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Volumn 63, Issue 22, 2006, Pages 2597-2607

Structural genomics for membrane proteins

Author keywords

Membrane proteins; Networks; Purification; Recombinant protein expression; Structural genomics; Structure determination

Indexed keywords

DRUG; MEMBRANE PROTEIN; PROTEIN;

EID: 33751290908     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-006-6252-y     Document Type: Review
Times cited : (54)

References (111)
  • 1
    • 6444234760 scopus 로고    scopus 로고
    • The role of the medicinal chemistry in drug discovery - Then and now
    • Lombardino, J. G. and Lowe, J. A. III (2004) The role of the medicinal chemistry in drug discovery - then and now. Nat. Rev. Drug Discov. 3, 853-862.
    • (2004) Nat. Rev. Drug Discov. , vol.3 , pp. 853-862
    • Lombardino, J.G.1    Lowe III, J.A.2
  • 2
    • 0030574268 scopus 로고    scopus 로고
    • Structure-based drug design
    • Blundell, T. L. (1996) Structure-based drug design. Nature 384S, 23-26.
    • (1996) Nature , vol.384 S , pp. 23-26
    • Blundell, T.L.1
  • 4
    • 0032996584 scopus 로고    scopus 로고
    • Development of neuroaminidase inhibitors as anti-influenza virus drugs
    • Varghese, J. N. (1999) Development of neuroaminidase inhibitors as anti-influenza virus drugs. Drug Dev. Res. 46, 176-196.
    • (1999) Drug Dev. Res. , vol.46 , pp. 176-196
    • Varghese, J.N.1
  • 5
    • 0041876269 scopus 로고    scopus 로고
    • Heterologous expression of G protein-coupled receptors: Comparison of expression from 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 from the standpoint of large-scale production and purification. Cell Mol. Life Ssi. 60, 1529-1546.
    • (2003) Cell Mol. Life Ssi. , vol.60 , pp. 1529-1546
    • Sarramegna, V.1    Talmont, F.2    Demange, P.3    Milon, A.4
  • 6
    • 28044444551 scopus 로고    scopus 로고
    • The future of G protein-coupled receptors as targets in drug discovery
    • Lundstrom, K. (2005) The future of G protein-coupled receptors as targets in drug discovery. IDrugs 8, 909-913.
    • (2005) IDrugs , vol.8 , pp. 909-913
    • Lundstrom, K.1
  • 8
    • 26444581283 scopus 로고    scopus 로고
    • Large-scale expression and purification of a G-protein-coupled receptor for structure determination - An overview
    • 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. Genom. 6, 159-163.
    • (2005) J. Struct. Funct. Genom. , vol.6 , pp. 159-163
    • Grisshammer, R.1    White, J.F.2    Trinh, L.B.3    Shiloach, J.4
  • 9
    • 0027190359 scopus 로고
    • Projection structure of rhodopsin
    • Schertler, G. F., Villa, C. and Henderson, R. (1993) Projection structure of rhodopsin. Nature 362, 770-772.
    • (1993) Nature , vol.362 , pp. 770-772
    • Schertler, G.F.1    Villa, C.2    Henderson, R.3
  • 10
    • 4243139636 scopus 로고    scopus 로고
    • Structural genomics on membrane proteins: Mini review
    • Lundstrom, K. (2004) Structural genomics on membrane proteins: mini review. Comb. Chem. High Throughput Screen. 7, 431-439.
    • (2004) Comb. Chem. High Throughput Screen. , vol.7 , pp. 431-439
    • Lundstrom, K.1
  • 11
    • 0028956268 scopus 로고
    • Topological analysis of the L-fucose-proton symport protein, FucP, of Escherichia coli
    • Gunn, F., Tate, C. G., Sansom, C. E. and Henderson, P. J.F. (1995) Topological analysis of the L-fucose-proton symport protein, FucP, of Escherichia coli. Mol. Microbiol. 15, 771-783.
    • (1995) Mol. Microbiol. , vol.15 , pp. 771-783
    • Gunn, F.1    Tate, C.G.2    Sansom, C.E.3    Henderson, P.J.F.4
  • 13
    • 4043142190 scopus 로고    scopus 로고
    • Structural genomics on membraneproteins: The MePNet approach
    • Lundstrom K (2004) Structural genomics on membraneproteins: the MePNet approach. Curr. Opin. Drug Discov. Dev. 7, 342-346.
    • (2004) Curr. Opin. Drug Discov. Dev. , vol.7 , pp. 342-346
    • Lundstrom, K.1
  • 15
    • 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
    • (in press)
