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Volumn 12, Issue , 2012, Pages

Beneficial 'unintended effects' of a cereal cystatin in transgenic lines of potato, Solanum tuberosum

Author keywords

Corn cystatin; Potato (Solanum tuberosum); Stress defense related proteome; Transgene pleiotropy; Transgenic crops; Unintended effects

Indexed keywords

HEXAPODA; SOLANUM TUBEROSUM; ZEA MAYS;

EID: 84868252434     PISSN: None     EISSN: 14712229     Source Type: Journal    
DOI: 10.1186/1471-2229-12-198     Document Type: Article
Times cited : (22)

References (67)
  • 1
    • 5344259633 scopus 로고    scopus 로고
    • Protein proteinase inhibitor genes in combat against insects, pests, and pathogens: natural and engineered phytoprotection
    • 10.1016/j.abb.2004.07.022, 15464737
    • Haq SK, Atif SM, Khan RH. Protein proteinase inhibitor genes in combat against insects, pests, and pathogens: natural and engineered phytoprotection. Arch Biochem Biophys 2004, 431:145-159. 10.1016/j.abb.2004.07.022, 15464737.
    • (2004) Arch Biochem Biophys , vol.431 , pp. 145-159
    • Haq, S.K.1    Atif, S.M.2    Khan, R.H.3
  • 3
    • 0037164073 scopus 로고    scopus 로고
    • Plant seed cystatins and their target enzymes of endogenous and exogenous origin
    • 10.1021/jf0201935, 12381160
    • Arai S, Matsumoto I, Emori Y, Abe K. Plant seed cystatins and their target enzymes of endogenous and exogenous origin. J Agric Food Chem 2002, 50:6612-6617. 10.1021/jf0201935, 12381160.
    • (2002) J Agric Food Chem , vol.50 , pp. 6612-6617
    • Arai, S.1    Matsumoto, I.2    Emori, Y.3    Abe, K.4
  • 6
    • 11844252119 scopus 로고    scopus 로고
    • A cut above the rest: the regulatory function of plant proteases
    • 10.1007/s00425-004-1407-2, 15517349
    • Schaller A. A cut above the rest: the regulatory function of plant proteases. Planta 2004, 220:183-197. 10.1007/s00425-004-1407-2, 15517349.
    • (2004) Planta , vol.220 , pp. 183-197
    • Schaller, A.1
  • 7
    • 44949258132 scopus 로고    scopus 로고
    • Plant proteases: from phenotypes to molecular mechanisms
    • 10.1146/annurev.arplant.59.032607.092835, 18257708
    • van den Hoorn RAL. Plant proteases: from phenotypes to molecular mechanisms. Annu Rev Plant Biol 2008, 59:191-223. 10.1146/annurev.arplant.59.032607.092835, 18257708.
    • (2008) Annu Rev Plant Biol , vol.59 , pp. 191-223
    • van den Hoorn, R.A.L.1
  • 8
    • 0027547272 scopus 로고
    • Expression of a cysteine proteinase inhibitor (oryzacystatin-I) in transgenic tobacco plants
    • 10.1007/BF00014548, 8448364
    • Masoud SA, Johnson LB, White FF, Reeck GR. Expression of a cysteine proteinase inhibitor (oryzacystatin-I) in transgenic tobacco plants. Plant Mol Biol 1993, 21:655-663. 10.1007/BF00014548, 8448364.
    • (1993) Plant Mol Biol , vol.21 , pp. 655-663
    • Masoud, S.A.1    Johnson, L.B.2    White, F.F.3    Reeck, G.R.4
  • 9
    • 33645503258 scopus 로고    scopus 로고
    • An in-built proteinase inhibitor system for the protection of recombinant proteins recovered from transgenic plants
    • 10.1111/j.1467-7652.2006.00187.x, 17147641
    • Rivard D, Anguenot R, Brunelle F, Le VQ, Vézina L-P, Trépanier S, Michaud D. An in-built proteinase inhibitor system for the protection of recombinant proteins recovered from transgenic plants. Plant Biotechnol J 2006, 4:359-368. 10.1111/j.1467-7652.2006.00187.x, 17147641.
    • (2006) Plant Biotechnol J , vol.4 , pp. 359-368
    • Rivard, D.1    Anguenot, R.2    Brunelle, F.3    Le, V.Q.4    Vézina, L.-P.5    Trépanier, S.6    Michaud, D.7
  • 10
    • 60549109649 scopus 로고    scopus 로고
    • Unintended molecular interactions in transgenic plants expressing clinically-useful proteins-The case of bovine aprotinin travelling the potato leaf cell secretory pathway
    • 10.1002/pmic.200700234, 19137543
    • Badri MA, Rivard D, Coenen K, Michaud D. Unintended molecular interactions in transgenic plants expressing clinically-useful proteins-The case of bovine aprotinin travelling the potato leaf cell secretory pathway. Proteomics 2009, 9:746-756. 10.1002/pmic.200700234, 19137543.
