메뉴 건너뛰기




Volumn 167, Issue 17, 2010, Pages 1507-1511

Analysis by phage display selection and site-directed retromutagenesis of the Mustard Trypsin Inhibitor 2 reactive site

Author keywords

Circular dichroism; Helicoverpa zea; Phage display; Proteinase inhibitor

Indexed keywords

MTI2 PROTEIN, SINAPIS ALBA; PEPTIDE HYDROLASE; PEPTIDE LIBRARY; TRYPSIN; VEGETABLE PROTEIN;

EID: 77957940512     PISSN: 01761617     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jplph.2010.05.025     Document Type: Article
Times cited : (5)

References (31)
  • 2
    • 0028969475 scopus 로고
    • The gene coding for the mustard trypsin inhibitor-2 is discontinuous and wound-inducible
    • Ceci L.R., Spoto N., de Virgilio M., Gallerani R. The gene coding for the mustard trypsin inhibitor-2 is discontinuous and wound-inducible. FEBS Lett 1995, 364:179-181.
    • (1995) FEBS Lett , vol.364 , pp. 179-181
    • Ceci, L.R.1    Spoto, N.2    de Virgilio, M.3    Gallerani, R.4
  • 3
    • 0037327370 scopus 로고    scopus 로고
    • Selection by phage display of a variant mustard trypsin inhibitor toxic against aphids
    • Ceci L.R., Volpicella M., Rahbe Y., Gallerani R., Beekwilder J., Jongsma M.A. Selection by phage display of a variant mustard trypsin inhibitor toxic against aphids. Plant J 2003, 33:557-566.
    • (2003) Plant J , vol.33 , pp. 557-566
    • Ceci, L.R.1    Volpicella, M.2    Rahbe, Y.3    Gallerani, R.4    Beekwilder, J.5    Jongsma, M.A.6
  • 4
    • 0028219989 scopus 로고
    • Purification, inhibitory properties, amino acid sequence and identification of the reactive site of a new serine proteinase inhibitor from oil-rape (Brassica napus) seed
    • Ceciliani F., Bortolotti F., Menegatti E., Ronchi S., Ascenzi P., Palmieri S. Purification, inhibitory properties, amino acid sequence and identification of the reactive site of a new serine proteinase inhibitor from oil-rape (Brassica napus) seed. FEBS Lett 1994, 342:221-224.
    • (1994) FEBS Lett , vol.342 , pp. 221-224
    • Ceciliani, F.1    Bortolotti, F.2    Menegatti, E.3    Ronchi, S.4    Ascenzi, P.5    Palmieri, S.6
  • 5
    • 1942485914 scopus 로고    scopus 로고
    • Functional divergence in tandemly duplicated Arabidopsis thaliana trypsin inhibitor genes
    • Clauss M.J., Mitchell-Olds T. Functional divergence in tandemly duplicated Arabidopsis thaliana trypsin inhibitor genes. Genetics 2004, 166:1419-1436.
    • (2004) Genetics , vol.166 , pp. 1419-1436
    • Clauss, M.J.1    Mitchell-Olds, T.2
  • 6
    • 0035957676 scopus 로고    scopus 로고
    • Effects of a mustard trypsin inhibitor expressed in different plants on three lepidopteran pests
    • De Leo F., Bonade-Bottino M., Ceci L.R., Gallerani R., Jouanin L. Effects of a mustard trypsin inhibitor expressed in different plants on three lepidopteran pests. Insect Biochem Mol Biol 2001, 31:593-602.
    • (2001) Insect Biochem Mol Biol , vol.31 , pp. 593-602
    • De Leo, F.1    Bonade-Bottino, M.2    Ceci, L.R.3    Gallerani, R.4    Jouanin, L.5
  • 7
    • 0000051893 scopus 로고    scopus 로고
    • Opposite effects on spodoptera littoralis larvae of high expression level of a trypsin proteinase inhibitor in transgenic plants
    • De Leo F., Bonade-Bottino M.A., Ceci L.R., Gallerani R., Jouanin L. Opposite effects on spodoptera littoralis larvae of high expression level of a trypsin proteinase inhibitor in transgenic plants. Plant Physiol 1998, 118:997-1004.
