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Volumn 65, Issue 11, 2008, Pages 1729-1755

Large-scale production of functional membrane proteins

Author keywords

Cell free expression; Detergents; Expression systems; Membrane proteins; Posttranslational modification

Indexed keywords

HYBRID PROTEIN; MEMBRANE PROTEIN;

EID: 44749088968     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-008-8067-5     Document Type: Review
Times cited : (129)

References (262)
  • 1
    • 0037450542 scopus 로고    scopus 로고
    • Assembly and overexpression of membrane proteins in Escherichia coli
    • Drew, D., Froderberg, L., Baars, L. and De Gier, J. W. (2003) Assembly and overexpression of membrane proteins in Escherichia coli. Biochim. Biophys. Acta 1610, 3-10.
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 3-10
    • Drew, D.1    Froderberg, L.2    Baars, L.3    De Gier, J.W.4
  • 2
    • 8844261812 scopus 로고    scopus 로고
    • Sec-translocase mediated membrane protein biogenesis
    • Dalbey, R. E. and Chen, M. (2004) Sec-translocase mediated membrane protein biogenesis. Biochim. Biophys. Acta 1694, 37-53.
    • (2004) Biochim. Biophys. Acta , vol.1694 , pp. 37-53
    • Dalbey, R.E.1    Chen, M.2
  • 3
    • 0037459073 scopus 로고    scopus 로고
    • Protein translocons: Multifunctional mediators of protein translocation across membranes
    • Schnell, D. J. and Hebert, D. N. (2003) Protein translocons: multifunctional mediators of protein translocation across membranes. Cell 112, 491-505.
    • (2003) Cell , vol.112 , pp. 491-505
    • Schnell, D.J.1    Hebert, D.N.2
  • 5
    • 8844231683 scopus 로고    scopus 로고
    • Membrane integration of E. coli model membrane proteins
    • Facey, S. J. and Kuhn, A. (2004) Membrane integration of E. coli model membrane proteins. Biochim. Biophys. Acta 1694, 55-66.
    • (2004) Biochim. Biophys. Acta , vol.1694 , pp. 55-66
    • Facey, S.J.1    Kuhn, A.2
  • 6
    • 0035099425 scopus 로고    scopus 로고
    • Strategies for prokaryotic expression of eukaryotic membrane proteins
    • Laage, R. and Langosch, D. (2001) Strategies for prokaryotic expression of eukaryotic membrane proteins. Traffic 2, 99-104.
    • (2001) Traffic , vol.2 , pp. 99-104
    • Laage, R.1    Langosch, D.2
  • 7
    • 0030271498 scopus 로고    scopus 로고
    • Errors of heterologous protein expression
    • Kurland, C. and Gallant, J. (1996) Errors of heterologous protein expression. Curr. Opin. Biotechnol. 7, 489-493.
    • (1996) Curr. Opin. Biotechnol , vol.7 , pp. 489-493
    • Kurland, C.1    Gallant, J.2
  • 8
    • 0037465682 scopus 로고    scopus 로고
    • Production of recombinant thermostable proteins expressed in Escherichia coli: Completion of protein synthesis is the bottleneck
    • Sorensen, H. P., Sperling-Petersen, H. U. and Mortensen, K. K. (2003) Production of recombinant thermostable proteins expressed in Escherichia coli: completion of protein synthesis is the bottleneck. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 786, 207-214.
    • (2003) J. Chromatogr. B Analyt. Technol. Biomed. Life Sci , vol.786 , pp. 207-214
    • Sorensen, H.P.1    Sperling-Petersen, H.U.2    Mortensen, K.K.3
  • 9
    • 19744376674 scopus 로고    scopus 로고
    • Global topology analysis of the Escherichia coli inner membrane proteome
    • Daley, D. O., Rapp, M., Granseth, E., Melen, K., Drew, D. and Von Heijne, G. (2005) Global topology analysis of the Escherichia coli inner membrane proteome. Science 308, 1321-1323.
    • (2005) Science , vol.308 , pp. 1321-1323
    • Daley, D.O.1    Rapp, M.2    Granseth, E.3    Melen, K.4    Drew, D.5    Von Heijne, G.6
  • 10
    • 0037450544 scopus 로고    scopus 로고
    • Specific lipid requirements of membrane proteins - a putative bottleneck in heterologous expression
    • Opekarova, M. and Tanner, W. (2003) Specific lipid requirements of membrane proteins - a putative bottleneck in heterologous expression. Biochim. Biophys. Acta 1610, 11-22.
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 11-22
    • Opekarova, M.1    Tanner, W.2
  • 11
    • 7044241302 scopus 로고    scopus 로고
    • How lipids affect the activities of integral membrane proteins
    • Lee, A. G. (2004) How lipids affect the activities of integral membrane proteins. Biochim. Biophys. Acta 1666, 62-87.
    • (2004) Biochim. Biophys. Acta , vol.1666 , pp. 62-87
    • Lee, A.G.1
  • 12
    • 27844436560 scopus 로고    scopus 로고
    • Specific protein-lipid interactions in membrane proteins
    • Hunte, C. (2005) Specific protein-lipid interactions in membrane proteins. Biochem. Soc. Trans. 33, 938-942.
    • (2005) Biochem. Soc. Trans , vol.33 , pp. 938-942
    • Hunte, C.1
  • 13
    • 33745860369 scopus 로고    scopus 로고
    • Phosphatidylethanolamine and monoglucosyldiacylglycerol are interchangeable in supporting topogenesis and function of the polytopic membrane protein lactose permease
    • Xie, J., Bogdanov, M., Heacock, P. and Dowhan, W. (2006) Phosphatidylethanolamine and monoglucosyldiacylglycerol are interchangeable in supporting topogenesis and function of the polytopic membrane protein lactose permease. J. Biol. Chem. 281, 19172-19178.
    • (2006) J. Biol. Chem , vol.281 , pp. 19172-19178
    • Xie, J.1    Bogdanov, M.2    Heacock, P.3    Dowhan, W.4
  • 14
    • 33646777423 scopus 로고    scopus 로고
    • Thematic review series: Lipid posttranslational modifications. CAAX modification and membrane targeting of Ras
    • Wright, L. P. and Philips, M. R. (2006) Thematic review series: lipid posttranslational modifications. CAAX modification and membrane targeting of Ras. J. Lipid Res. 47, 883-891.
    • (2006) J. Lipid Res , vol.47 , pp. 883-891
    • Wright, L.P.1    Philips, M.R.2
  • 15
    • 34548826770 scopus 로고    scopus 로고
    • Expression of recombinant G-protein coupled receptors for structural biology
    • Mancia, F. and Hendrickson, W. A. (2007) Expression of recombinant G-protein coupled receptors for structural biology. Mol. Biosyst. 3, 723-734.
    • (2007) Mol. Biosyst , vol.3 , pp. 723-734
    • Mancia, F.1    Hendrickson, W.A.2
  • 16
  • 17
    • 1642434197 scopus 로고    scopus 로고
    • Mimicking posttranslational modifications of proteins
    • Davis, B. G. (2004) Mimicking posttranslational modifications of proteins. Science 303, 480-482.
    • (2004) Science , vol.303 , pp. 480-482
    • Davis, B.G.1
  • 18
    • 0025367812 scopus 로고
    • Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: Implications for protein engineering
    • Gavel, Y. and Von Heijne, G. (1990) Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: implications for protein engineering. Protein Eng. 3, 433-442.
    • (1990) Protein Eng , vol.3 , pp. 433-442
    • Gavel, Y.1    Von Heijne, G.2
  • 19
    • 22844450442 scopus 로고    scopus 로고
    • Baculovirus as versatile vectors for protein expression in insect and mammalian cells
    • 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.
    • (2005) Nat. Biotechnol , vol.23 , pp. 567-575
    • Kost, T.A.1    Condreay, J.P.2    Jarvis, D.L.3
  • 20
    • 0005981053 scopus 로고    scopus 로고
    • Expression systems for production of heterologous proteins
    • Rai, M. and Padh, H. (2001) Expression systems for production of heterologous proteins. Curr. Sci. 80, 1121-1128.
    • (2001) Curr. Sci , vol.80 , pp. 1121-1128
    • Rai, M.1    Padh, H.2
  • 21
    • 0030700315 scopus 로고    scopus 로고
    • Baculovirus as expression vectors
    • Possee, R. D. (1997) Baculovirus as expression vectors. Curr. Opin. Biotechnol. 8, 569-572.
    • (1997) Curr. Opin. Biotechnol , vol.8 , pp. 569-572
    • Possee, R.D.1
  • 22
    • 0030298385 scopus 로고    scopus 로고
    • Heterologous expression of G-protein-coupled receptors
    • Tate, C. G. and Grisshammer, R. (1996) Heterologous expression of G-protein-coupled receptors. Trends Biotechnol. 14, 426-430.
    • (1996) Trends Biotechnol , vol.14 , pp. 426-430
    • Tate, C.G.1    Grisshammer, R.2
  • 23
    • 0037109074 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: High-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucosaminyl-transferase I-negative HEK293S stable mammalian cell line
    • Reeves, P. J., Callewaert, N., Contreras, R. and Khorana, H. G. (2002) Structure and function in rhodopsin: high-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucosaminyl-transferase I-negative HEK293S stable mammalian cell line. Proc. Natl. Acad. Sci. USA 99, 13419-13424.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 13419-13424
    • Reeves, P.J.1    Callewaert, N.2    Contreras, R.3    Khorana, H.G.4
  • 24
    • 22244478668 scopus 로고    scopus 로고
    • Design of improved membrane protein production experiments: Quantitation of the host response
    • Bonander, N., Hedfalk, K., Larsson, C., Mostad, P., Chang, C., Gustafsson, L. and Bill, R. M. (2005) Design of improved membrane protein production experiments: quantitation of the host response. Protein Sci. 14, 1729-1740.
    • (2005) Protein Sci , vol.14 , pp. 1729-1740
    • Bonander, N.1    Hedfalk, K.2    Larsson, C.3    Mostad, P.4    Chang, C.5    Gustafsson, L.6    Bill, R.M.7
  • 25
    • 0002650761 scopus 로고    scopus 로고
    • Cytoplasmic membranes
    • Neidhardt, F. C, ed, ASM Press, Washington DC
    • Kadner, R. J. (1996) Cytoplasmic membranes. In: Escherichia coli and Salmonella. Neidhardt, F. C. (ed.), ASM Press, Washington DC.
    • (1996) Escherichia coli and Salmonella
    • Kadner, R.J.1
  • 26
    • 33746813576 scopus 로고    scopus 로고
    • Understanding recombinant expression of membrane proteins
    • Grisshammer, R. (2006) Understanding recombinant expression of membrane proteins. Curr. Opin. Biotechnol. 17, 337-340.
    • (2006) Curr. Opin. Biotechnol , vol.17 , pp. 337-340
    • Grisshammer, R.1
  • 27
    • 0037450574 scopus 로고    scopus 로고
    • Practical aspects of overexpressing bacterial secondary membrane transporters for structural studies
    • Wang, D. N., Safferling, M., Lemieux, M. J., Griffith, H., Chen, Y. and Li, X. D. (2003) Practical aspects of overexpressing bacterial secondary membrane transporters for structural studies. Biochim. Biophys. Acta 1610, 23-36.
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 23-36
    • Wang, D.N.1    Safferling, M.2    Lemieux, M.J.3    Griffith, H.4    Chen, Y.5    Li, X.D.6
  • 28
    • 0030593468 scopus 로고    scopus 로고
    • Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • Miroux, B. and Walker, J. E. (1996) Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels. J. Mol. Biol. 260, 289-298.
    • (1996) J. Mol. Biol , vol.260 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 29
    • 0035984890 scopus 로고    scopus 로고
    • Functional reconstitution of purified metabotropic glutamate receptor expressed in the fly eye
    • 3, 491-496
    • Eroglu, C., Cronet, P., Panneels, V., Beaufils, P. and Sinning, I. (2002) Functional reconstitution of purified metabotropic glutamate receptor expressed in the fly eye. EMBO Rep. 3, 491-496.
    • (2002) EMBO Rep
    • Eroglu, C.1    Cronet, P.2    Panneels, V.3    Beaufils, P.4    Sinning, I.5
  • 30
    • 0036514182 scopus 로고    scopus 로고
    • Optimizing functional versus total expression of the human mu-opioid receptor in Pichia pastoris
    • Sarramegna, V., Demange, P., Milon, A. and Talmont, F. (2002) Optimizing functional versus total expression of the human mu-opioid receptor in Pichia pastoris. Protein Expr. Purif. 24, 212-220.
    • (2002) Protein Expr. Purif , vol.24 , pp. 212-220
    • Sarramegna, V.1    Demange, P.2    Milon, A.3    Talmont, F.4
  • 31
    • 33646155331 scopus 로고    scopus 로고
    • Enhancing functional production of G protein-coupled receptors in Pichia pastoris to levels required for structural studies via a single expression screen
    • Andre, N., Cherouati, N., Prual, C., Steffan, T., Zeder-Lutz, G., Magnin, T., Pattus, F., Michel, H., Wagner, R. and Reinhart, C. (2006) Enhancing functional production of G protein-coupled receptors in Pichia pastoris to levels required for structural studies via a single expression screen. Protein Sci. 15, 1115-1126.
    • (2006) Protein Sci , vol.15 , pp. 1115-1126
    • Andre, N.1    Cherouati, N.2    Prual, C.3    Steffan, T.4    Zeder-Lutz, G.5    Magnin, T.6    Pattus, F.7    Michel, H.8    Wagner, R.9    Reinhart, C.10
  • 32
    • 0033082145 scopus 로고    scopus 로고
    • Prokaryotic gene fusion expression systems and their use in structural and functional studies of proteins
    • Sheibani, N. (1999) Prokaryotic gene fusion expression systems and their use in structural and functional studies of proteins. Prep. Biochem. Biotechnol. 29, 77-90.
