메뉴 건너뛰기




Volumn 75, Issue 1, 2011, Pages 1-14

Production of protein complexes via co-expression

Author keywords

Multi protein complex; Protein protein interaction

Indexed keywords


EID: 78049308854     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2010.07.015     Document Type: Review
Times cited : (55)

References (171)
  • 2
    • 0031835267 scopus 로고    scopus 로고
    • Co-activators and co-repressors in the integration of transcriptional responses
    • J. Torchia, C. Glass, and M.G. Rosenfeld Co-activators and co-repressors in the integration of transcriptional responses Curr. Opin. Cell Biol. 10 1998 373 383
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 373-383
    • Torchia, J.1    Glass, C.2    Rosenfeld, M.G.3
  • 3
    • 33646807491 scopus 로고    scopus 로고
    • Transcriptional regulation by p53: One protein, many possibilities
    • O. Laptenko, and C. Prives Transcriptional regulation by p53: one protein, many possibilities Cell Death. Differ. 13 2006 951 961
    • (2006) Cell Death. Differ. , vol.13 , pp. 951-961
    • Laptenko, O.1    Prives, C.2
  • 4
    • 39049129643 scopus 로고    scopus 로고
    • Small Maf proteins in mammalian gene control: Mere dimerization partners or dynamic transcriptional regulators?
    • V. Blank Small Maf proteins in mammalian gene control: mere dimerization partners or dynamic transcriptional regulators? J. Mol. Biol. 376 2008 913 925
    • (2008) J. Mol. Biol. , vol.376 , pp. 913-925
    • Blank, V.1
  • 5
    • 3042523534 scopus 로고    scopus 로고
    • Small-molecule inhibitors of the p53 suppressor HDM2: Have protein-protein interactions come of age as drug targets?
    • P.M. Fischer, and D.P. Lane Small-molecule inhibitors of the p53 suppressor HDM2: have protein-protein interactions come of age as drug targets? Trends Pharmacol. Sci. 25 2004 343 346
    • (2004) Trends Pharmacol. Sci. , vol.25 , pp. 343-346
    • Fischer, P.M.1    Lane, D.P.2
  • 6
    • 0041312697 scopus 로고    scopus 로고
    • Diversity of protein-protein interactions
    • I.M. Nooren, and J.M. Thornton Diversity of protein-protein interactions EMBO J. 22 2003 3486 3492
    • (2003) EMBO J. , vol.22 , pp. 3486-3492
    • Nooren, I.M.1    Thornton, J.M.2
  • 7
    • 34347368461 scopus 로고    scopus 로고
    • A more complete, complexed and structured interactome
    • D. Devos, and R.B. Russell A more complete, complexed and structured interactome Curr. Opin. Struct. Biol. 17 2007 370 377
    • (2007) Curr. Opin. Struct. Biol. , vol.17 , pp. 370-377
    • Devos, D.1    Russell, R.B.2
  • 9
    • 34047202181 scopus 로고    scopus 로고
    • Deciphering protein-protein interactions. Part I. Experimental techniques and databases
    • B.A. Shoemaker, and A.R. Panchenko Deciphering protein-protein interactions. Part I. Experimental techniques and databases PLoS. Comput. Biol. 3 2007 e42
    • (2007) PLoS. Comput. Biol. , vol.3 , pp. 42
    • Shoemaker, B.A.1    Panchenko, A.R.2
  • 10
    • 34548418142 scopus 로고    scopus 로고
    • Methods for the detection and analysis of protein-protein interactions
    • T. Berggard, S. Linse, and P. James Methods for the detection and analysis of protein-protein interactions Proteomics. 7 2007 2833 2842
    • (2007) Proteomics. , vol.7 , pp. 2833-2842
    • Berggard, T.1    Linse, S.2    James, P.3
  • 12
    • 65549102777 scopus 로고    scopus 로고
    • Protein-protein interaction databases: Keeping up with growing interactomes
    • B. Lehne, and T. Schlitt Protein-protein interaction databases: keeping up with growing interactomes Hum. Genomics 3 2009 291 297
    • (2009) Hum. Genomics , vol.3 , pp. 291-297
    • Lehne, B.1    Schlitt, T.2
  • 13
    • 70349876879 scopus 로고    scopus 로고
    • Knowledge-guided inference of domain-domain interactions from incomplete protein-protein interaction networks
    • M. Liu, X.W. Chen, and R. Jothi Knowledge-guided inference of domain-domain interactions from incomplete protein-protein interaction networks Bioinformatics. 25 2009 2492 2499
    • (2009) Bioinformatics. , vol.25 , pp. 2492-2499
    • Liu, M.1    Chen, X.W.2    Jothi, R.3
  • 14
    • 63749117839 scopus 로고    scopus 로고
    • A top-down approach to infer and compare domain-domain interactions across eight model organisms
    • C. Guda, B.R. King, L.R. Pal, and P. Guda A top-down approach to infer and compare domain-domain interactions across eight model organisms PLoS. One. 4 2009 e5096
    • (2009) PLoS. One. , vol.4 , pp. 5096
    • Guda, C.1    King, B.R.2    Pal, L.R.3    Guda, P.4
  • 15
    • 70449707137 scopus 로고    scopus 로고
    • Evaluation of different domain-based methods in protein interaction prediction
    • H.X. Ta, and L. Holm Evaluation of different domain-based methods in protein interaction prediction Biochem. Biophys. Res. Commun. 390 2009 357 362
    • (2009) Biochem. Biophys. Res. Commun. , vol.390 , pp. 357-362
    • Ta, H.X.1    Holm, L.2
  • 16
    • 0032828715 scopus 로고    scopus 로고
    • A generic protein purification method for protein complex characterization and proteome exploration
    • G. Rigaut, A. Shevchenko, B. Rutz, M. Wilm, M. Mann, and B. Seraphin A generic protein purification method for protein complex characterization and proteome exploration Nat. Biotechnol. 17 1999 1030 1032
    • (1999) Nat. Biotechnol. , vol.17 , pp. 1030-1032
    • Rigaut, G.1    Shevchenko, A.2    Rutz, B.3    Wilm, M.4    Mann, M.5    Seraphin, B.6
  • 18
    • 77955415819 scopus 로고    scopus 로고
    • The tandem affinity purification method: An efficient system for protein complex purification and protein interaction identification
    • X. Xu, Y. Song, Y. Li, J. Chang, H. Zhang, and L. An The tandem affinity purification method: an efficient system for protein complex purification and protein interaction identification Protein Expr. Purif. 72 2010 149 156
    • (2010) Protein Expr. Purif. , vol.72 , pp. 149-156
    • Xu, X.1    Song, Y.2    Li, Y.3    Chang, J.4    Zhang, H.5    An, L.6
  • 19
    • 0035866279 scopus 로고    scopus 로고
    • A novel multiple affinity purification tag, its use in identification of proteins associated with a cyclin-CDK complex
    • S. Honey, B.L. Schneider, D.M. Schieltz, J.R. Yates, and B. Futcher A novel multiple affinity purification tag, its use in identification of proteins associated with a cyclin-CDK complex Nucleic Acids Res 29 2001 E24
