메뉴 건너뛰기




Volumn 92, Issue 11, 2010, Pages 1657-1666

Plant cystatins

Author keywords

Cys proteases; Phytocystatins; Plant cystatins; Plant defense; Protease inhibitors; Protein turnover; Storage protein processing

Indexed keywords

CYSTATIN; PESTICIDE;

EID: 78149358023     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2010.06.006     Document Type: Review
Times cited : (159)

References (172)
  • 2
    • 85004645817 scopus 로고
    • Purification and characterization of a rice cysteine proteinase inhibitor
    • Abe K., Hiroto K., Arai S. Purification and characterization of a rice cysteine proteinase inhibitor. Agric. Biol. Chem. 1987, 51:2763-2765.
    • (1987) Agric. Biol. Chem. , vol.51 , pp. 2763-2765
    • Abe, K.1    Hiroto, K.2    Arai, S.3
  • 3
    • 0023657047 scopus 로고
    • Molecular cloning of a cysteine proteinase inhibitor of rice (oryzacystatin). Homology with animal cystatins and transient expression in the ripening process of rice seeds
    • Abe K., Emori Y., Kondo H., Suzuki K., Arai S. Molecular cloning of a cysteine proteinase inhibitor of rice (oryzacystatin). Homology with animal cystatins and transient expression in the ripening process of rice seeds. J. Biol. Chem. 1987, 262:16793-16797.
    • (1987) J. Biol. Chem. , vol.262 , pp. 16793-16797
    • Abe, K.1    Emori, Y.2    Kondo, H.3    Suzuki, K.4    Arai, S.5
  • 4
    • 0025160575 scopus 로고
    • Two distinct cystatin species in rice seeds with different specificities against cysteine proteinases. Molecular cloning, expression, and biochemical studies on oryzacystatin-II
    • Kondo H., Abe K., Nishimura I., Watanabe H., Emori Y., Arai S. Two distinct cystatin species in rice seeds with different specificities against cysteine proteinases. Molecular cloning, expression, and biochemical studies on oryzacystatin-II. J. Biol. Chem. 1990, 265:15832-15837.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15832-15837
    • Kondo, H.1    Abe, K.2    Nishimura, I.3    Watanabe, H.4    Emori, Y.5    Arai, S.6
  • 5
    • 0037164073 scopus 로고    scopus 로고
    • Plant seed cystatins and their target enzymes of endogenous and exogenous origin
    • 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.
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 6612-6617
    • Arai, S.1    Matsumoto, I.2    Emori, Y.3    Abe, K.4
  • 6
    • 0003071651 scopus 로고    scopus 로고
    • Cystatin-based control of insects, with special reference to oryzacystatin
    • Landes Bioscience/Eurekah.com, Georgetown, TX, D. Michaud (Ed.)
    • Arai S., Abe K. Cystatin-based control of insects, with special reference to oryzacystatin. Recombinant Protease Inhibitors in Plants 2000, 27-42. Landes Bioscience/Eurekah.com, Georgetown, TX. D. Michaud (Ed.).
    • (2000) Recombinant Protease Inhibitors in Plants , pp. 27-42
    • Arai, S.1    Abe, K.2
  • 7
    • 0025965712 scopus 로고
    • Gene organization of oryzacystatin-II, a new cystatin superfamily member of plant origin, is closely related to that of oryzacystatin-I but different from those of animal cystatins
    • Kondo H., Abe K., Emori Y., Arai S. Gene organization of oryzacystatin-II, a new cystatin superfamily member of plant origin, is closely related to that of oryzacystatin-I but different from those of animal cystatins. FEBS Lett. 1991, 278:87-90.
    • (1991) FEBS Lett. , vol.278 , pp. 87-90
    • Kondo, H.1    Abe, K.2    Emori, Y.3    Arai, S.4
  • 8
    • 0002486962 scopus 로고
    • Cysteine proteinase inhibitors of the cystatin superfamily
    • Elsevier, Amsterdam, The Netherlands, A.J. Barrett, G. Salvesen (Eds.)
    • Barrett A.J., Rawlings N.D., Davies M.E., Machleidt W., Salvesen G., Turk V. Cysteine proteinase inhibitors of the cystatin superfamily. Proteinase Inhibitors 1986, 519-569. Elsevier, Amsterdam, The Netherlands. A.J. Barrett, G. Salvesen (Eds.).
    • (1986) Proteinase Inhibitors , pp. 519-569
    • Barrett, A.J.1    Rawlings, N.D.2    Davies, M.E.3    Machleidt, W.4    Salvesen, G.5    Turk, V.6
  • 9
    • 0025817602 scopus 로고
    • The cystatins: protein inhibitors of cysteine proteinases
    • Turk V., Bode W. The cystatins: protein inhibitors of cysteine proteinases. FEBS Lett. 1991, 285:213-219.
    • (1991) FEBS Lett. , vol.285 , pp. 213-219
    • Turk, V.1    Bode, W.2
  • 10
    • 0034610303 scopus 로고    scopus 로고
    • Three-dimensional solution structure of oryzacystatin-I, a cysteine proteinase inhibitor of the rice, Oryza sativa L. japonica
    • Nagata K., Kudo N., Abe K., Arai S., Tanokura M. Three-dimensional solution structure of oryzacystatin-I, a cysteine proteinase inhibitor of the rice, Oryza sativa L. japonica. Biochemistry 2000, 39:14753-14760.
    • (2000) Biochemistry , vol.39 , pp. 14753-14760
    • Nagata, K.1    Kudo, N.2    Abe, K.3    Arai, S.4    Tanokura, M.5
  • 11
    • 0024066065 scopus 로고
    • The 2.0 A X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases
    • Bode W., Engh R., Musil D., Thiele U., Huber R., Karshikov A., Brzin J., Kos J., Turk V. The 2.0 A X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases. EMBO J. 1988, 7:2593-2599.
    • (1988) EMBO J. , vol.7 , pp. 2593-2599
    • Bode, W.1    Engh, R.2    Musil, D.3    Thiele, U.4    Huber, R.5    Karshikov, A.6    Brzin, J.7    Kos, J.8    Turk, V.9
  • 12
    • 0024570048 scopus 로고
    • Mechanism of inhibition of papain by chicken egg white cystatin. Inhibition constants of N-terminally truncated forms and cyanogen bromide fragments of the inhibitor
    • Machleidt W., Thiele U., Laber B., Assfalg-Machleidt I., Esterl A., Wiegand G., Kos J., Turk V., Bode W. Mechanism of inhibition of papain by chicken egg white cystatin. Inhibition constants of N-terminally truncated forms and cyanogen bromide fragments of the inhibitor. FEBS Lett. 1989, 243:234-238.
    • (1989) FEBS Lett. , vol.243 , pp. 234-238
    • Machleidt, W.1    Thiele, U.2    Laber, B.3    Assfalg-Machleidt, I.4    Esterl, A.5    Wiegand, G.6    Kos, J.7    Turk, V.8    Bode, W.9
  • 13
    • 0025301658 scopus 로고
    • The refined 2.4 A X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: a novel type of proteinase inhibitor interaction
    • Stubbs M.T., Laber B., Bode W., Huber R., Jerala R., Lenarcic B., Turk V. The refined 2.4 A X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: a novel type of proteinase inhibitor interaction. EMBO J. 1990, 9:1939-1947.
    • (1990) EMBO J. , vol.9 , pp. 1939-1947
    • Stubbs, M.T.1    Laber, B.2    Bode, W.3    Huber, R.4    Jerala, R.5    Lenarcic, B.6    Turk, V.7
  • 14
    • 0028937017 scopus 로고
    • Probing the functional role of the N-terminal region of cystatins by equilibrium and kinetic studies of the binding of Gly-11 variants of recombinant human cystatin C to target proteinases
    • Björk I., Brieditis I., Abrahamson M. Probing the functional role of the N-terminal region of cystatins by equilibrium and kinetic studies of the binding of Gly-11 variants of recombinant human cystatin C to target proteinases. Biochem. J. 1994, 305:513-518.
    • (1994) Biochem. J. , vol.305 , pp. 513-518
    • Björk, I.1    Brieditis, I.2    Abrahamson, M.3
  • 15
    • 0032211213 scopus 로고    scopus 로고
    • Structural and phylogenetic relationships among plant and animal cystatins
    • Margis R., Reis E.M., Villeret V. Structural and phylogenetic relationships among plant and animal cystatins. Arch. Biochem. Biophys. 1998, 359:24-30.
    • (1998) Arch. Biochem. Biophys. , vol.359 , pp. 24-30
    • Margis, R.1    Reis, E.M.2    Villeret, V.3
  • 17
    • 0025964094 scopus 로고
    • Papain-inhibitory activity of oryzacystatin, a rice seed cysteine proteinase inhibitor, depends on the central Gln-Val-Val-Ala-Gly region conserved among cystatin superfamily members
    • Arai S., Watanabe H., Kondo H., Emori Y., Abe K. Papain-inhibitory activity of oryzacystatin, a rice seed cysteine proteinase inhibitor, depends on the central Gln-Val-Val-Ala-Gly region conserved among cystatin superfamily members. J. Biochem. 1991, 109:294-298.
    • (1991) J. Biochem. , vol.109 , pp. 294-298
    • Arai, S.1    Watanabe, H.2    Kondo, H.3    Emori, Y.4    Abe, K.5
  • 18
    • 0029328272 scopus 로고
    • Engineered oryzacystatin-I expressed in transgenic hairy roots confers resistance to Globodera pallida
    • Urwin P.E., Atkinson H.J., Waller D.A., Mcpherson M.J. Engineered oryzacystatin-I expressed in transgenic hairy roots confers resistance to Globodera pallida. Plant J. 1995, 8:121-131.