    • (1999) Prep. Biochem. Biotechnol , vol.29 , pp. 77-90
    • Sheibani, N.1
  • 33
    • 0035955445 scopus 로고    scopus 로고
    • Green fluorescent protein as an indicator to monitor membrane protein overexpression in Escherichia coli
    • Drew, D. E., Von Heijne, G., Nordlund, P. and De Gier, J. W. (2001) Green fluorescent protein as an indicator to monitor membrane protein overexpression in Escherichia coli. FEBS Lett. 507, 220-224.
    • (2001) FEBS Lett , vol.507 , pp. 220-224
    • Drew, D.E.1    Von Heijne, G.2    Nordlund, P.3    De Gier, J.W.4
  • 34
    • 33645454462 scopus 로고    scopus 로고
    • Drew, D., Lerch, M., Kunji, E., Slotboom, D. J. and De Gier, J. W. (2006) Optimization of membrane protein overexpression and purification using GFP fusions. Nat. Methods 3, 303-313.
    • Drew, D., Lerch, M., Kunji, E., Slotboom, D. J. and De Gier, J. W. (2006) Optimization of membrane protein overexpression and purification using GFP fusions. Nat. Methods 3, 303-313.
  • 35
    • 0032509329 scopus 로고    scopus 로고
    • High-level expression of soluble heterologous proteins in the cytoplasm of Escherichia coli by fusion to the bacteriophage lambda head protein D
    • Forrer, P. and Jaussi, R. (1998) High-level expression of soluble heterologous proteins in the cytoplasm of Escherichia coli by fusion to the bacteriophage lambda head protein D. Gene 224, 45-52.
    • (1998) Gene , vol.224 , pp. 45-52
    • Forrer, P.1    Jaussi, R.2
  • 36
    • 0035499892 scopus 로고    scopus 로고
    • Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 A resolution
    • Zhou, Y., Morais-Cabral, J. H., Kaufman, A. and Mackinnon, R. (2001) Chemistry of ion coordination and hydration revealed by a K+ channel-Fab complex at 2.0 A resolution. Nature 414, 43-48.
    • (2001) Nature , vol.414 , pp. 43-48
    • Zhou, Y.1    Morais-Cabral, J.H.2    Kaufman, A.3    Mackinnon, R.4
  • 37
    • 14544292475 scopus 로고    scopus 로고
    • NMR structure of Mistic, a membrane-integrating protein for membrane protein expression
    • Roosild, T. P., Greenwald, J., Vega, M., Castronovo, S., Riek, R. and Choe, S. (2005) NMR structure of Mistic, a membrane-integrating protein for membrane protein expression. Science 307, 1317-1321.
    • (2005) Science , vol.307 , pp. 1317-1321
    • Roosild, T.P.1    Greenwald, J.2    Vega, M.3    Castronovo, S.4    Riek, R.5    Choe, S.6
  • 38
    • 0032787876 scopus 로고    scopus 로고
    • Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused
    • Kapust, R. B. and Waugh, D. S. (1999) Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused. Protein Sci. 8, 1668-1674.
    • (1999) Protein Sci , vol.8 , pp. 1668-1674
    • Kapust, R.B.1    Waugh, D.S.2
  • 39
    • 33947171595 scopus 로고    scopus 로고
    • Preparative scale cell-free expression systems: New tools for the large scale preparation of integral membrane proteins for functional and structural studies
    • Schwarz, D., Klammt, C., Koglin, A., Lohr, F., Schneider, B., Dotsch, V. and Bernhard, F. (2007) Preparative scale cell-free expression systems: new tools for the large scale preparation of integral membrane proteins for functional and structural studies. Methods 41, 355-369.
    • (2007) Methods , vol.41 , pp. 355-369
    • Schwarz, D.1    Klammt, C.2    Koglin, A.3    Lohr, F.4    Schneider, B.5    Dotsch, V.6    Bernhard, F.7
  • 40
    • 0030743487 scopus 로고    scopus 로고
    • Characterization of d, k and m human opioid receptors overexpressed in baculovirus-infected insect cells
    • Massotte, D., Baroche, L., Simonin, F., Yu, L., Kieffer, B. and Pattus, F. (1997) Characterization of d, k and m human opioid receptors overexpressed in baculovirus-infected insect cells. J. Biol Chem. 272, 19987-19992.
    • (1997) J. Biol Chem , vol.272 , pp. 19987-19992
    • Massotte, D.1    Baroche, L.2    Simonin, F.3    Yu, L.4    Kieffer, B.5    Pattus, F.6
  • 41
    • 0032996996 scopus 로고    scopus 로고
    • Parameters influencing human m opioid receptor overexpression in baculovirus-infected insect cells
    • Massotte, D., Pereira, C. A., Pouliquen, Y. and Pattus, F. (1999) Parameters influencing human m opioid receptor overexpression in baculovirus-infected insect cells. J. Biotechnol. 69, 39-45.
    • (1999) J. Biotechnol , vol.69 , pp. 39-45
    • Massotte, D.1    Pereira, C.A.2    Pouliquen, Y.3    Pattus, F.4
  • 42
    • 0842288662 scopus 로고    scopus 로고
    • Membrane protein expression and production: Effects of polyhistidine tag length and position
    • Mohanty, A. K. and Wiener, M. C. (2004) Membrane protein expression and production: effects of polyhistidine tag length and position. Protein Expr. Purif. 33, 311-325.
    • (2004) Protein Expr. Purif , vol.33 , pp. 311-325
    • Mohanty, A.K.1    Wiener, M.C.2
  • 43
    • 0041876269 scopus 로고    scopus 로고
    • Heterologous expression of G-protein-coupled receptors: Comparison of expression systems fron the standpoint of large-scale production and purification
    • Sarramegna, V., Talmont, F., Demange, P. and Milon, A. (2003) Heterologous expression of G-protein-coupled receptors: comparison of expression systems fron the standpoint of large-scale production and purification. Cell. Mol. Life Sci. 60, 1529-1546.
    • (2003) Cell. Mol. Life Sci , vol.60 , pp. 1529-1546
    • Sarramegna, V.1    Talmont, F.2    Demange, P.3    Milon, A.4
  • 44
    • 0021856417 scopus 로고
    • Signal sequences. The limits of variation
    • Von Heijne, G. (1985) Signal sequences. The limits of variation. J. Mol. Biol. 184, 99-105.
    • (1985) J. Mol. Biol , vol.184 , pp. 99-105
    • Von Heijne, G.1
  • 45
    • 0029857118 scopus 로고    scopus 로고
    • In vivo reconstitution of dopamine D2S receptor-mediated G protein activation in baculovirus-infected insect cells: Preferred coupling to Gi1 versus Gi2
    • Grünewald, S., Reilander, H. and Michel, H. (1996) In vivo reconstitution of dopamine D2S receptor-mediated G protein activation in baculovirus-infected insect cells: preferred coupling to Gi1 versus Gi2. Biochemistry 35, 15162-15173.
    • (1996) Biochemistry , vol.35 , pp. 15162-15173
    • Grünewald, S.1    Reilander, H.2    Michel, H.3
  • 47
    • 0026564303 scopus 로고
    • Enhancement of membrane insertion and function in a type IIIb membrane protein following introduction of a cleavable signal peptide
    • Guan, X. M., Kobilka, T. S. and Kobilka, B. K. (1992) Enhancement of membrane insertion and function in a type IIIb membrane protein following introduction of a cleavable signal peptide. J. Biol. Chem. 267, 21995-21998.
    • (1992) J. Biol. Chem , vol.267 , pp. 21995-21998
    • Guan, X.M.1    Kobilka, T.S.2    Kobilka, B.K.3
  • 48
    • 7044272757 scopus 로고    scopus 로고
    • Membrane proteins, lipids and detergents: Not just a soap opera
    • Seddon, A. M., Curnow, P. and Booth, P. J. (2004) Membrane proteins, lipids and detergents: not just a soap opera. Biochim. Biophys. Acta 1666, 105-117.
    • (2004) Biochim. Biophys. Acta , vol.1666 , pp. 105-117
    • Seddon, A.M.1    Curnow, P.2    Booth, P.J.3
  • 49
    • 0348003908 scopus 로고    scopus 로고
    • Comparison of seven different heterologous protein expression systems for the production of the serotonin transporter
    • Tate, C. G., Haase, J., Baker, C., Boorsma, M., Magnani, F., Vallis, Y. and Williams, D. C. (2003) Comparison of seven different heterologous protein expression systems for the production of the serotonin transporter. Biochim. Biophys. Acta 1610, 141-153.
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 141-153
    • Tate, C.G.1    Haase, J.2    Baker, C.3    Boorsma, M.4    Magnani, F.5    Vallis, Y.6    Williams, D.C.7
  • 50
    • 0032521005 scopus 로고    scopus 로고
    • Comparative biochemical and pharmacological characterization of the mouse 5HT5A 5-hydroxytryptamine receptor and the human beta2-adrenergic receptor produced in the methylotrophic yeast Pichia pastoris
    • Weiss, H. M., Haase, W., Michel, H. and Reilander, H. (1998) Comparative biochemical and pharmacological characterization of the mouse 5HT5A 5-hydroxytryptamine receptor and the human beta2-adrenergic receptor produced in the methylotrophic yeast Pichia pastoris. Biochem. J. 330 ( Pt 3), 1137-1147.
    • (1998) Biochem. J , vol.330 , Issue.PART 3 , pp. 1137-1147
    • Weiss, H.M.1    Haase, W.2    Michel, H.3    Reilander, H.4
  • 52
    • 0037337308 scopus 로고    scopus 로고
    • The application of mass spectrometry to membrane proteomics
    • Wu, C. C. and Yates, J. R., 3rd (2003) The application of mass spectrometry to membrane proteomics. Nat. Biotechnol. 21, 262-267.
    • (2003) Nat. Biotechnol , vol.21 , pp. 262-267
    • Wu, C.C.1    Yates 3rd, J.R.2
  • 53
    • 34447643582 scopus 로고    scopus 로고
    • A novel approach to analyze membrane proteins by laser mass spectrometry: From protein subunits to the integral complex
    • Morgner, N., Kleinschroth, T., Barth, H. D., Ludwig, B. and Brutschy, B. (2007) A novel approach to analyze membrane proteins by laser mass spectrometry: from protein subunits to the integral complex. J. Am. Soc. Mass Spectrom. 18, 1429-1438.
    • (2007) J. Am. Soc. Mass Spectrom , vol.18 , pp. 1429-1438
    • Morgner, N.1    Kleinschroth, T.2    Barth, H.D.3    Ludwig, B.4    Brutschy, B.5
  • 55
    • 15544386013 scopus 로고    scopus 로고
    • Size determination of cyanobacterial and higher plant photosystem II by gel permeation chromatography, light scattering, and ultracentrifugation
    • Zouni, A., Kern, J., Frank, J., Hellweg, T., Behlke, J., Saenger, W. and Irrgang, K. D. (2005) Size determination of cyanobacterial and higher plant photosystem II by gel permeation chromatography, light scattering, and ultracentrifugation. Biochemistry 44, 4572-4581.
    • (2005) Biochemistry , vol.44 , pp. 4572-4581
    • Zouni, A.1    Kern, J.2    Frank, J.3    Hellweg, T.4    Behlke, J.5    Saenger, W.6    Irrgang, K.D.7
  • 56
    • 34250350252 scopus 로고    scopus 로고
    • High-level expression in Saccharomyces cerevisiae enables isolation and spectroscopic characterization of functional human adenosine A2a receptor
    • O'Malley, M. A., Lazarova, T., Britton, Z. T. and Robinson, A. S. (2007) High-level expression in Saccharomyces cerevisiae enables isolation and spectroscopic characterization of functional human adenosine A2a receptor. J. Struct. Biol. 159, 166-178.
    • (2007) J. Struct. Biol , vol.159 , pp. 166-178
    • O'Malley, M.A.1    Lazarova, T.2    Britton, Z.T.3    Robinson, A.S.4
  • 57
    • 85164050680 scopus 로고    scopus 로고
    • Koglin, A., Klammt, C., Trbovic, N., Schwarz, D., Schneider, B., Schafer, B., Lohr, F., Bernhard, F. and Dotsch, V. (2006) Combination of cell-free expression and NMR spectroscopy as a new approach for structural investigation of membrane proteins. Magn. Reson. Chem. 44 Spec. No., S17-23.
    • Koglin, A., Klammt, C., Trbovic, N., Schwarz, D., Schneider, B., Schafer, B., Lohr, F., Bernhard, F. and Dotsch, V. (2006) Combination of cell-free expression and NMR spectroscopy as a new approach for structural investigation of membrane proteins. Magn. Reson. Chem. 44 Spec. No., S17-23.
  • 58
    • 33750378958 scopus 로고    scopus 로고
    • Wittig, I., Braun, H. P. and Schagger, H. (2006) Blue native PAGE. Nat. Protoc. 1, 418-428.
    • Wittig, I., Braun, H. P. and Schagger, H. (2006) Blue native PAGE. Nat. Protoc. 1, 418-428.
  • 60
    • 34447277172 scopus 로고    scopus 로고
    • Yeast mitochondrial ADP/ATP carriers are monomeric in detergents as demonstrated by differential affinity purification
    • Bamber, L., Slotboom, D. J. and Kunji, E. R. (2007) Yeast mitochondrial ADP/ATP carriers are monomeric in detergents as demonstrated by differential affinity purification. J. Mol. Biol. 371, 388-395.
    • (2007) J. Mol. Biol , vol.371 , pp. 388-395
    • Bamber, L.1    Slotboom, D.J.2    Kunji, E.R.3
  • 65
    • 0742270983 scopus 로고    scopus 로고
    • FRET between cardiac Na+ channel subunits measured with a confocal microscope and a streak camera
    • Biskup, C., Zimmer, T. and Benndorf, K. (2004) FRET between cardiac Na+ channel subunits measured with a confocal microscope and a streak camera. Nat. Biotechnol. 22, 220-224.
