메뉴 건너뛰기




Volumn 442, Issue 1-2, 2009, Pages 88-98

Spatial and temporal expression patterns of diverse Pin-II proteinase inhibitor genes in Capsicum annuum Linn

Author keywords

CanPI; Capsicum annuum; Endogenous role; Pin II; Plant defense; Proteinase inhibitor

Indexed keywords

PIN II TYPE PROTEINASE INHIBITOR; PROTEINASE INHIBITOR; UNCLASSIFIED DRUG;

EID: 67349094500     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.gene.2009.04.012     Document Type: Article
Times cited : (24)

References (57)
  • 1
    • 0032549090 scopus 로고    scopus 로고
    • Induced responses to herbivory and increased plant performance
    • Agrawal A.A. Induced responses to herbivory and increased plant performance. Science 279 (1998) 1201-1202
    • (1998) Science , vol.279 , pp. 1201-1202
    • Agrawal, A.A.1
  • 2
    • 24344495312 scopus 로고    scopus 로고
    • Plant serine proteases: biochemical, physiological and molecular features
    • Antão C.M., and Malcata F.X. Plant serine proteases: biochemical, physiological and molecular features. Plant Physiol. Biochem. 43 (2005) 637-650
    • (2005) Plant Physiol. Biochem. , vol.43 , pp. 637-650
    • Antão, C.M.1    Malcata, F.X.2
  • 4
    • 0034769603 scopus 로고    scopus 로고
    • Proteins of circularly permuted sequence present within the same organism: the major serine proteinase inhibitor from Capsicum annum seeds
    • Antcheva N., Pintar A., Patthay A., et al. Proteins of circularly permuted sequence present within the same organism: the major serine proteinase inhibitor from Capsicum annum seeds. Protein Sci. 10 (2001) 2280-2290
    • (2001) Protein Sci. , vol.10 , pp. 2280-2290
    • Antcheva, N.1    Pintar, A.2    Patthay, A.3
  • 5
    • 0038267164 scopus 로고    scopus 로고
    • Structural basis of inhibition revealed by 1:2 complex of the two headed tomato inhibitor-II and subtilisin Carlsberg
    • Barrette-Ng I.H., Kenneth K.S.N., Cherney M.M., Pearce G., Ryan C.A., and James M.N.G. Structural basis of inhibition revealed by 1:2 complex of the two headed tomato inhibitor-II and subtilisin Carlsberg. J. Biol. Chem. 278 (2003) 24062-24071
    • (2003) J. Biol. Chem. , vol.278 , pp. 24062-24071
    • Barrette-Ng, I.H.1    Kenneth, K.S.N.2    Cherney, M.M.3    Pearce, G.4    Ryan, C.A.5    James, M.N.G.6
  • 6
    • 0036890373 scopus 로고    scopus 로고
    • Repeats with variations: accelerated evolution of the Pin2 family of proteinase inhibitors
    • Barta E., Pintar A., and Pongor S. Repeats with variations: accelerated evolution of the Pin2 family of proteinase inhibitors. Trends Genet. 18 (2002) 600-660
    • (2002) Trends Genet. , vol.18 , pp. 600-660
    • Barta, E.1    Pintar, A.2    Pongor, S.3
  • 7
    • 0034476852 scopus 로고    scopus 로고
    • Plant proteolytic enzymes: possible roles during programmed cell death
    • Beers E.P., Woffenden B.J., and Zhao C. Plant proteolytic enzymes: possible roles during programmed cell death. Plant Mol. Biol. 44 (2000) 399-415
    • (2000) Plant Mol. Biol. , vol.44 , pp. 399-415
    • Beers, E.P.1    Woffenden, B.J.2    Zhao, C.3
  • 8
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 9
    • 0034697794 scopus 로고    scopus 로고
    • Structure and stress-related expression of two cDNAs encoding proteinase inhibitor II of Nicotiana glutinosa
