cdd.4400297
    • Beers, E. P. (1997). Programmed cell death during plant growth and development. Cell Death Differ. 4, 649-661. doi: 10.1038/sj.cdd.4400297
    • (1997) Cell Death Differ. , vol.4 , pp. 649-661
    • Beers, E.P.1
  • 4
    • 0742322084 scopus 로고    scopus 로고
    • The S8 serine, C1A cysteine and A1 aspartic protease families in Arabidopsis
    • doi: 10.1016/j.phytochem.2003.09.005
    • Beers, E. P., Jones, A. M., and Dickerman, A. W. (2004). The S8 serine, C1A cysteine and A1 aspartic protease families in Arabidopsis. Phytochemistry 65, 43-58. doi: 10.1016/j.phytochem.2003.09.005
    • (2004) Phytochemistry , vol.65 , pp. 43-58
    • Beers, E.P.1    Jones, A.M.2    Dickerman, A.W.3
  • 5
    • 0034476852 scopus 로고    scopus 로고
    • Plant proteolytic enzymes: Possible role during programmed cell death
    • doi: 10.1023/A:1026556928624
    • Beers, E. P., Woffenden, B. J., and Zhao C. (2000). Plant proteolytic enzymes: possible role during programmed cell death. Plant Mol. Biol. 44, 399-415. doi: 10.1023/A:1026556928624
    • (2000) Plant Mol. Biol. , vol.44 , pp. 399-415
    • Beers, E.P.1    Woffenden, B.J.2    Zhao, C.3
  • 6
    • 0031225052 scopus 로고    scopus 로고
    • The cpr5 mutant of Arabidopsis expresses both NPR1-dependent and NPR1-independent resistance
    • doi: 10.1105/tpc.9.9.1573
    • Bowling, S. A., Clarke, J. D., Liu, Y., Klessig, D. F., and Dong, X. (1997). The cpr5 mutant of Arabidopsis expresses both NPR1-dependent and NPR1-independent resistance. Plant Cell 9, 1573-1584. doi: 10.1105/tpc.9.9.1573
    • (1997) Plant Cell , vol.9 , pp. 1573-1584
    • Bowling, S.A.1    Clarke, J.D.2    Liu, Y.3    Klessig, D.F.4    Dong, X.5
  • 7
    • 84855489042 scopus 로고    scopus 로고
    • Phytophthora infestans effector AVRblb2 prevents secretion of a plant immune protease at the haustorial interface
    • doi: 10.1073/pnas.1112708109
    • Bozkurt, T. O., Schornack, S., Win, J., Shindo, T., Ilyas, M., Oliva, R., et al. (2011). Phytophthora infestans effector AVRblb2 prevents secretion of a plant immune protease at the haustorial interface. Proc. Natl. Acad. Sci. U.S.A. 108, 20832-20837. doi: 10.1073/pnas.1112708109
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 20832-20837
    • Bozkurt, T.O.1    Schornack, S.2    Win, J.3    Shindo, T.4    Ilyas, M.5    Oliva, R.6
  • 8
    • 41149123874 scopus 로고    scopus 로고
    • Self-assembly of the plant cell wall requires an extensin scaffold
    • doi: 10.1073/pnas.0711980105
    • Cannon, M. C., Terneus, K., Hall, Q., Tan, L., Wang, Y., Wegenhart, B. L., et al. (2008). Self-assembly of the plant cell wall requires an extensin scaffold. Proc. Natl. Acad. Sci. U.S.A. 105, 2226-2231. doi: 10.1073/pnas.0711980105
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 2226-2231
    • Cannon, M.C.1    Terneus, K.2    Hall, Q.3    Tan, L.4    Wang, Y.5    Wegenhart, B.L.6
  • 9
    • 0033117455 scopus 로고    scopus 로고
    • Cloning and characterization of TPE4A, a thiol-protease gene induced during ovary senescence and seed germination in pea
    • doi: 10.1104/pp.119.4.1341
    • Cercos, M., Santamaria, S., and Carbonell, J. S. O. (1999). Cloning and characterization of TPE4A, a thiol-protease gene induced during ovary senescence and seed germination in pea. Plant Physiol. 119, 1341-1348. doi: 10.1104/pp.119.4.1341
    • (1999) Plant Physiol. , vol.119 , pp. 1341-1348
    • Cercos, M.1    Santamaria, S.2    Carbonell, J.S.O.3
  • 10
    • 0034519979 scopus 로고    scopus 로고
    • Roles of salicylic acid, jasmonic acid, and ethylene in cpr-induced resistance in Arabidopsis
    • doi: 10.1105/tpc.12.11.2175
