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Volumn 831, Issue , 2012, Pages 37-54

Isotope labeling in insect cells

Author keywords

Baculovirus; Insect cells; Isotope labeling; Nuclear magnetic resonance; Recombinant protein expression

Indexed keywords

AMINO ACID; CHAPERONE; NITROGEN; RECOMBINANT PROTEIN;

EID: 84855902846     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-61779-480-3_3     Document Type: Article
Times cited : (30)

References (50)
  • 1
    • 0033794450 scopus 로고    scopus 로고
    • New developments in isotope labeling strategies for protein solution NMR spectroscopy
    • Goto, N. K., and Kay, L. E. (2000) New developments in isotope labeling strategies for protein solution NMR spectroscopy. Curr. Opin. Struct. Biol. 10 , 585-592.
    • (2000) Curr. Opin. Struct. Biol , vol.10 , pp. 585-592
    • Goto, N.K.1    Kay, L.E.2
  • 2
    • 0026231855 scopus 로고
    • Optimizing protein folding to the native state in bacteria
    • Schein, C. H. (1991) Optimizing protein folding to the native state in bacteria. Curr Opin. Biotechnol. 2 , 746-750. (Pubitemid 121002752)
    • (1991) Current Opinion in Biotechnology , vol.2 , Issue.5 , pp. 746-750
    • Schein, C.H.1
  • 5
    • 33746744319 scopus 로고    scopus 로고
    • Enhancement of soluble protein expression through the use of fusion tags
    • DOI 10.1016/j.copbio.2006.06.003, PII S0958166906000875
    • Esposito, D., and Chatterjee, D. K. (2006) Enhancement of soluble protein expression through the use of fusion tags. Curr. Opin. Biotechnol. 17 , 353-358. (Pubitemid 44163452)
    • (2006) Current Opinion in Biotechnology , vol.17 , Issue.4 , pp. 353-358
    • Esposito, D.1    Chatterjee, D.K.2
  • 6
    • 0030830073 scopus 로고    scopus 로고
    • A new Escherichia coli gene, dsbG, encodes a periplasmic protein involved in disulphide bond formation, required for recycling DsbA/DsbB and DsbC redox proteins
    • Andersen, C. L., Matthey-Dupraz, A., Missiakas, D., and Raina, S. (1997) A new Escherichia coli gene, dsbG, encodes a periplasmic protein involved in disulphide bond formation, required for recycling DsbA/DsbB and DsbC redox proteins. Mol. Microbiol. 26 , 121-132. (Pubitemid 27438243)
    • (1997) Molecular Microbiology , vol.26 , Issue.1 , pp. 121-132
    • Andersen, C.L.1    Matthey-Dupraz, A.2    Missiakas, D.3    Raina, S.4
  • 7
    • 0028028387 scopus 로고
    • Building bridges: Disulphide bond formation in the cell
    • DOI 10.1111/j.1365-2958.1994.tb01281.x
    • Bardwell, J. C. (1994) Building bridges: disulphide bond formation in the cell. Mol. Microbiol. 14 , 199-205. (Pubitemid 24325797)
    • (1994) Molecular Microbiology , vol.14 , Issue.2 , pp. 199-205
    • Bardwell, J.C.A.1
  • 8
    • 4644304230 scopus 로고    scopus 로고
    • Isotopic labeling of recombinant proteins from the methylotrophic yeast Pichia pastoris
    • Pickford, A. R., and O'Leary, J. M. (2004) Isotopic labeling of recombinant proteins from the methylotrophic yeast Pichia pastoris . Methods Mol. Biol. 278 , 17-33.
    • (2004) Methods Mol. Biol , vol.278 , pp. 17-33
    • Pickford, A.R.1    O'leary, J.M.2
  • 9
    • 41749102204 scopus 로고    scopus 로고
    • Baculoviral vectors for gene delivery: A review
    • Hu, Y. C. (2008) Baculoviral vectors for gene delivery: a review. Curr. Gene Ther. 8 , 54-65.
