메뉴 건너뛰기




Volumn 565, Issue , 2015, Pages 289-307

Effective Isotope Labeling of Proteins in a Mammalian Expression System

Author keywords

Adenovirus vector; Glycoproteins; Isotope labeling; Mammalian expression

Indexed keywords

ADENOVIRUS VECTOR; AMINO ACID; CARBON 13; CRE RECOMBINASE; CYTOPLASM PROTEIN; DISULFIDE; GLYCOPROTEIN GP 120; ISOTOPE; MEMBRANE PROTEIN; NITROGEN 15; PROTEIN; VIRUS DNA;

EID: 84947224325     PISSN: 00766879     EISSN: 15577988     Source Type: Book Series    
DOI: 10.1016/bs.mie.2015.09.021     Document Type: Chapter
Times cited : (11)

References (68)
  • 1
    • 0000698416 scopus 로고
    • Magnetic resonance of a monoclonal anti-spin-label antibody
    • J. Anglister, T. Frey, and H.M. McConnell Magnetic resonance of a monoclonal anti-spin-label antibody Biochemistry 23 6 1984 1138 1142
    • (1984) Biochemistry , vol.23 , Issue.6 , pp. 1138-1142
    • Anglister, J.1    Frey, T.2    McConnell, H.M.3
  • 2
    • 0033041954 scopus 로고    scopus 로고
    • Efficient generation of recombinant adenoviral vectors by Cre-lox recombination in vitro
    • K. Aoki, C. Barker, X. Danthinne, M.J. Imperiale, and G.J. Nabel Efficient generation of recombinant adenoviral vectors by Cre-lox recombination in vitro Molecular Medicine 5 4 1999 224 231
    • (1999) Molecular Medicine , vol.5 , Issue.4 , pp. 224-231
    • Aoki, K.1    Barker, C.2    Danthinne, X.3    Imperiale, M.J.4    Nabel, G.J.5
  • 3
    • 0028674040 scopus 로고
    • Nuclear magnetic resonance study of antibodies: A multinuclear approach
    • Y. Arata, K. Kato, H. Takahashi, and I. Shimada Nuclear magnetic resonance study of antibodies: A multinuclear approach Methods in Enzymology 239 1994 440 464
    • (1994) Methods in Enzymology , vol.239 , pp. 440-464
    • Arata, Y.1    Kato, K.2    Takahashi, H.3    Shimada, I.4
  • 4
    • 57349106051 scopus 로고    scopus 로고
    • Dictyostelium discoideum - A promising expression system for the production of eukaryotic proteins
    • R. Arya, A. Bhattacharya, and K.S. Saini Dictyostelium discoideum - A promising expression system for the production of eukaryotic proteins The FASEB Journal 22 12 2008 4055 4066
    • (2008) The FASEB Journal , vol.22 , Issue.12 , pp. 4055-4066
    • Arya, R.1    Bhattacharya, A.2    Saini, K.S.3
  • 5
    • 0020602962 scopus 로고
    • Effect of adenovirus on metabolism of specific host mRNAs: Transport control and specific translational discrimination
    • A. Babich, L.T. Feldman, J.R. Nevins, J.E. Darnell Jr., and C. Weinberger Effect of adenovirus on metabolism of specific host mRNAs: Transport control and specific translational discrimination Molecular and Cellular Biology 3 7 1983 1212 1221
    • (1983) Molecular and Cellular Biology , vol.3 , Issue.7 , pp. 1212-1221
    • Babich, A.1    Feldman, L.T.2    Nevins, J.R.3    Darnell, J.E.4    Weinberger, C.5
  • 6
    • 50849109798 scopus 로고    scopus 로고
    • Rational vector design and multi-pathway modulation of HEK 293E cells yield recombinant antibody titers exceeding 1 g/l by transient transfection under serum-free conditions
    • G. Backliwal, M. Hildinger, S. Chenuet, S. Wulhfard, M. De Jesus, and F.M. Wurm Rational vector design and multi-pathway modulation of HEK 293E cells yield recombinant antibody titers exceeding 1 g/l by transient transfection under serum-free conditions Nucleic Acids Research 36 15 2008 e96