    • André, N., Cherouati, N., Prual, C., Steffan, T., Zeder-Lutz, G., Magnin, T., Pattus, F., Michel, H., Wagner, R. and Reinhart, C. (in press) Enhancing functional production of G protein-coupled receptors in Pichia pastoris to levels required for structural studies via a single expression screen. Protein Sci.
    • Protein Sci.
    • André, 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
  • 17
    • 0242488935 scopus 로고    scopus 로고
    • Structure and action of the nicotinicacetylcholine receptor explored by electron microscopy
    • Unwin, N. (2003) Structure and action of the nicotinicacetylcholine receptor explored by electron microscopy. FEBS Lett. 555, 91-95.
    • (2003) FEBS Lett. , vol.555 , pp. 91-95
    • Unwin, N.1
  • 18
    • 0029132713 scopus 로고
    • Purification and biochemical characterization of the neuropeptide Y2 receptor
    • Wimalawansa, S. J. (1995) Purification and biochemical characterization of the neuropeptide Y2 receptor. J. Biol. Chem. 270, 18523-18530.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18523-18530
    • Wimalawansa, S.J.1
  • 19
    • 0028825817 scopus 로고
    • Gene fusion expression systems in Escherichia coli
    • La Vallie, E. R. and McCoy, J. M. (1995) Gene fusion expression systems in Escherichia coli. Curr. Opin. Biotechnol. 6, 501-506.
    • (1995) Curr. Opin. Biotechnol. , vol.6 , pp. 501-506
    • La Vallie, E.R.1    McCoy, J.M.2
  • 21
    • 0029838532 scopus 로고    scopus 로고
    • Purification of a rat neurotensin receptor expressed in Escherichia coli
    • Tucker, J. and Grisshammer, R. (1996) Purification of a rat neurotensin receptor expressed in Escherichia coli. Biochem. J. 317, 891-899.
    • (1996) Biochem. J. , vol.317 , pp. 891-899
    • Tucker, J.1    Grisshammer, R.2
  • 22
    • 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
  • 23
    • 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
  • 24
    • 0037518197 scopus 로고    scopus 로고
    • The isolated N-terminal domain of the glucagon-like peptide-1 (GLP-1) receptor binds exendin peptides with much higher affinity than GLP-1
    • Lopez de Maturana, R., Willshaw, A., Kuntzsch, A., Rudolph, R. and Donnelly, D. (2003) The isolated N-terminal domain of the glucagon-like peptide-1 (GLP-1) receptor binds exendin peptides with much higher affinity than GLP-1. J. Biol. Chem. 278, 10195-10200.
    • (2003) J. Biol. Chem. , vol.278 , pp. 10195-10200
    • Lopez De Maturana, R.1    Willshaw, A.2    Kuntzsch, A.3    Rudolph, R.4    Donnelly, D.5
  • 25
    • 0037648337 scopus 로고    scopus 로고
    • Structure-based analysis of GPCR function: Conformational adaptation of both agonist and receptor upon leukotriene B4 binding to recombinant BLT1
    • Baneres, J. L., Martin, A., Hullot, P., Girard, J. P., Rossi, J. C. and Parello, J. (2003) Structure-based analysis of GPCR function: conformational adaptation of both agonist and receptor upon leukotriene B4 binding to recombinant BLT1. J. Mol. Biol. 329, 801-814.
    • (2003) J. Mol. Biol. , vol.329 , pp. 801-814
    • Baneres, J.L.1    Martin, A.2    Hullot, P.3    Girard, J.P.4    Rossi, J.C.5    Parello, J.6
  • 26
    • 20144385917 scopus 로고    scopus 로고
    • Molecular characterization of a purified 5-HT4 receptor: A structural basis for drug efficacy
    • Baneres, J. L., Mesnier, D., Martin, A., Joubert, L., Dumuis, A. and Bockaert, J. (2005) Molecular characterization of a purified 5-HT4 receptor: a structural basis for drug efficacy. J. Biol. Chem. 280, 20253-20260.
    • (2005) J. Biol. Chem. , vol.280 , pp. 20253-20260
    • Baneres, J.L.1    Mesnier, D.2    Martin, A.3    Joubert, L.4    Dumuis, A.5    Bockaert, J.6
  • 28
    • 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, 97108.
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 97108
    • Kunji, E.R.1    Slotboom, D.J.2    Poolman, B.3
  • 29
    • 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
  • 30
    • 0031008165 scopus 로고    scopus 로고
    • Expression and purification of the Saccharomyces cerevisiae alpha-factor receptor (Ste2p), a 7-transmembrane-segment G protein-coupled receptor