    • Clarke, J. D., Volko, S. M., Ledford, H., Ausubel, F. M., and Dong, X. (2000). Roles of salicylic acid, jasmonic acid, and ethylene in cpr-induced resistance in Arabidopsis. Plant Cell 12, 2175-2190. doi: 10.1105/tpc.12.11.2175
    • (2000) Plant Cell , vol.12 , pp. 2175-2190
    • Clarke, J.D.1    Volko, S.M.2    Ledford, H.3    Ausubel, F.M.4    Dong, X.5
  • 11
    • 0032447801 scopus 로고    scopus 로고
    • Floral dip: A simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana
    • doi: 10.1046/j.1365-313x.1998.00343.x
    • Clough, S. J., and Bent, A. F. (1998). Floral dip: a simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana. Plant J. 16, 735-743. doi: 10.1046/j.1365-313x.1998.00343.x
    • (1998) Plant J. , vol.16 , pp. 735-743
    • Clough, S.J.1    Bent, A.F.2
  • 12
    • 0034724178 scopus 로고    scopus 로고
    • Random GFP::CDNA fusions enable visualization of subcellular structures in cells of Arabidopsis at high frequency
    • doi: 10.1073/pnas.97.7.3718
    • Cutler, S. R., Ehrhardt, D. W., Griffitts, J. S., and Somerville, C. R. (2000). Random GFP::cDNA fusions enable visualization of subcellular structures in cells of Arabidopsis at high frequency. Proc. Natl. Acad. Sci. U.S.A. 97, 3718-3723. doi: 10.1073/pnas.97.7.3718
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 3718-3723
    • Cutler, S.R.1    Ehrhardt, D.W.2    Griffitts, J.S.3    Somerville, C.R.4
  • 13
    • 84881447152 scopus 로고    scopus 로고
    • Centrality of host cell death in plant-microbe interactions
    • doi: 10.1146/annurev-phyto-081211-173027
    • Dickman, M. B., and Fluhr, R. (2013). Centrality of host cell death in plant-microbe interactions. Annu. Rev. Phytopathol. 51, 543-570. doi: 10.1146/annurev-phyto-081211-173027
    • (2013) Annu. Rev. Phytopathol. , vol.51 , pp. 543-570
    • Dickman, M.B.1    Fluhr, R.2
  • 14
    • 51549096819 scopus 로고    scopus 로고
    • Auxin responses in mutants of the Arabidopsis CONSTITUTIVE PHOTOMORPHOGENIC9 signalosome
    • doi: 10.1104/pp.108.121061
    • Dohmann, E. M. N., Levesque, M. P., Isono, E., Schmid, M., and Schwechheimer, C. (2008). Auxin responses in mutants of the Arabidopsis CONSTITUTIVE PHOTOMORPHOGENIC9 signalosome. Plant Physiol. 147, 1369-1379. doi: 10.1104/pp.108.121061
    • (2008) Plant Physiol. , vol.147 , pp. 1369-1379
    • Dohmann, E.M.N.1    Levesque, M.P.2    Isono, E.3    Schmid, M.4    Schwechheimer, C.5
  • 15
    • 84873242737 scopus 로고    scopus 로고
    • Protein secretion: How many secretory routes does a plant cell have?
    • doi: 10.1016/j.plantsci.2012.12.017
    • Drakakaki, G., and Dandekar, A. (2013). Protein secretion: how many secretory routes does a plant cell have? Plant Sci. 203-204, 74-78. doi: 10.1016/j.plantsci.2012.12.017
    • (2013) Plant Sci , vol.203-204 , pp. 74-78
    • Drakakaki, G.1    Dandekar, A.2
  • 16
    • 67649496487 scopus 로고    scopus 로고
    • Rapid combinatorial analysis of membrane compartments in intact plants with a multicolor marker set
    • doi: 10.1111/j.1365-313X.2009.03851.x
    • Geldner, N., Denervaud-Tendon, V., Hyman, D. L., Mayer, U., Stierhof, Y.-D., and Chory, J. (2009). Rapid combinatorial analysis of membrane compartments in intact plants with a multicolor marker set. Plant J. 59, 169-178. doi: 10.1111/j.1365-313X.2009.03851.x
    • (2009) Plant J. , vol.59 , pp. 169-178
    • Geldner, N.1    Denervaud-Tendon, V.2    Hyman, D.L.3    Mayer, U.4    Stierhof, Y.-D.5    Chory, J.6
  • 17
    • 0029898756 scopus 로고    scopus 로고
    • Isolation of Arabidopsis mutants with enhanced disease susceptibility by direct screening
    • Glazebrook, J., Rogers, E. E., and Ausubel, F. M. (1996). Isolation of Arabidopsis mutants with enhanced disease susceptibility by direct screening. Genetics 143, 973-982.