    • (1995) Plant J. , vol.8 , pp. 121-131
    • Urwin, P.E.1    Atkinson, H.J.2    Waller, D.A.3    Mcpherson, M.J.4
  • 21
    • 14744275703 scopus 로고    scopus 로고
    • The power of phylogenetic comparison in revealing protein function
    • Yang Z. The power of phylogenetic comparison in revealing protein function. Proc. Natl. Acad. Sci. U.S.A. 2005, 102:3179-3180.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 3179-3180
    • Yang, Z.1
  • 23
  • 24
    • 0032032227 scopus 로고    scopus 로고
    • Amino acid substitutions in the N-terminal segment of cystatin C create selective protein inhibitors of lysosomal cysteine proteinases
    • Mason R.W., Sol-Church K., Abrahamson M. Amino acid substitutions in the N-terminal segment of cystatin C create selective protein inhibitors of lysosomal cysteine proteinases. Biochem. J. 1998, 330:833-838.
    • (1998) Biochem. J. , vol.330 , pp. 833-838
    • Mason, R.W.1    Sol-Church, K.2    Abrahamson, M.3
  • 25
    • 0141679317 scopus 로고    scopus 로고
    • Grafting of features of cystatins C or B into the N-terminal region or second binding loop of cystatin A (stefin A) substantially enhances inhibition of cysteine proteinases
    • Pavlova A., Björk I. Grafting of features of cystatins C or B into the N-terminal region or second binding loop of cystatin A (stefin A) substantially enhances inhibition of cysteine proteinases. Biochemistry 2003, 42:11326-11333.
    • (2003) Biochemistry , vol.42 , pp. 11326-11333
    • Pavlova, A.1    Björk, I.2
  • 26
    • 0024278653 scopus 로고
    • 2-terminal 21 amino acid residues are not essential for the papain-inhibitory activity of oryzacystatin, a member of the cystatin superfamily. Expression of oryzacystatin cDNA and its truncated fragments in Escherichia coli
    • 2-terminal 21 amino acid residues are not essential for the papain-inhibitory activity of oryzacystatin, a member of the cystatin superfamily. Expression of oryzacystatin cDNA and its truncated fragments in Escherichia coli. J. Biol. Chem. 1988, 263:7655-7659.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7655-7659
    • Abe, K.1    Emori, Y.2    Kondo, H.3    Arai, S.4    Suzuki, K.5
  • 27
    • 0026820709 scopus 로고
    • Rice cystatin: bacterial expression, purification, cysteine proteinase inhibitory activity, and insect growth suppressing activity of a truncated form of the protein
    • Chen M.-S., Johnson B., Wen L., Muthukrishnan S., Kramer K.J., Morgan T.D., Reeck G.R. Rice cystatin: bacterial expression, purification, cysteine proteinase inhibitory activity, and insect growth suppressing activity of a truncated form of the protein. Protein Expr. Purif. 1992, 3:41-49.
    • (1992) Protein Expr. Purif. , vol.3 , pp. 41-49
    • Chen, M.-S.1    Johnson, B.2    Wen, L.3    Muthukrishnan, S.4    Kramer, K.J.5    Morgan, T.D.6    Reeck, G.R.7
  • 28
    • 0029414805 scopus 로고
    • 2-terminal region of oryzacystatin-I in cysteine proteinase inhibition
    • 2-terminal region of oryzacystatin-I in cysteine proteinase inhibition. Protein Eng. 1995, 8:1303-1307.
    • (1995) Protein Eng. , vol.8 , pp. 1303-1307
    • Urwin, P.E.1    Atkinson, H.J.2    Mcpherson, M.J.3
  • 29
    • 0029899115 scopus 로고    scopus 로고
    • Purification, characterization, and sequencing of two cysteine proteinase inhibitors, Sca and Scb, from sunflower (Helianthus annuus) seeds
    • Kouzuma Y., Kawano K., Kimura M., Yamasaki N., Kadowaki T., Yamamoto K. Purification, characterization, and sequencing of two cysteine proteinase inhibitors, Sca and Scb, from sunflower (Helianthus annuus) seeds. J. Biochem. 1996, 119:1106-1113.
    • (1996) J. Biochem. , vol.119 , pp. 1106-1113
    • Kouzuma, Y.1    Kawano, K.2    Kimura, M.3    Yamasaki, N.4    Kadowaki, T.5    Yamamoto, K.6
  • 30
    • 0035316454 scopus 로고    scopus 로고
    • Molecular cloning and functional expression of cDNA encoding the cysteine proteinase inhibitor Sca from sunflower seeds
    • Kouzuma Y., Tsukigata K., Inanaga H., Doi-Kawano K., Yamasaki N., Kimura M. Molecular cloning and functional expression of cDNA encoding the cysteine proteinase inhibitor Sca from sunflower seeds. Biosci. Biotechnol. Biochem. 2001, 65:969-972.
    • (2001) Biosci. Biotechnol. Biochem. , vol.65 , pp. 969-972
    • Kouzuma, Y.1    Tsukigata, K.2    Inanaga, H.3    Doi-Kawano, K.4    Yamasaki, N.5    Kimura, M.6
  • 31
    • 0031759357 scopus 로고    scopus 로고
    • Molecular cloning, functional expression, and mutagenesis of cDNA encoding a cysteine proteinase inhibitor from sunflower seeds
    • Doi-Kawano K., Kouzuma Y., Yamasaki N., Kimura M. Molecular cloning, functional expression, and mutagenesis of cDNA encoding a cysteine proteinase inhibitor from sunflower seeds. J. Biochem. 1998, 124:911-916.
    • (1998) J. Biochem. , vol.124 , pp. 911-916
    • Doi-Kawano, K.1    Kouzuma, Y.2    Yamasaki, N.3    Kimura, M.4
  • 32
    • 70349261441 scopus 로고    scopus 로고
    • Steady-state and time-resolved fluorescence spectroscopic studies on interaction of the N-terminal region with the hairpin loop of the phytocystatin Scb
    • Doi-Kawano K., Nishimoto R., Kouzuma Y., Takahashi D., Yamashita S., Kimura K. Steady-state and time-resolved fluorescence spectroscopic studies on interaction of the N-terminal region with the hairpin loop of the phytocystatin Scb. J. Fluoresc. 2009, 19:631-639.
    • (2009) J. Fluoresc. , vol.19 , pp. 631-639
    • Doi-Kawano, K.1    Nishimoto, R.2    Kouzuma, Y.3    Takahashi, D.4    Yamashita, S.5    Kimura, K.6
  • 34
    • 0031013054 scopus 로고    scopus 로고
    • Friends and relations of the cystatin superfamily-new members and their evolution
    • Brown W.M., Dziegielewska K.M. Friends and relations of the cystatin superfamily-new members and their evolution. Protein Sci. 1997, 6:5-12.
    • (1997) Protein Sci. , vol.6 , pp. 5-12
    • Brown, W.M.1    Dziegielewska, K.M.2
  • 35
    • 0024424222 scopus 로고
    • Cloning and sequence analysis of the genomic DNA fragment encoding oryzacystatin
    • Kondo H., Emori Y., Abe K., Arai S. Cloning and sequence analysis of the genomic DNA fragment encoding oryzacystatin. Gene 1989, 81:259-265.
    • (1989) Gene , vol.81 , pp. 259-265
    • Kondo, H.1    Emori, Y.2    Abe, K.3    Arai, S.4
  • 36
    • 0027691245 scopus 로고
    • Characterization of a genomic sequence coding for potato multicystatin, an eight-domain cysteine proteinase inhibitor
    • Waldron C., Wegrich L.M., Owens Merlo P.A., Walsh T.A. Characterization of a genomic sequence coding for potato multicystatin, an eight-domain cysteine proteinase inhibitor. Plant Mol. Biol. 1993, 23:801-812.
    • (1993) Plant Mol. Biol. , vol.23 , pp. 801-812
    • Waldron, C.1    Wegrich, L.M.2    Owens Merlo, P.A.3    Walsh, T.A.4
  • 37
    • 72049098213 scopus 로고    scopus 로고
    • Phylogenomic analysis of the cystatin superfamily in eucaryotes and prokaryotes
    • Kordis D., Turk V. Phylogenomic analysis of the cystatin superfamily in eucaryotes and prokaryotes. BMC Evol. Biol. 2009, 9:266.
    • (2009) BMC Evol. Biol. , vol.9 , pp. 266
    • Kordis, D.1    Turk, V.2
  • 38
    • 52149099442 scopus 로고    scopus 로고
    • Molecular evolution and diversification of plant cysteine proteinase inhibitors: new insights after the poplar genome
    • Margis-Pinheiro M., Zolet A.C.T., Loss G., Pasquali G., Margis R. Molecular evolution and diversification of plant cysteine proteinase inhibitors: new insights after the poplar genome. Mol. Phylogenet. Evol. 2008, 49:349-355.
    • (2008) Mol. Phylogenet. Evol. , vol.49 , pp. 349-355
    • Margis-Pinheiro, M.1    Zolet, A.C.T.2    Loss, G.3    Pasquali, G.4    Margis, R.5
  • 39
    • 47649106761 scopus 로고    scopus 로고
    • The origin and evolution of plant cystatins and their target cysteine proteinases indicate a complex functional relationship
    • Martinez M., Diaz I. The origin and evolution of plant cystatins and their target cysteine proteinases indicate a complex functional relationship. BMC Evol. Biol. 2008, 8:198.
    • (2008) BMC Evol. Biol. , vol.8 , pp. 198
    • Martinez, M.1    Diaz, I.2
  • 40
    • 0027162768 scopus 로고
    • Sweet-tasting protein monellin is related to the cystatin family of thiol proteinase inhibitors
    • Murzin A. Sweet-tasting protein monellin is related to the cystatin family of thiol proteinase inhibitors. J. Mol. Biol. 1993, 230:689-694.