    • Choi D., Park J., Seo Y.S., Chun Y.J., and Kim W.T. Structure and stress-related expression of two cDNAs encoding proteinase inhibitor II of Nicotiana glutinosa. Biochim. Biophys. Acta 1492 (2000) 211-215
    • (2000) Biochim. Biophys. Acta , vol.1492 , pp. 211-215
    • Choi, D.1    Park, J.2    Seo, Y.S.3    Chun, Y.J.4    Kim, W.T.5
  • 10
    • 33744466558 scopus 로고    scopus 로고
    • Serine proteinase inhibitor proteins: exogenous and endogenous functions
    • Chye M.L., Sin S.F., Xu Z.F., and Yeung C. Serine proteinase inhibitor proteins: exogenous and endogenous functions. In Vitro Cell Dev. Biol. Plant 42 (2006) 100-108
    • (2006) In Vitro Cell Dev. Biol. Plant , vol.42 , pp. 100-108
    • Chye, M.L.1    Sin, S.F.2    Xu, Z.F.3    Yeung, C.4
  • 11
    • 27744593837 scopus 로고    scopus 로고
    • Higher accumulation of proteinase inhibitors in flowers than leaves and fruits as a possible basis for differential feeding preference of Helicoverpa armigera on tomato (Lycopersicon esculentum Mill, Cv. Dhanashree)
    • Damle M.S., Giri A.P., Sainani M.N., and Gupta V.S. Higher accumulation of proteinase inhibitors in flowers than leaves and fruits as a possible basis for differential feeding preference of Helicoverpa armigera on tomato (Lycopersicon esculentum Mill, Cv. Dhanashree). Phytochemistry 66 (2005) 2659-2667
    • (2005) Phytochemistry , vol.66 , pp. 2659-2667
    • Damle, M.S.1    Giri, A.P.2    Sainani, M.N.3    Gupta, V.S.4
  • 12
    • 27744605309 scopus 로고    scopus 로고
    • Engineering insect tolerant plants using plant defensive proteinase inhibitors
    • Pandalai S.G. (Ed), Research Signpost, India
    • Giri A.P., Chougule N.P., Telang M.A., and Gupta V.S. Engineering insect tolerant plants using plant defensive proteinase inhibitors. In: Pandalai S.G. (Ed). Recent Research Developments in Phytochemistry 8 (2005), Research Signpost, India 117-137
    • (2005) Recent Research Developments in Phytochemistry , vol.8 , pp. 117-137
    • Giri, A.P.1    Chougule, N.P.2    Telang, M.A.3    Gupta, V.S.4
  • 13
    • 0001068883 scopus 로고
    • Wound-induced proteinase inhibitor in plant leaves: a possible defense mechanism against insects
    • Green T.R., and Ryan C.A. Wound-induced proteinase inhibitor in plant leaves: a possible defense mechanism against insects. Science 175 (1972) 776-777
    • (1972) Science , vol.175 , pp. 776-777
    • Green, T.R.1    Ryan, C.A.2
  • 14
    • 0029025551 scopus 로고
    • Characterization of the protease processing sites in a multidomain proteinase inhibitor precursor from Nicotiana alata
    • Heath R.L., Barton P.A., Simpson R.J., Reid G.E., Lim G., and Anderson M.A. Characterization of the protease processing sites in a multidomain proteinase inhibitor precursor from Nicotiana alata. Eur. J. Biochem. 230 (1995) 250-257
    • (1995) Eur. J. Biochem. , vol.230 , pp. 250-257
    • Heath, R.L.1    Barton, P.A.2    Simpson, R.J.3    Reid, G.E.4    Lim, G.5    Anderson, M.A.6
  • 15
    • 0035115745 scopus 로고    scopus 로고
    • Molecular interactions between the specialist herbivore Manduca sexta (Lepidoptera, Sphingidae) and its natural host Nicotiana attenuata. I. Large-scale changes in the accumulation of growth- and defense-related plant mRNAs