    • (1996) Genetics , vol.143 , pp. 973-982
    • Glazebrook, J.1    Rogers, E.E.2    Ausubel, F.M.3
  • 18
    • 13844312452 scopus 로고    scopus 로고
    • Ricinosomes and endosperm transfer cell structure in programmed cell death of the nucellus during Ricinus seed development
    • doi: 10.1073/pnas.0409429102
    • Greenwood, J. S., Helm, M., and Gietl, C. (2005). Ricinosomes and endosperm transfer cell structure in programmed cell death of the nucellus during Ricinus seed development. Proc. Natl. Acad. Sci. U.S.A. 102, 2238-2243. doi: 10.1073/pnas.0409429102
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 2238-2243
    • Greenwood, J.S.1    Helm, M.2    Gietl, C.3
  • 19
    • 0001327668 scopus 로고    scopus 로고
    • Programmed senescence of plant organs
    • doi: 10.1038/sj.cdd.4400308
    • Hadfield, K. A., and Bennett, A. B. (1997). Programmed senescence of plant organs. Cell Death Differ. 4, 662-670. doi: 10.1038/sj.cdd.4400308
    • (1997) Cell Death Differ. , vol.4 , pp. 662-670
    • Hadfield, K.A.1    Bennett, A.B.2
  • 20
    • 79960228202 scopus 로고    scopus 로고
    • The role of vacuole in plant death
    • doi: 10.1038/cdd.2011.70
    • Hara-Nishimura, I., and Hatsugai, N. (2011). The role of vacuole in plant death. Cell Death Differ. 18, 1298-1304. doi: 10.1038/cdd.2011.70
    • (2011) Cell Death Differ. , vol.18 , pp. 1298-1304
    • Hara-Nishimura, I.1    Hatsugai, N.2
  • 21
    • 70350655656 scopus 로고    scopus 로고
    • A novel membrane fusion-mediated plant immunity against bacterial pathogens
    • doi: 10.1101/gad.1825209
    • Hatsugai, N., Iwasaki, S., Tamura, K., Kondo, M., Fuji, K., Ogasawara, K., et al. (2009). A novel membrane fusion-mediated plant immunity against bacterial pathogens. Genes Dev. 23, 2496-2506. doi: 10.1101/gad.1825209
    • (2009) Genes Dev. , vol.23 , pp. 2496-2506
    • Hatsugai, N.1    Iwasaki, S.2    Tamura, K.3    Kondo, M.4    Fuji, K.5    Ogasawara, K.6
  • 22
    • 0342803566 scopus 로고    scopus 로고
    • pGreen: A versatile and flexible binary Ti vector for Agrobacterium-mediated plant transformation
    • doi: 10.1023/A:1006496308160
    • Hellens, R. P., Edwards, E. A., Leyland, N. R., Bean, S., and Mulineaux, P. M. (2000). pGreen: a versatile and flexible binary Ti vector for Agrobacterium-mediated plant transformation. Plant Mol. Biol. 42, 819-832. doi: 10.1023/A:1006496308160
    • (2000) Plant Mol. Biol. , vol.42 , pp. 819-832
    • Hellens, R.P.1    Edwards, E.A.2    Leyland, N.R.3    Bean, S.4    Mulineaux, P.M.5
  • 23
    • 51349133279 scopus 로고    scopus 로고
    • KDEL-tailed cysteine endopeptidases involved in programmed cell death, intercalation of new cells and dismantling of extensin scaffolds
    • doi: 10.3732/ajb.2007404