    • (2009) Proteomics , vol.9 , pp. 746-756
    • Badri, M.A.1    Rivard, D.2    Coenen, K.3    Michaud, D.4
  • 11
    • 73949161292 scopus 로고    scopus 로고
    • A companion protease inhibitor for the protection of cytosol-targeted recombinant proteins in plants
    • 10.1111/j.1467-7652.2009.00470.x, 20051033
    • Goulet C, Benchabane M, Anguenot R, Brunelle F, Khalf M, Michaud D. A companion protease inhibitor for the protection of cytosol-targeted recombinant proteins in plants. Plant Biotechnol J 2010, 8:142-154. 10.1111/j.1467-7652.2009.00470.x, 20051033.
    • (2010) Plant Biotechnol J , vol.8 , pp. 142-154
    • Goulet, C.1    Benchabane, M.2    Anguenot, R.3    Brunelle, F.4    Khalf, M.5    Michaud, D.6
  • 13
    • 1542279127 scopus 로고    scopus 로고
    • Oryzacystatin I expression in transformed tobacco produces a conditional growth phenotype and enhances chilling tolerance
    • 10.1046/j.1467-7652.2003.00010.x, 17147747
    • Van der Vyver C, Schneidereit J, Driscoll S, Turner J, Kunert K, Foyer CH. Oryzacystatin I expression in transformed tobacco produces a conditional growth phenotype and enhances chilling tolerance. Plant Biotechnol J 2003, 1:101-112. 10.1046/j.1467-7652.2003.00010.x, 17147747.
    • (2003) Plant Biotechnol J , vol.1 , pp. 101-112
    • Van der Vyver, C.1    Schneidereit, J.2    Driscoll, S.3    Turner, J.4    Kunert, K.5    Foyer, C.H.6
  • 14
    • 44649165814 scopus 로고    scopus 로고
    • Cysteine proteinases regulate chloroplast protein content and composition in tobacco leaves: a model for dynamic interactions with ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) vesicular bodies
    • Prins A, van Heerden PDR, Olmos E, Kunert KJ, Foyer CH. Cysteine proteinases regulate chloroplast protein content and composition in tobacco leaves: a model for dynamic interactions with ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) vesicular bodies. J Exp Bot 2008, 59:1935-1950.
    • (2008) J Exp Bot , vol.59 , pp. 1935-1950
    • Prins, A.1    van Heerden, P.D.R.2    Olmos, E.3    Kunert, K.J.4    Foyer, C.H.5
  • 16
    • 48149110148 scopus 로고    scopus 로고
    • Two cysteine proteinase inhibitors from Arabidopsis thaliana, AtCYSa and AtCYSb, increasing the salt, drought, oxidation and cold tolerance
    • 10.1007/s11103-008-9357-x, 18523728
    • Zhang X, Liu S, Takano T. Two cysteine proteinase inhibitors from Arabidopsis thaliana, AtCYSa and AtCYSb, increasing the salt, drought, oxidation and cold tolerance. Plant Mol Biol 2008, 68:131-143. 10.1007/s11103-008-9357-x, 18523728.
    • (2008) Plant Mol Biol , vol.68 , pp. 131-143
    • Zhang, X.1    Liu, S.2    Takano, T.3
  • 17
    • 46949098779 scopus 로고    scopus 로고
    • A Bowman-Birk protease inhibitor is involved in the tolerance to salt stress in wheat
    • 10.1111/j.1365-3040.2008.01825.x, 18433440
    • Shan L, Li C, Chan F, Zhao S, Xia G. A Bowman-Birk protease inhibitor is involved in the tolerance to salt stress in wheat. Plant Cell Environ 2008, 31:1128-1137. 10.1111/j.1365-3040.2008.01825.x, 18433440.
    • (2008) Plant Cell Environ , vol.31 , pp. 1128-1137
    • Shan, L.1    Li, C.2    Chan, F.3    Zhao, S.4    Xia, G.5
  • 18
    • 63049089591 scopus 로고    scopus 로고
    • Constitutive expression of a trypsin protease inhibitor confers multiple stress tolerance in transgenic tobacco
    • 10.1093/pcp/pcp014, 19179349
    • Srinivasan T, Kumar KRR, Kirti PB. Constitutive expression of a trypsin protease inhibitor confers multiple stress tolerance in transgenic tobacco. Plant Cell Physiol 2009, 50:541-553. 10.1093/pcp/pcp014, 19179349.
    • (2009) Plant Cell Physiol , vol.50 , pp. 541-553
    • Srinivasan, T.1    Kumar, K.R.R.2    Kirti, P.B.3
  • 19
    • 85007864106 scopus 로고
    • Two distinct species of corn cystatin in corn kernels
    • 10.1271/bbb.59.756, 7772847
    • Abe M, Abe K, Domoto C, Arai S. Two distinct species of corn cystatin in corn kernels. Biosci Biotechnol Biochem 1995, 59:756-758. 10.1271/bbb.59.756, 7772847.
    • (1995) Biosci Biotechnol Biochem , vol.59 , pp. 756-758
    • Abe, M.1    Abe, K.2    Domoto, C.3    Arai, S.4
  • 20
    • 27744530768 scopus 로고    scopus 로고
    • A hybrid, broad-spectrum inhibitor of Colorado potato beetle aspartate and cysteine proteinases
    • 10.1002/arch.20078, 16116621
    • Brunelle F, Girard C, Cloutier C, Michaud D. A hybrid, broad-spectrum inhibitor of Colorado potato beetle aspartate and cysteine proteinases. Arch Insect Biochem Physiol 2005, 60:20-31. 10.1002/arch.20078, 16116621.