    • (2001) Nucleic Acids Res , vol.29 , pp. 24
    • Honey, S.1    Schneider, B.L.2    Schieltz, D.M.3    Yates, J.R.4    Futcher, B.5
  • 20
    • 0032103789 scopus 로고    scopus 로고
    • Reconstitution and purification of eukaryotic initiation factor 2B (eIF2B) expressed in Sf21 insect cells
    • J.R. Fabian, S.R. Kimball, and L.S. Jefferson Reconstitution and purification of eukaryotic initiation factor 2B (eIF2B) expressed in Sf21 insect cells Protein Expr. Purif. 13 1998 16 22
    • (1998) Protein Expr. Purif. , vol.13 , pp. 16-22
    • Fabian, J.R.1    Kimball, S.R.2    Jefferson, L.S.3
  • 21
    • 33750828366 scopus 로고    scopus 로고
    • In vitro reconstitution and preparative purification of complexes between the chemokine receptor CXCR4 and its ligands SDF-1alpha, gp120-CD4 and AMD3100
    • A. Dukkipati, J. Vaclavikova, D. Waghray, and K.C. Garcia In vitro reconstitution and preparative purification of complexes between the chemokine receptor CXCR4 and its ligands SDF-1alpha, gp120-CD4 and AMD3100 Protein Expr. Purif. 50 2006 203 214
    • (2006) Protein Expr. Purif. , vol.50 , pp. 203-214
    • Dukkipati, A.1    Vaclavikova, J.2    Waghray, D.3    Garcia, K.C.4
  • 23
    • 26844564067 scopus 로고    scopus 로고
    • Target selection of soluble protein complexes for structural proteomics studies
    • W. Shen, S. Yun, B. Tam, K. Dalal, and F.F. Pio Target selection of soluble protein complexes for structural proteomics studies Proteome. Sci. 3 2005 3
    • (2005) Proteome. Sci. , vol.3 , pp. 3
    • Shen, W.1    Yun, S.2    Tam, B.3    Dalal, K.4    Pio, F.F.5
  • 24
    • 0038353310 scopus 로고    scopus 로고
    • Overproduction and analysis of eukaryotic multiprotein complexes in Escherichia coli using a dual-vector strategy
    • J. Finkelstein, E. Antony, M.M. Hingorani, and M. O'Donnell Overproduction and analysis of eukaryotic multiprotein complexes in Escherichia coli using a dual-vector strategy Anal. Biochem. 319 2003 78 87
    • (2003) Anal. Biochem. , vol.319 , pp. 78-87
    • Finkelstein, J.1    Antony, E.2    Hingorani, M.M.3    O'Donnell, M.4
  • 25
    • 0035313152 scopus 로고    scopus 로고
    • Therapeutic antibody expression technology
    • H.E. Chadd, and S.M. Chamow Therapeutic antibody expression technology Curr. Opin. Biotechnol. 12 2001 188 194
    • (2001) Curr. Opin. Biotechnol. , vol.12 , pp. 188-194
    • Chadd, H.E.1    Chamow, S.M.2
  • 27
    • 0032190672 scopus 로고    scopus 로고
    • Expression of nuclear hormone receptors in Escherichia coli
    • D.E. Mossakowska Expression of nuclear hormone receptors in Escherichia coli Curr. Opin. Biotechnol. 9 1998 502 505
    • (1998) Curr. Opin. Biotechnol. , vol.9 , pp. 502-505
    • Mossakowska, D.E.1
  • 28
    • 0026551704 scopus 로고
    • RXR alpha, a promiscuous partner of retinoic acid and thyroid hormone receptors
    • T.H. Bugge, J. Pohl, O. Lonnoy, and H.G. Stunnenberg RXR alpha, a promiscuous partner of retinoic acid and thyroid hormone receptors EMBO J. 11 1992 1409 1418
    • (1992) EMBO J. , vol.11 , pp. 1409-1418
    • Bugge, T.H.1    Pohl, J.2    Lonnoy, O.3    Stunnenberg, H.G.4
  • 29
    • 0029562554 scopus 로고
    • The RXR heterodimers and orphan receptors
    • D.J. Mangelsdorf, and R.M. Evans The RXR heterodimers and orphan receptors Cell 83 1995 841 850
    • (1995) Cell , vol.83 , pp. 841-850
    • Mangelsdorf, D.J.1    Evans, R.M.2
  • 30
    • 0034615669 scopus 로고    scopus 로고
    • The SRC family of nuclear receptor coactivators
    • C. Leo, and J.D. Chen The SRC family of nuclear receptor coactivators Gene 245 2000 1 11
    • (2000) Gene , vol.245 , pp. 1-11
    • Leo, C.1    Chen, J.D.2
  • 31
    • 0030938085 scopus 로고    scopus 로고
    • Coexpression of nuclear receptor partners increases their solubility and biological activities
    • C. Li, J.W. Schwabe, E. Banayo, and R.M. Evans Coexpression of nuclear receptor partners increases their solubility and biological activities Proc. Natl. Acad. Sci. USA 94 1997 2278 2283
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2278-2283
    • Li, C.1    Schwabe, J.W.2    Banayo, E.3    Evans, R.M.4
  • 37
    • 0036030926 scopus 로고    scopus 로고
    • Use of in vitro pregnane X receptor assays to assess CYP3A4 induction potential of drug candidates
    • S.A. Jones, L.B. Moore, G.B. Wisely, and S.A. Kliewer Use of in vitro pregnane X receptor assays to assess CYP3A4 induction potential of drug candidates Methods Enzymol. 357 2002 161 170
    • (2002) Methods Enzymol. , vol.357 , pp. 161-170
    • Jones, S.A.1    Moore, L.B.2    Wisely, G.B.3    Kliewer, S.A.4
  • 40
    • 0023835289 scopus 로고
    • The glycoprotein alpha-subunit is critical for secretion and stability of the human thyrotropin beta-subunit
    • M.M. Matzuk, C.M. Kornmeier, G.K. Whitfield, I.A. Kourides, and I. Boime The glycoprotein alpha-subunit is critical for secretion and stability of the human thyrotropin beta-subunit Mol. Endocrinol. 2 1988 95 100
    • (1988) Mol. Endocrinol. , vol.2 , pp. 95-100
    • Matzuk, M.M.1    Kornmeier, C.M.2    Whitfield, G.K.3    Kourides, I.A.4    Boime, I.5
  • 41
    • 0023277697 scopus 로고
    • Gonadotropin beta subunits determine the rate of assembly and the oligosaccharide processing of hormone dimer in transfected cells
    • C.L. Corless, M.M. Matzuk, T.V. Ramabhadran, A. Krichevsky, and I. Boime Gonadotropin beta subunits determine the rate of assembly and the oligosaccharide processing of hormone dimer in transfected cells J. Cell Biol. 104 1987 1173 1181
    • (1987) J. Cell Biol. , vol.104 , pp. 1173-1181
    • Corless, C.L.1    Matzuk, M.M.2    Ramabhadran, T.V.3    Krichevsky, A.4    Boime, I.5
  • 42
    • 14544290168 scopus 로고    scopus 로고
    • Biological activities of recombinant equine luteinizing hormone/chorionic gonadotropin (eLH/CG) expressed in Sf9 and Mimic insect cell lines
    • S. Legardinier, M. Duonor-Cerutti, G. Devauchelle, Y. Combarnous, and C. Cahoreau Biological activities of recombinant equine luteinizing hormone/chorionic gonadotropin (eLH/CG) expressed in Sf9 and Mimic insect cell lines J. Mol. Endocrinol. 34 2005 47 60
    • (2005) J. Mol. Endocrinol. , vol.34 , pp. 47-60