    • Helm, M., Schmid, M., Hierl, G., Terneus, K., Tan, M., Lottspeich, F., et al. (2008). KDEL-tailed cysteine endopeptidases involved in programmed cell death, intercalation of new cells and dismantling of extensin scaffolds. Am. J. Bot. 95, 1049-1062. doi: 10.3732/ajb.2007404
    • (2008) Am. J. Bot. , vol.95 , pp. 1049-1062
    • Helm, M.1    Schmid, M.2    Hierl, G.3    Terneus, K.4    Tan, M.5    Lottspeich, F.6
  • 24
    • 0042695870 scopus 로고    scopus 로고
    • Proteases associated with programmed cell death of megagametophyte cells after germination of white spruce (Picea glauca) seeds
    • doi: 10.1023/A:1025008117046
    • He, X., and Kermode, A. R. (2003). Proteases associated with programmed cell death of megagametophyte cells after germination of white spruce (Picea glauca) seeds. Plant Mol. Biol. 52, 729-744. doi: 10.1023/A:1025008117046
    • (2003) Plant Mol. Biol. , vol.52 , pp. 729-744
    • He, X.1    Kermode, A.R.2
  • 25
    • 84896044639 scopus 로고    scopus 로고
    • Ex vivo processing for maturation of Arabidopsis KDEL-tailed cysteine endopeptidase 2 (AtCEP2) pro-enzyme and its storage in in endoplasmic reticulum derived organelles
    • Biol. doi: 10.1007/s11103-013-0157-6. [Epub ahead of print]
    • Hierl, G., Höwing, T., Isono, E., Lottspeich, F., and Gietl, C. (2013). Ex vivo processing for maturation of Arabidopsis KDEL-tailed cysteine endopeptidase 2 (AtCEP2) pro-enzyme and its storage in in endoplasmic reticulum derived organelles. Plant Mol. Biol. doi: 10.1007/s11103-013-0157-6. [Epub ahead of print].
    • (2013) Plant Mol.
    • Hierl, G.1    Höwing, T.2    Isono, E.3    Lottspeich, F.4    Gietl, C.5
  • 26
    • 84859848841 scopus 로고    scopus 로고
    • Programmed cell death in Ricinus and Arabidopsis: The function of KDEL cysteine peptidases in development
    • doi: 10.1111/j.1399-3054.2012.01580.x
    • Hierl, G., Vothknecht, U., and Gietl, C. (2012). Programmed cell death in Ricinus and Arabidopsis: the function of KDEL cysteine peptidases in development. Physiol. Plant. 145, 103-113. doi: 10.1111/j.1399-3054.2012.01580.x
    • (2012) Physiol. Plant. , vol.145 , pp. 103-113
    • Hierl, G.1    Vothknecht, U.2    Gietl, C.3
  • 27
    • 83055172811 scopus 로고    scopus 로고
    • Cell biology of the plant-powdery mildew interaction
    • doi: 10.1016/j.pbi.2011.08.002
    • Hückelhoven, R., and Panstruga, R. (2011). Cell biology of the plant-powdery mildew interaction. Curr. Opin. Plant Biol. 14, 738-746. doi: 10.1016/j.pbi.2011.08.002
    • (2011) Curr. Opin. Plant Biol. , vol.14 , pp. 738-746
    • Hückelhoven, R.1    Panstruga, R.2
  • 28
    • 0000502672 scopus 로고
    • KDEL-containing auxin-binding protein is secreted to the plasma membrane and cell wall
    • Jones, A. M., and Herman, E. M. (1993). KDEL-containing auxin-binding protein is secreted to the plasma membrane and cell wall. Plant Physiol. 101, 595-606.