    • (2005) Arch Insect Biochem Physiol , vol.60 , pp. 20-31
    • Brunelle, F.1    Girard, C.2    Cloutier, C.3    Michaud, D.4
  • 21
    • 60349086202 scopus 로고    scopus 로고
    • A SELDI-TOF MS procedure for the detection, quantitation, and preliminary characterization of low-molecular-weight recombinant proteins expressed in transgenic plants
    • 10.1002/pmic.200700233, 19086095
    • Badri MA, Rivard D, Coenen K, Vaillancourt L-P, Goulet C, Michaud D. A SELDI-TOF MS procedure for the detection, quantitation, and preliminary characterization of low-molecular-weight recombinant proteins expressed in transgenic plants. Proteomics 2009, 9:233-241. 10.1002/pmic.200700233, 19086095.
    • (2009) Proteomics , vol.9 , pp. 233-241
    • Badri, M.A.1    Rivard, D.2    Coenen, K.3    Vaillancourt, L.-P.4    Goulet, C.5    Michaud, D.6
  • 22
    • 0042831314 scopus 로고    scopus 로고
    • Oryzacystatin I expressed in transgenic potato induces digestive compensation in an insect natural predator via its herbivorous prey feeding on the plant
    • 10.1046/j.1365-294X.2003.01919.x, 12919481
    • Bouchard T, Cloutier C, Michaud D. Oryzacystatin I expressed in transgenic potato induces digestive compensation in an insect natural predator via its herbivorous prey feeding on the plant. Mol Ecol 2003, 12:2439-2446. 10.1046/j.1365-294X.2003.01919.x, 12919481.
    • (2003) Mol Ecol , vol.12 , pp. 2439-2446
    • Bouchard, T.1    Cloutier, C.2    Michaud, D.3
  • 23
    • 1642586903 scopus 로고    scopus 로고
    • Colorado potato beetles show differential digestive compensatory responses to host plants expressing distinct sets of defense proteins
    • 10.1002/arch.10136, 14981656
    • Rivard D, Cloutier C, Michaud D. Colorado potato beetles show differential digestive compensatory responses to host plants expressing distinct sets of defense proteins. Arch Insect Biochem Physiol 2004, 55:114-123. 10.1002/arch.10136, 14981656.
    • (2004) Arch Insect Biochem Physiol , vol.55 , pp. 114-123
    • Rivard, D.1    Cloutier, C.2    Michaud, D.3
  • 24
    • 33751243068 scopus 로고    scopus 로고
    • Enhanced tolerance of transgenic potato plants expressing both superoxide dismutase and ascorbate peroxidase in chloroplasts against oxidative stress and high temperature
    • 10.1007/s00299-006-0199-1, 16841217
    • Tang L, Kwon S-Y, Kim S-H, Kim J-S, Choi JS, Cho KY, Sung CK, Kwak S-S, Lee H-S. Enhanced tolerance of transgenic potato plants expressing both superoxide dismutase and ascorbate peroxidase in chloroplasts against oxidative stress and high temperature. Plant Cell Rep 2006, 25:1380-1386. 10.1007/s00299-006-0199-1, 16841217.
    • (2006) Plant Cell Rep , vol.25 , pp. 1380-1386
    • Tang, L.1    Kwon, S.-Y.2    Kim, S.-H.3    Kim, J.-S.4    Choi, J.S.5    Cho, K.Y.6    Sung, C.K.7    Kwak, S.-S.8    Lee, H.-S.9
  • 25
    • 46649121083 scopus 로고    scopus 로고
    • Enhanced tolerance of transgenic potato plants overexpressing nucleoside diphosphate kinase 2 against multiple environmental stresses
    • 10.1007/s11248-007-9155-2, 18027101
    • Tang L, Kim MD, Yang K-S, Kwon S-Y, Kim S-H, Kim J-S, Yun D-J, Kwak S-S, Lee H-S. Enhanced tolerance of transgenic potato plants overexpressing nucleoside diphosphate kinase 2 against multiple environmental stresses. Transgenic Res 2008, 17:705-715. 10.1007/s11248-007-9155-2, 18027101.
    • (2008) Transgenic Res , vol.17 , pp. 705-715
    • Tang, L.1    Kim, M.D.2    Yang, K.-S.3    Kwon, S.-Y.4    Kim, S.-H.5    Kim, J.-S.6    Yun, D.-J.7    Kwak, S.-S.8    Lee, H.-S.9
  • 26
    • 77952050772 scopus 로고    scopus 로고
    • Simultaneous expression of choline oxidase, superoxide dismutase and ascorbate peroxidase in potato plant chloroplasts provides synergistically enhanced protection against various abiotic stresses
    • 10.1111/j.1399-3054.2010.01348.x, 20059737
    • Ahmad R, Kim Y-H, Kim M-D, Kwon W-Y, Cho K, Lee H-S, Kwak S-S. Simultaneous expression of choline oxidase, superoxide dismutase and ascorbate peroxidase in potato plant chloroplasts provides synergistically enhanced protection against various abiotic stresses. Physiol Plant 2010, 138:520-533. 10.1111/j.1399-3054.2010.01348.x, 20059737.