    • Legardinier, S.1    Duonor-Cerutti, M.2    Devauchelle, G.3    Combarnous, Y.4    Cahoreau, C.5
  • 43
    • 0031041205 scopus 로고    scopus 로고
    • Expression of horse and donkey LH in COS-7 cells: Evidence for low FSH activity in donkey LH compared with horse LH
    • M. Chopineau, N. Martinat, C. Troispoux, H. Marichatou, Y. Combarnous, F. Stewart, and F. Guillou Expression of horse and donkey LH in COS-7 cells: evidence for low FSH activity in donkey LH compared with horse LH J. Endocrinol. 152 1997 371 377
    • (1997) J. Endocrinol. , vol.152 , pp. 371-377
    • Chopineau, M.1    Martinat, N.2    Troispoux, C.3    Marichatou, H.4    Combarnous, Y.5    Stewart, F.6    Guillou, F.7
  • 44
    • 42549166501 scopus 로고    scopus 로고
    • Stability and biological activities of heterodimeric and single-chain equine LH/chorionic gonadotropin variants
    • S. Legardinier, J.C. Poirier, D. Klett, Y. Combarnous, and C. Cahoreau Stability and biological activities of heterodimeric and single-chain equine LH/chorionic gonadotropin variants J. Mol. Endocrinol. 40 2008 185 198
    • (2008) J. Mol. Endocrinol. , vol.40 , pp. 185-198
    • Legardinier, S.1    Poirier, J.C.2    Klett, D.3    Combarnous, Y.4    Cahoreau, C.5
  • 45
    • 0029975957 scopus 로고    scopus 로고
    • Converting heterodimeric gonadotropins to genetically linked single chains: New approaches to structure activity relationships and analogue design
    • D. Ben-Menahem, and I. Boime Converting heterodimeric gonadotropins to genetically linked single chains: new approaches to structure activity relationships and analogue design Trends Endocrinol. Metab 7 1996 100 105
    • (1996) Trends Endocrinol. Metab , vol.7 , pp. 100-105
    • Ben-Menahem, D.1    Boime, I.2
  • 47
    • 11444270501 scopus 로고    scopus 로고
    • Production of biologically active tethered tilapia LHbetaalpha by the methylotrophic yeast Pichia pastoris
    • H. Kasuto, and B. Levavi-Sivan Production of biologically active tethered tilapia LHbetaalpha by the methylotrophic yeast Pichia pastoris Gen. Comp Endocrinol. 140 2005 222 232
    • (2005) Gen. Comp Endocrinol. , vol.140 , pp. 222-232
    • Kasuto, H.1    Levavi-Sivan, B.2
  • 48
    • 0037384140 scopus 로고    scopus 로고
    • Consequences of single-chain translation on the structures of two chorionic gonadotropin yoked analogs in alpha-beta and beta-alpha configurations
    • G.B. Fralish, P. Narayan, and D. Puett Consequences of single-chain translation on the structures of two chorionic gonadotropin yoked analogs in alpha-beta and beta-alpha configurations Mol. Endocrinol. 17 2003 757 767
    • (2003) Mol. Endocrinol. , vol.17 , pp. 757-767
    • Fralish, G.B.1    Narayan, P.2    Puett, D.3
  • 49
    • 0035046135 scopus 로고    scopus 로고
    • High-level expression of a functional single-chain human chorionic gonadotropin-luteinizing hormone receptor ectodomain complex in insect cells
    • G.B. Fralish, P. Narayan, and D. Puett High-level expression of a functional single-chain human chorionic gonadotropin-luteinizing hormone receptor ectodomain complex in insect cells Endocrinology 142 2001 1517 1524
    • (2001) Endocrinology , vol.142 , pp. 1517-1524
    • Fralish, G.B.1    Narayan, P.2    Puett, D.3
  • 50
    • 0029883778 scopus 로고    scopus 로고
    • Biophysical studies of T-cell receptors and their ligands
    • D.H. Fremont, W.A. Rees, and H. Kozono Biophysical studies of T-cell receptors and their ligands Curr. Opin. Immunol. 8 1996 93 100
    • (1996) Curr. Opin. Immunol. , vol.8 , pp. 93-100
    • Fremont, D.H.1    Rees, W.A.2    Kozono, H.3
  • 53
    • 0028168571 scopus 로고
    • Binding of a soluble alpha beta T-cell receptor to superantigen/major histocompatibility complex ligands
    • J. Kappler, J. White, H. Kozono, J. Clements, and P. Marrack Binding of a soluble alpha beta T-cell receptor to superantigen/major histocompatibility complex ligands Proc. Natl. Acad. Sci. USA 91 1994 8462 8466
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8462-8466
    • Kappler, J.1    White, J.2    Kozono, H.3    Clements, J.4    Marrack, P.5
  • 54
    • 0025314322 scopus 로고
    • Transmembrane helical interactions and the assembly of the T cell receptor complex
    • N. Manolios, J.S. Bonifacino, and R.D. Klausner Transmembrane helical interactions and the assembly of the T cell receptor complex Science 249 1990 274 277
    • (1990) Science , vol.249 , pp. 274-277
    • Manolios, N.1    Bonifacino, J.S.2    Klausner, R.D.3
  • 56
    • 0024384644 scopus 로고
    • Preferential heterodimer formation by isolated leucine zippers from fos and jun
    • E.K. O'Shea, R. Rutkowski, W.F. Stafford III, and P.S. Kim Preferential heterodimer formation by isolated leucine zippers from fos and jun Science 245 1989 646 648
    • (1989) Science , vol.245 , pp. 646-648
    • O'Shea, E.K.1    Rutkowski, R.2    Stafford III, W.F.3    Kim, P.S.4
  • 58
    • 0029808087 scopus 로고    scopus 로고
    • Expression of recombinant HLA-DR2 molecules. Replacement of the hydrophobic transmembrane region by a leucine zipper dimerization motif allows the assembly and secretion of soluble DR alpha beta heterodimers
    • A. Kalandadze, M. Galleno, L. Foncerrada, J.L. Strominger, and K.W. Wucherpfennig Expression of recombinant HLA-DR2 molecules. Replacement of the hydrophobic transmembrane region by a leucine zipper dimerization motif allows the assembly and secretion of soluble DR alpha beta heterodimers J. Biol. Chem. 271 1996 20156 20162
    • (1996) J. Biol. Chem. , vol.271 , pp. 20156-20162
    • Kalandadze, A.1    Galleno, M.2    Foncerrada, L.3    Strominger, J.L.4    Wucherpfennig, K.W.5
  • 59
    • 0029979998 scopus 로고    scopus 로고
    • Role of chain pairing for the production of functional soluble IA major histocompatibility complex class II molecules
    • C.A. Scott, K.C. Garcia, F.R. Carbone, I.A. Wilson, and L. Teyton Role of chain pairing for the production of functional soluble IA major histocompatibility complex class II molecules J. Exp. Med. 183 1996 2087 2095
    • (1996) J. Exp. Med. , vol.183 , pp. 2087-2095
    • Scott, C.A.1    Garcia, K.C.2    Carbone, F.R.3    Wilson, I.A.4    Teyton, L.5
  • 60
    • 33645395535 scopus 로고    scopus 로고
    • An efficient mammalian cell-free translation system supplemented with translation factors