    • Hermsmeier D., Schittko U., and Baldwin I.T. Molecular interactions between the specialist herbivore Manduca sexta (Lepidoptera, Sphingidae) and its natural host Nicotiana attenuata. I. Large-scale changes in the accumulation of growth- and defense-related plant mRNAs. Plant Physiol. 125 (2001) 683-700
    • (2001) Plant Physiol. , vol.125 , pp. 683-700
    • Hermsmeier, D.1    Schittko, U.2    Baldwin, I.T.3
  • 16
    • 33644795085 scopus 로고    scopus 로고
    • Differential elicitation of two processing proteases controls the processing pattern of the trypsin proteinase inhibitor precursor in Nicotiana attenuata
    • Horn M., Patankar A.G., Zavala J.A., et al. Differential elicitation of two processing proteases controls the processing pattern of the trypsin proteinase inhibitor precursor in Nicotiana attenuata. Plant Physiol. 139 (2005) 375-388
    • (2005) Plant Physiol. , vol.139 , pp. 375-388
    • Horn, M.1    Patankar, A.G.2    Zavala, J.A.3
  • 17
    • 0032760112 scopus 로고    scopus 로고
    • Suppressors of systemin signaling identify genes in the tomato wound response pathway
    • Howe G.A., and Ryan C.A. Suppressors of systemin signaling identify genes in the tomato wound response pathway. Genetics 153 (1999) 1411-1421
    • (1999) Genetics , vol.153 , pp. 1411-1421
    • Howe, G.A.1    Ryan, C.A.2
  • 18
    • 38949168852 scopus 로고    scopus 로고
    • The accumulation of a Kunitz trypsin inhibitor from chickpea (TPI-2) located in cell walls is increased in wounded leaves and elongating epicotyls
    • Jimenez T., Marti{dotless}n I., Hernandez-Nistal J., Labrador E., and Dopico B. The accumulation of a Kunitz trypsin inhibitor from chickpea (TPI-2) located in cell walls is increased in wounded leaves and elongating epicotyls. Physiol. Plant. 132 (2008) 306-317
    • (2008) Physiol. Plant. , vol.132 , pp. 306-317
    • Jimenez, T.1    Martin, I.2    Hernandez-Nistal, J.3    Labrador, E.4    Dopico, B.5
  • 19
    • 33947191038 scopus 로고    scopus 로고
    • Dual location of a family of proteinase inhibitors within the stigmas of Nicotiana alata
    • Johnson E.D., Miller E.A., and Anderson M.A. Dual location of a family of proteinase inhibitors within the stigmas of Nicotiana alata. Planta 225 (2007) 1265-1276
    • (2007) Planta , vol.225 , pp. 1265-1276
    • Johnson, E.D.1    Miller, E.A.2    Anderson, M.A.3
  • 20
    • 0031260101 scopus 로고    scopus 로고
    • The adaptation of insects to plant protease inhibitors
    • Jongsma M.A., and Bolter C. The adaptation of insects to plant protease inhibitors. J. Insect Physiol. 43 (1997) 885-895
    • (1997) J. Insect Physiol. , vol.43 , pp. 885-895
    • Jongsma, M.A.1    Bolter, C.2
  • 21
    • 0028310026 scopus 로고
    • Trypsin inhibitor activity in mature tobacco and tomato plants is mainly induced locally in response to insect attack, wounding and virus infection
    • Jongsma M.A., Bakker P.L., Visser B., and Stiekema W.J. Trypsin inhibitor activity in mature tobacco and tomato plants is mainly induced locally in response to insect attack, wounding and virus infection. Planta 195 (1994) 29-35
    • (1994) Planta , vol.195 , pp. 29-35
    • Jongsma, M.A.1    Bakker, P.L.2    Visser, B.3    Stiekema, W.J.4
  • 22
    • 0033593221 scopus 로고    scopus 로고