    • (2008) Curr. Gene Ther , vol.8 , pp. 54-65
    • Hu, Y.C.1
  • 10
    • 34247533256 scopus 로고    scopus 로고
    • Implementation of BacMam virus gene delivery technology in a drug discovery setting
    • DOI 10.1016/j.drudis.2007.02.017, PII S1359644607001006
    • Kost, T. A., Condreay, J. P., Ames, R. S., Rees, S., and Romanos, M. A. (2007) Implementation of BacMam virus gene delivery technology in a drug discovery setting. Drug Discov. Today 12 , 396-403. (Pubitemid 46646990)
    • (2007) Drug Discovery Today , vol.12 , Issue.9-10 , pp. 396-403
    • Kost, T.A.1    Condreay, J.P.2    Ames, R.S.3    Rees, S.4    Romanos, M.A.5
  • 11
    • 62149138458 scopus 로고    scopus 로고
    • Baculovirus expression systems for recombinant protein production in insect cells
    • Hitchman, R. B., Possee, R. D., and King, L. A. (2009) Baculovirus expression systems for recombinant protein production in insect cells. Recent Pat. Biotechnol. 3 , 46-54.
    • (2009) Recent Pat. Biotechnol , vol.3 , pp. 46-54
    • Hitchman, R.B.1    Possee, R.D.2    King, L.A.3
  • 12
    • 41549119862 scopus 로고    scopus 로고
    • Effect of differential N-linked and O-linked mannosylation on recognition of fungal antigens by dendritic cells
    • Lam, J. S., Huang, H., and Levitz, S. M. (2007) Effect of differential N-linked and O-linked mannosylation on recognition of fungal antigens by dendritic cells. PLoS One 2 , e1009.
    • (2007) PLoS One , vol.2
    • Lam, J.S.1    Huang, H.2    Levitz, S.M.3
  • 14
    • 0041589205 scopus 로고    scopus 로고
    • The biology and enzymology of protein tyrosine O-sulfation
    • DOI 10.1074/jbc.R300008200
    • Moore, K. L. (2003) The biology and enzymology of protein tyrosine O-sulfation. J. Biol. Chem. 278 , 24243-24246. (Pubitemid 37548571)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.27 , pp. 24243-24246
    • Moore, K.L.1
  • 15
    • 14744285206 scopus 로고    scopus 로고
    • Expression of heterologous proteins in Pichia pastoris: A useful experimental tool in protein engineenring and production
    • DOI 10.1002/jmr.687
    • Daly, R., and Hearn, M. T. (2005) Expression of heterologous proteins in Pichia pastoris : a useful experimental tool in protein engineering and production. J. Mol. Recognit. 18 , 119-138. (Pubitemid 40328574)
    • (2005) Journal of Molecular Recognition , vol.18 , Issue.2 , pp. 119-138
    • Daly, R.1    Hearn, M.T.W.2
  • 16
    • 36149001292 scopus 로고    scopus 로고
    • Glycosylation engineering in yeast: The advent of fully humanized yeast
    • DOI 10.1016/j.copbio.2007.09.001, PII S0958166907001139, Expression Technologies / Tissue and Cell Engineering
    • Hamilton, S. R., and Gerngross, T. U. (2007) Glycosylation engineering in yeast: the advent of fully humanized yeast. Curr. Opin. Biotechnol. 18 , 387-392. (Pubitemid 350116586)
    • (2007) Current Opinion in Biotechnology , vol.18 , Issue.5 , pp. 387-392
    • Hamilton, S.R.1    Gerngross, T.U.2
  • 17
    • 0025291371 scopus 로고
    • Molecular and genetic approach to enhancing protein secretion
    • DOI 10.1016/0076-6879(90)85039-Q
    • Chisholm, V., Chen, C. Y., Simpson, N. J., and Hitzeman, R. A. (1990) Molecular and genetic approach to enhancing protein secretion. Methods Enzymol. 185 , 471-482. (Pubitemid 20219842)
    • (1990) Methods in Enzymology , vol.185 , pp. 471-482
    • Chisholm, V.1    Chen, C.Y.2    Simpson, N.J.3    Hitzeman, R.A.4
  • 18
    • 0025351563 scopus 로고
    • Analysis of synthesis, processing, and secretion of proteins expressed in mammalian cells
    • DOI 10.1016/0076-6879(90)85046-Q
    • Dorner, A. J., and Kaufman, R. J. (1990) Analysis of synthesis, processing, and secretion of proteins expressed in mammalian cells. Methods Enzymol. 185 , 577-596. (Pubitemid 20219849)
    • (1990) Methods in Enzymology , vol.185 , pp. 577-596
    • Dorner, A.J.1    Kaufman, R.J.2
  • 19
    • 0024306386 scopus 로고
    • Yeast mutants with increased secretion efficiency
    • Moir, D. T. (1989) Yeast mutants with increased secretion efficiency. Biotechnology 13 , 215-231.