    • (1998) Plant Physiol , vol.118 , pp. 997-1004
    • De Leo, F.1    Bonade-Bottino, M.A.2    Ceci, L.R.3    Gallerani, R.4    Jouanin, L.5
  • 9
    • 31444442624 scopus 로고    scopus 로고
    • One of the three proteinase inhibitor genes newly identified in the Brassica napus genome codes for an inhibitor of glutamyl endopeptidase
    • De Leo F., Volpicella M., Sciancalepore M., Gallerani R., Ceci L.R. One of the three proteinase inhibitor genes newly identified in the Brassica napus genome codes for an inhibitor of glutamyl endopeptidase. FEBS Lett 2006, 580:948-954.
    • (2006) FEBS Lett , vol.580 , pp. 948-954
    • De Leo, F.1    Volpicella, M.2    Sciancalepore, M.3    Gallerani, R.4    Ceci, L.R.5
  • 10
    • 0027190626 scopus 로고
    • An interactive graphic program for calculating the secondary structure content of proteins from circular dichroism spectrum
    • Deleage G., Geourjon C. An interactive graphic program for calculating the secondary structure content of proteins from circular dichroism spectrum. Comput Appl Biosci 1993, 9:197-199.
    • (1993) Comput Appl Biosci , vol.9 , pp. 197-199
    • Deleage, G.1    Geourjon, C.2
  • 11
    • 0014691427 scopus 로고
    • Conformational aspects of polypeptide structure. XXX. Rotatory properties of cyclic and bicyclic amides. Restricted and rigid model compounds for peptide chromophores
    • Goodman M., Toniolo C., Falcetta J. Conformational aspects of polypeptide structure. XXX. Rotatory properties of cyclic and bicyclic amides. Restricted and rigid model compounds for peptide chromophores. J Am Chem Soc 1969, 91:1816-1822.
    • (1969) J Am Chem Soc , vol.91 , pp. 1816-1822
    • Goodman, M.1    Toniolo, C.2    Falcetta, J.3
  • 13
    • 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., 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.2    Guncar, G.3    Slapar, N.4    Strukelj, B.5    Jongsma, M.A.6
  • 14
    • 0034608931 scopus 로고    scopus 로고
    • Rapid and general profiling of protease specificity by using combinatorial fluorogenic substrate libraries
    • Harris J.L., Backes B.J., Leonetti F., Mahrus S., Ellman J.A., Craik C.S. Rapid and general profiling of protease specificity by using combinatorial fluorogenic substrate libraries. Proc Natl Acad Sci USA 2000, 97:7754-7759.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 7754-7759
    • Harris, J.L.1    Backes, B.J.2    Leonetti, F.3    Mahrus, S.4    Ellman, J.A.5    Craik, C.S.6
  • 15
    • 0018873523 scopus 로고
    • Protein inhibitors of proteinases
    • Laskowski M., Kato I. Protein inhibitors of proteinases. Annu Rev Biochem 1980, 49:593-626.
    • (1980) Annu Rev Biochem , vol.49 , pp. 593-626
    • Laskowski, M.1    Kato, I.2
  • 16
    • 34347386663 scopus 로고    scopus 로고
    • Plant protease inhibitors in control of phytophagous insects
    • Lawrence P., Koundal K. Plant protease inhibitors in control of phytophagous insects. Electron J Biotechnol 2002, 5:93-109.
    • (2002) Electron J Biotechnol , vol.5 , pp. 93-109
    • Lawrence, P.1    Koundal, K.2
  • 17
    • 0033576611 scopus 로고    scopus 로고
    • Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana
    • Lin X., Kaul S., Rounsley S., Shea T.P., Benito M.I., Town C.D., et al. Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana. Nature 1999, 402:761-768.
    • (1999) Nature , vol.402 , pp. 761-768