    • (1993) J. Mol. Biol. , vol.230 , pp. 689-694
    • Murzin, A.1
  • 41
    • 33845354985 scopus 로고    scopus 로고
    • The squash aspartic proteinase inhibitor SQAPI is widely present in the Cucurbitales, comprises a small multigene family, and is a member of the phytocystatin family
    • Christeller J.T., Farley P.C., Marchall R.K., Anandan A., Wright M.M., Newcomb R.D., Laing W. The squash aspartic proteinase inhibitor SQAPI is widely present in the Cucurbitales, comprises a small multigene family, and is a member of the phytocystatin family. J. Mol. Evol. 2006, 63:747-757.
    • (2006) J. Mol. Evol. , vol.63 , pp. 747-757
    • Christeller, J.T.1    Farley, P.C.2    Marchall, R.K.3    Anandan, A.4    Wright, M.M.5    Newcomb, R.D.6    Laing, W.7
  • 42
    • 28044470978 scopus 로고    scopus 로고
    • Evolutionary mechanisms acting on proteinase inhibitor variability
    • Christeller J.T. Evolutionary mechanisms acting on proteinase inhibitor variability. FEBS J. 2005, 272:5710-5722.
    • (2005) FEBS J. , vol.272 , pp. 5710-5722
    • Christeller, J.T.1
  • 43
    • 21544454156 scopus 로고    scopus 로고
    • Comparative phylogenetic analysis of cystatin gene families from arabidopsis, rice and barley
    • Martinez M., Abraham Z., Carbonero P., Diaz I. Comparative phylogenetic analysis of cystatin gene families from arabidopsis, rice and barley. Mol. Genet. Genomics 2005, 273:423-432.
    • (2005) Mol. Genet. Genomics , vol.273 , pp. 423-432
    • Martinez, M.1    Abraham, Z.2    Carbonero, P.3    Diaz, I.4
  • 44
    • 33845605556 scopus 로고    scopus 로고
    • Structural and functional diversity within the cystatin gene family of Hordeum vulgare
    • Abraham Z., Martinez M., Carbonero P., Diaz I. Structural and functional diversity within the cystatin gene family of Hordeum vulgare. J. Exp. Bot. 2006, 15:4245-4255.
    • (2006) J. Exp. Bot. , vol.15 , pp. 4245-4255
    • Abraham, Z.1    Martinez, M.2    Carbonero, P.3    Diaz, I.4
  • 46
    • 0027740380 scopus 로고
    • Proteolysis of the 85-kilodalton crystalline cysteine proteinase inhibitor from potato releases functional cystatin domains
    • Walsh T., Strickland J. Proteolysis of the 85-kilodalton crystalline cysteine proteinase inhibitor from potato releases functional cystatin domains. Plant Physiol. 1993, 103:1227-1234.
    • (1993) Plant Physiol. , vol.103 , pp. 1227-1234
    • Walsh, T.1    Strickland, J.2
  • 47
    • 0033834190 scopus 로고    scopus 로고
    • Purification and characterization of a cystatin from the leaves of methyl jasmonate treated tomato plants
    • Wu J., Haard N.F. Purification and characterization of a cystatin from the leaves of methyl jasmonate treated tomato plants. Comp. Biochem. Physiol. C 2000, 127:209-220.
    • (2000) Comp. Biochem. Physiol. C , vol.127 , pp. 209-220
    • Wu, J.1    Haard, N.F.2
  • 48
    • 0033861376 scopus 로고    scopus 로고
    • Molecular cloning and functional expression of cDNA encoding the cysteine proteinase inhibitor with three cystatin domains from sunflower seeds
    • Kouzuma Y., Inanaga H., Doi-Kawano K., Yamasaki N., Kimura M. Molecular cloning and functional expression of cDNA encoding the cysteine proteinase inhibitor with three cystatin domains from sunflower seeds. J. Biochem. 2000, 128:161-166.
    • (2000) J. Biochem. , vol.128 , pp. 161-166
    • Kouzuma, Y.1    Inanaga, H.2    Doi-Kawano, K.3    Yamasaki, N.4    Kimura, M.5
  • 50
    • 34250357224 scopus 로고    scopus 로고
    • Carboxy terminal extended phytocystatins are bifunctional inhibitors of papain and legumain cysteine proteinases
    • Martinez M., Diaz-Mendoza M., Carrillo L., Diaz I. Carboxy terminal extended phytocystatins are bifunctional inhibitors of papain and legumain cysteine proteinases. FEBS Lett. 2007, 581:2914-2918.
    • (2007) FEBS Lett. , vol.581 , pp. 2914-2918
    • Martinez, M.1    Diaz-Mendoza, M.2    Carrillo, L.3    Diaz, I.4
  • 51
    • 52449132094 scopus 로고    scopus 로고
    • Characterization of inhibitory mechanism and antifungal activity between group-1 and group-2 phytocystatins from taro (Colocasia esculenta)
    • Wang K.-M., Kumar S., Cheng Y.-S., Venkatagiri S., Yang A.-H., Yeh K.-W. Characterization of inhibitory mechanism and antifungal activity between group-1 and group-2 phytocystatins from taro (Colocasia esculenta). FEBS J. 2008, 275:4980-4989.
    • (2008) FEBS J. , vol.275 , pp. 4980-4989
    • Wang, K.-M.1    Kumar, S.2    Cheng, Y.-S.3    Venkatagiri, S.4    Yang, A.-H.5    Yeh, K.-W.6
  • 52
    • 0032523769 scopus 로고    scopus 로고
    • Purification, characterization and cloning of an aspartic proteinase inhibitor from squash phloem exudate
    • Christeller J.T., Farley P.C., Ramsay R.J., Sullivan P.A., Laing W.A. Purification, characterization and cloning of an aspartic proteinase inhibitor from squash phloem exudate. Eur. J. Biochem. 1998, 254:160-167.
    • (1998) Eur. J. Biochem. , vol.254 , pp. 160-167
    • Christeller, J.T.1    Farley, P.C.2    Ramsay, R.J.3    Sullivan, P.A.4    Laing, W.A.5
  • 53
    • 0035994086 scopus 로고    scopus 로고
    • Analysis of the interaction between the aspartic peptidase inhibitor SQAPI and aspartic peptidases using surface plasmon resonance
    • Farley P.C., Christeller J.T., Sullivan M.E., Sullivan P.A., Laing W.A. Analysis of the interaction between the aspartic peptidase inhibitor SQAPI and aspartic peptidases using surface plasmon resonance. J. Mol. Recognit. 2002, 15:135-144.
    • (2002) J. Mol. Recognit. , vol.15 , pp. 135-144
    • Farley, P.C.1    Christeller, J.T.2    Sullivan, M.E.3    Sullivan, P.A.4    Laing, W.A.5
  • 55
    • 70350686335 scopus 로고    scopus 로고
    • Characterization of the entire cystatin gene family in barley and their target cathepsin L-like cysteine proteases, partners in the hordein mobilization during seed germination
    • Martinez M., Cambra I., Carrillo L., Diaz-Mendoza M., Diaz I. Characterization of the entire cystatin gene family in barley and their target cathepsin L-like cysteine proteases, partners in the hordein mobilization during seed germination. Plant Physiol. 2009, 151:1531-1545.
    • (2009) Plant Physiol. , vol.151 , pp. 1531-1545
    • Martinez, M.1    Cambra, I.2    Carrillo, L.3    Diaz-Mendoza, M.4    Diaz, I.5
  • 56
    • 4644253630 scopus 로고    scopus 로고
    • Multifunctional role of plant cysteine proteinases
    • Grudkowska M., Zagdanska B. Multifunctional role of plant cysteine proteinases. Acta Biochim. Pol. 2004, 51:609-624.
    • (2004) Acta Biochim. Pol. , vol.51 , pp. 609-624
    • Grudkowska, M.1    Zagdanska, B.2
  • 57
    • 34548406409 scopus 로고    scopus 로고
    • Protein dynamics and proteolysis in plant vacuoles
    • Müntz K. Protein dynamics and proteolysis in plant vacuoles. J. Exp. Bot. 2007, 58:2391-2407.
    • (2007) J. Exp. Bot. , vol.58 , pp. 2391-2407
    • Müntz, K.1
  • 59
    • 67349130075 scopus 로고    scopus 로고
    • Developmentally linked changes in proteases and protease inhibitors suggest a role for potato multicystatin in regulating protein content of potato tubers
    • Weeda S.M., Kumar G.N.M., Knowles N.R. Developmentally linked changes in proteases and protease inhibitors suggest a role for potato multicystatin in regulating protein content of potato tubers. Planta 2009, 230:73-84.
    • (2009) Planta , vol.230 , pp. 73-84
    • Weeda, S.M.1    Kumar, G.N.M.2    Knowles, N.R.3
  • 62
    • 77950343440 scopus 로고    scopus 로고
    • Regulation of seed germination and seedling growth by an Arabidopsis phytocystatin isoform, AtCYS6
    • Hwang J.E., Hong J.K., Je J.H., Lee K.O., Kim D.Y., Lee S.Y., Lim C.O. Regulation of seed germination and seedling growth by an Arabidopsis phytocystatin isoform, AtCYS6. Plant Cell Rep. 2009, 28:1623-1632.
    • (2009) Plant Cell Rep. , vol.28 , pp. 1623-1632
    • Hwang, J.E.1    Hong, J.K.2    Je, J.H.3    Lee, K.O.4    Kim, D.Y.5    Lee, S.Y.6    Lim, C.O.7
  • 64
    • 34247095200 scopus 로고    scopus 로고
    • Gliadain, a gibberellin-inducible cysteine proteinase occurring in germinating seeds of wheat, Triticum aestivum L., specifically digests gliadin and is regulated by intrinsic cystatins
    • Kiyosaki T., Matsumoto I., Asakura T., Funaki J., Kuroda M., Misaka T., Arai S., Abe K. Gliadain, a gibberellin-inducible cysteine proteinase occurring in germinating seeds of wheat, Triticum aestivum L., specifically digests gliadin and is regulated by intrinsic cystatins. FEBS J. 2007, 274:1908-1917.