    • (2004) Nat. Biotechnol , vol.22 , pp. 220-224
    • Biskup, C.1    Zimmer, T.2    Benndorf, K.3
  • 66
    • 34848912009 scopus 로고    scopus 로고
    • Live cell FRET microscopy: Homo- and heterodimerization of two human peroxisomal ABC transporters, the adrenoleukodystrophy protein (ALDP, ABCD1) and PMP70 (ABCD3)
    • Hillebrand, M., Verrier, S. E., Ohlenbusch, A., Schafer, A., Soling, H. D., Wouters, F. S. and Gartner, J. (2007) Live cell FRET microscopy: homo- and heterodimerization of two human peroxisomal ABC transporters, the adrenoleukodystrophy protein (ALDP, ABCD1) and PMP70 (ABCD3). J. Biol. Chem. 282, 26997-27005.
    • (2007) J. Biol. Chem , vol.282 , pp. 26997-27005
    • Hillebrand, M.1    Verrier, S.E.2    Ohlenbusch, A.3    Schafer, A.4    Soling, H.D.5    Wouters, F.S.6    Gartner, J.7
  • 67
    • 0019321479 scopus 로고
    • Purification of acetylcholine receptors, reconstitution into lipid vesicles, and study of agonist-induced cation channel regulation
    • Lindstrom, J., Anholt, R., Einarson, B., Engel, A., Osame, M. and Montal, M. (1980) Purification of acetylcholine receptors, reconstitution into lipid vesicles, and study of agonist-induced cation channel regulation. J. Biol. Chem. 255, 8340-8350.
    • (1980) J. Biol. Chem , vol.255 , pp. 8340-8350
    • Lindstrom, J.1    Anholt, R.2    Einarson, B.3    Engel, A.4    Osame, M.5    Montal, M.6
  • 68
    • 24344479129 scopus 로고    scopus 로고
    • Kinetics of charge translocation in the passive downhill uptake mode of the Na+/H+ antiporter NhaA of Escherichia coli
    • Zuber, D., Krause, R., Venturi, M., Padan, E., Bamberg, E. and Fendler, K. (2005) Kinetics of charge translocation in the passive downhill uptake mode of the Na+/H+ antiporter NhaA of Escherichia coli. Biochim. Biophys. Acta 1709, 240-250.
    • (2005) Biochim. Biophys. Acta , vol.1709 , pp. 240-250
    • Zuber, D.1    Krause, R.2    Venturi, M.3    Padan, E.4    Bamberg, E.5    Fendler, K.6
  • 70
    • 0025346254 scopus 로고
    • Transmembrane protein structure: Spin labeling of bacteriorhodopsin mutants
    • Altenbach, C., Marti, T., Khorana, H. G. and Hubbell, W. L. (1990) Transmembrane protein structure: spin labeling of bacteriorhodopsin mutants. Science 248, 1088-1092.
    • (1990) Science , vol.248 , pp. 1088-1092
    • Altenbach, C.1    Marti, T.2    Khorana, H.G.3    Hubbell, W.L.4
  • 71
    • 0034614422 scopus 로고    scopus 로고
    • Cysteine scanning mutagenesis of the noncatalytic nucleotide binding site of the yeast V-ATPase
    • Vasilyeva, E., Liu, Q., Macleod, K. J., Baleja, J. D. and Forgac, M. (2000) Cysteine scanning mutagenesis of the noncatalytic nucleotide binding site of the yeast V-ATPase. J. Biol. Chem. 275, 255-260.
    • (2000) J. Biol. Chem , vol.275 , pp. 255-260
    • Vasilyeva, E.1    Liu, Q.2    Macleod, K.J.3    Baleja, J.D.4    Forgac, M.5
  • 72
    • 34447630299 scopus 로고    scopus 로고
    • Functional cell-free synthesis of a seven helix membrane protein: In situ insertion of bacteriorhodopsin into liposomes
    • Kalmbach, R., Chizhov, I., Schumacher, M. C., Friedrich, T., Bamberg, E. and Engelhard, M. (2007) Functional cell-free synthesis of a seven helix membrane protein: in situ insertion of bacteriorhodopsin into liposomes. J. Mol. Biol. 371, 639-648.
    • (2007) J. Mol. Biol , vol.371 , pp. 639-648
    • Kalmbach, R.1    Chizhov, I.2    Schumacher, M.C.3    Friedrich, T.4    Bamberg, E.5    Engelhard, M.6
  • 73
    • 0016376296 scopus 로고
    • Planar lipid bilayer membranes
    • Andreoli, T. E. (1974) Planar lipid bilayer membranes. Methods Enzymol. 32, 513-539.
    • (1974) Methods Enzymol , vol.32 , pp. 513-539
    • Andreoli, T.E.1
  • 75
    • 0032461892 scopus 로고    scopus 로고
    • Spectroscopic and biophysical approaches for studying the structure and function of the P-glycoprotein multidrug transporter
    • Sharom, F. J., Liu, R. and Romsicki, Y. (1998) Spectroscopic and biophysical approaches for studying the structure and function of the P-glycoprotein multidrug transporter. Biochem. Cell. Biol. 76, 695-708.
    • (1998) Biochem. Cell. Biol , vol.76 , pp. 695-708
    • Sharom, F.J.1    Liu, R.2    Romsicki, Y.3
  • 76
    • 0345035518 scopus 로고    scopus 로고
    • The secondary multidrug transporter LmrP contains multiple drug interaction sites
    • Putman, M., Koole, L. A., Van Veen, H. W. and Konings, W. N. (1999) The secondary multidrug transporter LmrP contains multiple drug interaction sites. Biochemistry 38, 13900-13905.
    • (1999) Biochemistry , vol.38 , pp. 13900-13905
    • Putman, M.1    Koole, L.A.2    Van Veen, H.W.3    Konings, W.N.4
  • 77
    • 0026738801 scopus 로고
    • Patch clamp techniques: An overview
    • Cahalan, M. and Neher, E. (1992) Patch clamp techniques: an overview. Methods Enzymol. 207, 3-14.
    • (1992) Methods Enzymol , vol.207 , pp. 3-14
    • Cahalan, M.1    Neher, E.2
  • 79
    • 34247893770 scopus 로고    scopus 로고
    • Structural genomics and drug discovery
    • Lundstrom, K. (2007) Structural genomics and drug discovery. J. Cell. Mol. Med. 11, 224-238.
    • (2007) J. Cell. Mol. Med , vol.11 , pp. 224-238
    • Lundstrom, K.1
  • 80
    • 0037450575 scopus 로고    scopus 로고
    • Lactococcus lactis as host for overproduction of functional membrane proteins
    • Kunji, E. R., Slotboom, D. J. and Poolman, B. (2003) Lactococcus lactis as host for overproduction of functional membrane proteins. Biochim. Biophys. Acta 1610, 97-108.
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 97-108
    • Kunji, E.R.1    Slotboom, D.J.2    Poolman, B.3
  • 81
    • 34347391677 scopus 로고    scopus 로고
    • Functional analysis of cell-free-produced human endothelin B receptor reveals transmembrane segment 1 as an essential area for ET-1 binding and homodimer formation
    • Klammt, C., Srivastava, A., Eifler, N., Junge, F., Beyermann, M., Schwarz, D., Michel, H., Doetsch, V. and Bernhard, F. (2007) Functional analysis of cell-free-produced human endothelin B receptor reveals transmembrane segment 1 as an essential area for ET-1 binding and homodimer formation. FEBS J. 274, 3257-3269.
    • (2007) FEBS J , vol.274 , pp. 3257-3269
    • Klammt, C.1    Srivastava, A.2    Eifler, N.3    Junge, F.4    Beyermann, M.5    Schwarz, D.6    Michel, H.7    Doetsch, V.8    Bernhard, F.9
  • 82
    • 33749238054 scopus 로고    scopus 로고
    • Direct analysis of a GPCR-agonist interaction by surface plasmon resonance
    • Harding, P. J., Hadingham, T. C., Mcdonnell, J. M. and Watts, A. (2006) Direct analysis of a GPCR-agonist interaction by surface plasmon resonance. Eur. Biophys. J. 35, 709-712.
    • (2006) Eur. Biophys. J , vol.35 , pp. 709-712
    • Harding, P.J.1    Hadingham, T.C.2    Mcdonnell, J.M.3    Watts, A.4
  • 84
    • 34250636733 scopus 로고    scopus 로고
    • Purification of human beta2-adrenergic receptor expressed in methylotrophic yeast Pichia pastoris
    • Noguchi, S. and Satow, Y. (2006) Purification of human beta2-adrenergic receptor expressed in methylotrophic yeast Pichia pastoris. J. Biochem. 140, 799-804.
    • (2006) J. Biochem , vol.140 , pp. 799-804
    • Noguchi, S.1    Satow, Y.2
  • 85
    • 12244292640 scopus 로고    scopus 로고
    • Purification and characterization of the human adenosine A(2a) receptor functionally expressed in Escherichia coli
    • Weiss, H. M. and Grisshammer, R. (2002) Purification and characterization of the human adenosine A(2a) receptor functionally expressed in Escherichia coli. Eur. J. Biochem. 269, 82-92.
    • (2002) Eur. J. Biochem , vol.269 , pp. 82-92
    • Weiss, H.M.1    Grisshammer, R.2
  • 87
    • 33750218146 scopus 로고    scopus 로고
    • Evidence for transmembrane proton transfer in a dihaem-containing membrane protein complex
    • Madej, M. G., Nasiri, H. R., Hilgendorff, N. S., Schwalbe, H. and Lancaster, C. R. (2006) Evidence for transmembrane proton transfer in a dihaem-containing membrane protein complex. EMBO J. 25, 4963-4970.
    • (2006) EMBO J , vol.25 , pp. 4963-4970
    • Madej, M.G.1    Nasiri, H.R.2    Hilgendorff, N.S.3    Schwalbe, H.4    Lancaster, C.R.5
  • 88
    • 0037040613 scopus 로고    scopus 로고
    • Molecular basis of proton motive force generation: Structure of formate dehydrogenase-N
    • Jormakka, M., Tornroth, S., Byrne, B. and Iwata, S. (2002) Molecular basis of proton motive force generation: structure of formate dehydrogenase-N. Science 295, 1863-1868.
    • (2002) Science , vol.295 , pp. 1863-1868
    • Jormakka, M.1    Tornroth, S.2    Byrne, B.3    Iwata, S.4
  • 90
    • 4344581120 scopus 로고    scopus 로고
    • The retinal conformation and its environment in rhodopsin in light of a new 2.2 A crystal structure
    • Okada, T., Sugihara, M., Bondar, A. N., Elstner, M., Entel, P. and Buss, V. (2004) The retinal conformation and its environment in rhodopsin in light of a new 2.2 A crystal structure. J. Mol. Biol. 342, 571-583.
    • (2004) J. Mol. Biol , vol.342 , pp. 571-583
    • Okada, T.1    Sugihara, M.2    Bondar, A.N.3    Elstner, M.4    Entel, P.5    Buss, V.6
  • 91
    • 9244232176 scopus 로고    scopus 로고
    • Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues
    • Toyoshima, C., Nomura, H. and Tsuda, T. (2004) Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues. Nature 432, 361-368.
    • (2004) Nature , vol.432 , pp. 361-368
    • Toyoshima, C.1    Nomura, H.2    Tsuda, T.3
  • 93
    • 0035979744 scopus 로고    scopus 로고
    • A refined structure of human aquaporin-1
    • De Groot, B. L., Engel, A. and Grubmuller, H. (2001) A refined structure of human aquaporin-1. FEBS Lett. 504, 206-211.
    • (2001) FEBS Lett , vol.504 , pp. 206-211
    • De Groot, B.L.1    Engel, A.2    Grubmuller, H.3
  • 94
    • 0034717007 scopus 로고    scopus 로고
    • Structure of the light-driven chloride pump halorhodopsin at 1.8 A resolution
    • Kolbe, M., Besir, H., Essen, L. O. and Oesterhelt, D. (2000) Structure of the light-driven chloride pump halorhodopsin at 1.8 A resolution. Science 288, 1390-1396.
    • (2000) Science , vol.288 , pp. 1390-1396
    • Kolbe, M.1    Besir, H.2    Essen, L.O.3    Oesterhelt, D.4
  • 97
    • 34648833810 scopus 로고    scopus 로고
    • Structure of the zinc transporter YiiP
    • Lu, M. and Fu, D. (2007) Structure of the zinc transporter YiiP. Science 317, 1746-1748.
    • (2007) Science , vol.317 , pp. 1746-1748
    • Lu, M.1    Fu, D.2
  • 98
    • 0037052565 scopus 로고    scopus 로고
    • The E. coli BtuCD structure: A framework for ABC transporter architecture and mechanism
    • Locher, K. P., Lee, A. T. and Rees, D. C. (2002) The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism. Science 296, 1091-1098.
    • (2002) Science , vol.296 , pp. 1091-1098
    • Locher, K.P.1    Lee, A.T.2    Rees, D.C.3
  • 99
    • 33646445156 scopus 로고    scopus 로고
    • Structure of the multidrug transporter EmrD from Escherichia coli
    • Yin, Y., He, X., Szewczyk, P., Nguyen, T. and Chang, G. (2006) Structure of the multidrug transporter EmrD from Escherichia coli. Science 312, 741-744.
    • (2006) Science , vol.312 , pp. 741-744
    • Yin, Y.1    He, X.2    Szewczyk, P.3    Nguyen, T.4    Chang, G.5
  • 100
    • 33747623998 scopus 로고    scopus 로고
    • Structure of the monomeric outer-membrane porin OmpG in the open and closed conformation
    • Yildiz, O., Vinothkumar, K. R., Goswami, P. and Kuhlbrandt, W. (2006) Structure of the monomeric outer-membrane porin OmpG in the open and closed conformation. EMBO J. 25, 3702-3713.