    • Genomic cluster containing four differentially regulated subtilisin like processing protease genes is in tomato plants
    • Jorda L.A., Coego V., and Conejero Vera P. Genomic cluster containing four differentially regulated subtilisin like processing protease genes is in tomato plants. J. Biol. Chem. 274 (1999) 2360-2365
    • (1999) J. Biol. Chem. , vol.274 , pp. 2360-2365
    • Jorda, L.A.1    Coego, V.2    Conejero Vera, P.3
  • 23
    • 33644926728 scopus 로고    scopus 로고
    • Phloem sap proteins: their identities and potential roles in the interaction between plants and phloem-feeding insects
    • Kehr J. Phloem sap proteins: their identities and potential roles in the interaction between plants and phloem-feeding insects. J. Exp. Bot. 57 (2006) 767-774
    • (2006) J. Exp. Bot. , vol.57 , pp. 767-774
    • Kehr, J.1
  • 24
    • 0035896350 scopus 로고    scopus 로고
    • Defensive function of herbivore-induced plant volatile emissions in nature
    • Kessler A., and Baldwin I.T. Defensive function of herbivore-induced plant volatile emissions in nature. Science 291 (2001) 2141-2144
    • (2001) Science , vol.291 , pp. 2141-2144
    • Kessler, A.1    Baldwin, I.T.2
  • 25
    • 0037002402 scopus 로고    scopus 로고
    • Plant responses to insect herbivory: the emerging molecular analysis
    • Kessler A., and Baldwin I.T. Plant responses to insect herbivory: the emerging molecular analysis. Annu. Rev. Plant Biol. 53 (2002) 299-328
    • (2002) Annu. Rev. Plant Biol. , vol.53 , pp. 299-328
    • Kessler, A.1    Baldwin, I.T.2
  • 26
    • 0034973578 scopus 로고    scopus 로고
    • Expression characteristics of serine proteinase inhibitor II under variable environmental stresses in hot pepper (Capsicum annum L.)
    • Kim S., Hong Y., An C.S., and Lee K. Expression characteristics of serine proteinase inhibitor II under variable environmental stresses in hot pepper (Capsicum annum L.). Plant Sci. 161 (2001) 27-33
    • (2001) Plant Sci. , vol.161 , pp. 27-33
    • Kim, S.1    Hong, Y.2    An, C.S.3    Lee, K.4
  • 27
    • 41949089739 scopus 로고    scopus 로고
    • Tandem duplication, circular permutation, molecular adaptation: how Solanaceae resist pests via inhibitors
    • Kong L., and Ranganathan S. Tandem duplication, circular permutation, molecular adaptation: how Solanaceae resist pests via inhibitors. BMC Bioinformatics 9 Suppl. 1 (2008) S22
    • (2008) BMC Bioinformatics , vol.9 , Issue.SUPPL. 1
    • Kong, L.1    Ranganathan, S.2
  • 28
    • 0037327730 scopus 로고    scopus 로고
    • The tomato mutant spr1 is defective in systemin perception and the production of a systemic wound signal for defense gene expression
    • Lee G.I., and Howe G.A. The tomato mutant spr1 is defective in systemin perception and the production of a systemic wound signal for defense gene expression. Plant J. 33 (2003) 567-576
    • (2003) Plant J. , vol.33 , pp. 567-576
    • Lee, G.I.1    Howe, G.A.2
  • 29
    • 0033017462 scopus 로고    scopus 로고
    • A novel two-chain proteinase inhibitor generated by circularization of a multidomain precursor protein
    • Lee M.C.S., Scalon M.J., Craik D.J., and Anderson M.A. A novel two-chain proteinase inhibitor generated by circularization of a multidomain precursor protein. Nat. Struct. Biol. 6 (1999) 526-530