    • David, N. E., Gee, M., Andersen, B., Naider, F., Thorner, J. and Stevens, R. C. (1997) Expression and purification of the Saccharomyces cerevisiae alpha-factor receptor (Ste2p), a 7-transmembrane-segment G protein-coupled receptor. J. Biol. Chem. 272, 15553-15561.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15553-15561
    • David, N.E.1    Gee, M.2    Andersen, B.3    Naider, F.4    Thorner, J.5    Stevens, R.C.6
  • 31
    • 0032081297 scopus 로고    scopus 로고
    • The human D1A dopamine receptor: Heterologous expression in Saccharomyces cerevisiae and purification of the functional receptor
    • Andersen, B. and Stevens, R. C. (1998) The human D1A dopamine receptor: heterologous expression in Saccharomyces cerevisiae and purification of the functional receptor. Protein Expr. Purif. 13, 111-119.
    • (1998) Protein Expr. Purif. , vol.13 , pp. 111-119
    • Andersen, B.1    Stevens, R.C.2
  • 34
    • 0032959440 scopus 로고    scopus 로고
    • Overview of N- and O-linked oligosaccharide structures found in various yeast species
    • Gemmill, T. R. and Trimble, R. B. (1999) Overview of N- and O-linked oligosaccharide structures found in various yeast species. Biochim. Biophys. Acta 1426, 227-237.
    • (1999) Biochim. Biophys. Acta , vol.1426 , pp. 227-237
    • Gemmill, T.R.1    Trimble, R.B.2
  • 35
    • 0028070288 scopus 로고
    • Constitutive expression of the human D2S-dopamine receptor in the unicellular yeast Saccharomyces cerevisiae
    • Sander, P., Grunewald, S., Maul, G., Reilander, H. and Michel, H. (1994) Constitutive expression of the human D2S-dopamine receptor in the unicellular yeast Saccharomyces cerevisiae. Biochim. Biophys. Acta 1193, 255-262.
    • (1994) Biochim. Biophys. Acta , vol.1193 , pp. 255-262
    • Sander, P.1    Grunewald, S.2    Maul, G.3    Reilander, H.4    Michel, H.5
  • 36
    • 0032148392 scopus 로고    scopus 로고
    • Pharmacological characterization of the D2 dopamine receptor expressed in the yeast Schizosaccharomyces pombe
    • Presland, J. and Strange, P. G. (1998) Pharmacological characterization of the D2 dopamine receptor expressed in the yeast Schizosaccharomyces pombe. Biochem. Pharmacol. 56, 577-582.
    • (1998) Biochem. Pharmacol. , vol.56 , pp. 577-582
    • Presland, J.1    Strange, P.G.2
  • 37
    • 0028847201 scopus 로고
    • Co-expression of the neurokinin NK2 receptor and protein components in the fission yeast Schizosaccharomyces pombe
    • Arkinstall, S., Edgerton, M., Payton, M. and Maundrell, K. (1995) Co-expression of the neurokinin NK2 receptor and protein components in the fission yeast Schizosaccharomyces pombe. FEMS Lett. 375, 183-187.
    • (1995) FEMS Lett. , vol.375 , pp. 183-187
    • Arkinstall, S.1    Edgerton, M.2    Payton, M.3    Maundrell, K.4
  • 38
    • 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
  • 39
    • 33646130717 scopus 로고    scopus 로고
    • Expression of membrane proteins in yeast
    • (Lundstrom, K., Ed.), CRC, Boca Raton
    • Reinhart, C. and Kettler, C. (2006) Expression of membrane proteins in yeast. In: Structural Genomics on Membrane Proteins (Lundstrom, K., Ed.), pp. 115-152. CRC, Boca Raton.
    • (2006) Structural Genomics on Membrane Proteins , pp. 115-152
    • Reinhart, C.1    Kettler, C.2
  • 41
    • 0027378859 scopus 로고
    • Baculovirus systems for the expression of human gene products
    • Luckow, V. A. (1993) Baculovirus systems for the expression of human gene products. Curr. Opin. Biotechnol. 4, 564-572.
    • (1993) Curr. Opin. Biotechnol. , vol.4 , pp. 564-572
    • Luckow, V.A.1
  • 42
    • 0034089238 scopus 로고    scopus 로고
    • Baculovirus expression system for expression and characterization of functional recombinant visual pigments
    • Klaassen, C. H. W. and De Grip, W. J. (2000) Baculovirus expression system for expression and characterization of functional recombinant visual pigments. Methods Enzymol. 315, 12-29.
    • (2000) Methods Enzymol. , vol.315 , pp. 12-29
    • Klaassen, C.H.W.1    De Grip, W.J.2
  • 43
    • 0028125669 scopus 로고
    • Expression and solubilization of a recombinant human neurokinin-1 receptor in insect cells