    • (2006) EMBO J , vol.25 , pp. 3702-3713
    • Yildiz, O.1    Vinothkumar, K.R.2    Goswami, P.3    Kuhlbrandt, W.4
  • 102
    • 27244444582 scopus 로고    scopus 로고
    • Crystal structure of the archaeal ammonium transporter Amt-1 from Archaeoglobus fulgidus
    • Andrade, S. L., Dickmanns, A., Ficner, R. and Einsle, O. (2005) Crystal structure of the archaeal ammonium transporter Amt-1 from Archaeoglobus fulgidus. Proc. Natl. Acad. Sci. USA 102, 14994-14999.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 14994-14999
    • Andrade, S.L.1    Dickmanns, A.2    Ficner, R.3    Einsle, O.4
  • 103
    • 24644470065 scopus 로고    scopus 로고
    • Crystal structure of a bacterial homologue of Na+/ Cl-dependent neurotransmitter transporters
    • Yamashita, A., Singh, S. K., Kawate, T., Jin, Y. and Gouaux, E. (2005) Crystal structure of a bacterial homologue of Na+/ Cl-dependent neurotransmitter transporters. Nature 437, 215-223.
    • (2005) Nature , vol.437 , pp. 215-223
    • Yamashita, A.1    Singh, S.K.2    Kawate, T.3    Jin, Y.4    Gouaux, E.5
  • 104
    • 33846505059 scopus 로고    scopus 로고
    • Coupling substrate and ion binding to extracellular gate of a sodium-dependent aspartate transporter
    • Boudker, O., Ryan, R. M., Yernool, D., Shimamoto, K. and Gouaux, E. (2007) Coupling substrate and ion binding to extracellular gate of a sodium-dependent aspartate transporter. Nature 445, 387-393.
    • (2007) Nature , vol.445 , pp. 387-393
    • Boudker, O.1    Ryan, R.M.2    Yernool, D.3    Shimamoto, K.4    Gouaux, E.5
  • 105
    • 33748644877 scopus 로고    scopus 로고
    • Structure of a bacterial multidrug ABC transporter
    • Dawson, R. J. and Locher, K. P. (2006) Structure of a bacterial multidrug ABC transporter. Nature 443, 180-185.
    • (2006) Nature , vol.443 , pp. 180-185
    • Dawson, R.J.1    Locher, K.P.2
  • 111
    • 34547631962 scopus 로고    scopus 로고
    • Crystal structure of a human membrane protein involved in cysteinyl leukotriene biosynthesis
    • Ago, H., Kanaoka, Y., Irikura, D., Lam, B. K., Shimamura, T., Austen, K. F. and Miyano, M. (2007) Crystal structure of a human membrane protein involved in cysteinyl leukotriene biosynthesis. Nature 448, 609-612.
    • (2007) Nature , vol.448 , pp. 609-612
    • Ago, H.1    Kanaoka, Y.2    Irikura, D.3    Lam, B.K.4    Shimamura, T.5    Austen, K.F.6    Miyano, M.7
  • 114
    • 36148942092 scopus 로고    scopus 로고
    • Breaking the bottleneck: Eukaryotic membrane protein expression for high-resolution structural studies
    • Midgett, C. R. and Madden, D. R. (2007) Breaking the bottleneck: eukaryotic membrane protein expression for high-resolution structural studies. J. Struct. Biol. 160, 265-274.
    • (2007) J. Struct. Biol , vol.160 , pp. 265-274
    • Midgett, C.R.1    Madden, D.R.2
  • 116
    • 33947172767 scopus 로고    scopus 로고
    • Detergents for the stabilization and crystallization of membrane proteins
    • Prive, G. G. (2007) Detergents for the stabilization and crystallization of membrane proteins. Methods 41, 388-397.
    • (2007) Methods , vol.41 , pp. 388-397
    • Prive, G.G.1
  • 117
    • 7244254186 scopus 로고    scopus 로고
    • Structure of a glutamate transporter homologue from Pyrococcus horikoshii
    • Yernool, D., Boudker, O., Jin, Y. and Gouaux, E. (2004) Structure of a glutamate transporter homologue from Pyrococcus horikoshii. Nature 431, 811-818.
    • (2004) Nature , vol.431 , pp. 811-818
    • Yernool, D.1    Boudker, O.2    Jin, Y.3    Gouaux, E.4
  • 118
    • 36048971123 scopus 로고    scopus 로고
    • Structure of outer membrane protein G by solution NMR spectroscopy
    • Liang, B. and Tamm, L. K. (2007) Structure of outer membrane protein G by solution NMR spectroscopy. Proc. Natl. Acad. Sci. USA 104, 16140-16145.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 16140-16145
    • Liang, B.1    Tamm, L.K.2
  • 120
    • 0036301007 scopus 로고    scopus 로고
    • Bicelle crystallization: A new method for crystallizing membrane proteins yields a monomeric bacteriorhodopsin structure
    • Faham, S. and Bowie, J. U. (2002) Bicelle crystallization: a new method for crystallizing membrane proteins yields a monomeric bacteriorhodopsin structure. J. Mol. Biol. 316, 1-6.
    • (2002) J. Mol. Biol , vol.316 , pp. 1-6
    • Faham, S.1    Bowie, J.U.2
  • 121
    • 36849088540 scopus 로고    scopus 로고
    • Solution NMR of membrane proteins in bilayer mimics: Small is beautiful, but sometimes bigger is better
    • Poget, S. F. and Girvin, M. E. (2007) Solution NMR of membrane proteins in bilayer mimics: small is beautiful, but sometimes bigger is better. Biochim. Biophys. Acta 1768, 3098-3106.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 3098-3106
    • Poget, S.F.1    Girvin, M.E.2
  • 122
    • 0037450548 scopus 로고    scopus 로고
    • The expression of outer membrane proteins for crystallization
    • Bannwarth, M. and Schulz, G. E. (2003) The expression of outer membrane proteins for crystallization. Biochim. Biophys. Acta 1610, 37-45.
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 37-45
    • Bannwarth, M.1    Schulz, G.E.2
  • 123
    • 0036667741 scopus 로고    scopus 로고
    • Crystallisation of membrane proteins mediated by antibody fragments
    • Hunte, C. and Michel, H. (2002) Crystallisation of membrane proteins mediated by antibody fragments. Curr. Opin. Struct. Biol. 12, 503-508.
    • (2002) Curr. Opin. Struct. Biol , vol.12 , pp. 503-508
    • Hunte, C.1    Michel, H.2
  • 126
    • 0035943457 scopus 로고    scopus 로고
    • Crystal structure of sensory rhodopsin II at 2.4 angstroms: Insights into color tuning and transducer interaction
    • Luecke, H., Schobert, B., Lanyi, J. K., Spudich, E. N. and Spudich, J. L. (2001) Crystal structure of sensory rhodopsin II at 2.4 angstroms: insights into color tuning and transducer interaction. Science 293, 1499-1503.
    • (2001) Science , vol.293 , pp. 1499-1503
    • Luecke, H.1    Schobert, B.2    Lanyi, J.K.3    Spudich, E.N.4    Spudich, J.L.5
  • 127
    • 0034831591 scopus 로고    scopus 로고
    • A third crystal form of Wolinella succinogenes quinol:fumarate reductase reveals domain closure at the site of fumarate reduction
    • Lancaster, C. R., Gross, R. and Simon, J. (2001) A third crystal form of Wolinella succinogenes quinol:fumarate reductase reveals domain closure at the site of fumarate reduction. Eur. J. Biochem. 268, 1820-1827.
    • (2001) Eur. J. Biochem , vol.268 , pp. 1820-1827
    • Lancaster, C.R.1    Gross, R.2    Simon, J.3
  • 128
    • 0344497439 scopus 로고    scopus 로고
    • An atypical haem in the cytochrome b(6)f complex
    • Stroebel, D., Choquet, Y., Popot, J. L. and Picot, D. (2003) An atypical haem in the cytochrome b(6)f complex. Nature 426, 413-418.
    • (2003) Nature , vol.426 , pp. 413-418
    • Stroebel, D.1    Choquet, Y.2    Popot, J.L.3    Picot, D.4
  • 129
    • 11144222920 scopus 로고    scopus 로고
    • Crystal structure of the drug discharge outer membrane protein, OprM, of Pseudomonas aeruginosa: Dual modes of membrane anchoring and occluded cavity end
    • Akama, H., Kanemaki, M., Yoshimura, M., Tsukihara, T., Kashiwagi, T., Yoneyama, H., Narita, S., Nakagawa, A. and Nakae, T. (2004) Crystal structure of the drug discharge outer membrane protein, OprM, of Pseudomonas aeruginosa: dual modes of membrane anchoring and occluded cavity end. J. Biol. Chem. 279, 52816-52819.
    • (2004) J. Biol. Chem , vol.279 , pp. 52816-52819
    • Akama, H.1    Kanemaki, M.2    Yoshimura, M.3    Tsukihara, T.4    Kashiwagi, T.5    Yoneyama, H.6    Narita, S.7    Nakagawa, A.8    Nakae, T.9
  • 130
    • 4043152888 scopus 로고    scopus 로고
    • X-ray structure of Rhodobacter capsulatus cytochrome bc (1): Comparison with its mitochondrial and chloroplast counterparts
    • Berry, E. A., Huang, L. S., Saechao, L. K., Pon, N. G., Valkova-Valchanova, M. and Daldal, F. (2004) X-ray structure of Rhodobacter capsulatus cytochrome bc (1): comparison with its mitochondrial and chloroplast counterparts. Photosynth. Res. 81, 251-275.
    • (2004) Photosynth. Res , vol.81 , pp. 251-275
    • Berry, E.A.1    Huang, L.S.2    Saechao, L.K.3    Pon, N.G.4    Valkova-Valchanova, M.5    Daldal, F.6
  • 131
    • 1842502604 scopus 로고    scopus 로고
    • X-Ray structure determination of three mutants of the bacterial photosynthetic reaction centers from Rb. sphaeroides; altered proton transfer pathways
    • Xu, Q., Axelrod, H. L., Abresch, E. C., Paddock, M. L., Okamura, M. Y. and Feher, G. (2004) X-Ray structure determination of three mutants of the bacterial photosynthetic reaction centers from Rb. sphaeroides; altered proton transfer pathways. Structure 12, 703-715.
    • (2004) Structure , vol.12 , pp. 703-715
    • Xu, Q.1    Axelrod, H.L.2    Abresch, E.C.3    Paddock, M.L.4    Okamura, M.Y.5    Feher, G.6
  • 132
    • 24044442616 scopus 로고    scopus 로고
    • A novel cryoprotection scheme for enhancing the diffraction of crystals of recombinant cytochrome ba3 oxidase from Thermus thermophilus
    • Hunsicker-Wang, L. M., Pacoma, R. L., Chen, Y., Fee, J. A. and Stout, C. D. (2005) A novel cryoprotection scheme for enhancing the diffraction of crystals of recombinant cytochrome ba3 oxidase from Thermus thermophilus. Acta Crystallogr. D Biol. Crystallogr. 61, 340-343.
    • (2005) Acta Crystallogr. D Biol. Crystallogr , vol.61 , pp. 340-343
    • Hunsicker-Wang, L.M.1    Pacoma, R.L.2    Chen, Y.3    Fee, J.A.4    Stout, C.D.5
  • 133
    • 29244487014 scopus 로고    scopus 로고
    • Experimental support for the 'E pathway hypothesis' of coupled transmembrane e- and H+ transfer in dihemic quinol:fumarate reductase
    • Lancaster, C. R., Sauer, U. S., Gross, R., Haas, A. H., Graf, J., Schwalbe, H., Mantele, W., Simon, J. and Madej, M. G. (2005) Experimental support for the 'E pathway hypothesis' of coupled transmembrane e- and H+ transfer in dihemic quinol:fumarate reductase. Proc. Natl. Acad. Sci. USA 102, 18860-18865.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 18860-18865
    • Lancaster, C.R.1    Sauer, U.S.2    Gross, R.3    Haas, A.H.4    Graf, J.5    Schwalbe, H.6    Mantele, W.7    Simon, J.8    Madej, M.G.9
  • 134
    • 0031985785 scopus 로고    scopus 로고
    • Structure of the sucrose-specific porin ScrY from Salmonella typhimurium and its complex with sucrose
    • Forst, D., Welte, W., Wacker, T. and Diederichs, K. (1998) Structure of the sucrose-specific porin ScrY from Salmonella typhimurium and its complex with sucrose. Nat. Struct. Biol. 5, 37-46.
    • (1998) Nat. Struct. Biol , vol.5 , pp. 37-46
    • Forst, D.1    Welte, W.2    Wacker, T.3    Diederichs, K.4
  • 135
    • 10644255526 scopus 로고    scopus 로고
    • Advanced genetic strategies for recombinant protein expression in Escherichia coli
    • Sorensen, H. P. and Mortensen, K. K. (2005) Advanced genetic strategies for recombinant protein expression in Escherichia coli. J. Biotechnol. 115, 113-128.
    • (2005) J. Biotechnol , vol.115 , pp. 113-128
    • Sorensen, H.P.1    Mortensen, K.K.2
  • 136
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • Guzman, L. M., Belin, D., Carson, M. J. and Beckwith, J. (1995) Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J. Bacteriol. 177, 4121-4130.
    • (1995) J. Bacteriol , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 138
    • 0032007853 scopus 로고    scopus 로고
    • Strategies for optimizing heterologous protein expression in Escherichia coli
    • Hannig, G. and Makrides, S. C. (1998) Strategies for optimizing heterologous protein expression in Escherichia coli. Trends Biotechnol. 16, 54-60.