    • (2010) Physiol Plant , vol.138 , pp. 520-533
    • Ahmad, R.1    Kim, Y.-H.2    Kim, M.-D.3    Kwon, W.-Y.4    Cho, K.5    Lee, H.-S.6    Kwak, S.-S.7
  • 27
    • 77956525559 scopus 로고    scopus 로고
    • Enhanced tolerance to methyl viologen-induced oxidative stress and high temperature in transgenic potato plants overexpressing the CuZnSOD, APX and NDPK2 genes
    • 10.1111/j.1399-3054.2010.01392.x, 20553417
    • Kim MD, Kim Y-H, Kwon W-Y, Yun D-J, Kwak S-S, Lee H-S. Enhanced tolerance to methyl viologen-induced oxidative stress and high temperature in transgenic potato plants overexpressing the CuZnSOD, APX and NDPK2 genes. Physiol Plant 2010, 140:153-162. 10.1111/j.1399-3054.2010.01392.x, 20553417.
    • (2010) Physiol Plant , vol.140 , pp. 153-162
    • Kim, M.D.1    Kim, Y.-H.2    Kwon, W.-Y.3    Yun, D.-J.4    Kwak, S.-S.5    Lee, H.-S.6
  • 28
    • 79952309382 scopus 로고    scopus 로고
    • Transgenic poplar expressing Arabidopsis NDPK2 enhances growth as well as oxidative stress tolerance
    • 10.1111/j.1467-7652.2010.00551.x, 20649941
    • Kim Y-H, Kim MD, Choi YI, Park S-C, Yun D-J, Noh EW, Lee H-S, Kwak S-S. Transgenic poplar expressing Arabidopsis NDPK2 enhances growth as well as oxidative stress tolerance. Plant Biotechnol J 2011, 9:334-347. 10.1111/j.1467-7652.2010.00551.x, 20649941.
    • (2011) Plant Biotechnol J , vol.9 , pp. 334-347
    • Kim, Y.-H.1    Kim, M.D.2    Choi, Y.I.3    Park, S.-C.4    Yun, D.-J.5    Noh, E.W.6    Lee, H.-S.7    Kwak, S.-S.8
  • 29
    • 0141652912 scopus 로고    scopus 로고
    • Systemic acquired resistance in sunflower (Heliothus annuus L.)
    • Dmitriev A, Tena M, Jorrin J. Systemic acquired resistance in sunflower (Heliothus annuus L.). Tsitol Genet 2003, 37:9-15.
    • (2003) Tsitol Genet , vol.37 , pp. 9-15
    • Dmitriev, A.1    Tena, M.2    Jorrin, J.3
  • 30
    • 33745661019 scopus 로고    scopus 로고
    • Induction of disease resistance by acibenzolar-S-methyl and o-hydroxyethylorutin against Botrytis cinerea in tomato plants
    • Malolepsza U. Induction of disease resistance by acibenzolar-S-methyl and o-hydroxyethylorutin against Botrytis cinerea in tomato plants. Crop Protect 2010, 25:956-962.
    • (2010) Crop Protect , vol.25 , pp. 956-962
    • Malolepsza, U.1
  • 31
    • 84857249571 scopus 로고    scopus 로고
    • Malus hupehensis NPR1 induces pathogenesis-related protein gene expression in transgenic tobacco
    • Zhang JY, Qiao YS, Ly D, Gao ZH, Qu SC, Zhang A. Malus hupehensis NPR1 induces pathogenesis-related protein gene expression in transgenic tobacco. Plant Biol Suppl 2012, 1:46-56.
    • (2012) Plant Biol Suppl , vol.1 , pp. 46-56
    • Zhang, J.Y.1    Qiao, Y.S.2    Ly, D.3    Gao, Z.H.4    Qu, S.C.5    Zhang, A.6
  • 32
    • 32444435764 scopus 로고    scopus 로고
    • Enhanced resistance to Botrytis cinerea mediated by the transgenic expression of the chitinase gene ch5B in strawberry
    • 10.1007/s11248-005-2543-6, 16475010
    • Vellicce GR, Diaz Ricci JC, Hernandez L, Castagnaro AP. Enhanced resistance to Botrytis cinerea mediated by the transgenic expression of the chitinase gene ch5B in strawberry. Transgenic Res 2006, 15:57-68. 10.1007/s11248-005-2543-6, 16475010.
    • (2006) Transgenic Res , vol.15 , pp. 57-68
    • Vellicce, G.R.1    Diaz Ricci, J.C.2    Hernandez, L.3    Castagnaro, A.P.4
  • 33
    • 50849129128 scopus 로고    scopus 로고
    • Defence-related gene expression in transgenic lemon plants producing an antimicrobial Trichoderma harzianum endochitinase during fungal infection
    • 10.1007/s11248-008-9172-9, 18306055
    • Distefano G, La Malfa S, Vitale A, Lorito M, Deng Z, Gentile A. Defence-related gene expression in transgenic lemon plants producing an antimicrobial Trichoderma harzianum endochitinase during fungal infection. Transgenic Res 2008, 17:873-879. 10.1007/s11248-008-9172-9, 18306055.