    • (2007) FEBS J. , vol.274 , pp. 1908-1917
    • Kiyosaki, T.1    Matsumoto, I.2    Asakura, T.3    Funaki, J.4    Kuroda, M.5    Misaka, T.6    Arai, S.7    Abe, K.8
  • 65
    • 14544275201 scopus 로고    scopus 로고
    • The barley cystatin gene (Icy) is regulated by DOF transcription factors in aleurone cells upon germination
    • Martinez M., Rubio-Somoza I., Fuentes R., Lara P., Carbonero P., Diaz I. The barley cystatin gene (Icy) is regulated by DOF transcription factors in aleurone cells upon germination. J. Exp. Bot. 2005, 56:547-556.
    • (2005) J. Exp. Bot. , vol.56 , pp. 547-556
    • Martinez, M.1    Rubio-Somoza, I.2    Fuentes, R.3    Lara, P.4    Carbonero, P.5    Diaz, I.6
  • 66
    • 0037338198 scopus 로고    scopus 로고
    • A cathepsin B-like cysteine protease gene from Hordeum vulgare (gene CatB) induced by GA in aleurone cells upon germination
    • Martinez M., Rubio-Somoza I., Carbonero P., Diaz I. A cathepsin B-like cysteine protease gene from Hordeum vulgare (gene CatB) induced by GA in aleurone cells upon germination. J. Exp. Bot. 2003, 54:951-959.
    • (2003) J. Exp. Bot. , vol.54 , pp. 951-959
    • Martinez, M.1    Rubio-Somoza, I.2    Carbonero, P.3    Diaz, I.4
  • 67
    • 74049111872 scopus 로고    scopus 로고
    • Correlative changes in proteases and protease inhibitors during mobilisation of protein from potato (Solanum tuberosum) seed tubers
    • Weeda S.M., Kumar G.N.M., Knowles N.R. Correlative changes in proteases and protease inhibitors during mobilisation of protein from potato (Solanum tuberosum) seed tubers. Funct. Plant Biol. 2010, 37:32-42.
    • (2010) Funct. Plant Biol. , vol.37 , pp. 32-42
    • Weeda, S.M.1    Kumar, G.N.M.2    Knowles, N.R.3
  • 68
    • 0031149202 scopus 로고    scopus 로고
    • An extracellular insoluble inhibitor of cysteine proteinases in cell cultures and seeds of carrot
    • Ojima A., Shiota H., Higashi K., Kamada H., Shimma Y., Wada M., Satoh S. An extracellular insoluble inhibitor of cysteine proteinases in cell cultures and seeds of carrot. Plant Mol. Biol. 1997, 34:99-109.
    • (1997) Plant Mol. Biol. , vol.34 , pp. 99-109
    • Ojima, A.1    Shiota, H.2    Higashi, K.3    Kamada, H.4    Shimma, Y.5    Wada, M.6    Satoh, S.7
  • 70
    • 0032190502 scopus 로고    scopus 로고
    • An endosperm-specific DOF protein from barley, highly conserved in wheat, binds to and inactivates transcription from the prolamine-box of a native B-hordein promoter in barley aleurone
    • Mena M., Vicente-Carbajosa J., Schmidt R.J., Carbonero P. An endosperm-specific DOF protein from barley, highly conserved in wheat, binds to and inactivates transcription from the prolamine-box of a native B-hordein promoter in barley aleurone. Plant J. 1998, 16:53-62.
    • (1998) Plant J. , vol.16 , pp. 53-62
    • Mena, M.1    Vicente-Carbajosa, J.2    Schmidt, R.J.3    Carbonero, P.4
  • 71
    • 0036740823 scopus 로고    scopus 로고
    • A role for the DOF transcription factor BPBF in the regulation of gibberellin-responsive genes in barley aleurone
    • Mena M., Cejudo F.J., Isabel-Lamoneda I., Carbonero P. A role for the DOF transcription factor BPBF in the regulation of gibberellin-responsive genes in barley aleurone. Plant Physiol. 2002, 130:111-119.
    • (2002) Plant Physiol. , vol.130 , pp. 111-119
    • Mena, M.1    Cejudo, F.J.2    Isabel-Lamoneda, I.3    Carbonero, P.4
  • 72
    • 0037263489 scopus 로고    scopus 로고
    • SAD: a new DOF protein from barley that activates transcription of a cathepsin B-like thiol protease gene in the aleurone of germinating seeds
    • Isabel-Lamoneda I., Diaz I., Martinez M., Mena M., Carbonero P. SAD: a new DOF protein from barley that activates transcription of a cathepsin B-like thiol protease gene in the aleurone of germinating seeds. Plant J. 2003, 33:129-140.
    • (2003) Plant J. , vol.33 , pp. 129-140
    • Isabel-Lamoneda, I.1    Diaz, I.2    Martinez, M.3    Mena, M.4    Carbonero, P.5
  • 73
    • 33845626168 scopus 로고    scopus 로고
    • Wheat Dof transcripton factor WPBF interacts with TaQM and activates transcription of an alpha-gliadin gene during wheat seed development
    • Dong G., Ni Z., Yao Y., Nie X., Sun Q. Wheat Dof transcripton factor WPBF interacts with TaQM and activates transcription of an alpha-gliadin gene during wheat seed development. Plant Mol. Biol. 2007, 63:73-84.
    • (2007) Plant Mol. Biol. , vol.63 , pp. 73-84
    • Dong, G.1    Ni, Z.2    Yao, Y.3    Nie, X.4    Sun, Q.5
  • 74
    • 34547109079 scopus 로고    scopus 로고
    • The HvDOF19 transcription factor mediates the abscisic acid-dependent repression of hydrolase genes in germinating barley aleurone
    • Moreno-Risueno M.A., Diaz I., Carrillo L., Fuentes R., Carbonero P. The HvDOF19 transcription factor mediates the abscisic acid-dependent repression of hydrolase genes in germinating barley aleurone. Plant J. 2007, 51:352-365.
    • (2007) Plant J. , vol.51 , pp. 352-365
    • Moreno-Risueno, M.A.1    Diaz, I.2    Carrillo, L.3    Fuentes, R.4    Carbonero, P.5
  • 76
    • 0036008857 scopus 로고    scopus 로고
    • Is a cysteine proteinase inhibitor involved in the regulation of petal wilting in senescing carnation (Dianthus caryophyllus L.) flowers?
    • Sugawara H., Shibuya K., Yoshioka T., Hashiba T., Satoh S. Is a cysteine proteinase inhibitor involved in the regulation of petal wilting in senescing carnation (Dianthus caryophyllus L.) flowers?. J. Exp. Bot. 2002, 53:407-413.
    • (2002) J. Exp. Bot. , vol.53 , pp. 407-413
    • Sugawara, H.1    Shibuya, K.2    Yoshioka, T.3    Hashiba, T.4    Satoh, S.5
  • 77
    • 34548687038 scopus 로고    scopus 로고
    • N-protein mobilisation associated with the leaf senescence process in oilseed rape is concomitant with the disappearance of trypsin inhibitor activity
    • Etienne P., Desclos M., Le Gou L., Gombert J., Bonnefoy J., Maurel K., Le Dily F., Ourry A., Avice J.-C. N-protein mobilisation associated with the leaf senescence process in oilseed rape is concomitant with the disappearance of trypsin inhibitor activity. Funct. Plant Biol. 2007, 34:895-906.
    • (2007) Funct. Plant Biol. , vol.34 , pp. 895-906
    • Etienne, P.1    Desclos, M.2    Le Gou, L.3    Gombert, J.4    Bonnefoy, J.5    Maurel, K.6    Le Dily, F.7    Ourry, A.8    Avice, J.-C.9
  • 78
    • 48149110148 scopus 로고    scopus 로고
    • Two cysteine proteinase inhibitors from Arabidopsis thaliana, AtCYSa and AtCYSb, increasing the salt, drought, oxidation and cold tolerance
    • 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.
    • (2008) Plant Mol. Biol. , vol.68 , pp. 131-143
    • Zhang, X.1    Liu, S.2    Takano, T.3
  • 79
    • 1542279127 scopus 로고    scopus 로고
    • Oryzacystatin I expression in transformed tobacco produces a conditional growth phenotype and enhances chilling tolerance
    • Van der Vyver C., Schneidereit J., Driscoll S., Turner J., Kunert K., Foyer C.H. Oryzacystatin I expression in transformed tobacco produces a conditional growth phenotype and enhances chilling tolerance. Plant Biotechnol. J. 2003, 1:101-112.
    • (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
  • 80
    • 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 P.D.R., Olmos E., Kunert K.J., Foyer C.H. 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
  • 81
    • 78149359053 scopus 로고    scopus 로고
    • Constitutive expression of endogenous defense proteins in transgenic potato lines expressing the Cys protease inhibitor corn cystatin II, Aspects Appl. Biol. (96), in press.
    • A. Munger, C. Goulet, L.-P. Vaillancourt, U. Schlüter, A. Kiggundu, K. Kunert, M.-C. Goulet, D. Michaud, Constitutive expression of endogenous defense proteins in transgenic potato lines expressing the Cys protease inhibitor corn cystatin II, Aspects Appl. Biol. (96), in press.
    • Munger, A.1    Goulet, C.2    Vaillancourt, L.-P.3    Schlüter, U.4    Kiggundu, A.5    Kunert, K.6    Goulet, M.-C.7    Michaud, D.8
  • 82
    • 70349634021 scopus 로고    scopus 로고
    • An extended AE-rich N-terminal trunk in secreted pineapple cystatin enhances inhibition of fruit bromelain and is posttranslationally removed during ripening
    • Neuteboom L.W., Matsumoto K.O., Christopher D.A. An extended AE-rich N-terminal trunk in secreted pineapple cystatin enhances inhibition of fruit bromelain and is posttranslationally removed during ripening. Plant Physiol. 2009, 151:515-527.