    • (1998) Trends Biotechnol , vol.16 , pp. 54-60
    • Hannig, G.1    Makrides, S.C.2
  • 139
    • 0034613080 scopus 로고    scopus 로고
    • Characterisation of new intracellular membranes in Escherichia coli accompanying large scale over-production of the b subunit of F(1)F(o) ATP synthase
    • Arechaga, I., Miroux, B., Karrasch, S., Huijbregts, R., De Kruijff, B., Runswick, M. J. and Walker, J. E. (2000) Characterisation of new intracellular membranes in Escherichia coli accompanying large scale over-production of the b subunit of F(1)F(o) ATP synthase. FEBS Lett. 482, 215-219.
    • (2000) FEBS Lett , vol.482 , pp. 215-219
    • Arechaga, I.1    Miroux, B.2    Karrasch, S.3    Huijbregts, R.4    De Kruijff, B.5    Runswick, M.J.6    Walker, J.E.7
  • 141
    • 0028798788 scopus 로고
    • Purification and characterization of recombinant human p50csk protein-tyrosine kinase from an Escherichia coli expression system overproducing the bacterial chaperones GroES and GroEL
    • Amrein, K. E., Takacs, B., Stieger, M., Molnos, J., Flint, N. A. and Burn, P. (1995) Purification and characterization of recombinant human p50csk protein-tyrosine kinase from an Escherichia coli expression system overproducing the bacterial chaperones GroES and GroEL. Proc. Natl. Acad. Sci. USA 92, 1048-1052.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1048-1052
    • Amrein, K.E.1    Takacs, B.2    Stieger, M.3    Molnos, J.4    Flint, N.A.5    Burn, P.6
  • 142
    • 0031860811 scopus 로고    scopus 로고
    • Nishihara, K., Kanemori, M., Kitagawa, M., Yanagi, H. and Yura, T. (1998) Chaperone coexpression plasmids: differential and synergistic roles of DnaK-DnaJ-GrpE and GroEL-GroES in assisting folding of an allergen of Japanese cedar pollen, Cryj2, in Escherichia coli. Appl. Environ. Microbiol. 64, 1694-1699.
    • Nishihara, K., Kanemori, M., Kitagawa, M., Yanagi, H. and Yura, T. (1998) Chaperone coexpression plasmids: differential and synergistic roles of DnaK-DnaJ-GrpE and GroEL-GroES in assisting folding of an allergen of Japanese cedar pollen, Cryj2, in Escherichia coli. Appl. Environ. Microbiol. 64, 1694-1699.
  • 144
    • 0025144003 scopus 로고
    • Synthesis of bluetongue virus-encoded phosphoprotein and formation of inclusion bodies by recombinant baculovirus in insect cells: It binds the single-stranded RNA species
    • Thomas, C. P., Booth, T. F. and Roy, P. (1990) Synthesis of bluetongue virus-encoded phosphoprotein and formation of inclusion bodies by recombinant baculovirus in insect cells: it binds the single-stranded RNA species. J. Gen. Virol. 71 (Pt 9), 2073-2083.
    • (1990) J. Gen. Virol , vol.71 , Issue.PART 9 , pp. 2073-2083
    • Thomas, C.P.1    Booth, T.F.2    Roy, P.3
  • 145
    • 0037450517 scopus 로고    scopus 로고
    • In vitro folding of alpha-helical membrane proteins
    • Kiefer, H. (2003) In vitro folding of alpha-helical membrane proteins. Biochim. Biophys. Acta 1610, 57-62.
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 57-62
    • Kiefer, H.1
  • 146
    • 18744422713 scopus 로고    scopus 로고
    • Expression of porin from Rhodopseudomonas blastica in Escherichia coli inclusion bodies and folding into exact native structure
    • Schmid, B., Kromer, M. and Schulz, G. E. (1996) Expression of porin from Rhodopseudomonas blastica in Escherichia coli inclusion bodies and folding into exact native structure. FEBS Lett. 381, 111-114.
    • (1996) FEBS Lett , vol.381 , pp. 111-114
    • Schmid, B.1    Kromer, M.2    Schulz, G.E.3
  • 147
    • 0030467888 scopus 로고    scopus 로고
    • Expression of an olfactory receptor in Escherichia coli: Purification, reconstitution, and ligand binding
    • Kiefer, H., Krieger, J., Olszewski, J. D., Von Heijne, G., Prestwich, G. D. and Breer, H. (1996) Expression of an olfactory receptor in Escherichia coli: purification, reconstitution, and ligand binding. Biochemistry 35, 16077-16084.
    • (1996) Biochemistry , vol.35 , pp. 16077-16084
    • Kiefer, H.1    Krieger, J.2    Olszewski, J.D.3    Von Heijne, G.4    Prestwich, G.D.5    Breer, H.6
  • 148
    • 36749026606 scopus 로고    scopus 로고
    • The process of folding proteins into membranes: Challenges and progress
    • Stanley, A. M. and Fleming, K. G. (2008) The process of folding proteins into membranes: challenges and progress. Arch. Biochem. Biophys. 469, 46-66.
    • (2008) Arch. Biochem. Biophys , vol.469 , pp. 46-66
    • Stanley, A.M.1    Fleming, K.G.2
  • 149
    • 0032584765 scopus 로고    scopus 로고
    • Refolding of Escherichia coli produced membrane protein inclusion bodies immobilised by nickel chelating chromatography
    • Rogl, H., Kosemund, K., Kuhlbrandt, W. and Collinson, I. (1998) Refolding of Escherichia coli produced membrane protein inclusion bodies immobilised by nickel chelating chromatography. FEBS Lett. 432, 21-26.
    • (1998) FEBS Lett , vol.432 , pp. 21-26
    • Rogl, H.1    Kosemund, K.2    Kuhlbrandt, W.3    Collinson, I.4
  • 150
    • 0033534176 scopus 로고    scopus 로고
    • Reconstitutive refolding of diacylglycerol kinase, an integral membrane protein
    • Gorzelle, B. M., Nagy, J. K., Oxenoid, K., Lonzer, W. L., Cafiso, D. S. and Sanders, C. R. (1999) Reconstitutive refolding of diacylglycerol kinase, an integral membrane protein. Biochemistry 38, 16373-16382.
    • (1999) Biochemistry , vol.38 , pp. 16373-16382
    • Gorzelle, B.M.1    Nagy, J.K.2    Oxenoid, K.3    Lonzer, W.L.4    Cafiso, D.S.5    Sanders, C.R.6
  • 152
    • 34250306407 scopus 로고    scopus 로고
    • Heterologous GPCR expression: A bottleneck to obtaining crystal structures
    • McCusker, E. C., Bane, S. E., O'Malley, M. A. and Robinson, A. S. (2007) Heterologous GPCR expression: a bottleneck to obtaining crystal structures. Biotechnol. Prog. 23, 540-547.
    • (2007) Biotechnol. Prog , vol.23 , pp. 540-547
    • McCusker, E.C.1    Bane, S.E.2    O'Malley, M.A.3    Robinson, A.S.4
  • 153
    • 0028652233 scopus 로고
    • Expression of rat NK-2 (neurokinin A) receptor in E. coli
    • Grisshammer, R., Little, J. and Aharony, D. (1994) Expression of rat NK-2 (neurokinin A) receptor in E. coli. Receptors Channels 2, 295-302.
    • (1994) Receptors Channels , vol.2 , pp. 295-302
    • Grisshammer, R.1    Little, J.2    Aharony, D.3
  • 154
    • 26444581283 scopus 로고    scopus 로고
    • Grisshammer, R., White, J. F., Trinh, L. B. and Shiloach, J. (2005) Large-scale expression and purification of a G-protein-coupled receptor for structure determination - an overview. J. Struct. Funct. Gen. 6, 159-163.
    • Grisshammer, R., White, J. F., Trinh, L. B. and Shiloach, J. (2005) Large-scale expression and purification of a G-protein-coupled receptor for structure determination - an overview. J. Struct. Funct. Gen. 6, 159-163.
  • 155
    • 33847145336 scopus 로고    scopus 로고
    • Expression of membrane proteins from Mycobacterium tuberculosis in Escherichia coli as fusions with maltose binding protein
    • Korepanova, A., Moore, J. D., Nguyen, H. B., Hua, Y., Cross, T. A. and Gao, F. (2007) Expression of membrane proteins from Mycobacterium tuberculosis in Escherichia coli as fusions with maltose binding protein. Protein Expr. Purif. 53, 24-30.
    • (2007) Protein Expr. Purif , vol.53 , pp. 24-30
    • Korepanova, A.1    Moore, J.D.2    Nguyen, H.B.3    Hua, Y.4    Cross, T.A.5    Gao, F.6
  • 156
    • 11144234979 scopus 로고    scopus 로고
    • Cloning and expression of multiple integral membrane proteins from Mycobacterium tuberculosis in Escherichia coli
    • Korepanova, A., Gao, F. P., Hua, Y., Qin, H., Nakamoto, R. K. and Cross, T. A. (2005) Cloning and expression of multiple integral membrane proteins from Mycobacterium tuberculosis in Escherichia coli. Protein Sci. 14, 148-158.
    • (2005) Protein Sci , vol.14 , pp. 148-158
    • Korepanova, A.1    Gao, F.P.2    Hua, Y.3    Qin, H.4    Nakamoto, R.K.5    Cross, T.A.6
  • 158
    • 33751290908 scopus 로고    scopus 로고
    • Structural genomics for membrane proteins
    • Lundstrom, K. (2006) Structural genomics for membrane proteins. Cell. Mol. Life Sci. 63, 2597-2607.
    • (2006) Cell. Mol. Life Sci , vol.63 , pp. 2597-2607
    • Lundstrom, K.1
  • 159
    • 0034830308 scopus 로고    scopus 로고
    • Escherichia coli as an expression system for K(+) transport systems from plants
    • Uozumi, N. (2001) Escherichia coli as an expression system for K(+) transport systems from plants. Am. J. Physiol. Cell. Physiol. 281, C733-739.
    • (2001) Am. J. Physiol. Cell. Physiol , vol.281
    • Uozumi, N.1
  • 161
    • 26844435071 scopus 로고    scopus 로고
    • Mierau, I., Olieman, K., Mond, J. and Smid, E. J. (2005) Optimization of the Lactococcus lactis nisin-controlled gene expression system NICE for industrial applications. Microb. Cell Fact. 4, 16.
    • Mierau, I., Olieman, K., Mond, J. and Smid, E. J. (2005) Optimization of the Lactococcus lactis nisin-controlled gene expression system NICE for industrial applications. Microb. Cell Fact. 4, 16.
  • 162
    • 28844468525 scopus 로고    scopus 로고
    • Functional expression of eukaryotic membrane proteins in Lactococcus lactis
    • Monne, M., Chan, K. W., Slotboom, D. J. and Kunji, E. R. (2005) Functional expression of eukaryotic membrane proteins in Lactococcus lactis. Protein Sci. 14, 3048-3056.
    • (2005) Protein Sci , vol.14 , pp. 3048-3056
    • Monne, M.1    Chan, K.W.2    Slotboom, D.J.3    Kunji, E.R.4
  • 164
    • 0029757175 scopus 로고    scopus 로고
    • Controlled gene expression systems for Lactococcus lactis with the food-grade inducer nisin
    • De Ruyter, P. G., Kuipers, O. P. and De Vos, W. M. (1996) Controlled gene expression systems for Lactococcus lactis with the food-grade inducer nisin. Appl. Environ. Microbiol. 62, 3662-3667.
    • (1996) Appl. Environ. Microbiol , vol.62 , pp. 3662-3667
    • De Ruyter, P.G.1    Kuipers, O.P.2    De Vos, W.M.3
  • 165
    • 0033534178 scopus 로고    scopus 로고
    • The purified and functionally reconstituted multidrug transporter LmrA of Lactococcus lactis mediates the transbilayer movement of specific fluorescent phospholipids
    • Margolles, A., Putman, M., Van Veen, H. W. and Konings, W. N. (1999) The purified and functionally reconstituted multidrug transporter LmrA of Lactococcus lactis mediates the transbilayer movement of specific fluorescent phospholipids. Biochemistry 38, 16298-16306.
    • (1999) Biochemistry , vol.38 , pp. 16298-16306
    • Margolles, A.1    Putman, M.2    Van Veen, H.W.3    Konings, W.N.4
  • 166
    • 33748129976 scopus 로고    scopus 로고
    • Comparative analysis and 'expression space' coverage of the production of prokaryotic membrane proteins for structural genomics
    • Surade, S., Klein, M., Stolt-Bergner, P. C., Muenke, C., Roy, A. and Michel, H. (2006) Comparative analysis and 'expression space' coverage of the production of prokaryotic membrane proteins for structural genomics. Protein Sci. 15, 2178-2189.
    • (2006) Protein Sci , vol.15 , pp. 2178-2189
    • Surade, S.1    Klein, M.2    Stolt-Bergner, P.C.3    Muenke, C.4    Roy, A.5    Michel, H.6
  • 167
    • 0026778048 scopus 로고
    • Foreign gene expression in yeast: A review
    • Romanos, M. A., Scorer, C. A. and Clare, J. J. (1992) Foreign gene expression in yeast: a review. Yeast 8, 423-488.
    • (1992) Yeast , vol.8 , pp. 423-488
    • Romanos, M.A.1    Scorer, C.A.2    Clare, J.J.3
  • 168
    • 0035158317 scopus 로고    scopus 로고
    • Yeast - a panacea for the structure-function analysis of membrane proteins? Curr
    • Bill, R. M. (2001)Yeast - a panacea for the structure-function analysis of membrane proteins? Curr. Genet. 40, 157-171.
    • (2001) Genet , vol.40 , pp. 157-171
    • Bill, R.M.1
  • 169
    • 17244363998 scopus 로고    scopus 로고
    • Heterologous protein production using the Pichia pastoris expression system
    • Macauley-Patrick, S., Fazenda, M. L., Mcneil, B. and Harvey, L. M. (2005) Heterologous protein production using the Pichia pastoris expression system. Yeast 22, 249-270.