    • S. Mikami, M. Masutani, N. Sonenberg, S. Yokoyama, and H. Imataka An efficient mammalian cell-free translation system supplemented with translation factors Protein Expr. Purif. 46 2006 348 357
    • (2006) Protein Expr. Purif. , vol.46 , pp. 348-357
    • Mikami, S.1    Masutani, M.2    Sonenberg, N.3    Yokoyama, S.4    Imataka, H.5
  • 61
    • 0034714288 scopus 로고    scopus 로고
    • Purification and kinetic analysis of eIF2B from Saccharomyces cerevisiae
    • J. Nika, W. Yang, G.D. Pavitt, A.G. Hinnebusch, and E.M. Hannig Purification and kinetic analysis of eIF2B from Saccharomyces cerevisiae J. Biol. Chem. 275 2000 26011 26017
    • (2000) J. Biol. Chem. , vol.275 , pp. 26011-26017
    • Nika, J.1    Yang, W.2    Pavitt, G.D.3    Hinnebusch, A.G.4    Hannig, E.M.5
  • 62
    • 38449120943 scopus 로고    scopus 로고
    • Purification of FLAG-tagged eukaryotic initiation factor 2B complexes, subcomplexes, and fragments from Saccharomyces cerevisiae
    • S.S. Mohammad-Qureshi, R. Haddad, K.S. Palmer, J.P. Richardson, E. Gomez, and G.D. Pavitt Purification of FLAG-tagged eukaryotic initiation factor 2B complexes, subcomplexes, and fragments from Saccharomyces cerevisiae Methods Enzymol. 431 2007 1 13
    • (2007) Methods Enzymol. , vol.431 , pp. 1-13
    • Mohammad-Qureshi, S.S.1    Haddad, R.2    Palmer, K.S.3    Richardson, J.P.4    Gomez, E.5    Pavitt, G.D.6
  • 63
    • 0025997947 scopus 로고
    • The encephalomyocarditis virus internal ribosome entry site allows efficient coexpression of two genes from a recombinant provirus in cultured cells and in embryos
    • I.R. Ghattas, J.R. Sanes, and J.E. Majors The encephalomyocarditis virus internal ribosome entry site allows efficient coexpression of two genes from a recombinant provirus in cultured cells and in embryos Mol. Cell Biol. 11 1991 5848 5859
    • (1991) Mol. Cell Biol. , vol.11 , pp. 5848-5859
    • Ghattas, I.R.1    Sanes, J.R.2    Majors, J.E.3
  • 64
    • 23744461088 scopus 로고    scopus 로고
    • Development of a bi-cistronic baculovirus expression vector by the Rhopalosiphum padi virus 5' internal ribosome entry site
    • Y.J. Chen, W.S. Chen, and T.Y. Wu Development of a bi-cistronic baculovirus expression vector by the Rhopalosiphum padi virus 5' internal ribosome entry site Biochem. Biophys. Res. Commun. 335 2005 616 623
    • (2005) Biochem. Biophys. Res. Commun. , vol.335 , pp. 616-623
    • Chen, Y.J.1    Chen, W.S.2    Wu, T.Y.3
  • 66
    • 0024492495 scopus 로고
    • Crystal structure of a retroviral protease proves relationship to aspartic protease family
    • DOI 10.1038/337576a0
    • M. Miller, M. Jaskolski, J.K. Rao, J. Leis, and A. Wlodawer Crystal structure of a retroviral protease proves relationship to aspartic protease family Nature 337 1989 576 579 (Pubitemid 19045546)
    • (1989) Nature , vol.337 , Issue.6207 , pp. 576-579
    • Miller, M.1    Jaskolski, M.2    Mohana Rao, J.K.3    Leis, J.4    Wlodawer, A.5
  • 67
    • 0025756193 scopus 로고
    • A range of catalytic efficiencies with avian retroviral protease subunits genetically linked to form single polypeptide chains
    • D. Bizub, I.T. Weber, C.E. Cameron, J.P. Leis, and A.M. Skalka A range of catalytic efficiencies with avian retroviral protease subunits genetically linked to form single polypeptide chains J. Biol. Chem. 266 1991 4951 4958
    • (1991) J. Biol. Chem. , vol.266 , pp. 4951-4958
    • Bizub, D.1    Weber, I.T.2    Cameron, C.E.3    Leis, J.P.4    Skalka, A.M.5
  • 68
    • 0032568591 scopus 로고    scopus 로고
    • Optimizing the stability of single-chain proteins by linker length and composition mutagenesis
    • C.R. Robinson, and R.T. Sauer Optimizing the stability of single-chain proteins by linker length and composition mutagenesis Proc. Natl. Acad. Sci. USA 95 1998 5929 5934
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5929-5934
    • Robinson, C.R.1    Sauer, R.T.2
  • 69
    • 0024338385 scopus 로고
    • Redesigning a sweet protein: Increased stability and renaturability
    • S.H. Kim, C.H. Kang, R. Kim, J.M. Cho, Y.B. Lee, and T.K. Lee Redesigning a sweet protein: increased stability and renaturability Protein Eng 2 1989 571 575
    • (1989) Protein Eng , vol.2 , pp. 571-575
    • Kim, S.H.1    Kang, C.H.2    Kim, R.3    Cho, J.M.4    Lee, Y.B.5    Lee, T.K.6
  • 72
    • 31344474305 scopus 로고    scopus 로고
    • Strategies for protein coexpression in Escherichia coli
    • N.H. Tolia, and L. Joshua-Tor Strategies for protein coexpression in Escherichia coli Nat. Methods 3 2006 55 64
    • (2006) Nat. Methods , vol.3 , pp. 55-64
    • Tolia, N.H.1    Joshua-Tor, L.2
  • 73
    • 0034170820 scopus 로고    scopus 로고
    • IRES-dependent second gene expression is significantly lower than cap-dependent first gene expression in a bicistronic vector
    • H. Mizuguchi, Z. Xu, A. Ishii-Watabe, E. Uchida, and T. Hayakawa IRES-dependent second gene expression is significantly lower than cap-dependent first gene expression in a bicistronic vector Mol. Ther. 1 2000 376 382
    • (2000) Mol. Ther. , vol.1 , pp. 376-382
    • Mizuguchi, H.1    Xu, Z.2    Ishii-Watabe, A.3    Uchida, E.4    Hayakawa, T.5
  • 74
    • 2442676387 scopus 로고    scopus 로고
    • Two-promoter vector is highly efficient for overproduction of protein complexes
    • K.J. Kim, H.E. Kim, K.H. Lee, W. Han, M.J. Yi, J. Jeong, and B.H. Oh Two-promoter vector is highly efficient for overproduction of protein complexes Protein Sci. 13 2004 1698 1703
    • (2004) Protein Sci. , vol.13 , pp. 1698-1703
    • Kim, K.J.1    Kim, H.E.2    Lee, K.H.3    Han, W.4    Yi, M.J.5    Jeong, J.6    Oh, B.H.7
  • 75
    • 13544259722 scopus 로고    scopus 로고
    • On the optimal ratio of heavy to light chain genes for efficient recombinant antibody production by CHO cells
    • S. Schlatter, S.H. Stansfield, D.M. Dinnis, A.J. Racher, J.R. Birch, and D.C. James On the optimal ratio of heavy to light chain genes for efficient recombinant antibody production by CHO cells Biotechnol. Prog. 21 2005 122 133
    • (2005) Biotechnol. Prog. , vol.21 , pp. 122-133
    • Schlatter, S.1    Stansfield, S.H.2    Dinnis, D.M.3    Racher, A.J.4    Birch, J.R.5    James, D.C.6
  • 78
    • 7444236455 scopus 로고    scopus 로고