    • (2008) Transgenic Res , vol.17 , pp. 873-879
    • Distefano, G.1    La Malfa, S.2    Vitale, A.3    Lorito, M.4    Deng, Z.5    Gentile, A.6
  • 34
    • 79952704512 scopus 로고    scopus 로고
    • Production of marker-free disease-resistant potato using isopentenyl transferase gene as a positive selection marker
    • 10.1007/s00299-010-0974-x, 21184230
    • Khan RS, Ntui VO, Chin DP, Nakamura I, Mii M. Production of marker-free disease-resistant potato using isopentenyl transferase gene as a positive selection marker. Plant Cell Rep 2011, 30:587-597. 10.1007/s00299-010-0974-x, 21184230.
    • (2011) Plant Cell Rep , vol.30 , pp. 587-597
    • Khan, R.S.1    Ntui, V.O.2    Chin, D.P.3    Nakamura, I.4    Mii, M.5
  • 37
    • 0034729657 scopus 로고    scopus 로고
    • The hypersensitive response facilitates plant infection by the necrotrophic pathogen Botrytis cinerea
    • 10.1016/S0960-9822(00)00560-1, 10898976
    • Govrin EM, Levine A. The hypersensitive response facilitates plant infection by the necrotrophic pathogen Botrytis cinerea. Curr Biol 2000, 10:751-757. 10.1016/S0960-9822(00)00560-1, 10898976.
    • (2000) Curr Biol , vol.10 , pp. 751-757
    • Govrin, E.M.1    Levine, A.2
  • 38
    • 33644913392 scopus 로고    scopus 로고
    • An elicitor from Botrytis cinerea induces the hypersensitive response in Arabidopsis thaliana and other plants and promotes the gray mold disease
    • 10.1094/PHYTO-96-0299, 18944445
    • Govrin EM, Rachmilevith S, Tiwari BS, Solomon M, Levine A. An elicitor from Botrytis cinerea induces the hypersensitive response in Arabidopsis thaliana and other plants and promotes the gray mold disease. Phytopathology 2006, 96:299-307. 10.1094/PHYTO-96-0299, 18944445.
    • (2006) Phytopathology , vol.96 , pp. 299-307
    • Govrin, E.M.1    Rachmilevith, S.2    Tiwari, B.S.3    Solomon, M.4    Levine, A.5
  • 39
    • 33745247390 scopus 로고    scopus 로고
    • Expression of barley BAX Inhibitor-1 in carrots confers resistance to Botrytis cinerea
    • 10.1111/j.1364-3703.2006.00339.x, 20507447
    • Imani J, Baltruschat H, Stein E, Jia G, Vogelsberg J, Kogel K-H, Hückelhoven R. Expression of barley BAX Inhibitor-1 in carrots confers resistance to Botrytis cinerea. Mol Plant Pathol 2006, 7:279-284. 10.1111/j.1364-3703.2006.00339.x, 20507447.
    • (2006) Mol Plant Pathol , vol.7 , pp. 279-284
    • Imani, J.1    Baltruschat, H.2    Stein, E.3    Jia, G.4    Vogelsberg, J.5    Kogel, K.-H.6    Hückelhoven, R.7
  • 40
    • 33846042529 scopus 로고    scopus 로고
    • Histochemical and genetic analysis of host and non-host interactions of Arabidopsis with three Botrytis species: an important role for cell death control
    • 10.1111/j.1364-3703.2006.00367.x, 20507477
    • van Baarlen P, Woltering EJ, Staats M, van Kan JAL. Histochemical and genetic analysis of host and non-host interactions of Arabidopsis with three Botrytis species: an important role for cell death control. Mol Plant Pathol 2007, 8:41-54. 10.1111/j.1364-3703.2006.00367.x, 20507477.
    • (2007) Mol Plant Pathol , vol.8 , pp. 41-54
    • van Baarlen, P.1    Woltering, E.J.2    Staats, M.3    van Kan, J.A.L.4
  • 41
    • 79960505724 scopus 로고    scopus 로고
    • The sesquiterpene botrydial produced by Botrytis cinerea induces the hypersensitive response on plant tissues and its action is modulated by salicylic acid and jasmonic acid signaling
    • 10.1094/MPMI-10-10-0248, 21751851
    • Rossi FR, Garriz A, Marina M, Romero FM, Gonzalez ME, Gonzalez Collado I, Pieckenstain FL. The sesquiterpene botrydial produced by Botrytis cinerea induces the hypersensitive response on plant tissues and its action is modulated by salicylic acid and jasmonic acid signaling. Mol Plant Microbe Interact 2011, 24:888-896. 10.1094/MPMI-10-10-0248, 21751851.
    • (2011) Mol Plant Microbe Interact , vol.24 , pp. 888-896
    • Rossi, F.R.1    Garriz, A.2    Marina, M.3    Romero, F.M.4    Gonzalez, M.E.5    Gonzalez Collado, I.6    Pieckenstain, F.L.7
  • 42
  • 43
    • 77953825646 scopus 로고    scopus 로고
    • 2-DE proteomic approach to the Botrytis cinerea secretome induced with different carbon sources and plant-based elicitors
    • 10.1002/pmic.200900408, 20376862
    • Fernandez-Acero FJ, Colby T, Harzen A, Carbu M, Wieneke U, Cantoral JM, Schmidt J. 2-DE proteomic approach to the Botrytis cinerea secretome induced with different carbon sources and plant-based elicitors. Proteomics 2010, 10:2270-2280. 10.1002/pmic.200900408, 20376862.