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 526-530
    • Lee, M.C.S.1    Scalon, M.J.2    Craik, D.J.3    Anderson, M.A.4
  • 30
    • 0036741891 scopus 로고    scopus 로고
    • Resistance of cultivated tomato to cell content-feeding herbivores is regulated by the octadecanoid-signaling pathway
    • Li C., Williams M.M., Loh Y.T., Lee G.I., and Howe G.A. Resistance of cultivated tomato to cell content-feeding herbivores is regulated by the octadecanoid-signaling pathway. Plant Physiol. 130 (2002) 494-503
    • (2002) Plant Physiol. , vol.130 , pp. 494-503
    • Li, C.1    Williams, M.M.2    Loh, Y.T.3    Lee, G.I.4    Howe, G.A.5
  • 31
    • 0034006114 scopus 로고    scopus 로고
    • Identification of a novel four-domain member of the proteinase inhibitor II family from the stigmas of Nicotiana alata
    • Miller E.A., Lee M.C., Atkinson A.H., and Anderson M.A. Identification of a novel four-domain member of the proteinase inhibitor II family from the stigmas of Nicotiana alata. Plant Mol. Biol. 42 (2000) 329-333
    • (2000) Plant Mol. Biol. , vol.42 , pp. 329-333
    • Miller, E.A.1    Lee, M.C.2    Atkinson, A.H.3    Anderson, M.A.4
  • 32
    • 0034965916 scopus 로고    scopus 로고
    • Wound-inducible proteinase inhibitors in pepper. Differential regulation upon wounding, systemin and methyl jasmonate
    • Moura D.S., and Ryan C.A. Wound-inducible proteinase inhibitors in pepper. Differential regulation upon wounding, systemin and methyl jasmonate. Plant Physiol. 126 (2001) 289-298
    • (2001) Plant Physiol. , vol.126 , pp. 289-298
    • Moura, D.S.1    Ryan, C.A.2
  • 33
    • 0742302398 scopus 로고    scopus 로고
    • The cellular localization of prosystemin: a functional role for phloem parenchyma in systemic wound signaling
    • Narváez-Vásquez J., and Ryan C.A. The cellular localization of prosystemin: a functional role for phloem parenchyma in systemic wound signaling. Planta 218 (2004) 360-369
    • (2004) Planta , vol.218 , pp. 360-369
    • Narváez-Vásquez, J.1    Ryan, C.A.2
  • 34
    • 0028823596 scopus 로고
    • Structures of a series of 6-kDa trypsin inhibitors isolated from the stigma of Nicotiana alata
    • Nielsen K.J., Heath R.L., Anderson M.A., and Craik D.J. Structures of a series of 6-kDa trypsin inhibitors isolated from the stigma of Nicotiana alata. Biochemistry 34 (1995) 14304-14311
    • (1995) Biochemistry , vol.34 , pp. 14304-14311
    • Nielsen, K.J.1    Heath, R.L.2    Anderson, M.A.3    Craik, D.J.4
  • 35
    • 0030051741 scopus 로고    scopus 로고
    • Synthesis and structure determination by NMR of a putative vacuolar targeting peptide and model of a proteinase inhibitor from Nicotiana alata
    • Nielsen K.J., Hill J.M., Anderson M.A., and Craik D.J. Synthesis and structure determination by NMR of a putative vacuolar targeting peptide and model of a proteinase inhibitor from Nicotiana alata. Biochemistry 35 (1996) 369-378
    • (1996) Biochemistry , vol.35 , pp. 369-378
    • Nielsen, K.J.1    Hill, J.M.2    Anderson, M.A.3    Craik, D.J.4
  • 36
    • 0025886794 scopus 로고
    • A polypeptide from tomato leaves induces wound-inducible proteinase inhibitor proteins
    • Pearce G., Strydom D., Johnson S., and Ryan C.A. A polypeptide from tomato leaves induces wound-inducible proteinase inhibitor proteins. Science 253 (1991) 895-898
