메뉴 건너뛰기




Volumn 483, Issue , 2009, Pages 265-273

Companion protease inhibitors to protect recombinant proteins in transgenic plant extracts

Author keywords

Clinically useful proteins; Companion protease inhibitors; Protein degradation; Protein stabilization; Recombinant proteins; Transgenic plants

Indexed keywords

PLANT EXTRACT; PROTEINASE INHIBITOR; RECOMBINANT PROTEIN;

EID: 60549105845     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-59745-407-0_15     Document Type: Article
Times cited : (14)

References (22)
  • 3
    • 33747141725 scopus 로고    scopus 로고
    • Foreign protein degradation and instability in plants and plant tissue cultures
    • Doran, P.M. (2006) Foreign protein degradation and instability in plants and plant tissue cultures. Trends Biotechnol. 24, 426-432.
    • (2006) Trends Biotechnol , vol.24 , pp. 426-432
    • Doran, P.M.1
  • 5
    • 14744298421 scopus 로고    scopus 로고
    • Protein modifications in the plant secretory pathway: Current status and practical implications in molecular pharming
    • Faye, L., Boulaflous, A., Benchabane, M., Gomord, V., and Michaud, D. (2005) Protein modifications in the plant secretory pathway: current status and practical implications in molecular pharming. Vaccine 23, 1770-1778.
    • (2005) Vaccine , vol.23 , pp. 1770-1778
    • Faye, L.1    Boulaflous, A.2    Benchabane, M.3    Gomord, V.4    Michaud, D.5
  • 6
    • 11844252119 scopus 로고    scopus 로고
    • A cut above the rest: The regulatory function of plant proteases
    • Schaller, A. (2004) A cut above the rest: the regulatory function of plant proteases. Planta 220, 183-197.
    • (2004) Planta , vol.220 , pp. 183-197
    • Schaller, A.1
  • 7
    • 0035212386 scopus 로고    scopus 로고
    • Medical molecular farming: Production of antibodies, biopharmaceuticals and edible vaccines in plants
    • Daniell, H., Streatfield, S.J., and Wycoff, K. (2001) Medical molecular farming: production of antibodies, biopharmaceuticals and edible vaccines in plants. Trends Plant Sci. 6, 219-226.
    • (2001) Trends Plant Sci , vol.6 , pp. 219-226
    • Daniell, H.1    Streatfield, S.J.2    Wycoff, K.3
  • 8
    • 4644232322 scopus 로고    scopus 로고
    • Downstream processing of recombinant proteins from transgenic feedstock
    • Nikolov, Z.L., and Woodard, S.L. (2004) Downstream processing of recombinant proteins from transgenic feedstock. Curr. Opin. Biotechnol. 15, 479-486.
    • (2004) Curr. Opin. Biotechnol , vol.15 , pp. 479-486
    • Nikolov, Z.L.1    Woodard, S.L.2
  • 9
    • 4043094059 scopus 로고    scopus 로고
    • Considerations for the recovery of recombinant proteins from plants
    • Menkhaus, T.J., Bai, Y., Zhang, C.M., Nikolov, Z.L., and Glatz, C.E. (2004) Considerations for the recovery of recombinant proteins from plants. Biotechnol. Progr. 20, 1001-1014.
    • (2004) Biotechnol. Progr , vol.20 , pp. 1001-1014
    • Menkhaus, T.J.1    Bai, Y.2    Zhang, C.M.3    Nikolov, Z.L.4    Glatz, C.E.5
  • 10
    • 0028965659 scopus 로고
    • Application to plant proteins of gel electrophoretic methods
    • Michaud, D., and Asselin, A. (1995) Application to plant proteins of gel electrophoretic methods. J. Chromatogr. A 698, 263-279.
    • (1995) J. Chromatogr. A , vol.698 , pp. 263-279
    • Michaud, D.1    Asselin, A.2
  • 11
    • 0032547704 scopus 로고    scopus 로고
    • Michaud, D. (1998) Gel electrophoresis of proteolytic enzymes. Anal. Biochim. Acta 372, 173-185.
    • Michaud, D. (1998) Gel electrophoresis of proteolytic enzymes. Anal. Biochim. Acta 372, 173-185.
  • 12
    • 14744299022 scopus 로고    scopus 로고