    • (2009) Plant Physiol. , vol.151 , pp. 515-527
    • Neuteboom, L.W.1    Matsumoto, K.O.2    Christopher, D.A.3
  • 83
    • 0344441434 scopus 로고    scopus 로고
    • The diverse roles of ubiquitin and the 26S proteasome in the life of plants
    • Sullivan J.A., Shirasu K., Deng X.W. The diverse roles of ubiquitin and the 26S proteasome in the life of plants. Nat. Rev. Genet. 2003, 4:948-958.
    • (2003) Nat. Rev. Genet. , vol.4 , pp. 948-958
    • Sullivan, J.A.1    Shirasu, K.2    Deng, X.W.3
  • 84
    • 3242665372 scopus 로고    scopus 로고
    • The ubiquitin 26S proteasome proteolytic pathway
    • Smalle J., Vierstra R.D. The ubiquitin 26S proteasome proteolytic pathway. Annu. Rev. Plant Biol. 2004, 55:555-590.
    • (2004) Annu. Rev. Plant Biol. , vol.55 , pp. 555-590
    • Smalle, J.1    Vierstra, R.D.2
  • 85
    • 0003026210 scopus 로고    scopus 로고
    • Plant cysteine proteinases in germination and senescence
    • Academic Press, London, U.K, A.J. Barrett, N.D. Rawlings, J.F. Woessner (Eds.)
    • Granell A., Cercos M., Carbonell J. Plant cysteine proteinases in germination and senescence. Handbook of Proteolytic Enzymes 1998, 578-583. Academic Press, London, U.K. A.J. Barrett, N.D. Rawlings, J.F. Woessner (Eds.).
    • (1998) Handbook of Proteolytic Enzymes , pp. 578-583
    • Granell, A.1    Cercos, M.2    Carbonell, J.3
  • 86
    • 11844252119 scopus 로고    scopus 로고
    • A cut above the rest: the regulatory function of plant proteases
    • Schaller A. A cut above the rest: the regulatory function of plant proteases. Planta 2004, 220:183-197.
    • (2004) Planta , vol.220 , pp. 183-197
    • Schaller, A.1
  • 87
    • 44949258132 scopus 로고    scopus 로고
    • Plant proteases: from phenotypes to molecular mechanisms
    • van den Hoorn R.A.L. Plant proteases: from phenotypes to molecular mechanisms. Annu. Rev. Plant Biol. 2008, 59:191-223.
    • (2008) Annu. Rev. Plant Biol. , vol.59 , pp. 191-223
    • van den Hoorn, R.A.L.1
  • 88
    • 0033101490 scopus 로고    scopus 로고
    • The involvement of cysteine proteases and protease inhibitor genes in the regulation of programmed cell death in plants
    • Solomon M., Belenghi B., Delledonne M., Menachem E., Levine A. The involvement of cysteine proteases and protease inhibitor genes in the regulation of programmed cell death in plants. Plant Cell 1999, 11:431-443.
    • (1999) Plant Cell , vol.11 , pp. 431-443
    • Solomon, M.1    Belenghi, B.2    Delledonne, M.3    Menachem, E.4    Levine, A.5
  • 91
    • 59349098502 scopus 로고    scopus 로고
    • Differential proteomic analysis of soluble extracellular proteins reveals the cysteine protease and cystatin involved in suspension-cultured cell proliferation in rice
    • Tian L., Zhang L., Zhang J., Song Y., Guo Y. Differential proteomic analysis of soluble extracellular proteins reveals the cysteine protease and cystatin involved in suspension-cultured cell proliferation in rice. Biochim. Biophys. Acta 2009, 1794:459-467.
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 459-467
    • Tian, L.1    Zhang, L.2    Zhang, J.3    Song, Y.4    Guo, Y.5
  • 93
    • 0342288677 scopus 로고    scopus 로고
    • Biotic and abiotic stress can induce cystatin expression in chestnut
    • Pernas M., Sanchez-Monge R., Salcedo G. Biotic and abiotic stress can induce cystatin expression in chestnut. FEBS Lett. 2000, 467:206-210.
    • (2000) FEBS Lett. , vol.467 , pp. 206-210
    • Pernas, M.1    Sanchez-Monge, R.2    Salcedo, G.3
  • 94
    • 63549131942 scopus 로고    scopus 로고
    • Molecular cloning and characterization of novel cystatin gene in leaves Cakile maritima halophyte
    • Megdiche W., Passaquet C., Zourrig W., Zuily-Fodil Y., Abdelly C. Molecular cloning and characterization of novel cystatin gene in leaves Cakile maritima halophyte. J. Plant Physiol. 2009, 166:739-749.
    • (2009) J. Plant Physiol. , vol.166 , pp. 739-749
    • Megdiche, W.1    Passaquet, C.2    Zourrig, W.3    Zuily-Fodil, Y.4    Abdelly, C.5
  • 95
    • 33646429223 scopus 로고    scopus 로고
    • A cold inducible multidomain cystatin from winter wheat inhibits growth of the snow mold fungus, Microdochium nivale
    • Christova P.K., Christov N.K., Imai R. A cold inducible multidomain cystatin from winter wheat inhibits growth of the snow mold fungus, Microdochium nivale. Planta 2006, 223:1207-1218.
    • (2006) Planta , vol.223 , pp. 1207-1218
    • Christova, P.K.1    Christov, N.K.2    Imai, R.3
  • 96
    • 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
    • Bouchard É., 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.
    • (2003) Mol. Ecol. , vol.12 , pp. 2439-2446
    • Bouchard, É.1    Cloutier, C.2    Michaud, D.3
  • 97
    • 0030296222 scopus 로고    scopus 로고
    • Differential expression of soybean cysteine proteinase inhibitor genes during development and in response to wounding and methyl jasmonate
    • Botella M.A., Xu Y., Prabha T.N., Zhao Y., Narasimhan M.L., Wilson K.A., Nielsen S.S., Bressan R.A., Hasegawa P.M. Differential expression of soybean cysteine proteinase inhibitor genes during development and in response to wounding and methyl jasmonate. Plant Physiol. 1996, 112:1201-1210.
    • (1996) Plant Physiol. , vol.112 , pp. 1201-1210
    • Botella, M.A.1    Xu, Y.2    Prabha, T.N.3    Zhao, Y.4    Narasimhan, M.L.5    Wilson, K.A.6    Nielsen, S.S.7    Bressan, R.A.8    Hasegawa, P.M.9
  • 98
    • 0027145853 scopus 로고
    • Methyl jasmonate induces papain inhibitor(s) in tomato leaves
    • Bolter C. Methyl jasmonate induces papain inhibitor(s) in tomato leaves. Plant Physiol. 1993, 103:1347-1353.
    • (1993) Plant Physiol. , vol.103 , pp. 1347-1353
    • Bolter, C.1
  • 99
    • 0032476613 scopus 로고    scopus 로고
    • Leaves of transgenic tomato plants overexpressing prosystemin accumulate high levels of cystatin
    • Jacinto T., Fernandes K.V.S., Machado O.L.T., Siqueira-Junior C.L. Leaves of transgenic tomato plants overexpressing prosystemin accumulate high levels of cystatin. Plant Sci. 1998, 138:35-42.
    • (1998) Plant Sci. , vol.138 , pp. 35-42
    • Jacinto, T.1    Fernandes, K.V.S.2    Machado, O.L.T.3    Siqueira-Junior, C.L.4
  • 101
    • 0001669667 scopus 로고
    • Identification of cathepsin B, D and H in the larval midgut of Colorado potato beetle, Leptinotarsa decemlineata Say (Coleoptera: Chrysomelidae)
    • Thie N.M., Houseman J.G. Identification of cathepsin B, D and H in the larval midgut of Colorado potato beetle, Leptinotarsa decemlineata Say (Coleoptera: Chrysomelidae). Insect Biochem. 1990, 20:313-318.
    • (1990) Insect Biochem. , vol.20 , pp. 313-318
    • Thie, N.M.1    Houseman, J.G.2
  • 102
    • 0029084013 scopus 로고
    • Carboxy-terminal truncation of oryzacystatin II by oryzacystatin-insensitive insect digestive proteinases
    • Michaud D., Cantin L., Vrain T.C. Carboxy-terminal truncation of oryzacystatin II by oryzacystatin-insensitive insect digestive proteinases. Arch. Biochem. Biophys. 1995, 322:469-474.
    • (1995) Arch. Biochem. Biophys. , vol.322 , pp. 469-474
    • Michaud, D.1    Cantin, L.2    Vrain, T.C.3
  • 103
    • 1842487375 scopus 로고    scopus 로고
    • Characterisation of cysteine proteinases responsible for digestive proteolysis in guts of larval western corn rootworm (Diabrotica virgifera) by expression in the yeast Pichia pastoris
    • Bown D.P., Wilkinson H.S., Jongsma M.A., Gatehouse J.A. Characterisation of cysteine proteinases responsible for digestive proteolysis in guts of larval western corn rootworm (Diabrotica virgifera) by expression in the yeast Pichia pastoris. Insect Biochem. Mol. Biol. 2004, 34:305-320.
    • (2004) Insect Biochem. Mol. Biol. , vol.34 , pp. 305-320
    • Bown, D.P.1    Wilkinson, H.S.2    Jongsma, M.A.3    Gatehouse, J.A.4
  • 105
    • 34447644452 scopus 로고    scopus 로고
    • Sequence analysis and molecular characterization of larval midgut cDNA transcripts encoding peptidases from the yellow mealworm, Tenebrio molitor L
    • Prabhakar S., Chen M.-S., Elpidina E.N., Vinokurov K.S., Smith C.S., Marshall J., Oppert B. Sequence analysis and molecular characterization of larval midgut cDNA transcripts encoding peptidases from the yellow mealworm, Tenebrio molitor L. Insect Mol. Biol. 2007, 16:455-468.