    • Lin, X.1    Kaul, S.2    Rounsley, S.3    Shea, T.P.4    Benito, M.I.5    Town, C.D.6
  • 18
    • 0009690903 scopus 로고
    • The n-πcotton effect of the peptide linkage
    • Litman B.J., Schelmann J.A. The n-πcotton effect of the peptide linkage. J Phys Chem 1965, 69:978-983.
    • (1965) J Phys Chem , vol.69 , pp. 978-983
    • Litman, B.J.1    Schelmann, J.A.2
  • 21
    • 4243468938 scopus 로고    scopus 로고
    • The Cationminus signpi interaction
    • Ma J.C., Dougherty D.A. The Cationminus signpi interaction. Chem Rev 1997, 97:1303-1324.
    • (1997) Chem Rev , vol.97 , pp. 1303-1324
    • Ma, J.C.1    Dougherty, D.A.2
  • 22
    • 0026552471 scopus 로고
    • Purification, inhibitory properties and amino acid sequence of a new serine proteinase inhibitor from white mustard (Sinapis alba L.) seed
    • Menegatti E., Tedeschi G., Ronchi S., Bortolotti F., Ascenzi P., Thomas R.M., et al. Purification, inhibitory properties and amino acid sequence of a new serine proteinase inhibitor from white mustard (Sinapis alba L.) seed. FEBS Lett 1992, 301:10-14.
    • (1992) FEBS Lett , vol.301 , pp. 10-14
    • Menegatti, E.1    Tedeschi, G.2    Ronchi, S.3    Bortolotti, F.4    Ascenzi, P.5    Thomas, R.M.6
  • 23
    • 0000180578 scopus 로고
    • Protease inhibitors in plants: genes for improving defences against insects and pathogens
    • Ryan C.A. Protease inhibitors in plants: genes for improving defences against insects and pathogens. Ann Rev Phytopathol 1990, 28:425-449.
    • (1990) Ann Rev Phytopathol , vol.28 , pp. 425-449
    • Ryan, C.A.1
  • 25
    • 11144245139 scopus 로고    scopus 로고
    • Role of inhibitors of proteolytic enzymes in plant defense against phytopathogenic microorganisms
    • Valueva T.A., Mosolov V. Role of inhibitors of proteolytic enzymes in plant defense against phytopathogenic microorganisms. Biochemistry 2004, 69:1600-1606.
    • (2004) Biochemistry , vol.69 , pp. 1600-1606
    • Valueva, T.A.1    Mosolov, V.2
  • 26
    • 0037221755 scopus 로고    scopus 로고
    • Properties of purified gut trypsin from Helicoverpa zea, adapted to proteinase inhibitors
    • Volpicella M., Ceci L.R., Cordewener J., America T., Gallerani R., Bode W., et al. Properties of purified gut trypsin from Helicoverpa zea, adapted to proteinase inhibitors. Eur J Biochem 2003, 270:10-19.
    • (2003) Eur J Biochem , vol.270 , pp. 10-19
    • Volpicella, M.1    Ceci, L.R.2    Cordewener, J.3    America, T.4    Gallerani, R.5    Bode, W.6
  • 30
    • 0033963158 scopus 로고    scopus 로고
    • Characterization of recombinant mustard trypsin inhibitor 2 (MTI2) expressed in Pichia pastoris
    • Volpicella M., Schipper A., Jongsma M.A., Spoto N., Gallerani R., Ceci L.R. Characterization of recombinant mustard trypsin inhibitor 2 (MTI2) expressed in Pichia pastoris. FEBS Lett 2000, 468:137-141.
    • (2000) FEBS Lett , vol.468 , pp. 137-141
    • Volpicella, M.1    Schipper, A.2    Jongsma, M.A.3    Spoto, N.4    Gallerani, R.5    Ceci, L.R.6
  • 31
    • 0037108093 scopus 로고    scopus 로고
    • NMR solution structure of ATTp, an Arabidopsis thaliana trypsin inhibitor
    • Zhao Q., Chae Y.K., Markley J.L. NMR solution structure of ATTp, an Arabidopsis thaliana trypsin inhibitor. Biochemistry 2002, 41:12284-12296.
    • (2002) Biochemistry , vol.41 , pp. 12284-12296
    • Zhao, Q.1    Chae, Y.K.2    Markley, J.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.