    • (1991) Science , vol.253 , pp. 895-898
    • Pearce, G.1    Strydom, D.2    Johnson, S.3    Ryan, C.A.4
  • 37
    • 0028273981 scopus 로고
    • Detection of electrophoretically separated proteinase inhibitors using X-ray film
    • Pichare M.M., and Kachole M.S. Detection of electrophoretically separated proteinase inhibitors using X-ray film. J. Biochem. Biophys Methods 28 (1994) 215-224
    • (1994) J. Biochem. Biophys Methods , vol.28 , pp. 215-224
    • Pichare, M.M.1    Kachole, M.S.2
  • 38
    • 10744227034 scopus 로고    scopus 로고
    • Molecular cloning and functional analysis of a novel type of Bowman-Birk Inhibitor gene family in rice
    • Qu L., Chen J., Liu M., et al. Molecular cloning and functional analysis of a novel type of Bowman-Birk Inhibitor gene family in rice. Plant Physiol. 133 (2003) 560-570
    • (2003) Plant Physiol. , vol.133 , pp. 560-570
    • Qu, L.1    Chen, J.2    Liu, M.3
  • 39
    • 0037373527 scopus 로고    scopus 로고
    • Toxicity to the pea aphid Acyrthosiphon pisum of anti-chymotrypsin isoforms and fragments of Bowman-Birk protease inhibitors from pea seeds
    • Rahbe Y., Ferrasson E., Rabesona H., and Quillien L. Toxicity to the pea aphid Acyrthosiphon pisum of anti-chymotrypsin isoforms and fragments of Bowman-Birk protease inhibitors from pea seeds. Insect Biochem. Mol. Biol. 33 (2003) 299-306
    • (2003) Insect Biochem. Mol. Biol. , vol.33 , pp. 299-306
    • Rahbe, Y.1    Ferrasson, E.2    Rabesona, H.3    Quillien, L.4
  • 40
    • 0000180578 scopus 로고
    • Proteinase inhibitors in plants, genes for improving defenses against insects and pathogens
    • Ryan C.A. Proteinase inhibitors in plants, genes for improving defenses against insects and pathogens. Annu. Rev. Phytopathol. 28 (1990) 425-449
    • (1990) Annu. Rev. Phytopathol. , vol.28 , pp. 425-449
    • Ryan, C.A.1
  • 41
    • 0034615558 scopus 로고    scopus 로고
    • The systemin signaling pathway: differential activation of plant defensive genes
    • Ryan C.A. The systemin signaling pathway: differential activation of plant defensive genes. Bioch. Biophys. Acta 1477 (2000) 112-121
    • (2000) Bioch. Biophys. Acta , vol.1477 , pp. 112-121
    • Ryan, C.A.1
  • 42
    • 0344630197 scopus 로고    scopus 로고
    • Systemins: a functionally defined family of peptide signals that regulate defensive genes in Solanaceae species
    • Ryan C.A., and Pearce G. Systemins: a functionally defined family of peptide signals that regulate defensive genes in Solanaceae species. Proc. Nat. Acad. Sci. U. S. A. 100 (2003) 14577-14580
    • (2003) Proc. Nat. Acad. Sci. U. S. A. , vol.100 , pp. 14577-14580
    • Ryan, C.A.1    Pearce, G.2
  • 43
    • 0033565476 scopus 로고    scopus 로고
    • Structure of a putative ancestral protein encoded by a single sequence repeat from a multidomain proteinase inhibitor gene from Nicotiana alata
    • Scanlon M.J., Lee M.C., Anderson M.A., and Craik D.J. Structure of a putative ancestral protein encoded by a single sequence repeat from a multidomain proteinase inhibitor gene from Nicotiana alata. Struct. Folding Design 7 (1999) 793-802
    • (1999) Struct. Folding Design , vol.7 , pp. 793-802