    • (2007) Insect Mol. Biol. , vol.16 , pp. 455-468
    • Prabhakar, S.1    Chen, M.-S.2    Elpidina, E.N.3    Vinokurov, K.S.4    Smith, C.S.5    Marshall, J.6    Oppert, B.7
  • 107
    • 0028100602 scopus 로고
    • Proteases of females of the phytoparasite Globodera pallida (potato cyst nematode)
    • Koritsas V.M., Atkinson H.J. Proteases of females of the phytoparasite Globodera pallida (potato cyst nematode). Parasitology 1994, 109:357-365.
    • (1994) Parasitology , vol.109 , pp. 357-365
    • Koritsas, V.M.1    Atkinson, H.J.2
  • 108
    • 0029743455 scopus 로고    scopus 로고
    • Characterisation of intestinally active proteases of cyst-nematodes
    • Lilley C.J., Urwin P.E., Mcpherson M.J., Atkinson H.J. Characterisation of intestinally active proteases of cyst-nematodes. Parasitology 1996, 113:415-424.
    • (1996) Parasitology , vol.113 , pp. 415-424
    • Lilley, C.J.1    Urwin, P.E.2    Mcpherson, M.J.3    Atkinson, H.J.4
  • 109
    • 0030946213 scopus 로고    scopus 로고
    • Characterisation of two cDNAs encoding cysteine proteases from the soybean cyst nematode Heterodera glycines
    • Urwin P.E., Lilley C.J., Mcpherson M.J., Atkinson H.J. Characterisation of two cDNAs encoding cysteine proteases from the soybean cyst nematode Heterodera glycines. Parasitology 1997, 114:605-613.
    • (1997) Parasitology , vol.114 , pp. 605-613
    • Urwin, P.E.1    Lilley, C.J.2    Mcpherson, M.J.3    Atkinson, H.J.4
  • 110
    • 0027437730 scopus 로고
    • Selective inhibition of Colorado potato beetle cathepsin H by oryzacystatins I and II
    • 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.
    • (1993) FEBS Lett. , vol.331 , pp. 173-176
    • Michaud, D.1    Nguyen-Quoc, B.2    Yelle, S.3
  • 111
    • 0029815027 scopus 로고    scopus 로고
    • Identification of stable plant cystatin/nematode proteinase complexes using mildly denaturing gelatin polyacrylamide gel electrophoresis
    • Michaud D., Cantin L., Bonadé-Bottino M., Jouanin L., Vrain T.C. Identification of stable plant cystatin/nematode proteinase complexes using mildly denaturing gelatin polyacrylamide gel electrophoresis. Electrophoresis 1996, 17:1373-1379.
    • (1996) Electrophoresis , vol.17 , pp. 1373-1379
    • Michaud, D.1    Cantin, L.2    Bonadé-Bottino, M.3    Jouanin, L.4    Vrain, T.C.5
  • 112
    • 0030046451 scopus 로고    scopus 로고
    • Assessing the stability of cystatin/cysteine proteinase complexes using mildly-denaturing gelatin polyacrylamide gel electrophoresis
    • Michaud D., Cantin L., Raworth D.A., Vrain T.C. Assessing the stability of cystatin/cysteine proteinase complexes using mildly-denaturing gelatin polyacrylamide gel electrophoresis. Electrophoresis 1996, 17:74-79.
    • (1996) Electrophoresis , vol.17 , pp. 74-79
    • Michaud, D.1    Cantin, L.2    Raworth, D.A.3    Vrain, T.C.4
  • 113
    • 0029682164 scopus 로고    scopus 로고
    • Response of digestive cysteine proteinases from the Colorado potato beetle (Leptinotarsa decemlineata) and the black vine weevil (Otiorynchus sulcatus) to a recombinant form of human stefin A
    • Michaud D., Nguyen-Quoc B., Vrain T.C., Fong D., Yelle S. Response of digestive cysteine proteinases from the Colorado potato beetle (Leptinotarsa decemlineata) and the black vine weevil (Otiorynchus sulcatus) to a recombinant form of human stefin A. Arch. Insect Biochem. Physiol. 1996, 31:451-464.
    • (1996) Arch. Insect Biochem. Physiol. , vol.31 , pp. 451-464
    • Michaud, D.1    Nguyen-Quoc, B.2    Vrain, T.C.3    Fong, D.4    Yelle, S.5
  • 114
    • 0030220996 scopus 로고    scopus 로고
    • Two wound-inducible soybean cysteine proteinase inhibitors have greater insect digestive proteinase inhibitory activities than a constitutive homolog
    • Zhao Y., Botella M.A., Subramanian L., Niu X., Nielsen S.S., Bressan R.A., Hasegawa P.M. Two wound-inducible soybean cysteine proteinase inhibitors have greater insect digestive proteinase inhibitory activities than a constitutive homolog. Plant Physiol. 1996, 111:1299-1306.
    • (1996) Plant Physiol. , vol.111 , pp. 1299-1306
    • Zhao, Y.1    Botella, M.A.2    Subramanian, L.3    Niu, X.4    Nielsen, S.S.5    Bressan, R.A.6    Hasegawa, P.M.7
  • 115
    • 0034857353 scopus 로고    scopus 로고
    • An electroblotting, two-step procedure for the detection of proteinases and the study of proteinase/inhibitor complexes in gelatin-containing polyacrylamide gels
    • Visal-Shah S.D., Vrain T.C., Yelle S., Nguyen-Quoc B., Michaud D. An electroblotting, two-step procedure for the detection of proteinases and the study of proteinase/inhibitor complexes in gelatin-containing polyacrylamide gels. Electrophoresis 2001, 22:2646-2652.
    • (2001) Electrophoresis , vol.22 , pp. 2646-2652
    • Visal-Shah, S.D.1    Vrain, T.C.2    Yelle, S.3    Nguyen-Quoc, B.4    Michaud, D.5
  • 119
    • 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
    • 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.
    • (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
  • 121
    • 21344450737 scopus 로고    scopus 로고
    • Molecular cloning, recombinant gene expression, and antifungal activity of cystatin from taro (Colocasia esculenta cv. Kaosiung no. 1)
    • Yang A.H., Yeh K.W. Molecular cloning, recombinant gene expression, and antifungal activity of cystatin from taro (Colocasia esculenta cv. Kaosiung no. 1). Planta 2005, 221:493-501.
    • (2005) Planta , vol.221 , pp. 493-501
    • Yang, A.H.1    Yeh, K.W.2
  • 123
    • 4544251201 scopus 로고    scopus 로고
    • Specific cysteine protease inhibitors act as deterrents of western flower thrips, Frankliniella occidentalis (Pergande), in transgenic potato
    • Outchkourov N.S., de Kogel W.J., Schuurman-de Bruin A., Abrahamson M., Jongsma M.A. Specific cysteine protease inhibitors act as deterrents of western flower thrips, Frankliniella occidentalis (Pergande), in transgenic potato. Plant Biotechnol. J. 2004, 2:439-448.
    • (2004) Plant Biotechnol. J. , vol.2 , pp. 439-448
    • Outchkourov, N.S.1    de Kogel, W.J.2    Schuurman-de Bruin, A.3    Abrahamson, M.4    Jongsma, M.A.5
  • 124
    • 4544362753 scopus 로고    scopus 로고
    • Engineered multidomain cysteine protease inhibitors yield resistance against western flower thrips (Frankliniella occidentalis) in greenhouse trials
    • Outchkourov N.S., de Kogel W.J., Wiegers G.L., Abrahamson M., Jongsma M.A. Engineered multidomain cysteine protease inhibitors yield resistance against western flower thrips (Frankliniella occidentalis) in greenhouse trials. Plant Biotechnol. J. 2004, 2:449-458.
    • (2004) Plant Biotechnol. J. , vol.2 , pp. 449-458
    • Outchkourov, N.S.1    de Kogel, W.J.2    Wiegers, G.L.3    Abrahamson, M.4    Jongsma, M.A.5
  • 125
    • 33846096920 scopus 로고    scopus 로고
    • Effects of potato plants expressing a barley cystatin on the predatory bug Podisus maculiventris via herbivorous prey feeding on the plant
    • Alvarez-Alfageme F., Martinez M., Pascual-Ruiz S., Castanera P., Diaz I., Ortego F. Effects of potato plants expressing a barley cystatin on the predatory bug Podisus maculiventris via herbivorous prey feeding on the plant. Transgenic Res. 2007, 16:1-13.
    • (2007) Transgenic Res. , vol.16 , pp. 1-13
    • Alvarez-Alfageme, F.1    Martinez, M.2    Pascual-Ruiz, S.3    Castanera, P.4    Diaz, I.5    Ortego, F.6
  • 127
    • 71949093356 scopus 로고    scopus 로고
    • Genetically pyramiding protease-inhibitor genes for dual broad-spectrum resistance against insect and phytopathogens in transgenic tobacco
    • Senthilkumar R., Cheng C.-P., Yeh K.-W. Genetically pyramiding protease-inhibitor genes for dual broad-spectrum resistance against insect and phytopathogens in transgenic tobacco. Plant Biotechnol. J. 2010, 8:65-75.
    • (2010) Plant Biotechnol. J. , vol.8 , pp. 65-75
    • Senthilkumar, R.1    Cheng, C.-P.2    Yeh, K.-W.3
  • 128
    • 0038040671 scopus 로고    scopus 로고
    • Expression of oryzacystatin I and II in alfalfa increases resistance to the root-lesion nematode
    • Samac D.A., Smigocki A.C. Expression of oryzacystatin I and II in alfalfa increases resistance to the root-lesion nematode. Phytopathology 2003, 93:799-804.
    • (2003) Phytopathology , vol.93 , pp. 799-804
    • Samac, D.A.1    Smigocki, A.C.2
  • 129
    • 0032055743 scopus 로고    scopus 로고
    • Enhanced transgenic plant resistance to nematodes by dual proteinase inhibitor constructs
    • Urwin P.E., Mcpherson M.J., Atkinson H.J. Enhanced transgenic plant resistance to nematodes by dual proteinase inhibitor constructs. Planta 1998, 204:472-479.