    • Concerted assembly and cloning of multiple DNA segments using in vitro site-specific recombination: Functional analysis of multi-segment expression clones
    • D.L. Cheo, S.A. Titus, D.R. Byrd, J.L. Hartley, G.F. Temple, and M.A. Brasch Concerted assembly and cloning of multiple DNA segments using in vitro site-specific recombination: functional analysis of multi-segment expression clones Genome Res. 14 2004 2111 2120
    • (2004) Genome Res. , vol.14 , pp. 2111-2120
    • Cheo, D.L.1    Titus, S.A.2    Byrd, D.R.3    Hartley, J.L.4    Temple, G.F.5    Brasch, M.A.6
  • 79
    • 49949085914 scopus 로고    scopus 로고
    • Multi-gene gateway clone design for expression of multiple heterologous genes in living cells: Eukaryotic clones containing two and three ORF multi-gene cassettes expressed from a single promoter
    • Y. Sasaki, T. Sone, K. Yahata, H. Kishine, J. Hotta, J.D. Chesnut, T. Honda, and F. Imamoto Multi-gene gateway clone design for expression of multiple heterologous genes in living cells: eukaryotic clones containing two and three ORF multi-gene cassettes expressed from a single promoter J. Biotechnol. 136 2008 103 112
    • (2008) J. Biotechnol. , vol.136 , pp. 103-112
    • Sasaki, Y.1    Sone, T.2    Yahata, K.3    Kishine, H.4    Hotta, J.5    Chesnut, J.D.6    Honda, T.7    Imamoto, F.8
  • 80
    • 13444294743 scopus 로고    scopus 로고
    • A pivotal role for reductive methylation in the de novo crystallization of a ternary complex composed of Yersinia pestis virulence factors YopN, SycN and YscB
    • F.D. Schubot, and D.S. Waugh A pivotal role for reductive methylation in the de novo crystallization of a ternary complex composed of Yersinia pestis virulence factors YopN, SycN and YscB Acta Crystallogr. D. Biol. Crystallogr. 60 2004 1981 1986
    • (2004) Acta Crystallogr. D. Biol. Crystallogr. , vol.60 , pp. 1981-1986
    • Schubot, F.D.1    Waugh, D.S.2
  • 81
    • 0034963119 scopus 로고    scopus 로고
    • A modular polycistronic expression system for overexpressing protein complexes in Escherichia coli
    • S. Tan A modular polycistronic expression system for overexpressing protein complexes in Escherichia coli Protein Expr. Purif. 21 2001 224 234
    • (2001) Protein Expr. Purif. , vol.21 , pp. 224-234
    • Tan, S.1
  • 82
    • 14844303376 scopus 로고    scopus 로고
    • The pST44 polycistronic expression system for producing protein complexes in Escherichia coli
    • S. Tan, R.C. Kern, and W. Selleck The pST44 polycistronic expression system for producing protein complexes in Escherichia coli Protein Expr. Purif. 40 2005 385 395
    • (2005) Protein Expr. Purif. , vol.40 , pp. 385-395
    • Tan, S.1    Kern, R.C.2    Selleck, W.3
  • 83
    • 11144340226 scopus 로고    scopus 로고
    • Baculovirus expression system for heterologous multiprotein complexes
    • I. Berger, D.J. Fitzgerald, and T.J. Richmond Baculovirus expression system for heterologous multiprotein complexes Nat. Biotechnol. 22 2004 1583 1587
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1583-1587
    • Berger, I.1    Fitzgerald, D.J.2    Richmond, T.J.3
  • 86
    • 77955962894 scopus 로고    scopus 로고
    • New baculovirus expression tools for recombinant protein complex production
    • doi:10.1016/j.jsb.2010.02.010
    • S. Trowitzsch, C. Bieniossek, Y. Nie, F. Garzoni, I. Berger, New baculovirus expression tools for recombinant protein complex production, J. Struct. Biol., 2010, doi:10.1016/j.jsb.2010.02.010.
    • (2010) J. Struct. Biol.
    • Trowitzsch, S.1    Bieniossek, C.2    Nie, Y.3    Garzoni, F.4    Berger, I.5
  • 87
    • 0020654318 scopus 로고
    • The origin of replication of plasmid p15A and comparative studies on the nucleotide sequences around the origin of related plasmids
    • G. Selzer, T. Som, T. Itoh, and J. Tomizawa The origin of replication of plasmid p15A and comparative studies on the nucleotide sequences around the origin of related plasmids Cell 32 1983 119 129
    • (1983) Cell , vol.32 , pp. 119-129
    • Selzer, G.1    Som, T.2    Itoh, T.3    Tomizawa, J.4
  • 88
    • 0034887510 scopus 로고    scopus 로고
    • A new method for protein coexpression in Escherichia coli using two incompatible plasmids
    • W. Yang, L. Zhang, Z. Lu, W. Tao, and Z. Zhai A new method for protein coexpression in Escherichia coli using two incompatible plasmids Protein Expr. Purif. 22 2001 472 478
    • (2001) Protein Expr. Purif. , vol.22 , pp. 472-478
    • Yang, W.1    Zhang, L.2    Lu, Z.3    Tao, W.4    Zhai, Z.5
  • 90
  • 91
    • 0029946383 scopus 로고    scopus 로고
    • 'Knobs-into-holes' engineering of antibody CH3 domains for heavy chain heterodimerization
    • J.B. Ridgway, L.G. Presta, and P. Carter 'Knobs-into-holes' engineering of antibody CH3 domains for heavy chain heterodimerization Protein Eng 9 1996 617 621
    • (1996) Protein Eng , vol.9 , pp. 617-621
    • Ridgway, J.B.1    Presta, L.G.2    Carter, P.3
  • 92
    • 0035661006 scopus 로고    scopus 로고
    • Polyionic fusion peptides function as specific dimerization motifs
    • S.A. Richter, K. Stubenrauch, H. Lilie, and R. Rudolph Polyionic fusion peptides function as specific dimerization motifs Protein Eng 14 2001 775 783
    • (2001) Protein Eng , vol.14 , pp. 775-783
    • Richter, S.A.1    Stubenrauch, K.2    Lilie, H.3    Rudolph, R.4
  • 93
    • 0037459221 scopus 로고    scopus 로고
    • Design of a modular immunotoxin connected by polyionic adapter peptides
    • M. Kleinschmidt, R. Rudolph, and H. Lilie Design of a modular immunotoxin connected by polyionic adapter peptides J. Mol. Biol. 327 2003 445 452
    • (2003) J. Mol. Biol. , vol.327 , pp. 445-452
    • Kleinschmidt, M.1    Rudolph, R.2    Lilie, H.3
  • 94
    • 0035823140 scopus 로고    scopus 로고
    • Helix-stabilized Fv (hsFv) antibody fragments: Substituting the constant domains of a Fab fragment for a heterodimeric coiled-coil domain
    • K.M. Arndt, K.M. Muller, and A. Pluckthun Helix-stabilized Fv (hsFv) antibody fragments: substituting the constant domains of a Fab fragment for a heterodimeric coiled-coil domain J. Mol. Biol. 312 2001 221 228
    • (2001) J. Mol. Biol. , vol.312 , pp. 221-228
    • Arndt, K.M.1    Muller, K.M.2    Pluckthun, A.3
  • 95
    • 20744445493 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae Piccolo NuA4 histone acetyltransferase complex requires the Enhancer of Polycomb A domain and chromodomain to acetylate nucleosomes