    • Scanlon, M.J.1    Lee, M.C.2    Anderson, M.A.3    Craik, D.J.4
  • 44
    • 33845612740 scopus 로고    scopus 로고
    • Systemin in Solanum nigrum. The tomato-homologous polypeptide does not mediate direct defense responses
    • Schmidt S., and Baldwin I. Systemin in Solanum nigrum. The tomato-homologous polypeptide does not mediate direct defense responses. Plant Physol. 142 (2006) 1751-1758
    • (2006) Plant Physol. , vol.142 , pp. 1751-1758
    • Schmidt, S.1    Baldwin, I.2
  • 45
    • 0034855725 scopus 로고    scopus 로고
    • Isolation of pepper mRNAs differentially expressed during the hypersensitive response to tobacco mosaic virus and characterization of a proteinase inhibitor gene
    • Shin R., Lee G., Park C., et al. Isolation of pepper mRNAs differentially expressed during the hypersensitive response to tobacco mosaic virus and characterization of a proteinase inhibitor gene. Plant Sci. 161 (2001) 727-737
    • (2001) Plant Sci. , vol.161 , pp. 727-737
    • Shin, R.1    Lee, G.2    Park, C.3
  • 46
    • 7044234943 scopus 로고    scopus 로고
    • Expression of proteinase inhibitor II proteins during floral development in Solanum americanum
    • Sin S.F., and Chye M.L. Expression of proteinase inhibitor II proteins during floral development in Solanum americanum. Planta 219 (2004) 1010-1022
    • (2004) Planta , vol.219 , pp. 1010-1022
    • Sin, S.F.1    Chye, M.L.2
  • 47
    • 14544285471 scopus 로고    scopus 로고
    • In vivo and in vitro effect of Capsicum annum proteinase inhibitors on Helicoverpa armigera gut proteinases
    • Tamhane V.A., Chougule N.P., Giri A.P., Dixit A.R., Sainani M.N., and Gupta V.S. In vivo and in vitro effect of Capsicum annum proteinase inhibitors on Helicoverpa armigera gut proteinases. Biochem. Biophys Acta 1722 (2005) 156-167
    • (2005) Biochem. Biophys Acta , vol.1722 , pp. 156-167
    • Tamhane, V.A.1    Chougule, N.P.2    Giri, A.P.3    Dixit, A.R.4    Sainani, M.N.5    Gupta, V.S.6
  • 48
    • 34748903471 scopus 로고    scopus 로고
    • Diverse forms of Pin-II family proteinase inhibitors from Capsicum annuum adversely affect the growth and development of Helicoverpa armigera
    • Tamhane V.A., Giri A.P., Sainani M.N., and Gupta V.S. Diverse forms of Pin-II family proteinase inhibitors from Capsicum annuum adversely affect the growth and development of Helicoverpa armigera. Gene 403 (2007) 29-38
    • (2007) Gene , vol.403 , pp. 29-38
    • Tamhane, V.A.1    Giri, A.P.2    Sainani, M.N.3    Gupta, V.S.4
  • 49
    • 0033578092 scopus 로고    scopus 로고
    • Jasmonate-inducible plant defense cause increased parasitism of herbivores
    • Thaler J.S. Jasmonate-inducible plant defense cause increased parasitism of herbivores. Nature 399 (1999) 686-688
    • (1999) Nature , vol.399 , pp. 686-688
    • Thaler, J.S.1
  • 50
    • 0026007288 scopus 로고
    • Larval damaged plants: source of volatile synomones that guide the parasitoid Cotesia marginiventris to the microhabitat of its hosts
    • 5951
    • Turlings T.C.J., Tumlinson J.H., Eller F.J., and Lewis W.J. Larval damaged plants: source of volatile synomones that guide the parasitoid Cotesia marginiventris to the microhabitat of its hosts. Entomol. Exp. Appl. 58 (1991) 75-82 5951
    • (1991) Entomol. Exp. Appl. , vol.58 , pp. 75-82