    • (1993) Plant Physiol. , vol.101 , pp. 595-606
    • Jones, A.M.1    Herman, E.M.2
  • 29
    • 0034476827 scopus 로고    scopus 로고
    • Caspase-like protease involvement in the control of plant cell death
    • doi: 10.1023/A:1026509012695
    • Lam, E., and del Pozo, O. (2000). Caspase-like protease involvement in the control of plant cell death. Plant Mol. Biol. 44, 417-428. doi: 10.1023/A:1026509012695
    • (2000) Plant Mol. Biol. , vol.44 , pp. 417-428
    • Lam, E.1    del Pozo, O.2
  • 30
    • 84862580444 scopus 로고    scopus 로고
    • Dual disease resistance mediated by the immune receptor Cf-2 in tomato requires a common virulence target of a fungus and a nematode
    • doi: 10.1073/pnas.1202867109
    • Lozano-Torres, J. L., Wilbers, R. H., Gawronski, P., Boshoven, J. C., Finkers-Tomczak, A., Cordewener, J. H., et al. (2012). Dual disease resistance mediated by the immune receptor Cf-2 in tomato requires a common virulence target of a fungus and a nematode. Proc. Natl. Acad. Sci. U.S.A. 109, 10119-10124. doi: 10.1073/pnas.1202867109
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 10119-10124
    • Lozano-Torres, J.L.1    Wilbers, R.H.2    Gawronski, P.3    Boshoven, J.C.4    Finkers-Tomczak, A.5    Cordewener, J.H.6
  • 31
    • 0000528945 scopus 로고
    • Studies on seeds. V. Microbodies, glyoxysomes, and ricinosomes of castor bean endosperm
    • doi: 10.1104/pp.46.6.794 794-700
    • Mollenhauer, H. H., and Totten, C. (1970). Studies on seeds. V. Microbodies, glyoxysomes, and ricinosomes of castor bean endosperm. Plant Physiol. 46, 794-700. doi: 10.1104/pp.46.6.794
    • (1970) Plant Physiol. , vol.46
    • Mollenhauer, H.H.1    Totten, C.2
  • 32
    • 34548406409 scopus 로고    scopus 로고
    • Protein dynamics and proteolysis in plant vacuoles
    • doi: 10.1093/jxb/erm089
    • Müntz, K. (2007). Protein dynamics and proteolysis in plant vacuoles. J. Exp. Bot. 58, 2391-2407. doi: 10.1093/jxb/erm089
    • (2007) J. Exp. Bot. , vol.58 , pp. 2391-2407
    • Müntz, K.1
  • 33
    • 0019321718 scopus 로고
    • Rapid isolation of high-molecular-weight plant DNA
    • doi: 10.1093/nar/8.19.4321
    • Murray, M. G., and Thompson, W. F. (1980). Rapid isolation of high-molecular-weight plant DNA. Nucl. Acid. Res. 8, 4321-4325. doi: 10.1093/nar/8.19.4321
    • (1980) Nucl. Acid. Res. , vol.8 , pp. 4321-4325
    • Murray, M.G.1    Thompson, W.F.2
  • 34
    • 0030087963 scopus 로고    scopus 로고
    • Ovule development: Identification of stage-specific and tissue-specific cDNAs
    • doi: 10.1105/tpc.8.2.213
    • Nadeau, J. A., Zhang, X. S., Li, J., and O'Neill, S. D. (1996). Ovule development: identification of stage-specific and tissue-specific cDNAs. Plant Cell 8, 213-239. doi: 10.1105/tpc.8.2.213
    • (1996) Plant Cell , vol.8 , pp. 213-239
    • Nadeau, J.A.1    Zhang, X.S.2    Li, J.3    O'Neill, S.D.4
  • 35
    • 0036008869 scopus 로고    scopus 로고
    • Organization of cell walls in Sandersonia aurantiaca floral tissues
    • doi: 10.1093/jexbot/53.368.513
    • O'Donghue, E. M., Somerfield, S. D., and Heyes, J. A. (2002). Organization of cell walls in Sandersonia aurantiaca floral tissues. J. Exp. Bot. 53, 513-523. doi: 10.1093/jexbot/53.368.513
    • (2002) J. Exp. Bot. , vol.53 , pp. 513-523
    • O'Donghue, E.M.1    Somerfield, S.D.2    Heyes, J.A.3
  • 36
    • 0041464460 scopus 로고    scopus 로고
    • C-terminal KDEL sequence of a KDEL-tailed cysteine proteinase (sulfhydryl-endopeptidase) is involved in formation of KDEL vesicle and in efficient vacuolar transport of sulfhydryl-endopeptidase
    • doi: 10.1104/pp.103.021147