    • (2008) Nucleic Acids Research , vol.36 , Issue.15 , pp. e96
    • Backliwal, G.1    Hildinger, M.2    Chenuet, S.3    Wulhfard, S.4    De Jesus, M.5    Wurm, F.M.6
  • 7
    • 0022963959 scopus 로고
    • Adenovirus promoters and E1A transactivation
    • (Review)
    • A.J. Berk Adenovirus promoters and E1A transactivation Annual Review of Genetics 20 1986 45 79 (Review)
    • (1986) Annual Review of Genetics , vol.20 , pp. 45-79
    • Berk, A.J.1
  • 8
    • 0042927956 scopus 로고    scopus 로고
    • High throughput protein production for functional proteomics
    • P. Braun, and J. LaBaer High throughput protein production for functional proteomics Trends in Biotechnology 21 9 2003 383 388
    • (2003) Trends in Biotechnology , vol.21 , Issue.9 , pp. 383-388
    • Braun, P.1    LaBaer, J.2
  • 10
    • 80052329329 scopus 로고    scopus 로고
    • Methods to construct recombinant adenovirus vectors
    • M. Chillon, and R. Alemany Methods to construct recombinant adenovirus vectors Methods in Molecular Biology 737 2011 117 138
    • (2011) Methods in Molecular Biology , vol.737 , pp. 117-138
    • Chillon, M.1    Alemany, R.2
  • 13
    • 27544491928 scopus 로고    scopus 로고
    • Purification of adenovirus and adeno-associated virus: Comparison of novel membrane-based technology to conventional techniques
    • A.M. Duffy, A.M. O'Doherty, T. O'Brien, and P.M. Strappe Purification of adenovirus and adeno-associated virus: Comparison of novel membrane-based technology to conventional techniques Gene Therapy 12 S1 2005 S62 S72
    • (2005) Gene Therapy , vol.12 , Issue.S1 , pp. S62-S72
    • Duffy, A.M.1    O'Doherty, A.M.2    O'Brien, T.3    Strappe, P.M.4
  • 14
    • 0026317511 scopus 로고
    • Glycosidase inhibitors: Inhibitors of N-linked oligosaccharide processing
    • A.D. Elbein Glycosidase inhibitors: Inhibitors of N-linked oligosaccharide processing The FASEB Journal 5 15 1991 3055 3063
    • (1991) The FASEB Journal , vol.5 , Issue.15 , pp. 3055-3063
    • Elbein, A.D.1
  • 15
    • 0025076063 scopus 로고
    • Kifunensine, a potent inhibitor of the glycoprotein processing mannosidase I
    • A.D. Elbein, J.E. Tropea, M. Mitchell, and G.P. Kaushal Kifunensine, a potent inhibitor of the glycoprotein processing mannosidase I Journal of Biological Chemistry 265 26 1990 15599 15605
    • (1990) Journal of Biological Chemistry , vol.265 , Issue.26 , pp. 15599-15605
    • Elbein, A.D.1    Tropea, J.E.2    Mitchell, M.3    Kaushal, G.P.4
  • 16
    • 71549154680 scopus 로고    scopus 로고
    • Chapter 15 recombinant protein production by transient gene transfer into mammalian cells
    • R.B. Richard, P.D. Murray, Academic Press San Diego
    • S. Geisse, and C. Fux Chapter 15 recombinant protein production by transient gene transfer into mammalian cells R.B. Richard, P.D. Murray, Methods in enzymology Vol. 463 2009 Academic Press San Diego 223 238
    • (2009) Methods in Enzymology , vol.463 , pp. 223-238
    • Geisse, S.1    Fux, C.2
  • 17
    • 0003001738 scopus 로고
    • Helper-free adenovirus type-5 vectors
    • Y. Gluzman, Cold Spring Harbor Laboratory Cold Spring Harbor, NY
    • Y. Gluzman, H. Reichl, and D. Solnick Helper-free adenovirus type-5 vectors Y. Gluzman, Eukaryotic viral vectors 1982 Cold Spring Harbor Laboratory Cold Spring Harbor, NY 187 192
    • (1982) Eukaryotic Viral Vectors , pp. 187-192
    • Gluzman, Y.1    Reichl, H.2    Solnick, D.3
  • 18
    • 84855276227 scopus 로고    scopus 로고