    • Turlings, T.C.J.1    Tumlinson, J.H.2    Eller, F.J.3    Lewis, W.J.4
  • 51
    • 4644235830 scopus 로고    scopus 로고
    • An analysis of plant-aphid interactions by different microarray hybridization strategies
    • Voelckel C., Weisser W.W., and Baldwin I.T. An analysis of plant-aphid interactions by different microarray hybridization strategies. Mol. Ecol. 13 (2004) 3187-3195
    • (2004) Mol. Ecol. , vol.13 , pp. 3187-3195
    • Voelckel, C.1    Weisser, W.W.2    Baldwin, I.T.3
  • 52
    • 0033758802 scopus 로고    scopus 로고
    • The myriad plant responses to herbivores
    • Walling L.L. The myriad plant responses to herbivores. J. Plant Growth Regul. 19 (2000) 195-216
    • (2000) J. Plant Growth Regul. , vol.19 , pp. 195-216
    • Walling, L.L.1
  • 53
    • 33747847975 scopus 로고    scopus 로고
    • Evolution of proteinase inhibitor defenses in North American allopolyploid species of Nicotiana
    • Wu J., Hettenhausen C., and Baldwin I.T. Evolution of proteinase inhibitor defenses in North American allopolyploid species of Nicotiana. Planta 224 (2006) 750-760
    • (2006) Planta , vol.224 , pp. 750-760
    • Wu, J.1    Hettenhausen, C.2    Baldwin, I.T.3
  • 54
    • 0035543848 scopus 로고    scopus 로고
    • A proteinase inhibitor II of Solanum americanum is expressed in phloem
    • Xu Z.F., Qi W.Q., Ouyang X.Z., Yeung E., and Chye M.L. A proteinase inhibitor II of Solanum americanum is expressed in phloem. Plant Mol. Biol. 47 (2001) 727-738
    • (2001) Plant Mol. Biol. , vol.47 , pp. 727-738
    • Xu, Z.F.1    Qi, W.Q.2    Ouyang, X.Z.3    Yeung, E.4    Chye, M.L.5
  • 55
    • 1442291008 scopus 로고    scopus 로고
    • Inhibition of endogenous trypsin- and chymotrypsin-like activities in transgenic lettuce expressing heterogeneous proteinase inhibitor SaPIN2a
    • Xu Z.F., Teng W.L., and Chye M.L. Inhibition of endogenous trypsin- and chymotrypsin-like activities in transgenic lettuce expressing heterogeneous proteinase inhibitor SaPIN2a. Planta 218 (2004) 623-629
    • (2004) Planta , vol.218 , pp. 623-629
    • Xu, Z.F.1    Teng, W.L.2    Chye, M.L.3
  • 56
    • 1242274638 scopus 로고    scopus 로고
    • Constitutive and inducible trypsin proteinase inhibitor production incurs large fitness costs in Nicotiana attenuata
    • Zavala J.A., Patankar A.G., Gase K., and Baldwin I.T. Constitutive and inducible trypsin proteinase inhibitor production incurs large fitness costs in Nicotiana attenuata. Proc. Nat. Acad. Sci. U. S. A. 101 (2004) 1607-1612
    • (2004) Proc. Nat. Acad. Sci. U. S. A. , vol.101 , pp. 1607-1612
    • Zavala, J.A.1    Patankar, A.G.2    Gase, K.3    Baldwin, I.T.4
  • 57
    • 1642506571 scopus 로고    scopus 로고
    • Manipulation of endogenous trypsin proteinase inhibitor production in Nicotiana attenuata demonstrates their function as antiherbivore defenses
    • Zavala J.A., Patankar A.G., Gase K., Hui D., and Baldwin I.T. Manipulation of endogenous trypsin proteinase inhibitor production in Nicotiana attenuata demonstrates their function as antiherbivore defenses. Plant Physiol. 134 (2004) 1181-1190
    • (2004) Plant Physiol. , vol.134 , pp. 1181-1190
    • Zavala, J.A.1    Patankar, A.G.2    Gase, K.3    Hui, D.4    Baldwin, I.T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.