    • W. Selleck, I. Fortin, D. Sermwittayawong, J. Cote, and S. Tan The Saccharomyces cerevisiae Piccolo NuA4 histone acetyltransferase complex requires the Enhancer of Polycomb A domain and chromodomain to acetylate nucleosomes Mol. Cell Biol. 25 2005 5535 5542
    • (2005) Mol. Cell Biol. , vol.25 , pp. 5535-5542
    • Selleck, W.1    Fortin, I.2    Sermwittayawong, D.3    Cote, J.4    Tan, S.5
  • 96
    • 0030985897 scopus 로고    scopus 로고
    • Baculovirus multigene expression vectors and their use for understanding the assembly process of architecturally complex virus particles
    • P. Roy, M. Mikhailov, and D.H. Bishop Baculovirus multigene expression vectors and their use for understanding the assembly process of architecturally complex virus particles Gene 190 1997 119 129
    • (1997) Gene , vol.190 , pp. 119-129
    • Roy, P.1    Mikhailov, M.2    Bishop, D.H.3
  • 97
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • H.J. Dyson, and P.E. Wright Intrinsically unstructured proteins and their functions Nat. Rev. Mol. Cell Biol. 6 2005 197 208
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 99
    • 0042622240 scopus 로고    scopus 로고
    • GlobPlot: Exploring protein sequences for globularity and disorder
    • R. Linding, R.B. Russell, V. Neduva, and T.J. Gibson GlobPlot: exploring protein sequences for globularity and disorder Nucleic Acids Res. 31 2003 3701 3708
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3701-3708
    • Linding, R.1    Russell, R.B.2    Neduva, V.3    Gibson, T.J.4
  • 102
    • 56349083255 scopus 로고    scopus 로고
    • Construction of a new polycistronic vector for over-expression and rapid purification of human hemoglobin
    • E. Domingues, T. Brillet, C. Vasseur, V. Agier, M.C. Marden, and V. Baudin-Creuza Construction of a new polycistronic vector for over-expression and rapid purification of human hemoglobin Plasmid 61 2009 71 77
    • (2009) Plasmid , vol.61 , pp. 71-77
    • Domingues, E.1    Brillet, T.2    Vasseur, C.3    Agier, V.4    Marden, M.C.5    Baudin-Creuza, V.6
  • 103
    • 0021988550 scopus 로고
    • Stable replication of plasmids derived from Epstein-Barr virus in various mammalian cells
    • J.L. Yates, N. Warren, and B. Sugden Stable replication of plasmids derived from Epstein-Barr virus in various mammalian cells Nature 313 1985 812 815
    • (1985) Nature , vol.313 , pp. 812-815
    • Yates, J.L.1    Warren, N.2    Sugden, B.3
  • 104
    • 0033825821 scopus 로고    scopus 로고
    • Episomal vectors for gene expression in mammalian cells
    • C.K. Van, P. Vanhoenacker, and G. Haegeman Episomal vectors for gene expression in mammalian cells Eur. J. Biochem. 267 2000 5665 5678
    • (2000) Eur. J. Biochem. , vol.267 , pp. 5665-5678
    • Van, C.K.1    Vanhoenacker, P.2    Haegeman, G.3
  • 106
    • 54049097435 scopus 로고    scopus 로고
    • BacMam system for high-level expression of recombinant soluble and membrane glycoproteins for structural studies
    • A. Dukkipati, H.H. Park, D. Waghray, S. Fischer, and K.C. Garcia BacMam system for high-level expression of recombinant soluble and membrane glycoproteins for structural studies Protein Expr. Purif. 62 2008 160 170
    • (2008) Protein Expr. Purif. , vol.62 , pp. 160-170
    • Dukkipati, A.1    Park, H.H.2    Waghray, D.3    Fischer, S.4    Garcia, K.C.5
  • 107
    • 34147125994 scopus 로고    scopus 로고
    • Recombinant protein production by large-scale transient gene expression in mammalian cells: State of the art and future perspectives
    • L. Baldi, D.L. Hacker, M. Adam, and F.M. Wurm Recombinant protein production by large-scale transient gene expression in mammalian cells: state of the art and future perspectives Biotechnol. Lett. 29 2007 677 684
    • (2007) Biotechnol. Lett. , vol.29 , pp. 677-684
    • Baldi, L.1    Hacker, D.L.2    Adam, M.3    Wurm, F.M.4
  • 108
    • 33846027830 scopus 로고    scopus 로고
    • An OriP/EBNA-1-based baculovirus vector with prolonged and enhanced transgene expression
    • L. Shan, L. Wang, J. Yin, P. Zhong, and J. Zhong An OriP/EBNA-1-based baculovirus vector with prolonged and enhanced transgene expression J. Gene Med. 8 2006 1400 1406
    • (2006) J. Gene Med. , vol.8 , pp. 1400-1406
    • Shan, L.1    Wang, L.2    Yin, J.3    Zhong, P.4    Zhong, J.5
  • 109
    • 0345734204 scopus 로고    scopus 로고
    • Long-term transgene expression in proliferating cells mediated by episomally maintained high-capacity adenovirus vectors
    • F. Kreppel, and S. Kochanek Long-term transgene expression in proliferating cells mediated by episomally maintained high-capacity adenovirus vectors J. Virol. 78 2004 9 22
    • (2004) J. Virol. , vol.78 , pp. 9-22
    • Kreppel, F.1    Kochanek, S.2
  • 110
    • 0042825878 scopus 로고    scopus 로고
    • Virus-like particles as immunogens
    • R. Noad, and P. Roy Virus-like particles as immunogens Trends Microbiol. 11 2003 438 444
    • (2003) Trends Microbiol. , vol.11 , pp. 438-444
    • Noad, R.1    Roy, P.2
  • 114
    • 0030817962 scopus 로고    scopus 로고
    • In vitro translation and assembly of a complete T cell receptor-CD3 complex
    • J.B. Huppa, and H.L. Ploegh In vitro translation and assembly of a complete T cell receptor-CD3 complex J. Exp. Med. 186 1997 393 403
    • (1997) J. Exp. Med. , vol.186 , pp. 393-403
    • Huppa, J.B.1    Ploegh, H.L.2
  • 115
    • 34547673538 scopus 로고    scopus 로고
    • SIMPLEX: Single-molecule PCR-linked in vitro expression: A novel method for high-throughput construction and screening of protein libraries
    • S. Rungpragayphan, T. Yamane, and H. Nakano SIMPLEX: single-molecule PCR-linked in vitro expression: a novel method for high-throughput construction and screening of protein libraries Methods Mol. Biol. 375 2007 79 94
    • (2007) Methods Mol. Biol. , vol.375 , pp. 79-94
    • Rungpragayphan, S.1    Yamane, T.2    Nakano, H.3
  • 116
    • 0442289581 scopus 로고    scopus 로고
    • Prokaryotic systems for in vitro expression
    • M.P. Weiner, Q. Lu (Eds.) Westborough, MA
    • M.C. Jewett, A. Voloshin, J.R. Swartz, Prokaryotic systems for in vitro expression, in: M.P. Weiner, Q. Lu (Eds.), Gene Cloning and Expression Technologies, Westborough, MA, 2002, pp. 391-411.