    • (2005) Yeast , vol.22 , pp. 249-270
    • Macauley-Patrick, S.1    Fazenda, M.L.2    Mcneil, B.3    Harvey, L.M.4
  • 170
    • 0028788937 scopus 로고
    • Budding yeast morphogenesis: Signalling, cytoskeleton and cell cycle
    • Kron, S. J. and Gow, N. A. (1995) Budding yeast morphogenesis: signalling, cytoskeleton and cell cycle. Curr. Opin. Cell Biol. 7, 845-855.
    • (1995) Curr. Opin. Cell Biol , vol.7 , pp. 845-855
    • Kron, S.J.1    Gow, N.A.2
  • 171
    • 23244456428 scopus 로고    scopus 로고
    • Crystal structure of a mammalian voltage-dependent Shaker family K+ channel
    • Long, S. B., Campbell, E. B. and Mackinnon, R. (2005) Crystal structure of a mammalian voltage-dependent Shaker family K+ channel. Science 309, 897-903.
    • (2005) Science , vol.309 , pp. 897-903
    • Long, S.B.1    Campbell, E.B.2    Mackinnon, R.3
  • 172
    • 0030272217 scopus 로고    scopus 로고
    • Quality and authenticity of heterologous proteins synthesized in yeast
    • Eckart, M. R. and Bussineau, C. M. (1996) Quality and authenticity of heterologous proteins synthesized in yeast. Curr. Opin. Biotechnol. 7, 525-530.
    • (1996) Curr. Opin. Biotechnol , vol.7 , pp. 525-530
    • Eckart, M.R.1    Bussineau, C.M.2
  • 174
    • 0033955337 scopus 로고    scopus 로고
    • Heterologous protein expression in the methylotrophic yeast Pichia pastoris
    • Cereghino, J. L. and Cregg, J. M. (2000) Heterologous protein expression in the methylotrophic yeast Pichia pastoris. FEMS Microbiol. Rev. 24, 45-66.
    • (2000) FEMS Microbiol. Rev , vol.24 , pp. 45-66
    • Cereghino, J.L.1    Cregg, J.M.2
  • 177
    • 0343067131 scopus 로고    scopus 로고
    • Rapid detection of efflux pumps and their relation with drug resistance in yeast cells
    • Prudencio, C., Sansonetty, F., Sousa, M. J., Corte-Real, M. and Leao, C. (2000) Rapid detection of efflux pumps and their relation with drug resistance in yeast cells. Cytometry 39, 26-35.
    • (2000) Cytometry , vol.39 , pp. 26-35
    • Prudencio, C.1    Sansonetty, F.2    Sousa, M.J.3    Corte-Real, M.4    Leao, C.5
  • 178
    • 0032032550 scopus 로고    scopus 로고
    • Physiological characterization of the yeast plasma membrane outward rectifying K+ channel, DUK1 (TOK1), in situ
    • Bertl, A., Bihler, H., Reid, J. D., Kettner, C. and Slayman, C. L. (1998) Physiological characterization of the yeast plasma membrane outward rectifying K+ channel, DUK1 (TOK1), in situ. J. Membr. Biol. 162, 67-80.
    • (1998) J. Membr. Biol , vol.162 , pp. 67-80
    • Bertl, A.1    Bihler, H.2    Reid, J.D.3    Kettner, C.4    Slayman, C.L.5
  • 179
    • 0033579812 scopus 로고    scopus 로고
    • Hourglass pore-forming domains restrict aquaporin-1 tetramer assembly
    • Mathai, J. C. and Agre, P. (1999) Hourglass pore-forming domains restrict aquaporin-1 tetramer assembly. Biochemistry 38, 923-928.
    • (1999) Biochemistry , vol.38 , pp. 923-928
    • Mathai, J.C.1    Agre, P.2
  • 180
    • 0025315790 scopus 로고
    • Expression and pharmacological characterization of the human M1 muscarinic receptor in Saccharomyces cerevisiae
    • Payette, P., Gossard, F., Whiteway, M. and Dennis, M. (1990) Expression and pharmacological characterization of the human M1 muscarinic receptor in Saccharomyces cerevisiae. FEBS Lett. 266, 21-25.
    • (1990) FEBS Lett , vol.266 , pp. 21-25
    • Payette, P.1    Gossard, F.2    Whiteway, M.3    Dennis, M.4
  • 181
    • 0026563171 scopus 로고
    • Functional expression of rat M5 muscarinic acetylcholine receptor in yeast
    • Huang, H. J., Liao, C. F., Yang, B. C. and Kuo, T. T. (1992) Functional expression of rat M5 muscarinic acetylcholine receptor in yeast. Biochem. Biophys. Res. Commun. 182, 1180-1186.
    • (1992) Biochem. Biophys. Res. Commun , vol.182 , pp. 1180-1186
    • Huang, H.J.1    Liao, C.F.2    Yang, B.C.3    Kuo, T.T.4
  • 182
    • 0025153120 scopus 로고
    • Control of yeast mating signal transduction by a mammalian beta 2-adrenergic receptor and Gs alpha subunit
    • King, K., Dohlman, H. G., Thorner, J., Caron, M. G. and Lefkowitz, R. J. (1990) Control of yeast mating signal transduction by a mammalian beta 2-adrenergic receptor and Gs alpha subunit. Science 250, 121-123.
    • (1990) Science , vol.250 , pp. 121-123
    • King, K.1    Dohlman, H.G.2    Thorner, J.3    Caron, M.G.4    Lefkowitz, R.J.5
  • 183
    • 0032191422 scopus 로고    scopus 로고
    • Production of G-protein-coupled receptors in yeast
    • Reiländer, H. and Weiss, H. M. (1998) Production of G-protein-coupled receptors in yeast. Curr. Opin. Biotechnol. 9, 510-517.
    • (1998) Curr. Opin. Biotechnol , vol.9 , pp. 510-517
    • Reiländer, H.1    Weiss, H.M.2
  • 184
    • 44749091401 scopus 로고    scopus 로고
    • Design of improved membrane protein production experiments in yeast: Quantitation of the host response
    • Suppl 1:S34, 1-3
    • Bonander, N., Hedfalk, K., Larsson, C., Mostad, P., Chang, C., Gustafsson, L. And Bill, R. M. (2006) Design of improved membrane protein production experiments in yeast: quantitation of the host response. Microb. Cell. Fact. 5 (Suppl 1):S34, 1-3.
    • (2006) Microb. Cell. Fact , vol.5
    • Bonander, N.1    Hedfalk, K.2    Larsson, C.3    Mostad, P.4    Chang, C.5    Gustafsson, L.6    And Bill, R.M.7
  • 185
    • 34447339394 scopus 로고    scopus 로고
    • Expression of 25 human ABC transporters in the yeast Pichia pastoris and characterization of the purified ABCC3 ATPase activity
    • Chloupkova, M., Pickert, A., Lee, J. Y., Souza, S., Trinh, Y. T., Connelly, S. M., Dumont, M. E., Dean, M. and Urbatsch, I. L. (2007) Expression of 25 human ABC transporters in the yeast Pichia pastoris and characterization of the purified ABCC3 ATPase activity. Biochemistry 46, 7992-8003.
    • (2007) Biochemistry , vol.46 , pp. 7992-8003
    • Chloupkova, M.1    Pickert, A.2    Lee, J.Y.3    Souza, S.4    Trinh, Y.T.5    Connelly, S.M.6    Dumont, M.E.7    Dean, M.8    Urbatsch, I.L.9
  • 186
    • 23244441222 scopus 로고    scopus 로고
    • Voltage sensor of Kv1.2: Structural basis of electromechanical coupling
    • Long, S. B., Campbell, E. B. and Mackinnon, R. (2005) Voltage sensor of Kv1.2: structural basis of electromechanical coupling. Science 309, 903-908.
    • (2005) Science , vol.309 , pp. 903-908
    • Long, S.B.1    Campbell, E.B.2    Mackinnon, R.3
  • 187
    • 0032869411 scopus 로고    scopus 로고
    • Heterologous expression of a deuterated membrane-integrated receptor and partial deuteration in methylotrophic yeasts
    • Massou, S., Puech, V., Talmont, F., Demange, P., Lindley, N. D., Tropis, M. and Milon, A. (1999) Heterologous expression of a deuterated membrane-integrated receptor and partial deuteration in methylotrophic yeasts. J. Biomol. NMR 14, 231-239.
    • (1999) J. Biomol. NMR , vol.14 , pp. 231-239
    • Massou, S.1    Puech, V.2    Talmont, F.3    Demange, P.4    Lindley, N.D.5    Tropis, M.6    Milon, A.7
  • 188
    • 0021010433 scopus 로고
    • Production of human b-interferon in insect cells infected with a baculovirus expression vector
    • Smith, G., Summers, M. and Fraser, M. (1983) Production of human b-interferon in insect cells infected with a baculovirus expression vector. Mol. Cell. Biol. 3, 2156-2165.
    • (1983) Mol. Cell. Biol , vol.3 , pp. 2156-2165
    • Smith, G.1    Summers, M.2    Fraser, M.3
  • 189
    • 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. Mol. Cell. Biol. 3, 2156-2165.
    • (1983) Mol. Cell. Biol , vol.3 , pp. 2156-2165
    • Smith, G.E.1    Summers, M.D.2    Fraser, M.J.3
  • 190
    • 0021401669 scopus 로고
    • Strong and regulated expression of Escherichia coli β-galactosidase in insect cells with a baculovirus vector
    • Pennock, G. D., Shoemaker, C. and Miller, L. K. (1984) Strong and regulated expression of Escherichia coli β-galactosidase in insect cells with a baculovirus vector. Mol. Cell. Biol. 4, 399-406.
    • (1984) Mol. Cell. Biol , vol.4 , pp. 399-406
    • Pennock, G.D.1    Shoemaker, C.2    Miller, L.K.3
  • 191
    • 0001751353 scopus 로고
    • Overproduction of membrane proteins
    • Schertler, G. F. X. (1992) Overproduction of membrane proteins. Curr. Opin. Struct. Biol. 2, 534-544.
    • (1992) Curr. Opin. Struct. Biol , vol.2 , pp. 534-544
    • Schertler, G.F.X.1
  • 192
    • 0032848027 scopus 로고    scopus 로고
    • Insect cells as hosts for the expression of recombinant glycoproteins
    • Altmann, F., Staudacher, E., Wilson, I. B. H. and März, L. (1999) Insect cells as hosts for the expression of recombinant glycoproteins. Glycoconj. J. 16, 109-123.
    • (1999) Glycoconj. J , vol.16 , pp. 109-123
    • Altmann, F.1    Staudacher, E.2    Wilson, I.B.H.3    März, L.4
  • 193
    • 0025337872 scopus 로고
    • A baculovirus expression vector derived from the basic protein promoter of Autographa califonica nuclear polygedrosis virus
    • Hill-Perkins, M. S. and Possee, R. D. (1990) A baculovirus expression vector derived from the basic protein promoter of Autographa califonica nuclear polygedrosis virus. J. Gen. Virol. 71, 971-976.
    • (1990) J. Gen. Virol , vol.71 , pp. 971-976
    • Hill-Perkins, M.S.1    Possee, R.D.2
  • 194
    • 0037450518 scopus 로고    scopus 로고
    • Calnexin coexpression and the use of weaker promoters increase the expression of correctly assembled Shaker potassium channel in insect cells
    • Higgins, M. K., Demir, M. and Tate, C. G. (2003) Calnexin coexpression and the use of weaker promoters increase the expression of correctly assembled Shaker potassium channel in insect cells. Biochim. Biophys. Acta 124-132.
    • (2003) Biochim. Biophys. Acta , pp. 124-132
    • Higgins, M.K.1    Demir, M.2    Tate, C.G.3
  • 195
    • 0037450572 scopus 로고    scopus 로고
    • G protein-coupled receptor overexpression with the baculovirus-insect cell system: A tool for structural and functional studies
    • Massotte, D. (2003) G protein-coupled receptor overexpression with the baculovirus-insect cell system: a tool for structural and functional studies. Biochim. Biophys. Acta 1610, 77-89.
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 77-89
    • Massotte, D.1
  • 196
    • 0032073746 scopus 로고    scopus 로고
    • Heterologous expression fo G-protein-coupled receptors: Human opioid receptors under scrutiny
    • Stanasila, L., Pattus, F. and Massotte, D. (1998) Heterologous expression fo G-protein-coupled receptors: human opioid receptors under scrutiny. Biochimie 80, 563-571.
    • (1998) Biochimie , vol.80 , pp. 563-571
    • Stanasila, L.1    Pattus, F.2    Massotte, D.3
  • 198
    • 0028878873 scopus 로고
    • Baculovirus and insect cell gene expression: Review of baculovirus biotechnology
    • Patterson, R. M., Selkirk, J. K. and Merrick, B. A. (1995) Baculovirus and insect cell gene expression: review of baculovirus biotechnology. Environ. Health Perspect. 103, 756-759.
    • (1995) Environ. Health Perspect , vol.103 , pp. 756-759
    • Patterson, R.M.1    Selkirk, J.K.2    Merrick, B.A.3
  • 199
    • 0033199389 scopus 로고    scopus 로고
    • Large-scale production and purification of functional recombinant bovine rhodopsin with the use of the baculovirus expression system
    • Klaassen, C. H., Bovee-Geurts, P. H., Decaluwe, G. L. and Degrip, W. J. (1999) Large-scale production and purification of functional recombinant bovine rhodopsin with the use of the baculovirus expression system. Biochem. J. 342 (Pt 2), 293-300.
    • (1999) Biochem. J , vol.342 , Issue.PART 2 , pp. 293-300
    • Klaassen, C.H.1    Bovee-Geurts, P.H.2    Decaluwe, G.L.3    Degrip, W.J.4
  • 200
    • 0025348276 scopus 로고
    • Baculovirus-directed expression of the human insulin receptor and an insulin-binding ectodomain
    • Paul, J. I., Tavaré, J., Denton, R. M. and Steiner, D. F. (1990) Baculovirus-directed expression of the human insulin receptor and an insulin-binding ectodomain. J. Biol. Chem. 265, 13074-13083.