    • A simple protocol for amino acid type selective isotope labeling in insect cells with improved yields and high reproducibility
    • A. Gossert, A. Hinniger, S. Gutmann, W. Jahnke, A. Strauss, and C. Fernández A simple protocol for amino acid type selective isotope labeling in insect cells with improved yields and high reproducibility Journal of Biomolecular NMR 51 4 2011 449 456
    • (2011) Journal of Biomolecular NMR , vol.51 , Issue.4 , pp. 449-456
    • Gossert, A.1    Hinniger, A.2    Gutmann, S.3    Jahnke, W.4    Strauss, A.5    Fernández, C.6
  • 19
    • 0017710978 scopus 로고
    • Characteristics of a human cell line transformed by DNA from human adenovirus type 5
    • F.L. Graham, J. Smiley, W.C. Russell, and R. Nairn Characteristics of a human cell line transformed by DNA from human adenovirus type 5 Journal of General Virology 36 1 1977 59 72
    • (1977) Journal of General Virology , vol.36 , Issue.1 , pp. 59-72
    • Graham, F.L.1    Smiley, J.2    Russell, W.C.3    Nairn, R.4
  • 20
    • 0027068109 scopus 로고
    • A practical method for uniform isotopic labeling of recombinant proteins in mammalian cells
    • A.P. Hansen, A.M. Petros, A.P. Mazar, T.M. Pederson, A. Rueter, and S.W. Fesik A practical method for uniform isotopic labeling of recombinant proteins in mammalian cells Biochemistry 31 51 1992 12713 12718
    • (1992) Biochemistry , vol.31 , Issue.51 , pp. 12713-12718
    • Hansen, A.P.1    Petros, A.M.2    Mazar, A.P.3    Pederson, T.M.4    Rueter, A.5    Fesik, S.W.6
  • 21
    • 0028292224 scopus 로고
    • Solution structure of the amino-terminal fragment of urokinase-type plasminogen activator
    • A.P. Hansen, A.M. Petros, R.P. Meadows, D.G. Nettesheim, A.P. Mazar, E.T. Olejniczak, and et al. Solution structure of the amino-terminal fragment of urokinase-type plasminogen activator Biochemistry 33 16 1994 4847 4864
    • (1994) Biochemistry , vol.33 , Issue.16 , pp. 4847-4864
    • Hansen, A.P.1    Petros, A.M.2    Meadows, R.P.3    Nettesheim, D.G.4    Mazar, A.P.5    Olejniczak, E.T.6
  • 22
    • 8944220232 scopus 로고    scopus 로고
    • Transforming growth factor β1: Three-dimensional structure in solution and comparison with the X-ray structure of transforming growth factor β2 †,‡
    • A.P. Hinck, S.J. Archer, S.W. Qian, A.B. Roberts, M.B. Sporn, J.A. Weatherbee, and et al. Transforming growth factor β1: Three-dimensional structure in solution and comparison with the X-ray structure of transforming growth factor β2 †,‡ Biochemistry 35 26 1996 8517 8534
    • (1996) Biochemistry , vol.35 , Issue.26 , pp. 8517-8534
    • Hinck, A.P.1    Archer, S.J.2    Qian, S.W.3    Roberts, A.B.4    Sporn, M.B.5    Weatherbee, J.A.6
  • 23
    • 80555135882 scopus 로고    scopus 로고
    • Optimizing transient recombinant protein expression in mammalian cells
    • J.L. Hartley, Humana Press New York
    • R.F. Hopkins, V.E. Wall, and D. Esposito Optimizing transient recombinant protein expression in mammalian cells J.L. Hartley, Protein expression in mammalian cells Vol. 801 2012 Humana Press New York 251 268
    • (2012) Protein Expression in Mammalian Cells , vol.801 , pp. 251-268
    • Hopkins, R.F.1    Wall, V.E.2    Esposito, D.3
  • 24
    • 0020645066 scopus 로고
    • Eukaryotic cloning vectors derived from bovine papillomavirus DNA
    • L.G.K.M. Ray Wu, Academic Press