    • (1989) Biotechnology , vol.13 , pp. 215-231
    • Moir, D.T.1
  • 20
    • 0025774743 scopus 로고
    • The large surface protein of hepatitis B virus is retained in the yeast endoplasmic reticulum and provokes its unique enlargement
    • Biemans, R., Thines, D., Rutgers, T., De Wilde, M., and Cabezon, T. (1991) The large surface protein of hepatitis B virus is retained in the yeast endoplasmic reticulum and provokes its unique enlargement. DNA Cell. Biol. 10 , 191-200.
    • (1991) DNA Cell. Biol , vol.10 , pp. 191-200
    • Biemans, R.1    Thines, D.2    Rutgers, T.3    De Wilde, M.4    Cabezon, T.5
  • 21
    • 0026001288 scopus 로고
    • Quantitative immunocytochemical staining for recombinant tissue-type plasminogen activator in transfected Chinese hamster ovary cells
    • Gennaro, D. E., Hoffstein, S. T., Marks, G., Ramos, L., Oka, M. S., Reff, M. E., Hart, T. K., and Bugelski, P. J. (1991) Quantitative immunocytochemical staining for recombinant tissue-type plasminogen activator in transfected Chinese hamster ovary cells. Proc. Soc. Exp. Biol. Med. 198 , 591-598.
    • (1991) Proc. Soc. Exp. Biol. Med , vol.198 , pp. 591-598
    • Gennaro, D.E.1    Hoffstein, S.T.2    Marks, G.3    Ramos, L.4    Oka, M.S.5    Reff, M.E.6    Hart, T.K.7    Bugelski, P.J.8
  • 22
    • 0026232555 scopus 로고
    • Gene expression in yeast: Protein secretion
    • Shuster, J. R. (1991) Gene expression in yeast: protein secretion. Curr. Opin. Biotechnol. 2 , 685-690. (Pubitemid 121002741)
    • (1991) Current Opinion in Biotechnology , vol.2 , Issue.5 , pp. 685-690
    • Shuster, J.R.1
  • 24
    • 0028219869 scopus 로고
    • Protein disulfide isomerase overexpression increases secretion of foreign proteins in Saccharomyces cerevisiae
    • Robinson, A. S., Hines, V., and Wittrup, K. D. (1994) Protein disulfide isomerase overexpression increases secretion of foreign proteins in Saccharomyces cerevisiae . Biotechnology (N Y) 12 , 381-384.
    • (1994) Biotechnology (N Y) , vol.12 , pp. 381-384
    • Robinson, A.S.1    Hines, V.2    Wittrup, K.D.3
  • 25
    • 0031879861 scopus 로고    scopus 로고
    • Increasing the secretory capacity of Saccharomyces cerevisiae for production of single-chain antibody fragments
    • DOI 10.1038/nbt0898-773
    • Shusta, E. V., Raines, R. T., Pluckthun, A., and Wittrup, K. D. (1998) Increasing the secretory capacity of Saccharomyces cerevisiae for production of single-chain antibody fragments. Nat. Biotechnol. 16 , 773-777. (Pubitemid 28363761)
    • (1998) Nature Biotechnology , vol.16 , Issue.8 , pp. 773-777
    • Shusta, E.V.1    Raines, R.T.2    Pluckthun, A.3    Wittrup, K.D.4
  • 26
    • 0141533196 scopus 로고    scopus 로고
    • Co-expression of molecular chaperones does not improve the heterologous expression of mammalian G-protein coupled receptor expression in yeast
    • DOI 10.1002/bit.10771
    • Butz, J. A., Niebauer, R. T., and Robinson, A. S. (2003) Co-expression of molecular chaperones does not improve the heterologous expression of mammalian G-protein coupled receptor expression in yeast. Biotechnol. Bioeng. 84 , 292-304. (Pubitemid 37221531)
    • (2003) Biotechnology and Bioengineering , vol.84 , Issue.3 , pp. 292-304
    • Butz, J.A.1    Niebauer, R.T.2    Robinson, A.S.3
  • 27
    • 70449710875 scopus 로고    scopus 로고
    • Expression systems for therapeutic glycoprotein production
    • Durocher, Y., and Butler, M. (2009) Expression systems for therapeutic glycoprotein production. Curr. Opin. Biotechnol. 20 , 700-707.