    • (2002) Gene Cloning and Expression Technologies , pp. 391-411
    • Jewett, M.C.1    Voloshin, A.2    Swartz, J.R.3
  • 120
    • 0032575057 scopus 로고    scopus 로고
    • Atomic structure of progesterone complexed with its receptor
    • S.P. Williams, and P.B. Sigler Atomic structure of progesterone complexed with its receptor Nature 393 1998 392 396
    • (1998) Nature , vol.393 , pp. 392-396
    • Williams, S.P.1    Sigler, P.B.2
  • 121
    • 3242788127 scopus 로고    scopus 로고
    • Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes
    • C. Mackintosh Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes Biochem. J. 381 2004 329 342
    • (2004) Biochem. J. , vol.381 , pp. 329-342
    • MacKintosh, C.1
  • 122
    • 0035917466 scopus 로고    scopus 로고
    • Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase complex. A role for scaffolding in enzyme regulation
    • T. Obsil, R. Ghirlando, D.C. Klein, S. Ganguly, and F. Dyda Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase complex. a role for scaffolding in enzyme regulation Cell 105 2001 257 267
    • (2001) Cell , vol.105 , pp. 257-267
    • Obsil, T.1    Ghirlando, R.2    Klein, D.C.3    Ganguly, S.4    Dyda, F.5
  • 123
    • 33645034035 scopus 로고    scopus 로고
    • Intrinsic disorder is a key characteristic in partners that bind 14-3-3 proteins
    • D.M. Bustos, and A.A. Iglesias Intrinsic disorder is a key characteristic in partners that bind 14-3-3 proteins Proteins 63 2006 35 42
    • (2006) Proteins , vol.63 , pp. 35-42
    • Bustos, D.M.1    Iglesias, A.A.2
  • 124
    • 0033056950 scopus 로고    scopus 로고
    • Functional differences of two forms of the inhibitor of caspase-activated DNase, ICAD-L, and ICAD-S
    • H. Sakahira, M. Enari, and S. Nagata Functional differences of two forms of the inhibitor of caspase-activated DNase, ICAD-L, and ICAD-S J. Biol. Chem. 274 1999 15740 15744
    • (1999) J. Biol. Chem. , vol.274 , pp. 15740-15744
    • Sakahira, H.1    Enari, M.2    Nagata, S.3
  • 133
    • 18744376914 scopus 로고    scopus 로고
    • Online predicted human interaction database
    • K.R. Brown, and I. Jurisica Online predicted human interaction database Bioinformatics. 21 2005 2076 2082
    • (2005) Bioinformatics. , vol.21 , pp. 2076-2082
    • Brown, K.R.1    Jurisica, I.2
  • 134
    • 58149178567 scopus 로고    scopus 로고
    • PIPs: Human protein-protein interaction prediction database
    • M.D. McDowall, M.S. Scott, and G.J. Barton PIPs: human protein-protein interaction prediction database Nucleic Acids Res. 37 2009 D651 D656
    • (2009) Nucleic Acids Res. , vol.37
    • McDowall, M.D.1    Scott, M.S.2    Barton, G.J.3
  • 135
    • 33845220382 scopus 로고    scopus 로고
    • IntNetDB v1.0: An integrated protein-protein interaction network database generated by a probabilistic model, BMC
    • K. Xia, D. Dong, and J.D. Han IntNetDB v1.0: an integrated protein-protein interaction network database generated by a probabilistic model, BMC Bioinformatics. 7 2006 508
    • (2006) Bioinformatics. , vol.7 , pp. 508
    • Xia, K.1    Dong, D.2    Han, J.D.3
  • 137
    • 63549137956 scopus 로고    scopus 로고
    • HAPPI: An online database of comprehensive human annotated and predicted protein interactions, BMC
    • J.Y. Chen, S. Mamidipalli, and T. Huan HAPPI: an online database of comprehensive human annotated and predicted protein interactions, BMC Genomics 10 Suppl 1 2009 S16
    • (2009) Genomics , vol.10 , Issue.SUPPL. 1 , pp. 16
    • Chen, J.Y.1    Mamidipalli, S.2    Huan, T.3
  • 138
    • 0032825991 scopus 로고    scopus 로고
    • Overexpression of multisubunit replication factors in yeast
    • Peter M.J. Burgers Overexpression of multisubunit replication factors in yeast Method: A companion to Methods in Enzymology 18 1999 349 355
    • (1999) Method: A Companion to Methods in Enzymology , vol.18 , pp. 349-355
    • Burgers, P.M.J.1
  • 139
    • 0027285205 scopus 로고
    • Development of baculovirus triple and quadruple expression vectors: Co-expression of three or four bluetongue virus proteins and the synthesis of bluetongue virus-like particles in insect cells
    • A.S. Belyaev, and P. Roy Development of baculovirus triple and quadruple expression vectors: co-expression of three or four bluetongue virus proteins and the synthesis of bluetongue virus-like particles in insect cells Nucleic Acids Res. 21 1993 1219 1223
    • (1993) Nucleic Acids Res. , vol.21 , pp. 1219-1223
    • Belyaev, A.S.1    Roy, P.2
  • 140
    • 33746257485 scopus 로고    scopus 로고
    • Co-expression of multiple subunits enables recombinant SNAPC assembly and function for transcription by human RNA polymerases II and III
    • A. Hanzlowsky, B. Jelencic, G. Jawdekar, C.S. Hinkley, J.H. Geiger, and R.W. Henry Co-expression of multiple subunits enables recombinant SNAPC assembly and function for transcription by human RNA polymerases II and III Protein Expr. Purif. 48 2006 215 223
    • (2006) Protein Expr. Purif. , vol.48 , pp. 215-223
    • Hanzlowsky, A.1    Jelencic, B.2    Jawdekar, G.3    Hinkley, C.S.4    Geiger, J.H.5    Henry, R.W.6
  • 141
    • 17644410781 scopus 로고    scopus 로고
    • Nucleosome binding and histone methyltransferase activity of Drosophila PRC2
    • M. Nekrasov, B. Wild, and J. Muller Nucleosome binding and histone methyltransferase activity of Drosophila PRC2 EMBO Rep. 6 2005 348 353
    • (2005) EMBO Rep. , vol.6 , pp. 348-353
    • Nekrasov, M.1    Wild, B.2    Muller, J.3
  • 143
    • 32244449481 scopus 로고    scopus 로고
    • Polycistronic expression and purification of the ESCRT-II endosomal trafficking complex
    • A. Hierro, J. Kim, and J.H. Hurley Polycistronic expression and purification of the ESCRT-II endosomal trafficking complex Methods Enzymol. 403 2005 322 332
    • (2005) Methods Enzymol. , vol.403 , pp. 322-332
    • Hierro, A.1    Kim, J.2    Hurley, J.H.3
  • 144
    • 36249027069 scopus 로고    scopus 로고
    • Co-expression of LKB1, MO25alpha and STRADalpha in bacteria yield the functional and active heterotrimeric complex
    • D. Neumann, M. Suter, R. Tuerk, U. Riek, and T. Wallimann Co-expression of LKB1, MO25alpha and STRADalpha in bacteria yield the functional and active heterotrimeric complex Mol. Biotechnol. 36 2007 220 231
    • (2007) Mol. Biotechnol. , vol.36 , pp. 220-231
    • Neumann, D.1    Suter, M.2    Tuerk, R.3    Riek, U.4    Wallimann, T.5
  • 146
    • 58749107128 scopus 로고    scopus 로고
    • High yield bacterial expression and purification of active recombinant PA28alphabeta complex
    • A.Y. Le Feuvre, C. ntas-Barbosa, V. Baldin, and O. Coux High yield bacterial expression and purification of active recombinant PA28alphabeta complex Protein Expr. Purif. 64 2009 219 224
    • (2009) Protein Expr. Purif. , vol.64 , pp. 219-224
    • Le Feuvre, A.Y.1    Ntas-Barbosa, C.2    Baldin, V.3    Coux, O.4
  • 149
    • 0027397943 scopus 로고
    • Self-assembly of human papillomavirus type 1 capsids by expression of the L1 protein alone or by coexpression of the L1 and L2 capsid proteins
    • M.E. Hagensee, N. Yaegashi, and D.A. Galloway Self-assembly of human papillomavirus type 1 capsids by expression of the L1 protein alone or by coexpression of the L1 and L2 capsid proteins J. Virol. 67 1993 315 322
    • (1993) J. Virol. , vol.67 , pp. 315-322
    • Hagensee, M.E.1    Yaegashi, N.2    Galloway, D.A.3
  • 150
    • 0027267418 scopus 로고
    • High level expression of mammalian protein farnesyltransferase in a baculovirus system. The purified protein contains zinc