    • P.M. Howley, N. Sarver, and M.-F. Law Eukaryotic cloning vectors derived from bovine papillomavirus DNA L.G.K.M. Ray Wu, Methods in enzymology Vol. 101 1983 Academic Press 387 402
    • (1983) Methods in Enzymology , vol.101 , pp. 387-402
    • Howley, P.M.1    Sarver, N.2    Law, M.-F.3
  • 26
    • 0029837484 scopus 로고    scopus 로고
    • Getting the glycosylation right: Implications for the biotechnology industry
    • N. Jenkins, R.B. Parekh, and D.C. James Getting the glycosylation right: Implications for the biotechnology industry Nature Biotechnology 14 8 1996 975 981
    • (1996) Nature Biotechnology , vol.14 , Issue.8 , pp. 975-981
    • Jenkins, N.1    Parekh, R.B.2    James, D.C.3
  • 28
    • 78650180127 scopus 로고    scopus 로고
    • Calcium phosphate transfection
    • John Wiley & Sons, Inc. New York, NY
    • R.E. Kingston, C.A. Chen, and H. Okayama Calcium phosphate transfection Current protocols in immunology Vol 31 2001 John Wiley & Sons, Inc. New York, NY 10.13.1 10.13.9
    • (2001) Current Protocols in Immunology , vol.31 VOL , pp. 10131-10139
    • Kingston, R.E.1    Chen, C.A.2    Okayama, H.3
  • 31
    • 77957271989 scopus 로고    scopus 로고
    • Expression-system-dependent modulation of HIV-1 envelope glycoprotein antigenicity and immunogenicity
    • L. Kong, N.C. Sheppard, G.B.E. Stewart-Jones, C.L. Robson, H. Chen, X. Xu, and et al. Expression-system-dependent modulation of HIV-1 envelope glycoprotein antigenicity and immunogenicity Journal of Molecular Biology 403 1 2010 131 147
    • (2010) Journal of Molecular Biology , vol.403 , Issue.1 , pp. 131-147
    • Kong, L.1    Sheppard, N.C.2    Stewart-Jones, G.B.E.3    Robson, C.L.4    Chen, H.5    Xu, X.6
  • 32
    • 0021239085 scopus 로고
    • Point mutations close to the AUG initiator codon affect the efficiency of translation of rat preproinsulin in vivo
    • M. Kozak Point mutations close to the AUG initiator codon affect the efficiency of translation of rat preproinsulin in vivo Nature 308 5956 1984 241 246 10.1038/308241a0
    • (1984) Nature , vol.308 , Issue.5956 , pp. 241-246
    • Kozak, M.1
  • 33
    • 0023665902 scopus 로고
    • An analysis of 5′-noncoding sequences from 699 vertebrate messenger RNAs
    • M. Kozak An analysis of 5′-noncoding sequences from 699 vertebrate messenger RNAs Nucleic Acids Research 15 20 1987 8125 8148
    • (1987) Nucleic Acids Research , vol.15 , Issue.20 , pp. 8125-8148
    • Kozak, M.1
  • 36
    • 33845906594 scopus 로고    scopus 로고
    • A comparative study of different vector designs for the mammalian expression of recombinant IgG antibodies
    • J. Li, C. Menzel, D. Meier, C. Zhang, S. Dübel, and T. Jostock A comparative study of different vector designs for the mammalian expression of recombinant IgG antibodies Journal of Immunological Methods 318 1-2 2007 113 124
    • (2007) Journal of Immunological Methods , vol.318 , Issue.1-2 , pp. 113-124
    • Li, J.1    Menzel, C.2    Meier, D.3    Zhang, C.4    Dübel, S.5    Jostock, T.6
  • 37
    • 84883595274 scopus 로고    scopus 로고
    • Generating mammalian stable cell lines by electroporation
    • J. Lorsch, Academic Press Waltham, MA
    • P.A. Longo, J.M. Kavran, M.-S. Kim, and D.J. Leahy Generating mammalian stable cell lines by electroporation J. Lorsch, Methods in Enzymology Vol. 529 2013 Academic Press Waltham, MA 209 226
    • (2013) Methods in Enzymology , vol.529 , pp. 209-226
    • Longo, P.A.1    Kavran, J.M.2    Kim, M.-S.3    Leahy, D.J.4