    • (1998) Planta , vol.204 , pp. 472-479
    • Urwin, P.E.1    Mcpherson, M.J.2    Atkinson, H.J.3
  • 130
    • 3242879430 scopus 로고    scopus 로고
    • Preferential expression of a plant cystatin at nematode feeding sites confers resistance to Meloidogyne incognita and Globodera pallida
    • Lilley C.J., Urwin P.E., Johnston K.A., Atkinson H.J. Preferential expression of a plant cystatin at nematode feeding sites confers resistance to Meloidogyne incognita and Globodera pallida. Plant Biotechnol. J. 2004, 2:3-12.
    • (2004) Plant Biotechnol. J. , vol.2 , pp. 3-12
    • Lilley, C.J.1    Urwin, P.E.2    Johnston, K.A.3    Atkinson, H.J.4
  • 131
    • 77950922399 scopus 로고    scopus 로고
    • Heterologous expression of taro cystatin protects transgenic tomato against Meloidogyne incognita infection by means of interfering sex determination and suppressing gall formation
    • Chan Y.L., Yang A.-H., Chen J.-T., Yeh K.-W., Chan M.-T. Heterologous expression of taro cystatin protects transgenic tomato against Meloidogyne incognita infection by means of interfering sex determination and suppressing gall formation. Plant Cell Rep. 2010, 29:231-238.
    • (2010) Plant Cell Rep. , vol.29 , pp. 231-238
    • Chan, Y.L.1    Yang, A.-H.2    Chen, J.-T.3    Yeh, K.-W.4    Chan, M.-T.5
  • 132
    • 0032787406 scopus 로고    scopus 로고
    • The use of cysteine proteinase inhibitors to engineer resistance against potyviruses in transgenic tobacco plants
    • Guttiérrez-Campos R., Torres-Acosta J.A., Saucedo-Arias L.J., Gomez-Lin M.A. The use of cysteine proteinase inhibitors to engineer resistance against potyviruses in transgenic tobacco plants. Nat. Biotechnol. 1999, 17:1223-1226.
    • (1999) Nat. Biotechnol. , vol.17 , pp. 1223-1226
    • Guttiérrez-Campos, R.1    Torres-Acosta, J.A.2    Saucedo-Arias, L.J.3    Gomez-Lin, M.A.4
  • 134
    • 5344259633 scopus 로고    scopus 로고
    • Protein proteinase inhibitor genes in combat against insects, pests, and pathogens: natural and engineered phytoprotection
    • Haq S.K., Atif S.M., Khan R.H. Protein proteinase inhibitor genes in combat against insects, pests, and pathogens: natural and engineered phytoprotection. Arch. Biochem. Biophys. 2004, 431:145-159.
    • (2004) Arch. Biochem. Biophys. , vol.431 , pp. 145-159
    • Haq, S.K.1    Atif, S.M.2    Khan, R.H.3
  • 135
    • 17844383232 scopus 로고    scopus 로고
    • Insect-resistant GM rice in farmers' fields: assessing productivity and health effects in China
    • Huang J., Hu R., Rozelle S., Pray C. Insect-resistant GM rice in farmers' fields: assessing productivity and health effects in China. Science 2005, 388:688-690.
    • (2005) Science , vol.388 , pp. 688-690
    • Huang, J.1    Hu, R.2    Rozelle, S.3    Pray, C.4
  • 136
    • 54049088543 scopus 로고    scopus 로고
    • Is China ready for GM rice?
    • Qiu J. Is China ready for GM rice?. Nature 2008, 455:850-852.
    • (2008) Nature , vol.455 , pp. 850-852
    • Qiu, J.1
  • 137
    • 0011834985 scopus 로고    scopus 로고
    • Control of phytophagous insect pests using serine proteinase inhibitors
    • Landes Bioscience/Eurekah.com, Georgetown, TX, D. Michaud (Ed.)
    • Gatehouse J.A., Gatehouse A.M.R., Bown D.P. Control of phytophagous insect pests using serine proteinase inhibitors. Recombinant Protease Inhibitors in Plants 2000, 9-26. Landes Bioscience/Eurekah.com, Georgetown, TX. D. Michaud (Ed.).
    • (2000) Recombinant Protease Inhibitors in Plants , pp. 9-26
    • Gatehouse, J.A.1    Gatehouse, A.M.R.2    Bown, D.P.3
  • 138
    • 0002534018 scopus 로고    scopus 로고
    • Protein hydrolysis by Colorado potato beetle, Leptinotarsa decemlineata, digestive proteases: the catalytic role of cathepsin D
    • Brunelle F., Nguyen-Quoc B., Cloutier C., Michaud D. Protein hydrolysis by Colorado potato beetle, Leptinotarsa decemlineata, digestive proteases: the catalytic role of cathepsin D. Arch. Insect Biochem. Physiol. 1999, 42:88-98.
    • (1999) Arch. Insect Biochem. Physiol. , vol.42 , pp. 88-98
    • Brunelle, F.1    Nguyen-Quoc, B.2    Cloutier, C.3    Michaud, D.4
  • 140
    • 0037298743 scopus 로고    scopus 로고
    • Diverse enzymatic specificities of digestive proteases, 'intestains', enable Colorado potato beetle larvae to counteract the potato defence mechanism
    • Gruden K., Popovic T., Cimerman N., Krizaj I., Strukelj B. Diverse enzymatic specificities of digestive proteases, 'intestains', enable Colorado potato beetle larvae to counteract the potato defence mechanism. Biol. Chem. 2003, 384:305-310.
    • (2003) Biol. Chem. , vol.384 , pp. 305-310
    • Gruden, K.1    Popovic, T.2    Cimerman, N.3    Krizaj, I.4    Strukelj, B.5
  • 141
    • 64849083217 scopus 로고    scopus 로고
    • Digestive proteolysis organization in two closely related tenebrionid beetles: red flour beetle (Tribolium castaneum) and confused flour beetle (Tribolium confusum)
    • Vinokurov K.S., Elpidina E.N., Zhuzhikov D.P., Oppert B., Kodrik D., Sehnal F. Digestive proteolysis organization in two closely related tenebrionid beetles: red flour beetle (Tribolium castaneum) and confused flour beetle (Tribolium confusum). Arch. Insect Biochem. Physiol. 2009, 70:254-279.
    • (2009) Arch. Insect Biochem. Physiol. , vol.70 , pp. 254-279
    • Vinokurov, K.S.1    Elpidina, E.N.2    Zhuzhikov, D.P.3    Oppert, B.4    Kodrik, D.5    Sehnal, F.6
  • 142
    • 0034201087 scopus 로고    scopus 로고
    • Adult Colorado potato beetles, Leptinotarsa decemlineata compensate for nutritional stress on oryzacystatin I-transgenic potato plants by hypertrophic behaviour and over-production of insensitive proteinases
    • 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 behaviour and over-production of insensitive proteinases. Arch. Insect Physiol. Biochem. 2000, 44:69-81.
    • (2000) Arch. Insect Physiol. Biochem. , vol.44 , pp. 69-81
    • Cloutier, C.1    Jean, C.2    Fournier, M.3    Yelle, S.4    Michaud, D.5
  • 143
    • 11144311087 scopus 로고    scopus 로고
    • Functional roles of specific bruchid protease isoforms in adaptation to a soybean protease inhibitor
    • Ahn J.-E., Salzman R.A., Braunagel S.C., Koiwa H., Zhu-Salzman K. Functional roles of specific bruchid protease isoforms in adaptation to a soybean protease inhibitor. Insect Mol. Biol. 2004, 13:649-657.
    • (2004) Insect Mol. Biol. , vol.13 , pp. 649-657
    • Ahn, J.-E.1    Salzman, R.A.2    Braunagel, S.C.3    Koiwa, H.4    Zhu-Salzman, K.5
  • 144
    • 0028817235 scopus 로고
    • Constitutive expression of digestive cysteine proteinase forms during development of the Colorado potato beetle, Leptinotarsa decemlineata Say (Coleoptera: Chrysomelidae)
    • Michaud D., Bernier-Vadnais N., Overney S., Yelle S. Constitutive expression of digestive cysteine proteinase forms during development of the Colorado potato beetle, Leptinotarsa decemlineata Say (Coleoptera: Chrysomelidae). Insect Biochem. Mol. Biol. 1995, 25:1041-1048.
    • (1995) Insect Biochem. Mol. Biol. , vol.25 , pp. 1041-1048
    • Michaud, D.1    Bernier-Vadnais, N.2    Overney, S.3    Yelle, S.4
  • 146
    • 0002714379 scopus 로고    scopus 로고
    • Growth compensation and faster development of Colorado potato beetle (Coleoptera: Chrysomelidae) feeding on potato foliage expressing oryzacystatin I
    • Cloutier C., Fournier M., Jean C., Yelle S., Michaud D. Growth compensation and faster development of Colorado potato beetle (Coleoptera: Chrysomelidae) feeding on potato foliage expressing oryzacystatin I. Arch. Insect Biochem. Physiol. 1999, 40:69-79.
    • (1999) Arch. Insect Biochem. Physiol. , vol.40 , pp. 69-79
    • Cloutier, C.1    Fournier, M.2    Jean, C.3    Yelle, S.4    Michaud, D.5
  • 147
    • 0345146929 scopus 로고    scopus 로고
    • Cowpea bruchid Callosobruchus maculatus uses a three-component strategy to overcome a plant defensive cysteine protease inhibitor
    • Zhu-Salzman K., Koiwa H., Salzman R.A., Shade R.E., Ahn J.-E. Cowpea bruchid Callosobruchus maculatus uses a three-component strategy to overcome a plant defensive cysteine protease inhibitor. Insect Mol. Biol. 2003, 12:135-145.