    • (2010) Proteomics , vol.10 , pp. 2270-2280
    • Fernandez-Acero, F.J.1    Colby, T.2    Harzen, A.3    Carbu, M.4    Wieneke, U.5    Cantoral, J.M.6    Schmidt, J.7
  • 44
    • 0001709810 scopus 로고
    • The roles of aspartic protease and endo-pectin lyase enzymes in the primary stages of infection and pathogenesis of various host tissues by different isolates of Botrytis cinerea Pesr. ex Pers
    • Movahedi S, Heale JB. The roles of aspartic protease and endo-pectin lyase enzymes in the primary stages of infection and pathogenesis of various host tissues by different isolates of Botrytis cinerea Pesr. ex Pers. Physiol Mol Plant Pathol 1990, 36:303-324.
    • (1990) Physiol Mol Plant Pathol , vol.36 , pp. 303-324
    • Movahedi, S.1    Heale, J.B.2
  • 45
    • 4344605203 scopus 로고    scopus 로고
    • An aspartic proteinase gene family in the filamentous fungus Botrytis cinerea contains members with novel features
    • 10.1099/mic.0.27058-0, 15256589
    • ten Have A, Dekkers E, Kay J, Phylip LH, van Kan JAL. An aspartic proteinase gene family in the filamentous fungus Botrytis cinerea contains members with novel features. Microbiology 2004, 150:2475-2489. 10.1099/mic.0.27058-0, 15256589.
    • (2004) Microbiology , vol.150 , pp. 2475-2489
    • ten Have, A.1    Dekkers, E.2    Kay, J.3    Phylip, L.H.4    van Kan, J.A.L.5
  • 46
    • 67650745015 scopus 로고    scopus 로고
    • PH controls both transcription and post-translational processing of the protease BcACP1 in the phytopathogenic fungus Botrytis cinerea
    • 10.1099/mic.0.025999-0, 19359322
    • Rolland S, Bruel C, Rascle C, Girard V, Billon-Grand G, Poussereau N. pH controls both transcription and post-translational processing of the protease BcACP1 in the phytopathogenic fungus Botrytis cinerea. Microbiology 2009, 155:2097-2105. 10.1099/mic.0.025999-0, 19359322.
    • (2009) Microbiology , vol.155 , pp. 2097-2105
    • Rolland, S.1    Bruel, C.2    Rascle, C.3    Girard, V.4    Billon-Grand, G.5    Poussereau, N.6
  • 47
    • 0032547704 scopus 로고    scopus 로고
    • Gel electrophoresis of proteolytic enzymes
    • Michaud D. Gel electrophoresis of proteolytic enzymes. Anal Chim Acta 1998, 372:173-185.
    • (1998) Anal Chim Acta , vol.372 , pp. 173-185
    • Michaud, D.1
  • 48
    • 21344450737 scopus 로고    scopus 로고
    • Molecular cloning, recombinant gene expression, and antifungal activity of cystatin from taro (Colocasia esculenta cv. Kaosiung no. 1)
    • 10.1007/s00425-004-1462-8, 15647900
    • Yang AH, Yeh KW. Molecular cloning, recombinant gene expression, and antifungal activity of cystatin from taro (Colocasia esculenta cv. Kaosiung no. 1). Planta 2005, 221:493-501. 10.1007/s00425-004-1462-8, 15647900.
    • (2005) Planta , vol.221 , pp. 493-501
    • Yang, A.H.1    Yeh, K.W.2
  • 49
    • 33646429223 scopus 로고    scopus 로고
    • A cold inducible multidomain cystatin from winter wheat inhibits growth of the snow mold fungus, Microdochium nivale
    • 10.1007/s00425-005-0169-9, 16320069
    • Christova PK, Christov NK, Imai R. A cold inducible multidomain cystatin from winter wheat inhibits growth of the snow mold fungus, Microdochium nivale. Planta 2006, 223:1207-1218. 10.1007/s00425-005-0169-9, 16320069.
    • (2006) Planta , vol.223 , pp. 1207-1218
    • Christova, P.K.1    Christov, N.K.2    Imai, R.3
  • 50
    • 80053213775 scopus 로고    scopus 로고
    • Differential in vitro and in vivo effect of barley cysteine and serine protease inhibitors on phytopathogenic microorganisms
    • 10.1016/j.plaphy.2011.03.012, 21482127
    • Carrillo L, Herrero I, Cambra I, Sanchez-Monge R, Diaz I, Martinez M. Differential in vitro and in vivo effect of barley cysteine and serine protease inhibitors on phytopathogenic microorganisms. Plant Physiol Biochem 2011, 49:1191-1200. 10.1016/j.plaphy.2011.03.012, 21482127.
    • (2011) Plant Physiol Biochem , vol.49 , pp. 1191-1200
    • Carrillo, L.1    Herrero, I.2    Cambra, I.3    Sanchez-Monge, R.4    Diaz, I.5    Martinez, M.6
  • 51
    • 17344392459 scopus 로고    scopus 로고
    • Inhibition of plant-pathogenic fungi by the barley cystatin Hv-VPI (gene Icy) is not associated with its cysteine-proteinase inhibitory properties
    • 10.1094/MPMI.2003.16.10.876, 14558689
    • Martinez M, Lopez-Solanilla E, Rodriguez-Palenzuela P, Carbonero P, Diaz I. Inhibition of plant-pathogenic fungi by the barley cystatin Hv-VPI (gene Icy) is not associated with its cysteine-proteinase inhibitory properties. Mol Plant Microbe Interact 2003, 16:876-883. 10.1094/MPMI.2003.16.10.876, 14558689.