  • 38
    • 84883580134 scopus 로고    scopus 로고
    • Transient mammalian cell transfection with Polyethylenimine (PEI)
    • J. Lorsch, Academic Press Waltham, MA
    • P.A. Longo, J.M. Kavran, M.-S. Kim, and D.J. Leahy Transient mammalian cell transfection with Polyethylenimine (PEI) J. Lorsch, Methods in Enzymology Vol. 529 2013 Academic Press Waltham, MA 227 240
    • (2013) Methods in Enzymology , vol.529 , pp. 227-240
    • Longo, P.A.1    Kavran, J.M.2    Kim, M.-S.3    Leahy, D.J.4
  • 39
    • 0030167995 scopus 로고    scopus 로고
    • Expression of human chorionic gonadotropin uniformly labeled with NMR isotpes in Chinese hamster ovary cells: An advance toward rapid determination of glycoprotein structures
    • J.W. Lustbader, S. Birken, S. Pollak, A. Pound, B.T. Chait, U.A. Mirza, and et al. Expression of human chorionic gonadotropin uniformly labeled with NMR isotpes in Chinese hamster ovary cells: An advance toward rapid determination of glycoprotein structures Journal of Biomolecular NMR 7 4 1996 295 304
    • (1996) Journal of Biomolecular NMR , vol.7 , Issue.4 , pp. 295-304
    • Lustbader, J.W.1    Birken, S.2    Pollak, S.3    Pound, A.4    Chait, B.T.5    Mirza, U.A.6
  • 40
    • 80555135901 scopus 로고    scopus 로고
    • Identification and characterization of protein glycosylation using specific endo- and exoglycosidases
    • J.L. Hartley, Humana Press New York
    • P. Magnelli, A. Bielik, and E. Guthrie Identification and characterization of protein glycosylation using specific endo- and exoglycosidases J.L. Hartley, Protein expression in mammalian cells Vol. 801 2012 Humana Press New York 189 211
    • (2012) Protein Expression in Mammalian Cells , vol.801 , pp. 189-211
    • Magnelli, P.1    Bielik, A.2    Guthrie, E.3
  • 41
    • 84878349946 scopus 로고    scopus 로고
    • Structure of RSV fusion glycoprotein trimer bound to a prefusion-specific neutralizing antibody
    • J.S. McLellan, M. Chen, S. Leung, K.W. Graepel, X. Du, Y. Yang, and et al. Structure of RSV fusion glycoprotein trimer bound to a prefusion-specific neutralizing antibody Science (New York, N.Y.) 340 6136 2013 1113 1117
    • (2013) Science (New York, N.Y.) , vol.340 , Issue.6136 , pp. 1113-1117
    • McLellan, J.S.1    Chen, M.2    Leung, S.3    Graepel, K.W.4    Du, X.5    Yang, Y.6
  • 42
    • 0002486655 scopus 로고    scopus 로고
    • Purification and concentration of DNA from aqueous solutions
    • John Wiley & Sons, Inc. New York, NY
    • D. Moore, and D. Dowhan Purification and concentration of DNA from aqueous solutions Current protocols in molecular biology Vol. 59 2002 John Wiley & Sons, Inc. New York, NY 2.1.1 2.1.10
    • (2002) Current Protocols in Molecular Biology , vol.59 , pp. 211-2110
    • Moore, D.1    Dowhan, D.2
  • 43
    • 0018377943 scopus 로고
    • Synthesis of rabbit [beta]-globin in cultured monkey kidney cells following infection with a SV40 [beta]-globin recombinant genome
    • R.C. Mulligan, B.H. Howard, and P. Berg Synthesis of rabbit [beta]-globin in cultured monkey kidney cells following infection with a SV40 [beta]-globin recombinant genome Nature 277 5692 1979 108 114
    • (1979) Nature , vol.277 , Issue.5692 , pp. 108-114
    • Mulligan, R.C.1    Howard, B.H.2    Berg, P.3
  • 45
    • 84909640954 scopus 로고    scopus 로고
    • Structure and immune recognition of trimeric prefusion HIV-1 Env
