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Volumn 42, Issue 4, 2008, Pages 271-277

Stable-isotope labeling using an inducible viral infection system in suspension-cultured plant cells

Author keywords

BY 2; Inducible virus vector; Stable isotope labeling

Indexed keywords

CALMODULIN; DIHYDROFOLATE REDUCTASE; PHOSPHOPROTEIN PHOSPHATASE INHIBITOR; PROTEIN KINASE C; TRYPSIN INHIBITOR; VIRUS VECTOR;

EID: 55949130921     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-008-9283-x     Document Type: Article
Times cited : (18)

References (28)
  • 2
    • 34548829124 scopus 로고    scopus 로고
    • Expression of active enzymes from an inducible tomato-mosaic virus-based vector in cultured transgenic tobacco BY-2 cells
    • Dohi K, Mori M (2007) Expression of active enzymes from an inducible tomato-mosaic virus-based vector in cultured transgenic tobacco BY-2 cells. Plant Biotechnol 24:367-373
    • (2007) Plant Biotechnol , vol.24 , pp. 367-373
    • Dohi, K.1    Mori, M.2
  • 3
    • 33744503909 scopus 로고    scopus 로고
    • Inducible virus-mediated expression of a foreign protein in suspension-cultured cells
    • Dohi K, Nishikiori M, Tamai A, Ishikawa M, Meshi T, Mori M (2006) Inducible virus-mediated expression of a foreign protein in suspension-cultured cells. Arch Virol 151:1075-1084
    • (2006) Arch Virol , vol.151 , pp. 1075-1084
    • Dohi, K.1    Nishikiori, M.2    Tamai, A.3    Ishikawa, M.4    Meshi, T.5    Mori, M.6
  • 4
    • 0034026065 scopus 로고    scopus 로고
    • Foreign protein production in plant tissue cultures
    • Doran PM (2000) Foreign protein production in plant tissue cultures. Curr Opin Biotechnol 11:199-204
    • (2000) Curr Opin Biotechnol , vol.11 , pp. 199-204
    • Doran, P.M.1
  • 5
    • 0028438718 scopus 로고
    • 1 H, 15 N, and 13 C resonance assignments, secondary structure, and the conformation of substrate in the binary folate complex of Escherichia coli dihydrofolate reductase
    • Falzone CJ, Cavanagh J, Cowart M, Palmer AGIII, Matthews CR, Benkovic SJ, Wright PE (1994) 1 H, 15 N, and 13 C resonance assignments, secondary structure, and the conformation of substrate in the binary folate complex of Escherichia coli dihydrofolate reductase. J Biomol NMR 4:349-366
    • (1994) J Biomol NMR , vol.4 , pp. 349-366
    • Falzone, C.J.1    Cavanagh, J.2    Cowart, M.3    Palmer III, A.G.4    Matthews, C.R.5    Benkovic, S.J.6    Wright, P.E.7
  • 6
    • 0035477961 scopus 로고    scopus 로고
    • Transgenic plants as protein factories
    • Giddings G (2001) Transgenic plants as protein factories. Curr Opin Biotechnol 12:450-454
    • (2001) Curr Opin Biotechnol , vol.12 , pp. 450-454
    • Giddings, G.1
  • 7
    • 1542291118 scopus 로고    scopus 로고
    • Posttranslational modification of therapeutic proteins in plants
    • Gomord V, Faye L (2004) Posttranslational modification of therapeutic proteins in plants. Curr Opin Plant Biol 7:171-181
    • (2004) Curr Opin Plant Biol , vol.7 , pp. 171-181
    • Gomord, V.1    Faye, L.2
  • 8
    • 8344236780 scopus 로고    scopus 로고
    • Plant cell cultures for the production of recombinant proteins
    • Hellwig S, Drossard J, Twyman RM, Fischer R (2004) Plant cell cultures for the production of recombinant proteins. Nat Biotech 22:1415-1422
    • (2004) Nat Biotech , vol.22 , pp. 1415-1422