    • (2003) Mol Plant Microbe Interact , vol.16 , pp. 876-883
    • Martinez, M.1    Lopez-Solanilla, E.2    Rodriguez-Palenzuela, P.3    Carbonero, P.4    Diaz, I.5
  • 52
    • 21344448153 scopus 로고    scopus 로고
    • The strawberry gene Cyf1 encodes a phytocystatin with antifungal properties
    • 10.1093/jxb/eri172, 15897228
    • Martinez M, Abraham Z, Gambardella M, Echaide M, Carbonero P, Diaz I. The strawberry gene Cyf1 encodes a phytocystatin with antifungal properties. J Exp Bot 2005, 56:1821-1829. 10.1093/jxb/eri172, 15897228.
    • (2005) J Exp Bot , vol.56 , pp. 1821-1829
    • Martinez, M.1    Abraham, Z.2    Gambardella, M.3    Echaide, M.4    Carbonero, P.5    Diaz, I.6
  • 54
    • 33846921346 scopus 로고    scopus 로고
    • A multicomponent, elicitor-inducible cystatin complex in tomato, Solanum lycopersicum
    • 10.1111/j.1469-8137.2007.01968.x, 17286832
    • Girard C, Rivard D, Kiggundu A, Kunert K, Gleddie SC, Cloutier C, Michaud D. A multicomponent, elicitor-inducible cystatin complex in tomato, Solanum lycopersicum. New Phytol 2007, 173:841-851. 10.1111/j.1469-8137.2007.01968.x, 17286832.
    • (2007) New Phytol , vol.173 , pp. 841-851
    • Girard, C.1    Rivard, D.2    Kiggundu, A.3    Kunert, K.4    Gleddie, S.C.5    Cloutier, C.6    Michaud, D.7
  • 55
    • 77954065435 scopus 로고    scopus 로고
    • Deficiencies in jasmonate-mediated plant defense reveal quantitative variation in Botrytis cinerea pathogenesis
    • Rowe HC, Walley JW, Corwin J, Chan EK-F, Dehesh K, Kliebenstein DJ. Deficiencies in jasmonate-mediated plant defense reveal quantitative variation in Botrytis cinerea pathogenesis. PLoS Path 2010, 6(4):e1000861.
    • (2010) PLoS Path , vol.6 , Issue.4
    • Rowe, H.C.1    Walley, J.W.2    Corwin, J.3    Chan, E.K.-F.4    Dehesh, K.5    Kliebenstein, D.J.6
  • 56
    • 1242300208 scopus 로고    scopus 로고
    • The salicylic acid-dependent defence pathway is effective against different pathogens in tomato and tobacco
    • Achuo EA, Audenaert K, Meziane H, Höfte M. The salicylic acid-dependent defence pathway is effective against different pathogens in tomato and tobacco. Plant Pathol 2004, 53:65-72.
    • (2004) Plant Pathol , vol.53 , pp. 65-72
    • Achuo, E.A.1    Audenaert, K.2    Meziane, H.3    Höfte, M.4
  • 57
    • 79960923169 scopus 로고    scopus 로고
    • Botrytis cinereamanipulates the antagonistic effects between immune pathways to promote disease development in tomato
    • 10.1105/tpc.111.083394, 3160041, 21665999
    • El Oirdi M, El Rahman TA, Rigano L, El Hadrami A, Rodriguez MC, Daayf F, Vojnov A, Bouarab K. Botrytis cinereamanipulates the antagonistic effects between immune pathways to promote disease development in tomato. Plant Cell 2011, 23:2405-2421. 10.1105/tpc.111.083394, 3160041, 21665999.
    • (2011) Plant Cell , vol.23 , pp. 2405-2421
    • El Oirdi, M.1    El Rahman, T.A.2    Rigano, L.3    El Hadrami, A.4    Rodriguez, M.C.5    Daayf, F.6    Vojnov, A.7    Bouarab, K.8
  • 58
    • 33749997790 scopus 로고    scopus 로고
    • Modulating the proteinase inhibitory profile of a plant cystatin by single mutations at positively selected amino acid sites
    • 10.1111/j.1365-313X.2006.02878.x, 16965553
    • Kiggundu A, Goulet M-C, Goulet C, Dubuc J-F, Rivard D, Benchabane M, Pépin G, van der Vyver C, Kunert K, Michaud D. Modulating the proteinase inhibitory profile of a plant cystatin by single mutations at positively selected amino acid sites. Plant J 2006, 48:403-413. 10.1111/j.1365-313X.2006.02878.x, 16965553.