    • Okamoto, T., Shimada, T., Hara-Nishimura, I., Nishimura, M., and Minamikawa, T. (2003). C-terminal KDEL sequence of a KDEL-tailed cysteine proteinase (sulfhydryl-endopeptidase) is involved in formation of KDEL vesicle and in efficient vacuolar transport of sulfhydryl-endopeptidase. Plant Physiol. 132, 1892-1900. doi: 10.1104/pp.103.021147
    • (2003) Plant Physiol. , vol.132 , pp. 1892-1900
    • Okamoto, T.1    Shimada, T.2    Hara-Nishimura, I.3    Nishimura, M.4    Minamikawa, T.5
  • 37
    • 0033025377 scopus 로고    scopus 로고
    • Developmental biology of the cereal endosperm
    • doi: 10.1016/S1360-1385(99)01431-4
    • Olsen, O. A., Linnestad, C., and Nichols, S. E. (1999). Developmental biology of the cereal endosperm. Trends Plant Sci. 4, 253-257. doi: 10.1016/S1360-1385(99)01431-4
    • (1999) Trends Plant Sci. , vol.4 , pp. 253-257
    • Olsen, O.A.1    Linnestad, C.2    Nichols, S.E.3
  • 38
    • 0031419356 scopus 로고    scopus 로고
    • Programmed cell death in plants
    • doi: 10.1105/tpc.9.7.1157
    • Pennel, R. I., and Lamb C. (1997). Programmed cell death in plants. Plant Cell 9, 1157-1168. doi: 10.1105/tpc.9.7.1157
    • (1997) Plant Cell , vol.9 , pp. 1157-1168
    • Pennel, R.I.1    Lamb, C.2
  • 39
    • 0032174012 scopus 로고    scopus 로고
    • Jasmonate and salicylate as global signals for defense gene expression
    • doi: 10.1016/S1369-5266(98)80264-1
    • Reymond, P., and Farmer, E. E. (1998). Jasmonate and salicylate as global signals for defense gene expression. Curr. Opin. Plant Biol. 1, 404-411. doi: 10.1016/S1369-5266(98)80264-1
    • (1998) Curr. Opin. Plant Biol. , vol.1 , pp. 404-411
    • Reymond, P.1    Farmer, E.E.2
  • 40
    • 11844252119 scopus 로고    scopus 로고
    • A cut above the rest: The regulatory function of plant proteases
    • doi: 10.1007/s00425-004-1407-2
    • Schaller, A. (2004). A cut above the rest: the regulatory function of plant proteases. Planta 220, 183-197. doi: 10.1007/s00425-004-1407-2
    • (2004) Planta , vol.220 , pp. 183-197
    • Schaller, A.1
  • 41
    • 0033598774 scopus 로고    scopus 로고
    • Programmed cell death in castor bean endosperm is associated with the accumulation and release of a cysteine endopeptidase from ricinosomes
    • doi: 10.1073/pnas.96.24.14159
    • Schmid, M., Simpson, D., and Gietl, C. (1999). Programmed cell death in castor bean endosperm is associated with the accumulation and release of a cysteine endopeptidase from ricinosomes. Proc. Natl. Acad. Sci. U.S.A. 96, 14159-14164. doi: 10.1073/pnas.96.24.14159
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 14159-14164
    • Schmid, M.1    Simpson, D.2    Gietl, C.3
  • 42
    • 0035942237 scopus 로고    scopus 로고
    • The ricinosomes of senescing plant tissue bud from the endoplasmic reticulum
    • doi: 10.1073/pnas.061038298
    • Schmid, M., Simpson, D. J., Sarioglu, H., Lottspeich, F., and Gietl, C. (2001). The ricinosomes of senescing plant tissue bud from the endoplasmic reticulum. Proc. Natl. Acad. Sci. U.S.A. 98, 5353-5358. doi: 10.1073/pnas.061038298
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 5353-5358
    • Schmid, M.1    Simpson, D.J.2    Sarioglu, H.3    Lottspeich, F.4    Gietl, C.5
  • 43
    • 0032189507 scopus 로고    scopus 로고
    • A cysteine endopeptidase with a C-terminal KDEL motif isolated from castor bean endosperm is a marker enzyme for the ricinosome, a putative lytic compartment
    • doi: 10.1007/s004250050423
    • Schmid, M., Simpson, D., Kalousek, F., and Gietl, C. (1998). A cysteine endopeptidase with a C-terminal KDEL motif isolated from castor bean endosperm is a marker enzyme for the ricinosome, a putative lytic compartment. Planta 206, 466-475. doi: 10.1007/s004250050423