    • W.J. Chen, J.F. Moomaw, L. Overton, T.A. Kost, and P.J. Casey High level expression of mammalian protein farnesyltransferase in a baculovirus system. The purified protein contains zinc J. Biol. Chem. 268 1993 9675 9680
    • (1993) J. Biol. Chem. , vol.268 , pp. 9675-9680
    • Chen, W.J.1    Moomaw, J.F.2    Overton, L.3    Kost, T.A.4    Casey, P.J.5
  • 152
    • 0242349122 scopus 로고    scopus 로고
    • Immunogenicity and protective efficacy of rotavirus 2/6-virus-like particles produced by a dual baculovirus expression vector and administered intramuscularly
    • A. Bertolotti-Ciarlet, M. Ciarlet, S.E. Crawford, M.E. Conner, and M.K. Estes Immunogenicity and protective efficacy of rotavirus 2/6-virus-like particles produced by a dual baculovirus expression vector and administered intramuscularly Intranasally, or orally to mice, Vaccine 21 2003 3885 3900
    • (2003) Intranasally, or Orally to Mice, Vaccine , vol.21 , pp. 3885-3900
    • Bertolotti-Ciarlet, A.1    Ciarlet, M.2    Crawford, S.E.3    Conner, M.E.4    Estes, M.K.5
  • 153
    • 0030057511 scopus 로고    scopus 로고
    • Construction of a double recombinant adenovirus vector expressing a heterodimeric cytokine: In vitro and in vivo production of biologically active interleukin-12
    • J. Bramson, M. Hitt, W.S. Gallichan, K.L. Rosenthal, J. Gauldie, and F.L. Graham Construction of a double recombinant adenovirus vector expressing a heterodimeric cytokine: in vitro and in vivo production of biologically active interleukin-12 Hum. Gene Ther. 7 1996 333 342
    • (1996) Hum. Gene Ther. , vol.7 , pp. 333-342
    • Bramson, J.1    Hitt, M.2    Gallichan, W.S.3    Rosenthal, K.L.4    Gauldie, J.5    Graham, F.L.6
  • 154
    • 0032763630 scopus 로고    scopus 로고
    • Production of biologically active, heterodimeric porcine interleukin-12 using a monocistronic baculoviral expression system
    • T. Kokuho, S. Watanabe, Y. Yokomizo, and S. Inumaru Production of biologically active, heterodimeric porcine interleukin-12 using a monocistronic baculoviral expression system Vet. Immunol. Immunopathol. 72 1999 289 302
    • (1999) Vet. Immunol. Immunopathol. , vol.72 , pp. 289-302
    • Kokuho, T.1    Watanabe, S.2    Yokomizo, Y.3    Inumaru, S.4
  • 155
    • 5344225676 scopus 로고    scopus 로고
    • General co-expression vectors for the overexpression of heterodimeric protein complexes in Escherichia coli
    • O.K. Dzivenu, H.H. Park, and H. Wu General co-expression vectors for the overexpression of heterodimeric protein complexes in Escherichia coli Protein Expr. Purif. 38 2004 1 8
    • (2004) Protein Expr. Purif. , vol.38 , pp. 1-8
    • Dzivenu, O.K.1    Park, H.H.2    Wu, H.3
  • 156
    • 33646095238 scopus 로고    scopus 로고
    • A set of ligation-independent expression vectors for co-expression of proteins in Escherichia coli
    • P.K. Chanda, W.A. Edris, and J.D. Kennedy A set of ligation-independent expression vectors for co-expression of proteins in Escherichia coli Protein Expr. Purif. 47 2006 217 224
    • (2006) Protein Expr. Purif. , vol.47 , pp. 217-224
    • Chanda, P.K.1    Edris, W.A.2    Kennedy, J.D.3
  • 157
    • 0034719111 scopus 로고    scopus 로고
    • Oligomerization properties of the viral oncoproteins adenovirus E1A and human papillomavirus E7 and their complexes with the retinoblastoma protein
    • A. Clements, K. Johnston, J.M. Mazzarelli, R.P. Ricciardi, and R. Marmorstein Oligomerization properties of the viral oncoproteins adenovirus E1A and human papillomavirus E7 and their complexes with the retinoblastoma protein Biochemistry 39 2000 16033 16045
    • (2000) Biochemistry , vol.39 , pp. 16033-16045
    • Clements, A.1    Johnston, K.2    Mazzarelli, J.M.3    Ricciardi, R.P.4    Marmorstein, R.5
  • 158
    • 0029993499 scopus 로고    scopus 로고
    • Examining rhodopsin folding and assembly through expression of polypeptide fragments
    • K.D. Ridge, S.S. Lee, and N.G. Abdulaev Examining rhodopsin folding and
    • (1996) J. Biol. Chem. , vol.271 , pp. 7860-7867
    • Ridge, K.D.1    Lee, S.S.2    Abdulaev, N.G.3
  • 159
    • 38349104234 scopus 로고    scopus 로고
    • The RNA polymerase factory: A robotic in vitro assembly platform for high-throughput production of recombinant protein complexes
    • S. Nottebaum, L. Tan, D. Trzaska, H.C. Carney, and R.O. Weinzierl The RNA polymerase factory: a robotic in vitro assembly platform for high-throughput production of recombinant protein complexes Nucleic Acids Res. 36 2008 245 252
    • (2008) Nucleic Acids Res. , vol.36 , pp. 245-252
    • Nottebaum, S.1    Tan, L.2    Trzaska, D.3    Carney, H.C.4    Weinzierl, R.O.5
  • 160
    • 9644302663 scopus 로고    scopus 로고
    • Expression of the C-terminus of HIV-1 reverse transcriptase p66 and p51 subunits as a single polypeptide with RNase H activity
    • R. Zuniga, S. Sengupta, C. Snyder, O. Leon, and M.J. Roth Expression of the C-terminus of HIV-1 reverse transcriptase p66 and p51 subunits as a single polypeptide with RNase H activity Protein Eng. Des. Sel. 17 2004 581 587
    • (2004) Protein Eng. Des. Sel. , vol.17 , pp. 581-587
    • Zuniga, R.1    Sengupta, S.2    Snyder, C.3    Leon, O.4    Roth, M.J.5
  • 163
    • 0033662861 scopus 로고    scopus 로고
    • Coexpression of proteins in bacteria using T7-based expression plasmids: Expression of heteromeric cell-cycle and transcriptional regulatory complexes
    • K. Johnston, A. Clements, R.N. Venkataramani, R.C. Trievel, and R. Marmorstein Coexpression of proteins in bacteria using T7-based expression plasmids: expression of heteromeric cell-cycle and transcriptional regulatory complexes Protein Expr. Purif. 20 2000 435 443
    • (2000) Protein Expr. Purif. , vol.20 , pp. 435-443
    • Johnston, K.1    Clements, A.2    Venkataramani, R.N.3    Trievel, R.C.4    Marmorstein, R.5
  • 164
    • 0035895435 scopus 로고    scopus 로고
    • Dissecting the interaction network of multiprotein complexes by pairwise coexpression of subunits in E. coli
    • S. Fribourg, C. Romier, S. Werten, Y.G. Gangloff, A. Poterszman, and D. Moras Dissecting the interaction network of multiprotein complexes by pairwise coexpression of subunits in E. coli J. Mol. Biol. 306 2001 363 373
    • (2001) J. Mol. Biol. , vol.306 , pp. 363-373
    • Fribourg, S.1    Romier, C.2    Werten, S.3    Gangloff, Y.G.4    Poterszman, A.5    Moras, D.6
  • 167
    • 0031789165 scopus 로고    scopus 로고
    • Construction, expression, and characterization of a novel fully activated recombinant single-chain hepatitis C virus protease
    • S.S. Taremi, B. Beyer, M. Maher, N. Yao, W. Prosise, P.C. Weber, and B.A. Malcolm Construction, expression, and characterization of a novel fully activated recombinant single-chain hepatitis C virus protease Protein Sci. 7 1998 2143 2149
    • (1998) Protein Sci. , vol.7 , pp. 2143-2149
    • Taremi, S.S.1    Beyer, B.2    Maher, M.3    Yao, N.4    Prosise, W.5    Weber, P.C.6    Malcolm, B.A.7
  • 170
    • 0035375110 scopus 로고    scopus 로고
    • Solution structure, backbone dynamics, and stability of a double mutant single-chain monellin. Structural origin of sweetness
    • Y.H. Sung, J. Shin, H.J. Chang, J.M. Cho, and W. Lee Solution structure, backbone dynamics, and stability of a double mutant single-chain monellin. Structural origin of sweetness J. Biol. Chem. 276 2001 19624 19630
    • (2001) J. Biol. Chem. , vol.276 , pp. 19624-19630
    • Sung, Y.H.1    Shin, J.2    Chang, H.J.3    Cho, J.M.4    Lee, W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.