    • (1990) J. Biol. Chem , vol.265 , pp. 13074-13083
    • Paul, J.I.1    Tavaré, J.2    Denton, R.M.3    Steiner, D.F.4
  • 203
    • 0033231184 scopus 로고    scopus 로고
    • Components of vectors for gene transfer and expression in mammalian cells
    • Makrides, S. C. (1999) Components of vectors for gene transfer and expression in mammalian cells. Protein Expr. Purif. 17, 183-202.
    • (1999) Protein Expr. Purif , vol.17 , pp. 183-202
    • Makrides, S.C.1
  • 204
    • 0037450521 scopus 로고    scopus 로고
    • Semliki Forest virus vectors for rapid and high-level expression of integral membrane proteins
    • Lundstrom, K. (2003) Semliki Forest virus vectors for rapid and high-level expression of integral membrane proteins. Biochim. Biophys. Acta 1610, 90-96.
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 90-96
    • Lundstrom, K.1
  • 207
    • 0028988530 scopus 로고
    • Expression of the mu-opioid receptor in CHO cells: Ability of mu-opioid ligands to promote alpha-azidoanilido[32P]GTP labeling of multiple G protein alpha subunits
    • Chakrabarti, S., Prather, P. L., Yu, L., Law, P. Y. and Loh, H. H. (1995) Expression of the mu-opioid receptor in CHO cells: ability of mu-opioid ligands to promote alpha-azidoanilido[32P]GTP labeling of multiple G protein alpha subunits. J. Neurochem. 64, 2534-2543.
    • (1995) J. Neurochem , vol.64 , pp. 2534-2543
    • Chakrabarti, S.1    Prather, P.L.2    Yu, L.3    Law, P.Y.4    Loh, H.H.5
  • 209
    • 39149143698 scopus 로고    scopus 로고
    • Schwarz, D., Junge, F., Durst, F., Frolich, N., Schneider, B., Reckel, S., Sobhanifar, S., Dotsch, V. and Bernhard, F. (2007) Preparative scale expression of membrane proteins in Escherichia coli-based continuous exchange cell-free systems. Nat. Protoc. 2, 2945-2957.
    • Schwarz, D., Junge, F., Durst, F., Frolich, N., Schneider, B., Reckel, S., Sobhanifar, S., Dotsch, V. and Bernhard, F. (2007) Preparative scale expression of membrane proteins in Escherichia coli-based continuous exchange cell-free systems. Nat. Protoc. 2, 2945-2957.
  • 210
    • 37149014145 scopus 로고    scopus 로고
    • A cell-free translation and proteoliposome reconstitution system for functional analysis of plant solute transporters
    • Nozawa, A., Nanamiya, H., Miyata, T., Linka, N., Endo, Y., Weber, A. P. and Tozawa, Y. (2007) A cell-free translation and proteoliposome reconstitution system for functional analysis of plant solute transporters. Plant Cell Physiol. 48, 1815-1820.
    • (2007) Plant Cell Physiol , vol.48 , pp. 1815-1820
    • Nozawa, A.1    Nanamiya, H.2    Miyata, T.3    Linka, N.4    Endo, Y.5    Weber, A.P.6    Tozawa, Y.7
  • 211
    • 0015871909 scopus 로고
    • In vitro synthesis of protein in microbial systems
    • Zubay, G. (1973) In vitro synthesis of protein in microbial systems. Annu. Rev. Genet. 7, 267-287.
    • (1973) Annu. Rev. Genet , vol.7 , pp. 267-287
    • Zubay, G.1
  • 212
    • 0034681174 scopus 로고    scopus 로고
    • A highly efficient and robust cell-free protein synthesis system prepared from wheat embryos: Plants apparently contain a suicide system directed at ribosomes
    • Madin, K., Sawasaki, T., Ogasawara, T. and Endo, Y. (2000)A highly efficient and robust cell-free protein synthesis system prepared from wheat embryos: plants apparently contain a suicide system directed at ribosomes. Proc. Natl. Acad. Sci. USA 97, 559-564.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 559-564
    • Madin, K.1    Sawasaki, T.2    Ogasawara, T.3    Endo, Y.4
  • 216
    • 44749092559 scopus 로고    scopus 로고
    • Continuous-exchange protein-synthesizing systems
    • 2nd edn, Grandi, G, ed, Humana Press, Totowa, NJ
    • Shirokov, V. A. (2007) Continuous-exchange protein-synthesizing systems. In: In Vitro Transcription and Translation Protocols, 2nd edn., Grandi, G. (ed.), Humana Press, Totowa, NJ.
    • (2007) In Vitro Transcription and Translation Protocols
    • Shirokov, V.A.1
  • 217
    • 0035921172 scopus 로고    scopus 로고
    • Regeneration of adenosine triphosphate from glycolytic intermediates for cell-free protein synthesis
    • Kim, D. M. and Swartz, J. R. (2001) Regeneration of adenosine triphosphate from glycolytic intermediates for cell-free protein synthesis. Biotechnol. Bioeng. 74, 309-316.
    • (2001) Biotechnol. Bioeng , vol.74 , pp. 309-316
    • Kim, D.M.1    Swartz, J.R.2
  • 219
    • 23244440886 scopus 로고    scopus 로고
    • An economical method for cell-free protein synthesis using glucose and nucleoside monophosphates
    • Calhoun, K. A. and Swartz, J. R. (2005) An economical method for cell-free protein synthesis using glucose and nucleoside monophosphates. Biotechnol. Prog. 21, 1146-1153.
    • (2005) Biotechnol. Prog , vol.21 , pp. 1146-1153
    • Calhoun, K.A.1    Swartz, J.R.2
  • 220
    • 0033166764 scopus 로고    scopus 로고
    • A modified procedure for fast purification of T7 RNA polymerase
    • Li, Y., Wang, E. and Wang, Y. (1999) A modified procedure for fast purification of T7 RNA polymerase. Protein Expr. Purif. 16, 355-358.
    • (1999) Protein Expr. Purif , vol.16 , pp. 355-358
    • Li, Y.1    Wang, E.2    Wang, Y.3
  • 221
    • 4744351698 scopus 로고    scopus 로고
    • Cell-free synthesis of a functional ion channel in the absence of a membrane and in the presence of detergent
    • Berrier, C., Park, K. H., Abes, S., Bibonne, A., Betton, J. M. and Ghazi, A. (2004) Cell-free synthesis of a functional ion channel in the absence of a membrane and in the presence of detergent. Biochemistry 43, 12585-12591.
    • (2004) Biochemistry , vol.43 , pp. 12585-12591
    • Berrier, C.1    Park, K.H.2    Abes, S.3    Bibonne, A.4    Betton, J.M.5    Ghazi, A.6
  • 222
    • 1242319564 scopus 로고    scopus 로고
    • In vitro synthesis of fully functional EmrE, a multidrug transporter, and study of its oligomeric state
    • Elbaz, Y., Steiner-Mordoch, S., Danieli, T. and Schuldiner, S. (2004) In vitro synthesis of fully functional EmrE, a multidrug transporter, and study of its oligomeric state. Proc. Natl. Acad. Sci. USA 101, 1519-1524.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 1519-1524
    • Elbaz, Y.1    Steiner-Mordoch, S.2    Danieli, T.3    Schuldiner, S.4
  • 223
    • 7044260891 scopus 로고    scopus 로고
    • Functional expression and characterization of a bacterial light-harvesting membrane protein in Escherichia coli and cell-free synthesis systems
    • Shimada, Y., Wang, Z. Y., Mochizuki, Y., Kobayashi, M. and Nozawa, T. (2004) Functional expression and characterization of a bacterial light-harvesting membrane protein in Escherichia coli and cell-free synthesis systems. Biosci. Biotechnol. Biochem. 68, 1942-1948.
    • (2004) Biosci. Biotechnol. Biochem , vol.68 , pp. 1942-1948
    • Shimada, Y.1    Wang, Z.Y.2    Mochizuki, Y.3    Kobayashi, M.4    Nozawa, T.5
  • 224
    • 15744391469 scopus 로고    scopus 로고
    • Expression of G protein coupled receptors in a cell-free translational system using detergents and thioredoxin-fusion vectors
    • Ishihara, G., Goto, M., Saeki, M., Ito, K., Hori, T., Kigawa, T., Shirouzu, M. and Yokoyama, S. (2005) Expression of G protein coupled receptors in a cell-free translational system using detergents and thioredoxin-fusion vectors. Protein Expr. Purif. 41, 27-37.
    • (2005) Protein Expr. Purif , vol.41 , pp. 27-37
    • Ishihara, G.1    Goto, M.2    Saeki, M.3    Ito, K.4    Hori, T.5    Kigawa, T.6    Shirouzu, M.7    Yokoyama, S.8
  • 225
    • 28244458078 scopus 로고    scopus 로고
    • Evaluation of detergents for the soluble expression of alpha-helical and beta-barrel-type integral membrane proteins by a preparative scale individual cell-free expression system
    • Klammt, C., Schwarz, D., Fendler, K., Haase, W., Dotsch, V. and Bernhard, F. (2005) Evaluation of detergents for the soluble expression of alpha-helical and beta-barrel-type integral membrane proteins by a preparative scale individual cell-free expression system. FEBS J. 272, 6024-6038.
    • (2005) FEBS J , vol.272 , pp. 6024-6038
    • Klammt, C.1    Schwarz, D.2    Fendler, K.3    Haase, W.4    Dotsch, V.5    Bernhard, F.6
  • 226
    • 39749126981 scopus 로고    scopus 로고
    • GPCR proteomics: Mass spectrometric and functional analysis of histamine H1 receptor after baculovirus-driven and in vitro cell free expression
    • Sansuk, K., Balog, C. I., Van Der Does, A. M., Booth, R., De Grip, W. J., Deelder, A. M., Bakker, R. A., Leurs, R. and Hensbergen, P. J. (2008) GPCR proteomics: mass spectrometric and functional analysis of histamine H1 receptor after baculovirus-driven and in vitro cell free expression. J. Proteome Res. 7, 621-629.
    • (2008) J. Proteome Res , vol.7 , pp. 621-629
    • Sansuk, K.1    Balog, C.I.2    Van Der Does, A.M.3    Booth, R.4    De Grip, W.J.5    Deelder, A.M.6    Bakker, R.A.7    Leurs, R.8    Hensbergen, P.J.9
  • 227
    • 44749083038 scopus 로고    scopus 로고
    • Cell-free expression approaches for the production and characterization of membrane proteins
    • Kudliki, W, Katzen, F. and Bennett, R, eds, Landes Bioscience, Austin, TX
    • Schwarz, D. (2007) Cell-free expression approaches for the production and characterization of membrane proteins. In: Cell-Free Expression, Kudliki, W., Katzen, F. and Bennett, R. (eds.), Landes Bioscience, Austin, TX.
    • (2007) Cell-Free Expression
    • Schwarz, D.1
  • 230
    • 33748307399 scopus 로고    scopus 로고
    • Cell-free expression as an emerging technique for the large scale production of integral membrane protein
    • Klammt, C., Schwarz, D., Lohr, F., Schneider, B., Dotsch, V. and Bernhard, F. (2006) Cell-free expression as an emerging technique for the large scale production of integral membrane protein. FEBS J. 273, 4141-4153.
    • (2006) FEBS J , vol.273 , pp. 4141-4153
    • Klammt, C.1    Schwarz, D.2    Lohr, F.3    Schneider, B.4    Dotsch, V.5    Bernhard, F.6
  • 232
    • 0031021109 scopus 로고    scopus 로고
    • Functional antibody production using cell-free translation: Effects of protein disulfide isomerase and chaperones
    • Ryabova, L. A., Desplancq, D., Spirin, A. S. and Pluckthun, A. (1997) Functional antibody production using cell-free translation: effects of protein disulfide isomerase and chaperones. Nat. Biotechnol. 15, 79-84.
    • (1997) Nat. Biotechnol , vol.15 , pp. 79-84
    • Ryabova, L.A.1    Desplancq, D.2    Spirin, A.S.3    Pluckthun, A.4
  • 233
    • 0037070555 scopus 로고    scopus 로고
    • Expression of Fab fragment of catalytic antibody 6D9 in an Escherichia coli in vitro coupled transcription/translation system
    • Jiang, X., Ookubo, Y., Fujii, I., Nakano, H. and Yamane, T. (2002) Expression of Fab fragment of catalytic antibody 6D9 in an Escherichia coli in vitro coupled transcription/translation system. FEBS Lett. 514, 290-294.
    • (2002) FEBS Lett , vol.514 , pp. 290-294
    • Jiang, X.1    Ookubo, Y.2    Fujii, I.3    Nakano, H.4    Yamane, T.5
  • 234
    • 0034595692 scopus 로고    scopus 로고
    • Co-translational folding of an eukaryotic multidomain protein in a prokaryotic translation system
    • Kolb, V. A., Makeyev, E. V. and Spirin, A. S. (2000) Co-translational folding of an eukaryotic multidomain protein in a prokaryotic translation system. J. Biol. Chem. 275, 16597-16601.
    • (2000) J. Biol. Chem , vol.275 , pp. 16597-16601
    • Kolb, V.A.1    Makeyev, E.V.2    Spirin, A.S.3
  • 235
    • 0020997221 scopus 로고
    • Cell-free translation of messenger RNA in a wheat germ system
    • Erickson, A. H. and Blobel, G. (1983) Cell-free translation of messenger RNA in a wheat germ system. Methods Enzymol. 96, 38-50.