    • Hellwig, S.1    Drossard, J.2    Twyman, R.M.3    Fischer, R.4
  • 9
    • 0025341339 scopus 로고
    • A novel approach for sequential assignment of 1 H, 13 C, and 15 N spectra of proteins: Heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin
    • Ikura M, Kay LE, Bax A (1990) A novel approach for sequential assignment of 1 H, 13 C, and 15 N spectra of proteins: Heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin. Biochemistry 29:4659-4667
    • (1990) Biochemistry , vol.29 , pp. 4659-4667
    • Ikura, M.1    Kay, L.E.2    Bax, A.3
  • 11
    • 44949291986 scopus 로고
    • Three-dimensional triple-resonance NMR spectroscopy of isotopically enriched proteins
    • Kay LE, Ikura M, Tschudin R, Bax A (1990) Three-dimensional triple-resonance NMR spectroscopy of isotopically enriched proteins. J Magn Reson 89:496-514
    • (1990) J Magn Reson , vol.89 , pp. 496-514
    • Kay, L.E.1    Ikura, M.2    Tschudin, R.3    Bax, A.4
  • 12
    • 0029365773 scopus 로고
    • Cell-free synthesis and amino acid-selective stable isotope labeling of proteins for NMR analysis
    • Kigawa T, Muto Y, Yokoyama S (1995) Cell-free synthesis and amino acid-selective stable isotope labeling of proteins for NMR analysis. J Biomol NMR 6:129-134
    • (1995) J Biomol NMR , vol.6 , pp. 129-134
    • Kigawa, T.1    Muto, Y.2    Yokoyama, S.3
  • 13
    • 0034711091 scopus 로고    scopus 로고
    • High pressure NMR reveals active-site hinge motion of folate-bound Escherichia coli dihydrofolate reductase
    • Kitahara R, Sareth S, Yamada H, Ohmae E, Gekko K, Akasaka K (2000) High pressure NMR reveals active-site hinge motion of folate-bound Escherichia coli dihydrofolate reductase. Biochemistry 39:12789-12795
    • (2000) Biochemistry , vol.39 , pp. 12789-12795
    • Kitahara, R.1    Sareth, S.2    Yamada, H.3    Ohmae, E.4    Gekko, K.5    Akasaka, K.6
  • 14
    • 0035913884 scopus 로고    scopus 로고
    • Labelling approaches for protein structural studies by solution-state and solid-state NMR
    • Lian LY, Middleton DA (2001) Labelling approaches for protein structural studies by solution-state and solid-state NMR. Prog.NMR Spectrosc 39:171-190
    • (2001) Prog.NMR Spectrosc , vol.39 , pp. 171-190
    • Lian, L.Y.1    Middleton, D.A.2
  • 15
    • 0038583721 scopus 로고    scopus 로고
    • A wheat germ cell-free system is a novel way to screen protein folding and function
    • Morita EH, Sawasaki T, Tanaka R, Endo Y, Kohno T (2003) A wheat germ cell-free system is a novel way to screen protein folding and function. Protein Sci 12:1216-1221
    • (2003) Protein Sci , vol.12 , pp. 1216-1221
    • Morita, E.H.1    Sawasaki, T.2    Tanaka, R.3    Endo, Y.4    Kohno, T.5
  • 16
    • 0026568783 scopus 로고
    • Tobacco BY-2 cell-line as the HeLa-cell in the cell biology of higher plants
    • Nagata T, Nemoto Y, Hasezawa S (1992) Tobacco BY-2 cell-line as the HeLa-cell in the cell biology of higher plants. Int Rev Cytol 132:1-30
    • (1992) Int Rev Cytol , vol.132 , pp. 1-30
    • Nagata, T.1    Nemoto, Y.2    Hasezawa, S.3
  • 17
    • 0030615247 scopus 로고    scopus 로고
    • Identification of Mg 2+ binding sites and the role of Mg 2+ on target recognition by calmodulin
    • Ohki S, Ikura M, Zhang M (1997) Identification of Mg 2+ binding sites and the role of Mg 2+ on target recognition by calmodulin. Biochemistry 36:4309-4316