    • (2009) Curr. Opin. Biotechnol , vol.20 , pp. 700-707
    • Durocher, Y.1    Butler, M.2
  • 28
    • 71549150895 scopus 로고    scopus 로고
    • Baculovirus-insect cell expression systems
    • Jarvis, D. L. (2009) Baculovirus-insect cell expression systems. Methods Enzymol. 463 , 191-222.
    • (2009) Methods Enzymol , vol.463 , pp. 191-222
    • Jarvis, D.L.1
  • 31
    • 13844271129 scopus 로고    scopus 로고
    • From gene to protein: A review of new and enabling technologies for multi-parallel protein expression
    • DOI 10.1016/j.pep.2004.10.018
    • Hunt, I. (2005) From gene to protein: a review of new and enabling technologies for multiparallel protein expression. Protein Expr. Purif. 40 , 1-22. (Pubitemid 40240966)
    • (2005) Protein Expression and Purification , vol.40 , Issue.1 , pp. 1-22
    • Hunt, I.1
  • 32
    • 0022234394 scopus 로고
    • Baculovirus-mediated expression of bacterial genes in dipteran and mammalian cells
    • Carbonell, L. F., Klowden, M. J., and Miller, L. K. (1985) Baculovirus-mediated expression of bacterial genes in dipteran and mammalian cells. J. Virol. 56 , 153-160. (Pubitemid 16256867)
    • (1985) Journal of Virology , vol.56 , Issue.1 , pp. 153-160
    • Carbonell, L.F.1    Klowden, M.J.2    Miller, L.K.3
  • 33
    • 0021010433 scopus 로고
    • Production of human beta interferon in insect cells infected with a baculovirus expression vector
    • Smith, G. E., Summers, M. D., and Fraser, M. J. (1983) Production of human beta interferon in insect cells infected with a baculovirus expression vector. Molecular Cell. Biol. 3 , 2156-2165.
    • (1983) Molecular Cell. Biol , vol.3 , pp. 2156-2165
    • Smith, G.E.1    Summers, M.D.2    Fraser, M.J.3
  • 34
    • 0028086144 scopus 로고
    • The complete DNA sequence of Autographa californica nuclear polyhedrosis virus
    • DOI 10.1006/viro.1994.1380
    • Ayres, M. D., Howard, S. C., Kuzio, J., Lopez- Ferber, M., and Possee, R. D. (1994) The complete DNA sequence of Autographa californica nuclear polyhedrosis virus. Virology 202 , 586-605. (Pubitemid 24254872)
    • (1994) Virology , vol.202 , Issue.2 , pp. 586-605
    • Ayres, M.D.1    Howard, S.C.2    Kuzio, J.3    Lopez-Ferber, M.4    Possee, R.D.5
  • 35
    • 0027273755 scopus 로고
    • A method for producing recombinant baculovirus expression vectors at high frequency
    • Kitts, P. A., and Possee, R. D. (1993) A method for producing recombinant baculovirus expression vectors at high frequency. Biotechniques 14 , 810-817.
    • (1993) Biotechniques , vol.14 , pp. 810-817
    • Kitts, P.A.1    Possee, R.D.2
  • 36
    • 22844450442 scopus 로고    scopus 로고
    • Baculovirus as versatile vectors for protein expression in insect and mammalian cells
    • DOI 10.1038/nbt1095
    • Kost, T. A., Condreay, J. P., and Jarvis, D. L. (2005) Baculovirus as versatile vectors for protein expression in insect and mammalian cells. Nat. Biotechnol. 23 , 567-575. (Pubitemid 41724895)
    • (2005) Nature Biotechnology , vol.23 , Issue.5 , pp. 567-575
    • Kost, T.A.1    Condreay, J.P.2    Jarvis, D.L.3
  • 37
    • 0025282331 scopus 로고
    • Gene organization and transcription of TED, a lepidopteran retrotransposon integrated within the baculovirus genome
    • Friesen, P. D., and Nissen, M. S. (1990) Gene organization and transcription of TED, a lepidopteran retrotransposon integrated within the baculovirus genome. Mol. Cell. Biol. 10 , 3067-3077.