    • (1998) Planta , vol.206 , pp. 466-475
    • Schmid, M.1    Simpson, D.2    Kalousek, F.3    Gietl, C.4
  • 44
    • 60249086952 scopus 로고    scopus 로고
    • Ricinosomes predict programmed cell death leading to anther dehiscence in tomato
    • doi: 10.1104/pp.108.132720
    • Senatore, A., Trobacher, C. P., and Greenwood, J. S. (2009). Ricinosomes predict programmed cell death leading to anther dehiscence in tomato. Plant Physiol. 149, 775-790. doi: 10.1104/pp.108.132720
    • (2009) Plant Physiol. , vol.149 , pp. 775-790
    • Senatore, A.1    Trobacher, C.P.2    Greenwood, J.S.3
  • 45
    • 37349092681 scopus 로고    scopus 로고
    • Papain-like cysteine proteases: Key players at molecular battlefields employed by both plants and their invaders
    • doi: 10.1111/j.1364-3703.2007.00439.x
    • Shindo, T., and Van der Hoorn, R. A. (2008). Papain-like cysteine proteases: key players at molecular battlefields employed by both plants and their invaders. Mol. Plant Pathol. 9, 119-125. doi: 10.1111/j.1364-3703.2007.00439.x
    • (2008) Mol. Plant Pathol. , vol.9 , pp. 119-125
    • Shindo, T.1    Van der Hoorn, R.A.2
  • 46
    • 0026176684 scopus 로고
    • Nucleotide sequence of cDNA for an endopeptidase (EP-C1) from pods of maturing Phaseolus vulgaris fruits
    • doi: 10.1007/BF00016081
    • Tanaka, T., Yamauchi, D., and Minamikawa, T. (1991). Nucleotide sequence of cDNA for an endopeptidase (EP-C1) from pods of maturing Phaseolus vulgaris fruits. Plant Mol. Biol. 16, 1083-1084. doi: 10.1007/BF00016081
    • (1991) Plant Mol. Biol. , vol.16 , pp. 1083-1084
    • Tanaka, T.1    Yamauchi, D.2    Minamikawa, T.3
  • 47
    • 1242317042 scopus 로고    scopus 로고
    • The 2.0-Å crystal structure of the KDEL-tailed cysteine endopeptidase from germinating endosperm of Ricinus communis confirms its function in the final stage of programmed cell death
    • doi: 10.1016/j.jmb.2003.12.075
    • Than, M. E., Helm, M., Simpson, D. J., Lottspeich, F., Huber, R., and Gietl, C. (2004). The 2.0-Å crystal structure of the KDEL-tailed cysteine endopeptidase from germinating endosperm of Ricinus communis confirms its function in the final stage of programmed cell death. J. Mol. Biol. 336, 1103-1116. doi: 10.1016/j.jmb.2003.12.075
    • (2004) J. Mol. Biol. , vol.336 , pp. 1103-1116
    • Than, M.E.1    Helm, M.2    Simpson, D.J.3    Lottspeich, F.4    Huber, R.5    Gietl, C.6
  • 48
    • 0034614933 scopus 로고    scopus 로고
    • Mass transport of a KDEL-tailed cysteine protease (SH-EP) to protein storage vacuoles by endoplasmic reticulum-derived vesicle is involved in protein mobilization in germinating seeds
    • doi: 10.1083/jcb.148.3.453
    • Toyooka, K., Okamoto, T., and Minamikawa, T. (2000). Mass transport of a KDEL-tailed cysteine protease (SH-EP) to protein storage vacuoles by endoplasmic reticulum-derived vesicle is involved in protein mobilization in germinating seeds. J. Cell Biol. 148, 453-463. doi: 10.1083/jcb.148.3.453
    • (2000) J. Cell Biol. , vol.148 , pp. 453-463
    • Toyooka, K.1    Okamoto, T.2    Minamikawa, T.3
  • 49
    • 84874339107 scopus 로고    scopus 로고
    • Induction of a ricinosomal-protease and programmed cell death in tomato endosperm by gibberellic acid
    • doi: 10.1007/s00425-012-1780-1
    • Trobacher, C. P., Senatore, A., Holley, C., and Greenwood, J. S. (2013). Induction of a ricinosomal-protease and programmed cell death in tomato endosperm by gibberellic acid. Planta 237, 665-679. doi: 10.1007/s00425-012-1780-1