    • Opportunities for recombinant antigen and antibody expression in transgenic plants - technology assessment
    • Schillberg, S., Twyman, R.M., and Fischer, R. (2005) Opportunities for recombinant antigen and antibody expression in transgenic plants - technology assessment. Vaccine 23, 1764-1769.
    • (2005) Vaccine , vol.23 , pp. 1764-1769
    • Schillberg, S.1    Twyman, R.M.2    Fischer, R.3
  • 13
    • 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., Vezina, L.P., Trepanier, S., and Michaud, D. (2006) An in-built proteinase inhibitor system for the protection of recombinant proteins recovered from transgenic plants. Plant Biotechnol. J. 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    Vezina, L.P.5    Trepanier, S.6    Michaud, D.7
  • 14
    • 0021413421 scopus 로고    scopus 로고
    • Smith, B.J. (1984) SDS polyacrylamide gel electrophoresis of proteins, In J.M. Walker (Eds.), Methods in Molecular Biology, 1: Proteins (pp. 165-178 ). NJ: Clifton, Humana Press
    • Smith, B.J. (1984) SDS polyacrylamide gel electrophoresis of proteins, In J.M. Walker (Eds.), Methods in Molecular Biology, vol. 1: Proteins (pp. 165-178 ). NJ: Clifton, Humana Press
  • 15
    • 60549092006 scopus 로고    scopus 로고
    • Gooderham, K. (1984) Transfer techniques in protein blotting, In J.M. Walker (Eds.), Methods in Molecular Biology, 1: Proteins (pp. 165-178 ). NJ: Clifton, Humana Press
    • Gooderham, K. (1984) Transfer techniques in protein blotting, In J.M. Walker (Eds.), Methods in Molecular Biology, vol. 1: Proteins (pp. 165-178 ). NJ: Clifton, Humana Press
  • 16
    • 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., and Yelle, S. (1996) 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. 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
  • 18
    • 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., and Michaud, D. (2005) A hybrid, broad-spectrum inhibitor of Colorado potato beetle aspartate and cysteine digestive proteinases. Arch. Insect Biochem. Physiol. 60, 20-31.
    • (2005) Arch. Insect Biochem. Physiol , vol.60 , pp. 20-31
    • Brunelle, F.1    Girard, C.2    Cloutier, C.3    Michaud, D.4
  • 19
    • 0033829810 scopus 로고    scopus 로고
    • Effect of climate conditions and plant developmental stage on the stability of antibodies expressed in transgenic tobacco
    • Stevens, L.H., Stoopen, G.M., Elbers, I.J.W., Molthoff, J.W., Bakker, H.A.C., Lommen, A., Bosch, D., and Jordi, W. (2000) Effect of climate conditions and plant developmental stage on the stability of antibodies expressed in transgenic tobacco. Plant Physiol. 124, 173-182.
    • (2000) Plant Physiol , vol.124 , pp. 173-182
    • Stevens, L.H.1    Stoopen, G.M.2    Elbers, I.J.W.3    Molthoff, J.W.4    Bakker, H.A.C.5    Lommen, A.6    Bosch, D.7    Jordi, W.8
  • 20
    • 34247186321 scopus 로고    scopus 로고
    • Vacuolar cysteine proteases of wheat (Triticum aestivum L.) are common to leaf senescence induced by different factors
    • Martinez, D.E., Bartoli, C.G., Grbic, V., and Guiamet, J.J. (2007) Vacuolar cysteine proteases of wheat (Triticum aestivum L.) are common to leaf senescence induced by different factors. J. Exp. Bot. 58, 1099-1107.
    • (2007) J. Exp. Bot , vol.58 , pp. 1099-1107
    • Martinez, D.E.1    Bartoli, C.G.2    Grbic, V.3    Guiamet, J.J.4
  • 21
    • 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., and Foyer, C. (2003) Oryzacystatin I expression in transformed tobacco produces a conditional growth phenotype and enhances chilling tolerance. Plant Biotechnol. J. 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.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.