    • M. Pancera, T. Zhou, A. Druz, I.S. Georgiev, C. Soto, J. Gorman, and et al. Structure and immune recognition of trimeric prefusion HIV-1 Env Nature 514 7523 2014 455 461
    • (2014) Nature , vol.514 , Issue.7523 , pp. 455-461
    • Pancera, M.1    Zhou, T.2    Druz, A.3    Georgiev, I.S.4    Soto, C.5    Gorman, J.6
  • 46
    • 69649090931 scopus 로고    scopus 로고
    • Transfection by electroporation
    • John Wiley & Sons, Inc. New York, NY
    • H. Potter, and R. Heller Transfection by electroporation Current protocols in molecular biology Vol. 62 2003 John Wiley & Sons, Inc. New York, NY 9.3.1 9.3.6
    • (2003) Current Protocols in Molecular Biology , vol.62 , pp. 931-936
    • Potter, H.1    Heller, R.2
  • 47
    • 0029644480 scopus 로고
    • BIAcore: A microchip-based system for analyzing the formation of macromolecular complexes
    • M. Raghavan, and P.J. Bjorkman BIAcore: A microchip-based system for analyzing the formation of macromolecular complexes Structure 3 4 1995 331 333
    • (1995) Structure , vol.3 , Issue.4 , pp. 331-333
    • Raghavan, M.1    Bjorkman, P.J.2
  • 48
    • 73249137770 scopus 로고    scopus 로고
    • Grading the commercial optical biosensor literature - Class of 2008: 'The Mighty Binders'
    • R.L. Rich, and D.G. Myszka Grading the commercial optical biosensor literature - Class of 2008: 'The Mighty Binders' Journal of Molecular Recognition 23 1 2010 1 64
    • (2010) Journal of Molecular Recognition , vol.23 , Issue.1 , pp. 1-64
    • Rich, R.L.1    Myszka, D.G.2
  • 49
    • 84870452744 scopus 로고    scopus 로고
    • Mammalian expression of isotopically labeled proteins for NMR spectroscopy
    • H.S. Atreya, Springer The Netherlands
    • M. Sastry, C. Bewley, and P. Kwong Mammalian expression of isotopically labeled proteins for NMR spectroscopy H.S. Atreya, Isotope labeling in biomolecular NMR Vol. 992 2012 Springer The Netherlands 197 211
    • (2012) Isotope Labeling in Biomolecular NMR , vol.992 , pp. 197-211
    • Sastry, M.1    Bewley, C.2    Kwong, P.3
  • 50
    • 80051663513 scopus 로고    scopus 로고
    • Mammalian production of an isotopically enriched outer domain of the HIV-1 gp120 glycoprotein for NMR spectroscopy
    • M. Sastry, L. Xu, I. Georgiev, C. Bewley, G. Nabel, and P. Kwong Mammalian production of an isotopically enriched outer domain of the HIV-1 gp120 glycoprotein for NMR spectroscopy Journal of Biomolecular NMR 50 3 2011 197 207
    • (2011) Journal of Biomolecular NMR , vol.50 , Issue.3 , pp. 197-207
    • Sastry, M.1    Xu, L.2    Georgiev, I.3    Bewley, C.4    Nabel, G.5    Kwong, P.6
  • 51
    • 0033626216 scopus 로고    scopus 로고
    • Letter to the Editor: Backbone 1H, 13C, and 15 N resonance assignments of the anti-dansyl antibody Fv fragment
    • K. Shindo, K. Masuda, H. Takahashi, Y. Arata, and I. Shimada Letter to the Editor: Backbone 1H, 13C, and 15 N resonance assignments of the anti-dansyl antibody Fv fragment Journal of Biomolecular NMR 17 4 2000 357 358
    • (2000) Journal of Biomolecular NMR , vol.17 , Issue.4 , pp. 357-358
    • Shindo, K.1    Masuda, K.2    Takahashi, H.3    Arata, Y.4    Shimada, I.5
  • 52
    • 0019989719 scopus 로고
    • Transformation of mammalian cell to antibiotic resistance with a bacterial gene under control of the SV40 early region promoter
    • P. Southern, and P. Berg Transformation of mammalian cell to antibiotic resistance with a bacterial gene under control of the SV40 early region promoter Journal of Molecular and Applied Genetics 1 1982 327 341