    • (1983) Methods Enzymol , vol.96 , pp. 38-50
    • Erickson, A.H.1    Blobel, G.2
  • 236
    • 33644810868 scopus 로고    scopus 로고
    • The wheat germ cell-free expression system: Methods for high-throughput materialization of genetic information
    • Sawasaki, T., Gouda, M. D., Kawasaki, T., Tsuboi, T., Tozawa, Y., Takai, K. and Endo, Y. (2005) The wheat germ cell-free expression system: methods for high-throughput materialization of genetic information. Methods Mol. Biol. 310, 131-144.
    • (2005) Methods Mol. Biol , vol.310 , pp. 131-144
    • Sawasaki, T.1    Gouda, M.D.2    Kawasaki, T.3    Tsuboi, T.4    Tozawa, Y.5    Takai, K.6    Endo, Y.7
  • 237
    • 44749083340 scopus 로고    scopus 로고
    • The wheat germ cell-Free protein synthesis system
    • Spirin, A. S. and Swartz, J. R, eds, John Wiley, Weinheim, Germany
    • Sawasaki, T. and Endo, Y. (2007) The wheat germ cell-Free protein synthesis system. In: Cell-free Protein Synthesis: Methods and Protocols, Spirin, A. S. and Swartz, J. R. (eds.), John Wiley, Weinheim, Germany.
    • (2007) Cell-free Protein Synthesis: Methods and Protocols
    • Sawasaki, T.1    Endo, Y.2
  • 238
    • 0020671498 scopus 로고
    • Preparation of a cell-free protein-synthesizing system from wheat germ
    • Anderson, C. W., Straus, J. W. and Dudock, B. S. (1983) Preparation of a cell-free protein-synthesizing system from wheat germ. Methods Enzymol. 101, 635-644.
    • (1983) Methods Enzymol , vol.101 , pp. 635-644
    • Anderson, C.W.1    Straus, J.W.2    Dudock, B.S.3
  • 239
    • 4644269746 scopus 로고    scopus 로고
    • High-throughput cell-free systems for synthesis of functionally active proteins
    • Spirin, A. S. (2004) High-throughput cell-free systems for synthesis of functionally active proteins. Trends Biotechnol. 22, 538-545.
    • (2004) Trends Biotechnol , vol.22 , pp. 538-545
    • Spirin, A.S.1
  • 240
    • 1542720448 scopus 로고    scopus 로고
    • Mimicking the Escherichia coli cytoplasmic environment activates long-lived and efficient cell-free protein synthesis
    • Jewett, M. C. and Swartz, J. R. (2004) Mimicking the Escherichia coli cytoplasmic environment activates long-lived and efficient cell-free protein synthesis. Biotechnol. Bioeng. 86, 19-26.
    • (2004) Biotechnol. Bioeng , vol.86 , pp. 19-26
    • Jewett, M.C.1    Swartz, J.R.2
  • 241
    • 0036207282 scopus 로고    scopus 로고
    • Untranslated regions of mRNAs
    • reviews 0004.1-0004.10
    • Mignone, F., Gissi, C., Liuni, S. and Pesole, G. (2002) Untranslated regions of mRNAs. Genome Biol. 3, reviews 0004.1-0004.10.
    • (2002) Genome Biol , vol.3
    • Mignone, F.1    Gissi, C.2    Liuni, S.3    Pesole, G.4
  • 242
    • 0037069324 scopus 로고    scopus 로고
    • A cell-free protein synthesis system for high-throughput proteomics
    • Sawasaki, T., Ogasawara, T., Morishita, R. and Endo, Y. (2002) A cell-free protein synthesis system for high-throughput proteomics. Proc. Natl. Acad. Sci. USA 99, 14652-14657.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 14652-14657
    • Sawasaki, T.1    Ogasawara, T.2    Morishita, R.3    Endo, Y.4
  • 243
    • 0141975780 scopus 로고    scopus 로고
    • High-throughput, genome-scale protein production method based on the wheat germ cell-free expression system
    • Endo, Y. and Sawasaki, T. (2003) High-throughput, genome-scale protein production method based on the wheat germ cell-free expression system. Biotechnol. Adv. 21, 695-713.
    • (2003) Biotechnol. Adv , vol.21 , pp. 695-713
    • Endo, Y.1    Sawasaki, T.2
  • 244
    • 44749094754 scopus 로고    scopus 로고
    • Methods for high-throughput materialization of genetic information based on wheat germ cell-free expression system
    • 2nd edn, Grandi, G, ed, Humana Press, Totawa, NJ
    • Sawasaki, T. (2007) Methods for high-throughput materialization of genetic information based on wheat germ cell-free expression system. In: In Vitro Transcription and Translation Protocols, 2nd edn., Grandi, G. (ed.), Humana Press, Totawa, NJ.
    • (2007) In Vitro Transcription and Translation Protocols
    • Sawasaki, T.1
  • 245
    • 14344256801 scopus 로고    scopus 로고
    • Vinarov, D. A., Lytle, B. L., Peterson, F. C., Tyler, E. M., Volkman, B. F. and Markley, J. L. (2004) Cell-free protein production and labeling protocol for NMR-based structural proteomics. Nat. Methods 1, 149-153.
    • Vinarov, D. A., Lytle, B. L., Peterson, F. C., Tyler, E. M., Volkman, B. F. and Markley, J. L. (2004) Cell-free protein production and labeling protocol for NMR-based structural proteomics. Nat. Methods 1, 149-153.
  • 246
    • 0031035737 scopus 로고    scopus 로고
    • Membrane insertion, glycosylation, and oligomerization of inositol trisphosphate receptors in a cell-free translation system
    • Joseph, S. K., Boehning, D., Pierson, S. and Nicchitta, C. V. (1997) Membrane insertion, glycosylation, and oligomerization of inositol trisphosphate receptors in a cell-free translation system. J. Biol. Chem. 272, 1579-1588.
    • (1997) J. Biol. Chem , vol.272 , pp. 1579-1588
    • Joseph, S.K.1    Boehning, D.2    Pierson, S.3    Nicchitta, C.V.4
  • 247
    • 0033520449 scopus 로고    scopus 로고
    • Cell-free expression and functional reconstitution of homo-oligomeric alpha7 nicotinic acetylcholine receptors into planar lipid bilayers
    • Lyford, L. K. and Rosenberg, R. L. (1999) Cell-free expression and functional reconstitution of homo-oligomeric alpha7 nicotinic acetylcholine receptors into planar lipid bilayers. J. Biol. Chem. 274, 25675-25681.
    • (1999) J. Biol. Chem , vol.274 , pp. 25675-25681
    • Lyford, L.K.1    Rosenberg, R.L.2
  • 249
    • 44749085757 scopus 로고    scopus 로고
    • The role of cell-free rabbit reticulocyte expression systems in functional proteomics
    • Kudlicki, W, Katzen, F. and Bennett, R, ed, Landes Bioscience, Austin, TX
    • Arduengo, M., Schenborn, E. and Hurst, R. (2007) The role of cell-free rabbit reticulocyte expression systems in functional proteomics. In: Cell-Free Protein Expression, Kudlicki, W., Katzen, F. and Bennett, R. (ed.), Landes Bioscience, Austin, TX.
    • (2007) Cell-Free Protein Expression
    • Arduengo, M.1    Schenborn, E.2    Hurst, R.3
  • 250
    • 0027183935 scopus 로고
    • Evidence from transgenic mice that glucose transport is rate-limiting for glycogen deposition and glycolysis in skeletal muscle
    • Ren, J. M., Marshall, B. A., Gulve, E. A., Gao, J., Johnson, D. W., Holloszy, J. O. and Mueckler, M. (1993) Evidence from transgenic mice that glucose transport is rate-limiting for glycogen deposition and glycolysis in skeletal muscle. J. Biol. Chem. 268, 16113-16115.
    • (1993) J. Biol. Chem , vol.268 , pp. 16113-16115
    • Ren, J.M.1    Marshall, B.A.2    Gulve, E.A.3    Gao, J.4    Johnson, D.W.5    Holloszy, J.O.6    Mueckler, M.7
  • 251
    • 18144423143 scopus 로고    scopus 로고
    • Membrane topology mapping of vitamin K epoxide reductase by in vitro translation/cotranslocation
    • Tie, J. K., Nicchitta, C., Von Heijne, G. and Stafford, D. W. (2005) Membrane topology mapping of vitamin K epoxide reductase by in vitro translation/cotranslocation. J. Biol. Chem. 280, 16410-16416.
    • (2005) J. Biol. Chem , vol.280 , pp. 16410-16416
    • Tie, J.K.1    Nicchitta, C.2    Von Heijne, G.3    Stafford, D.W.4
  • 252
    • 0019877192 scopus 로고
    • NH2-terminal acetylation of Dictyostelium discoideum actin in a cell-free protein-synthesizing system
    • Rubenstein, P., Smith, P., Deuchler, J. and Redman, K. (1981) NH2-terminal acetylation of Dictyostelium discoideum actin in a cell-free protein-synthesizing system. J. Biol. Chem. 256, 8149-8155.
    • (1981) J. Biol. Chem , vol.256 , pp. 8149-8155
    • Rubenstein, P.1    Smith, P.2    Deuchler, J.3    Redman, K.4
  • 253
    • 0025773525 scopus 로고
    • Gamma-subunits of G proteins, but not their alpha- or beta-subunits, are polyisoprenylated. Studies on post-translational modifications using in vitro translation with rabbit reticulocyte lysates
    • Sanford, J., Codina, J. and Birnbaumer, L. (1991) Gamma-subunits of G proteins, but not their alpha- or beta-subunits, are polyisoprenylated. Studies on post-translational modifications using in vitro translation with rabbit reticulocyte lysates. J. Biol. Chem. 266, 9570-9579.
    • (1991) J. Biol. Chem , vol.266 , pp. 9570-9579
    • Sanford, J.1    Codina, J.2    Birnbaumer, L.3
  • 254
    • 25844528201 scopus 로고    scopus 로고
    • Efficient strategy for the rapid backbone assignment of membrane proteins
    • Trbovic, N., Klammt, C., Koglin, A., Lohr, F., Bernhard, F. and Dotsch, V. (2005) Efficient strategy for the rapid backbone assignment of membrane proteins. J. Am. Chem. Soc. 127, 13504-13505.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 13504-13505
    • Trbovic, N.1    Klammt, C.2    Koglin, A.3    Lohr, F.4    Bernhard, F.5    Dotsch, V.6
  • 255
    • 33748311913 scopus 로고    scopus 로고
    • N-Labelled proteins by cell-free protein synthesis. Strategies for high-throughput NMR studies of proteins and protein-ligand complexes
    • Ozawa, K., Wu, P. S., Dixon, N. E. and Otting, G. (2006) N-Labelled proteins by cell-free protein synthesis. Strategies for high-throughput NMR studies of proteins and protein-ligand complexes. FEBS J. 273, 4154-4159.
    • (2006) FEBS J , vol.273 , pp. 4154-4159
    • Ozawa, K.1    Wu, P.S.2    Dixon, N.E.3    Otting, G.4
  • 256
    • 35448953299 scopus 로고    scopus 로고
    • Cell-free protein synthesis of perdeuterated proteins for NMR studies
    • Etezady-Esfarjani, T., Hiller, S., Villalba, C. and Wuthrich, K. (2007) Cell-free protein synthesis of perdeuterated proteins for NMR studies. J. Biomol. NMR 39, 229-238.
    • (2007) J. Biomol. NMR , vol.39 , pp. 229-238
    • Etezady-Esfarjani, T.1    Hiller, S.2    Villalba, C.3    Wuthrich, K.4
  • 257
    • 0024968835 scopus 로고
    • A general method for site-specific incorporation of unnatural amino acids into proteins
    • Noren, C. J., Anthony-Cahill, S. J., Griffith, M. C. and Schultz, P. G. (1989) A general method for site-specific incorporation of unnatural amino acids into proteins. Science 244, 182-188.
    • (1989) Science , vol.244 , pp. 182-188
    • Noren, C.J.1    Anthony-Cahill, S.J.2    Griffith, M.C.3    Schultz, P.G.4
  • 258
    • 0842281352 scopus 로고    scopus 로고
    • Cell-free N-terminal protein labeling using initiator suppressor tRNA
    • Mamaev, S., Olejnik, J., Olejnik, E. K. and Rothschild, K. J. (2004) Cell-free N-terminal protein labeling using initiator suppressor tRNA. Anal. Biochem. 326, 25-32.
    • (2004) Anal. Biochem , vol.326 , pp. 25-32
    • Mamaev, S.1    Olejnik, J.2    Olejnik, E.K.3    Rothschild, K.J.4
  • 259
    • 13944274948 scopus 로고    scopus 로고
    • The past, present and future of cell-free protein synthesis
    • Katzen, F., Chang, G. and Kudlicki, W. (2005) The past, present and future of cell-free protein synthesis. Trends Biotechnol. 23, 150-156.
    • (2005) Trends Biotechnol , vol.23 , pp. 150-156
    • Katzen, F.1    Chang, G.2    Kudlicki, W.3
  • 261
    • 4344670572 scopus 로고    scopus 로고
    • Substrate replenishment extends protein synthesis with an in vitro translation system designed to mimic the cytoplasm
    • Jewett, M. C. and Swartz, J. R. (2004) Substrate replenishment extends protein synthesis with an in vitro translation system designed to mimic the cytoplasm. Biotechnol. Bioeng. 87, 465-472.
    • (2004) Biotechnol. Bioeng , vol.87 , pp. 465-472
    • Jewett, M.C.1    Swartz, J.R.2
  • 262
    • 1142269592 scopus 로고    scopus 로고
    • Rapid expression and purification of 100 nmol quantities of active protein using cell-free protein synthesis
    • Jewett, M. C. and Swartz, J. R. (2004) Rapid expression and purification of 100 nmol quantities of active protein using cell-free protein synthesis. Biotechnol. Prog. 20, 102-109.
    • (2004) Biotechnol. Prog , vol.20 , pp. 102-109
    • Jewett, M.C.1    Swartz, J.R.2


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