    • (2003) Insect Mol. Biol. , vol.12 , pp. 135-145
    • Zhu-Salzman, K.1    Koiwa, H.2    Salzman, R.A.3    Shade, R.E.4    Ahn, J.-E.5
  • 148
    • 4744351645 scopus 로고    scopus 로고
    • Transcriptional regulation in southern corn rootworm larvae challenged by soyacystatin N
    • Liu Y., Salzman R.A., Pankiw T., Zhu-Salzman K. Transcriptional regulation in southern corn rootworm larvae challenged by soyacystatin N. Insect Biochem. Mol. Biol. 2004, 34:1069-1077.
    • (2004) Insect Biochem. Mol. Biol. , vol.34 , pp. 1069-1077
    • Liu, Y.1    Salzman, R.A.2    Pankiw, T.3    Zhu-Salzman, K.4
  • 149
    • 1842591814 scopus 로고    scopus 로고
    • Molecular basis of Colorado potato beetle adaptation to potato plant defence at the level of digestive cysteine proteinases
    • Gruden K., Kuipers A.G.J., Guncar G., Slapar N., Strukelj B., Jongsma M.A. Molecular basis of Colorado potato beetle adaptation to potato plant defence at the level of digestive cysteine proteinases. Insect Biochem. Mol. Biol. 2004, 34:365-375.
    • (2004) Insect Biochem. Mol. Biol. , vol.34 , pp. 365-375
    • Gruden, K.1    Kuipers, A.G.J.2    Guncar, G.3    Slapar, N.4    Strukelj, B.5    Jongsma, M.A.6
  • 151
    • 1642586903 scopus 로고    scopus 로고
    • Colorado potato beetles show differential digestive compensatory responses to host plants expressing distinct sets of defense proteins
    • 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.
    • (2004) Arch. Insect Biochem. Physiol. , vol.55 , pp. 114-123
    • Rivard, D.1    Cloutier, C.2    Michaud, D.3
  • 156
    • 0035490515 scopus 로고    scopus 로고
    • Protein engineering of novel proteinase inhibitors and their effects on the growth of Spodoptera exigua larvae
    • Inanaga H., Kobayasi D., Kouzuma Y., Aoki-Yasunaga C., Iiyama K., Kimura M. Protein engineering of novel proteinase inhibitors and their effects on the growth of Spodoptera exigua larvae. Biosci. Biotechnol. Biochem. 2001, 65:2259-2264.
    • (2001) Biosci. Biotechnol. Biochem. , vol.65 , pp. 2259-2264
    • Inanaga, H.1    Kobayasi, D.2    Kouzuma, Y.3    Aoki-Yasunaga, C.4    Iiyama, K.5    Kimura, M.6
  • 157
    • 0344154314 scopus 로고    scopus 로고
    • Fusion of a soybean cysteine protease inhibitor and a legume lectin enhances anti-insect activity synergistically
    • Zhu-Salzman K., Ahn J.-E., Salzman R.A., Koiwa H., Shade H., Balfe S. Fusion of a soybean cysteine protease inhibitor and a legume lectin enhances anti-insect activity synergistically. Agric. Forest Entomol. 2003, 5:317-323.
    • (2003) Agric. Forest Entomol. , vol.5 , pp. 317-323
    • Zhu-Salzman, K.1    Ahn, J.-E.2    Salzman, R.A.3    Koiwa, H.4    Shade, H.5    Balfe, S.6
  • 158
    • 27744530768 scopus 로고    scopus 로고
    • A hybrid, broad-spectrum inhibitor of Colorado potato beetle aspartate and cysteine digestive proteinases
    • Brunelle F., Girard C., Cloutier C., Michaud D. A hybrid, broad-spectrum inhibitor of Colorado potato beetle aspartate and cysteine digestive proteinases. Arch. Insect Physiol. Biochem. 2005, 60:20-31.
    • (2005) Arch. Insect Physiol. Biochem. , vol.60 , pp. 20-31
    • Brunelle, F.1    Girard, C.2    Cloutier, C.3    Michaud, D.4
  • 159
    • 46749099728 scopus 로고    scopus 로고
    • Hybrid protease inhibitors for pest and pathogen control-a functional cost for the fusion partners?
    • Benchabane M., Goulet M.-C., Dallaire C., Côté P.-L., Michaud D. Hybrid protease inhibitors for pest and pathogen control-a functional cost for the fusion partners?. Plant Physiol. Biochem. 2008, 46:701-708.
    • (2008) Plant Physiol. Biochem. , vol.46 , pp. 701-708
    • Benchabane, M.1    Goulet, M.-C.2    Dallaire, C.3    Côté, P.-L.4    Michaud, D.5
  • 161
    • 0942279592 scopus 로고    scopus 로고
    • Prima facie evidence that a phytocystatin for transgenic plant resistance to nematodes is not a toxic risk in the human diet
    • Atkinson H.J., Johnston K.A., Robbins M. Prima facie evidence that a phytocystatin for transgenic plant resistance to nematodes is not a toxic risk in the human diet. J. Nutr. 2004, 134:431-434.
    • (2004) J. Nutr. , vol.134 , pp. 431-434
    • Atkinson, H.J.1    Johnston, K.A.2    Robbins, M.3
  • 162
    • 0042831317 scopus 로고    scopus 로고
    • Molecular interactions between an insect predator and its herbivore prey on transgenic potato expressing a cysteine proteinase inhibitor from rice
    • Bouchard É., Michaud D., Cloutier C. Molecular interactions between an insect predator and its herbivore prey on transgenic potato expressing a cysteine proteinase inhibitor from rice. Mol. Ecol. 2003, 12:2429-2437.
    • (2003) Mol. Ecol. , vol.12 , pp. 2429-2437
    • Bouchard, É.1    Michaud, D.2    Cloutier, C.3
  • 163
    • 12444252149 scopus 로고    scopus 로고
    • Impact of oilseed rape expressing the insecticidal serine protease inhibitor, mustard trypsin inhibitor-2 on the beneficial predator Pterostichus madidus
    • Ferry N., Jouanin L., Ceci R., Mulligan E.A., Emami K., Gatehouse J.A., Gatehouse A.M. Impact of oilseed rape expressing the insecticidal serine protease inhibitor, mustard trypsin inhibitor-2 on the beneficial predator Pterostichus madidus. Mol. Ecol. 2005, 14:337-349.
    • (2005) Mol. Ecol. , vol.14 , pp. 337-349
    • Ferry, N.1    Jouanin, L.2    Ceci, R.3    Mulligan, E.A.4    Emami, K.5    Gatehouse, J.A.6    Gatehouse, A.M.7
  • 165
    • 0005625379 scopus 로고    scopus 로고
    • Protease inhibitors in food processing
    • Landes Bioscience/Eurekah.com, Georgetown, TX, D. Michaud (Ed.)
    • García-Carreño F.L., An H., Haard N.F. Protease inhibitors in food processing. Recombinant Protease Inhibitors in Plants 2000, 215-223. Landes Bioscience/Eurekah.com, Georgetown, TX. D. Michaud (Ed.).
    • (2000) Recombinant Protease Inhibitors in Plants , pp. 215-223
    • García-Carreño, F.L.1    An, H.2    Haard, N.F.3
  • 167
    • 29744461973 scopus 로고    scopus 로고
    • Inhibition of protease in intact fish fillets by soaking in or injection of recombinant soy cystatin or bovine plasma
    • Kang I., Lanier T.C. Inhibition of protease in intact fish fillets by soaking in or injection of recombinant soy cystatin or bovine plasma. J. Agric. Food Chem. 2005, 53:9795-9799.
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 9795-9799
    • Kang, I.1    Lanier, T.C.2
  • 168
    • 70350031599 scopus 로고    scopus 로고
    • Leishmania infantum: Antiproliferative effect of recombinant plant cystatins on promastigotes and intracellular amastigotes estimated by direct counting and real-time PCR
    • Ordonez-Gutiérrez L., Martinez M., Rubio-Somoza I., Diaz I., Mendez S., Alunda J.M. Leishmania infantum: Antiproliferative effect of recombinant plant cystatins on promastigotes and intracellular amastigotes estimated by direct counting and real-time PCR. Exp. Parasitol. 2009, 123:341-346.
    • (2009) Exp. Parasitol. , vol.123 , pp. 341-346
    • Ordonez-Gutiérrez, L.1    Martinez, M.2    Rubio-Somoza, I.3    Diaz, I.4    Mendez, S.5    Alunda, J.M.6
  • 169
    • 33747144853 scopus 로고    scopus 로고
    • Cosecretion of protease inhibitor stabilizes antibodies produced by plant roots
    • Komarnytsky S., Borisjuk N., Yakoby N., Garvey A., Raskin I. Cosecretion of protease inhibitor stabilizes antibodies produced by plant roots. Plant Physiol. 2006, 141:1185-1193.
    • (2006) Plant Physiol. , vol.141 , pp. 1185-1193
    • Komarnytsky, S.1    Borisjuk, N.2    Yakoby, N.3    Garvey, A.4    Raskin, I.5
  • 170
    • 33645503258 scopus 로고    scopus 로고
    • An in-built proteinase inhibitor system for the protection of recombinant proteins recovered from transgenic plants
    • Rivard D., Anguenot R., Brunelle F., Le V.Q., 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.
    • (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
  • 171
    • 60549105845 scopus 로고    scopus 로고
    • Companion protease inhibitors to protect recombinant proteins in transgenic plant extracts
    • Benchabane M., Rivard D., Girard C., Michaud D. Companion protease inhibitors to protect recombinant proteins in transgenic plant extracts. Methods Mol. Biol. 2009, 483:265-273.
    • (2009) Methods Mol. Biol. , vol.483 , pp. 265-273
    • Benchabane, M.1    Rivard, D.2    Girard, C.3    Michaud, D.4
  • 172
    • 73949161292 scopus 로고    scopus 로고
    • A companion protease inhibitor for the protection of cytosol-targeted recombinant proteins in plants
    • 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.
    • (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.