    • (1990) Mol. Cell. Biol , vol.10 , pp. 3067-3077
    • Friesen, P.D.1    Nissen, M.S.2
  • 38
    • 33748742271 scopus 로고    scopus 로고
    • Protein N-Glycosylation in the Baculovirus-Insect Cell Expression System and Engineering of Insect Cells to Produce "Mammalianized" Recombinant Glycoproteins
    • DOI 10.1016/S0065-3527(06)68005-6, PII S0065352706680056, Insect Viruses: Biotechnological Applications
    • Harrison, R. L., and Jarvis, D. L. (2006) Protein N-glycosylation in the baculovirusinsect cell expression system and engineering of insect cells to produce "mammalianized" recombinant glycoproteins. Adv. Virus Res. 68 , 159-191. (Pubitemid 44402211)
    • (2006) Advances in Virus Research , vol.68 , pp. 159-191
    • Harrison, R.L.1    Jarvis, D.L.2
  • 41
    • 0033571455 scopus 로고    scopus 로고
    • Producing selenomethionine-labeled proteins with a baculovirus expression vector system
    • DOI 10.1016/S0969-2126(00)80020-9
    • Bellizzi, J. J., Widom, J., Kemp, C. W., and Clardy, J. (1999) Producing selenomethioninelabeled proteins with a baculovirus expression vector system. Structure 7 , R263-267. (Pubitemid 29529871)
    • (1999) Structure , vol.7 , Issue.11
    • Bellizzi III, J.J.1    Widom, J.2    Kemp, C.W.3    Clardy, J.4
  • 43
    • 0038386883 scopus 로고    scopus 로고
    • Amino-acid-type selective isotope labeling of proteins expressed in Baculovirus-infected insect cells useful for NMR studies
    • DOI 10.1023/A:1024013111478
    • Strauss, A., Bitsch, F., Cutting, B., Fendrich, G., Graff, P., Liebetanz, J., Zurini, M., and Jahnke, W. (2003) Amino-acid-type selective isotope labeling of proteins expressed in Baculovirus-infected insect cells useful for NMR studies. J. Biomol. NMR 26 , 367-372. (Pubitemid 36818136)
    • (2003) Journal of Biomolecular NMR , vol.26 , Issue.4 , pp. 367-372
    • Strauss, A.1    Bitsch, F.2    Cutting, B.3    Fendrich, G.4    Graff, P.5    Liebetanz, J.6    Zurini, M.7    Jahnke, W.8
  • 44
    • 24644483798 scopus 로고    scopus 로고
    • Efficient uniform isotope labeling of Abl kinase expressed in Baculovirus-infected insect cells
    • DOI 10.1007/s10858-005-2451-3
    • Strauss, A., Bitsch, F., Fendrich, G., Graff, P., Knecht, R., Meyhack, B., and Jahnke, W. (2005) Efficient uniform isotope labeling of Abl kinase expressed in Baculovirus-infected insect cells. J. Biomol. NMR 31 , 343-349. (Pubitemid 41348910)
    • (2005) Journal of Biomolecular NMR , vol.31 , Issue.4 , pp. 343-349
    • Strauss, A.1    Bitsch, F.2    Fendrich, G.3    Graff, P.4    Knecht, R.5    Meyhack, B.6    Jahnke, W.7
  • 50
    • 0034992645 scopus 로고    scopus 로고
    • A method for efficient isotopic labeling of recombinant proteins
    • DOI 10.1023/A:1011254402785
    • Marley, J., Lu, M., and Bracken, C. (2001) A method for efficient isotopic labeling of recombinant proteins. J. Biomol. NMR 20 , 71-75. (Pubitemid 32519656)
    • (2001) Journal of Biomolecular NMR , vol.20 , Issue.1 , pp. 71-75
    • Marley, J.1    Lu, M.2    Bracken, C.3


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