    • (1982) Journal of Molecular and Applied Genetics , vol.1 , pp. 327-341
    • Southern, P.1    Berg, P.2
  • 53
    • 65649133551 scopus 로고    scopus 로고
    • NMR assignment of prespore specific antigen - A cell surface adhesion glycoprotein from Dictyostelium discoideum
    • J. Swarbrick, L. Cubeddu, G. Ball, P.G. Curmi, A. Gooley, K. Williams, and et al. NMR assignment of prespore specific antigen - A cell surface adhesion glycoprotein from Dictyostelium discoideum Biomolecular NMR Assignments 3 1 2009 1 3
    • (2009) Biomolecular NMR Assignments , vol.3 , Issue.1 , pp. 1-3
    • Swarbrick, J.1    Cubeddu, L.2    Ball, G.3    Curmi, P.G.4    Gooley, A.5    Williams, K.6
  • 54
    • 33746843704 scopus 로고    scopus 로고
    • A novel and simple method for construction of recombinant adenoviruses
    • R. Tan, C. Li, S. Jiang, and L. Ma A novel and simple method for construction of recombinant adenoviruses Nucleic Acids Research 34 12 2006 e89
    • (2006) Nucleic Acids Research , vol.34 , Issue.12 , pp. e89
    • Tan, R.1    Li, C.2    Jiang, S.3    Ma, L.4
  • 55
    • 81355148543 scopus 로고    scopus 로고
    • Light it up: Highly efficient multigene delivery in mammalian cells
    • S. Trowitzsch, M. Klumpp, R. Thoma, J.-P. Carralot, and I. Berger Light it up: Highly efficient multigene delivery in mammalian cells BioEssays 33 12 2011 946 955
    • (2011) BioEssays , vol.33 , Issue.12 , pp. 946-955
    • Trowitzsch, S.1    Klumpp, M.2    Thoma, R.3    Carralot, J.-P.4    Berger, I.5
  • 56
    • 80555156119 scopus 로고    scopus 로고
    • Recombinant protein expression in the baculovirus-infected insect cell system
    • E.D. Zanders, Humana Press New York
    • T. Unger, and Y. Peleg Recombinant protein expression in the baculovirus-infected insect cell system E.D. Zanders, Chemical genomics and proteomics Vol. 800 2012 Humana Press New York 187 199
    • (2012) Chemical Genomics and Proteomics , vol.800 , pp. 187-199
    • Unger, T.1    Peleg, Y.2
  • 58
    • 75949102840 scopus 로고    scopus 로고
    • Agarose gel electrophoresis
    • John Wiley & Sons, Inc. New York, NY (pp. 2.5A.1-2.5A.9)
    • D. Voytas Agarose gel electrophoresis Current protocols in molecular biology Vol. 51 2001 John Wiley & Sons, Inc. New York, NY (pp. 2.5A.1-2.5A.9)
    • (2001) Current Protocols in Molecular Biology , vol.51
    • Voytas, D.1
  • 60
    • 0037136420 scopus 로고    scopus 로고
    • Glycans as endocytosis signals: The cases of the asialoglycoprotein and hyaluronan/chondroitin sulfate receptors
    • P.H. Weigel, and J.H.N. Yik Glycans as endocytosis signals: The cases of the asialoglycoprotein and hyaluronan/chondroitin sulfate receptors Biochimica et Biophysica Acta (BBA) - General Subjects 1572 2-3 2002 341 363
    • (2002) Biochimica et Biophysica Acta (BBA) - General Subjects , vol.1572 , Issue.2-3 , pp. 341-363
    • Weigel, P.H.1    Yik, J.H.N.2
  • 61
    • 37849009111 scopus 로고    scopus 로고
    • Isotope labeling of mammalian GPCRs in HEK293 cells and characterization of the C-terminus of bovine rhodopsin by high resolution liquid NMR spectroscopy
    • K. Werner, C. Richter, J. Klein-Seetharaman, and H. Schwalbe Isotope labeling of mammalian GPCRs in HEK293 cells and characterization of the C-terminus of bovine rhodopsin by high resolution liquid NMR spectroscopy Journal of Biomolecular NMR 40 1 2008 49 53