    • (2013) Planta , vol.237 , pp. 665-679
    • Trobacher, C.P.1    Senatore, A.2    Holley, C.3    Greenwood, J.S.4
  • 51
    • 0029310458 scopus 로고
    • Up-regulation of a cysteine protease accompanies the ethylene-insensitive senescence of daylily (Hemerocallis) flowers
    • doi: 10.1007/BF00020403
    • Valpuesta, V., Lange, N. E., Guerriero, C., and Reid, M. S. (1995). Up-regulation of a cysteine protease accompanies the ethylene-insensitive senescence of daylily (Hemerocallis) flowers. Plant Mol. Biol. 28, 575-582 doi: 10.1007/BF00020403
    • (1995) Plant Mol. Biol. , vol.28 , pp. 575-582
    • Valpuesta, V.1    Lange, N.E.2    Guerriero, C.3    Reid, M.S.4
  • 52
    • 84860129593 scopus 로고    scopus 로고
    • A maize cystatin suppresses host immunity by inhibiting apoplastic cysteine proteases
    • doi: 10.1105/tpc.111.093732
    • van der Linde, K., Hemetsberger, C., Kastner, C., Kaschani, F., van der Hoorn, R. A., Kumlehn, J., et al. (2012). A maize cystatin suppresses host immunity by inhibiting apoplastic cysteine proteases. Plant Cell 24, 1285-1300. doi: 10.1105/tpc.111.093732
    • (2012) Plant Cell , vol.24 , pp. 1285-1300
    • van der Linde, K.1    Hemetsberger, C.2    Kastner, C.3    Kaschani, F.4    van der Hoorn, R.A.5    Kumlehn, J.6
  • 53
    • 79960260879 scopus 로고    scopus 로고
    • A plant alternative to animal caspases: Subtilisin-like proteases
    • doi: 10.1038/cdd.2011.49
    • Vartapetian, A. B., Tuzhikov, A. I., Chichkova, N. V., Taliansky, M., and Wolpert, T. J. (2011). A plant alternative to animal caspases: subtilisin-like proteases. Cell Death Differ. 18, 1289-1297. doi: 10.1038/cdd.2011.49
    • (2011) Cell Death Differ. , vol.18 , pp. 1289-1297
    • Vartapetian, A.B.1    Tuzhikov, A.I.2    Chichkova, N.V.3    Taliansky, M.4    Wolpert, T.J.5
  • 54
    • 0014837856 scopus 로고
    • Cytochemical and developmental changes in microbodies (glyoxysomes) and related organelles of castor bean endosperm
    • doi: 10.1083/jcb.46.3.435
    • Vigil, E. L. (1970). Cytochemical and developmental changes in microbodies (glyoxysomes) and related organelles of castor bean endosperm. J. Cell Biol. 46, 435-454. doi: 10.1083/jcb.46.3.435
    • (1970) J. Cell Biol. , vol.46 , pp. 435-454
    • Vigil, E.L.1
  • 55
    • 70450181685 scopus 로고    scopus 로고
    • Plant caspase-like proteases in plant programmed cell death
    • doi: 10.4161/psb.4.9.9531
    • Xu, Q., and Zhang, L. (2009). Plant caspase-like proteases in plant programmed cell death. Plant Signal. Behav. 4, 902-904. doi: 10.4161/psb.4.9.9531
    • (2009) Plant Signal. Behav. , vol.4 , pp. 902-904
    • Xu, Q.1    Zhang, L.2
  • 56
    • 0034480320 scopus 로고    scopus 로고
    • Programmed cell death during endosperm development
    • doi: 10.1023/A:1026588408152
    • Young, T. E., and Gallie, D. R. (2000). Programmed cell death during endosperm development. Plant Mol. Biol. 44, 283-301. doi: 10.1023/A:1026588408152
    • (2000) Plant Mol. Biol. , vol.44 , pp. 283-301
    • Young, T.E.1    Gallie, D.R.2
  • 57
    • 13444264729 scopus 로고    scopus 로고
    • Arabidopsis microarray database and analysis toolbox
    • GENEVESTIGATOR, doi: 10.1104/pp.104.046367
    • Zimmermann, P., Hirsch-Hoffmann, M., Hennig L., and Gruissem, W. (2004). GENEVESTIGATOR. Arabidopsis microarray database and analysis toolbox. Plant Physiol. 136, 2621-2632. doi: 10.1104/pp.104.046367
    • (2004) Plant Physiol. , vol.136 , pp. 2621-2632
    • Zimmermann, P.1    Hirsch-Hoffmann, M.2    Hennig, L.3    Gruissem, W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.