    • (1997) Biochemistry , vol.36 , pp. 4309-4316
    • Ohki, S.1    Ikura, M.2    Zhang, M.3
  • 18
    • 0037424627 scopus 로고    scopus 로고
    • Distinctive solution conformation of phosphatase inhibitor CPI-17 substituted with aspartate at the phosphorylation-site threonine residue
    • Ohki S, Eto M, Shimizu M, Takada R, Brautigan DL, Kainosho M (2003) Distinctive solution conformation of phosphatase inhibitor CPI-17 substituted with aspartate at the phosphorylation-site threonine residue. J Mol Biol 5:1539-1547
    • (2003) J Mol Biol , vol.5 , pp. 1539-1547
    • Ohki, S.1    Eto, M.2    Shimizu, M.3    Takada, R.4    Brautigan, D.L.5    Kainosho, M.6
  • 19
    • 0042908539 scopus 로고    scopus 로고
    • Modern methods for expression of proteins in isotopically enriched form
    • In: Zerbe O (ed) Wiley-VCH Verlag GmbH & Co. KgaA, Weinheim
    • Patzelt H, Goto N, Iwai H, Lundstrom K, Fernholz E (2002) Modern methods for expression of proteins in isotopically enriched form. In: Zerbe O (ed) BioNMR in drug research. Wiley-VCH Verlag GmbH & Co. KgaA, Weinheim, pp 1-38
    • (2002) BioNMR in Drug Research , pp. 1-38
    • Patzelt, H.1    Goto, N.2    Iwai, H.3    Lundstrom, K.4    Fernholz, E.5
  • 22
    • 33846928691 scopus 로고    scopus 로고
    • Quantitative dynamics and binding studies of the 20S proteasome by NMR
    • Sprangers R, Kay LE (2007) Quantitative dynamics and binding studies of the 20S proteasome by NMR. Nature 445:618-622
    • (2007) Nature , vol.445 , pp. 618-622
    • Sprangers, R.1    Kay, L.E.2
  • 23
    • 0037255597 scopus 로고    scopus 로고
    • Overview of tag protein fusions: From molecular and biochemical fundamentals to commercial systems
    • Terpe K (2003) Overview of tag protein fusions: From molecular and biochemical fundamentals to commercial systems. Appl Microbiol Biotechnol 60:523-533
    • (2003) Appl Microbiol Biotechnol , vol.60 , pp. 523-533
    • Terpe, K.1
  • 24
    • 11244300993 scopus 로고    scopus 로고
    • Efficient production of isotopically labeled proteins by cell-free synthesis: A practical protocol
    • Torizawa T, Shimizu M, Taoka M, Miyano H, Kainosho M (2004) Efficient production of isotopically labeled proteins by cell-free synthesis: A practical protocol. J Biomol NMR 30:311-325
    • (2004) J Biomol NMR , vol.30 , pp. 311-325
    • Torizawa, T.1    Shimizu, M.2    Taoka, M.3    Miyano, H.4    Kainosho, M.5
  • 27
    • 0029018778 scopus 로고
    • Contribution of individual side-chains to the stability of BPTI examined by alanine-scanning mutagenesis
    • Yu MH, Weissman JS, Kim PS (1995) Contribution of individual side-chains to the stability of BPTI examined by alanine-scanning mutagenesis. J Mol Biol 249:388-397
    • (1995) J Mol Biol , vol.249 , pp. 388-397
    • Yu, M.H.1    Weissman, J.S.2    Kim, P.S.3
  • 28
    • 0034304056 scopus 로고    scopus 로고
    • An estrogen receptor-based transactivator XVE mediates highly inducible gene expression in transgenic plants
    • Zuo J, Niu Q, Chua NH (2000) An estrogen receptor-based transactivator XVE mediates highly inducible gene expression in transgenic plants. Plant J 24:265-273
    • (2000) Plant J , vol.24 , pp. 265-273
    • Zuo, J.1    Niu, Q.2    Chua, N.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.