    • (2006) Plant J , vol.48 , pp. 403-413
    • Kiggundu, A.1    Goulet, M.-C.2    Goulet, C.3    Dubuc, J.-F.4    Rivard, D.5    Benchabane, M.6    Pépin, G.7    van der Vyver, C.8    Kunert, K.9    Michaud, D.10
  • 59
    • 48949107741 scopus 로고    scopus 로고
    • Tailoring the specificity of a plant cystatin toward herbivorous insect digestive cysteine proteases by single mutations at positively selected amino acid sites
    • 10.1104/pp.108.115741, 2259044, 18192440
    • Goulet M-C, Dallaire C, Vaillancourt L-P, Khalf M, Badri MA, Preradov A, Duceppe M-O, Goulet C, Cloutier C, Michaud D. Tailoring the specificity of a plant cystatin toward herbivorous insect digestive cysteine proteases by single mutations at positively selected amino acid sites. Plant Physiol 2008, 146:1010-1019. 10.1104/pp.108.115741, 2259044, 18192440.
    • (2008) Plant Physiol , vol.146 , pp. 1010-1019
    • Goulet, M.-C.1    Dallaire, C.2    Vaillancourt, L.-P.3    Khalf, M.4    Badri, M.A.5    Preradov, A.6    Duceppe, M.-O.7    Goulet, C.8    Cloutier, C.9    Michaud, D.10
  • 60
    • 60549094811 scopus 로고    scopus 로고
    • On-chip detection of low-molecular-weight recombinant proteins in plant crude extracts by SELDI-TOF MS
    • Badri MA, Coenen K, Vaillancourt L-P, Goulet C, Michaud D. On-chip detection of low-molecular-weight recombinant proteins in plant crude extracts by SELDI-TOF MS. Meth Mol Biol 2009, 483:313-324.
    • (2009) Meth Mol Biol , vol.483 , pp. 313-324
    • Badri, M.A.1    Coenen, K.2    Vaillancourt, L.-P.3    Goulet, C.4    Michaud, D.5
  • 61
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • 10.1016/0003-2697(76)90527-3, 942051
    • Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976, 72:248-254. 10.1016/0003-2697(76)90527-3, 942051.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 62
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 10.1038/227680a0, 5432063
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685. 10.1038/227680a0, 5432063.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 64
    • 0027437730 scopus 로고
    • Selective inhibition of Colorado potato beetle cathepsin H by oryzacystatins I and II
    • 10.1016/0014-5793(93)80320-T, 8405400
    • Michaud D, Nguyen-Quoc B, Yelle S. Selective inhibition of Colorado potato beetle cathepsin H by oryzacystatins I and II. FEBS Lett 1993, 331:173-176. 10.1016/0014-5793(93)80320-T, 8405400.
    • (1993) FEBS Lett , vol.331 , pp. 173-176
    • Michaud, D.1    Nguyen-Quoc, B.2    Yelle, S.3
  • 65
    • 0030046451 scopus 로고    scopus 로고
    • Assessing the stability of cystatin/cysteine proteinase complexes using mildly-denaturing gelatin-polyacrylamide gel electrophoresis
    • 10.1002/elps.1150170113, 8907521
    • Michaud D, Cantin L, Raworth DA, Vrain TC. Assessing the stability of cystatin/cysteine proteinase complexes using mildly-denaturing gelatin-polyacrylamide gel electrophoresis. Electrophoresis 1996, 17:74-79. 10.1002/elps.1150170113, 8907521.
    • (1996) Electrophoresis , vol.17 , pp. 74-79
    • Michaud, D.1    Cantin, L.2    Raworth, D.A.3    Vrain, T.C.4
  • 66
    • 0027202477 scopus 로고
    • Purification and characterization of the extracellular aspartyl proteinase of Candida albicans: removal of extraneous proteins and cell wall mannoprotein and evidence for lack of glycosylation
    • 10.1099/00221287-139-6-1177, 8360611
    • Morrisson CJ, Hurst SF, Bragg SL, Kuykendall RJ, Diaz H, McLaughlin DW, Reiss E. Purification and characterization of the extracellular aspartyl proteinase of Candida albicans: removal of extraneous proteins and cell wall mannoprotein and evidence for lack of glycosylation. J Gen Microbiol 1993, 139:1177-1186. 10.1099/00221287-139-6-1177, 8360611.
    • (1993) J Gen Microbiol , vol.139 , pp. 1177-1186
    • Morrisson, C.J.1    Hurst, S.F.2    Bragg, S.L.3    Kuykendall, R.J.4    Diaz, H.5    McLaughlin, D.W.6    Reiss, E.7
  • 67
    • 0034201087 scopus 로고    scopus 로고
    • Adult Colorado potato beetles, Leptinotarsa decemlineata compensate for nutritional stress on oryzacystatin I transgenic potato plants by hypertrophic behavior and over-production of insensitive proteases
    • 10.1002/1520-6327(200006)44:2<69::AID-ARCH2>3.0.CO;2-6, 10861867
    • Cloutier C, Jean C, Fournier M, Yelle S, Michaud D. Adult Colorado potato beetles, Leptinotarsa decemlineata compensate for nutritional stress on oryzacystatin I transgenic potato plants by hypertrophic behavior and over-production of insensitive proteases. Arch Insect Biochem Physiol 2000, 44:69-81. 10.1002/1520-6327(200006)44:2<69::AID-ARCH2>3.0.CO;2-6, 10861867.
    • (2000) Arch Insect Biochem Physiol , vol.44 , pp. 69-81
    • Cloutier, C.1    Jean, C.2    Fournier, M.3    Yelle, S.4    Michaud, D.5


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