    • (2008) Journal of Biomolecular NMR , vol.40 , Issue.1 , pp. 49-53
    • Werner, K.1    Richter, C.2    Klein-Seetharaman, J.3    Schwalbe, H.4
  • 62
    • 33744470143 scopus 로고    scopus 로고
    • Cross-clade recognition and neutralization by the V3 region from clade C human immunodeficiency virus-1 envelope
    • L. Wu, Z.-Y. Yang, L. Xu, B. Welcher, S. Winfrey, Y. Shao, and et al. Cross-clade recognition and neutralization by the V3 region from clade C human immunodeficiency virus-1 envelope Vaccine 24 23 2006 4995 5002
    • (2006) Vaccine , vol.24 , Issue.23 , pp. 4995-5002
    • Wu, L.1    Yang, Z.-Y.2    Xu, L.3    Welcher, B.4    Winfrey, S.5    Shao, Y.6
  • 63
    • 0029133626 scopus 로고
    • Conformation and function of the N-linked glycan in the adhesion domain of human CD2
    • D.F. Wyss, J. Choi, J. Li, M. Knoppers, K. Willis, A. Arulanandam, and et al. Conformation and function of the N-linked glycan in the adhesion domain of human CD2 Science 269 5228 1995 1273 1278
    • (1995) Science , vol.269 , Issue.5228 , pp. 1273-1278
    • Wyss, D.F.1    Choi, J.2    Li, J.3    Knoppers, M.4    Willis, K.5    Arulanandam, A.6
  • 64
    • 0030891425 scopus 로고    scopus 로고
    • The counterreceptor binding site of human CD2 exhibits an extended surface patch with multiple conformations fluctuating with millisecond to microsecond motions
    • D.F. Wyss, K.T. Dayie, and G. Wagner The counterreceptor binding site of human CD2 exhibits an extended surface patch with multiple conformations fluctuating with millisecond to microsecond motions Protein Science 6 3 1997 534 542
    • (1997) Protein Science , vol.6 , Issue.3 , pp. 534-542
    • Wyss, D.F.1    Dayie, K.T.2    Wagner, G.3
  • 65
    • 0027340004 scopus 로고
    • Proton resonance assignments and secondary structure of the 13.6 kDa glycosylated adhesion domain of human CD2
    • D.F. Wyss, J.M. Withka, M.H. Knoppers, K.A. Sterne, M.A. Recny, and G. Wagner Proton resonance assignments and secondary structure of the 13.6 kDa glycosylated adhesion domain of human CD2 Biochemistry 32 41 1993 10995 11006
    • (1993) Biochemistry , vol.32 , Issue.41 , pp. 10995-11006
    • Wyss, D.F.1    Withka, J.M.2    Knoppers, M.H.3    Sterne, K.A.4    Recny, M.A.5    Wagner, G.6
  • 66
    • 28844456641 scopus 로고    scopus 로고
    • High levels of protein expression using different mammalian CMV promoters in several cell lines
    • W. Xia, P. Bringmann, J. McClary, P.P. Jones, W. Manzana, Y. Zhu, and et al. High levels of protein expression using different mammalian CMV promoters in several cell lines Protein Expression and Purification 45 1 2006 115 124
    • (2006) Protein Expression and Purification , vol.45 , Issue.1 , pp. 115-124
    • Xia, W.1    Bringmann, P.2    McClary, J.3    Jones, P.P.4    Manzana, W.5    Zhu, Y.6
  • 68
    • 84930418589 scopus 로고    scopus 로고
    • Structural repertoire of HIV-1-neutralizing antibodies targeting the CD4 supersite in 14 donors
    • T. Zhou, R.M. Lynch, L. Chen, P. Acharya, X. Wu, N.A. Doria-Rose, and et al. Structural repertoire of HIV-1-neutralizing antibodies targeting the CD4 supersite in 14 donors Cell 161 6 2015 1280 1292
    • (2015) Cell , vol.161 , Issue.6 , pp. 1280-1292
    • Zhou, T.1    Lynch, R.M.2    Chen, L.3    Acharya, P.4    Wu, X.5    Doria-Rose, N.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.