    • Mazina, K. E., Strader, C. D. and Fong, T. M. (1994) Expression and solubilization of a recombinant human neurokinin-1 receptor in insect cells. J. Recept. Res. 14, 63-73.
    • (1994) J. Recept. Res. , vol.14 , pp. 63-73
    • Mazina, K.E.1    Strader, C.D.2    Fong, T.M.3
  • 45
  • 46
    • 0141762594 scopus 로고    scopus 로고
    • Expression of EGFP-amino-tagged human mu opioid receptor in Drosophila Schneider 2 cells: A potential expression system for large-scale production of G protein coupled receptors
    • Perret, B. G., Wagner, R., Lecat, S., Brillet, K., Rabut, G., Bucher, B. and Pattus, F. (2003) Expression of EGFP-amino-tagged human mu opioid receptor in Drosophila Schneider 2 cells: a potential expression system for large-scale production of G protein coupled receptors. Protein Expr. Purif. 31, 123-132.
    • (2003) Protein Expr. Purif. , vol.31 , pp. 123-132
    • Perret, B.G.1    Wagner, R.2    Lecat, S.3    Brillet, K.4    Rabut, G.5    Bucher, B.6    Pattus, F.7
  • 47
  • 49
    • 0026691409 scopus 로고
    • Expression of a cloned gamma-aminobutyric acid transporter in mammalian cells
    • Keynan, S., Suh, Y. J., Kanner, B. I. and Rudnick, G. (1992) Expression of a cloned gamma-aminobutyric acid transporter in mammalian cells. Biochemistry 31, 1974-1979.
    • (1992) Biochemistry , vol.31 , pp. 1974-1979
    • Keynan, S.1    Suh, Y.J.2    Kanner, B.I.3    Rudnick, G.4
  • 50
    • 0026611075 scopus 로고
    • + channels expressed transiently in human embryonic kidney cells: Biochemical and biophysical properties
    • + channels expressed transiently in human embryonic kidney cells: biochemical and biophysical properties. Neuron 8, 663-676.
    • (1992) Neuron , vol.8 , pp. 663-676
    • Ukomadu, C.1    Zhou, J.2    Sigworth, F.J.3    Agnew, W.S.4
  • 51
    • 0026773808 scopus 로고
    • Subcellular distribution and activity of glucose transporter isoforms GLUT1 and GLUT4 transiently expressed in COS-7 cells
    • Schurmann, A., Monden, I., Joost, H. G. and Keller, K. (1992) Subcellular distribution and activity of glucose transporter isoforms GLUT1 and GLUT4 transiently expressed in COS-7 cells. Biochim. Biophys. Acta 1131, 245-252.
    • (1992) Biochim. Biophys. Acta , vol.1131 , pp. 245-252
    • Schurmann, A.1    Monden, I.2    Joost, H.G.3    Keller, K.4
  • 52
    • 14844304726 scopus 로고    scopus 로고
    • Transient transfection of CHO-K1-S using serum-free medium in suspension: A rapid mammalian protein expression system
    • Rosser, M. P., Xia, W., Hartsell, S., McCaman, M., Zhu, Y., Wang, S., Harvey, S., Bringmann, P. and Cobb, R. R. (2005) Transient transfection of CHO-K1-S using serum-free medium in suspension: a rapid mammalian protein expression system. Protein Expr. Purif. 40, 237-243.
    • (2005) Protein Expr. Purif. , vol.40 , pp. 237-243
    • Rosser, M.P.1    Xia, W.2    Hartsell, S.3    McCaman, M.4    Zhu, Y.5    Wang, S.6    Harvey, S.7    Bringmann, P.8    Cobb, R.R.9
  • 53
    • 0037109080 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: A tetracycline-inducible system in stable mammalian cell lines for high-level expression of opsin mutants
    • Reeves, P. J., Kim, J. M. and Khorana, H. G. (2002) Structure and function in rhodopsin: a tetracycline-inducible system in stable mammalian cell lines for high-level expression of opsin mutants. Proc. Natl. Acad. Sci. USA 99, 13413-13418.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 13413-13418
    • Reeves, P.J.1    Kim, J.M.2    Khorana, H.G.3
  • 54
    • 0026509349 scopus 로고
    • Stable overexpression of human beta 2-adrenergic receptors in mammalian cells
    • Lohse, M. J. (1992) Stable overexpression of human beta 2-adrenergic receptors in mammalian cells. Naunyn Schmiedebergs Arch. Pharmacol. 345, 444-451
    • (1992) Naunyn Schmiedebergs Arch. Pharmacol. , vol.345 , pp. 444-451
    • Lohse, M.J.1
  • 55
    • 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 DC. (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
  • 56
    • 6344294305 scopus 로고    scopus 로고
    • Gene therapy applications of viral vectors
    • Lundstrom, K. (2004) Gene therapy applications of viral vectors. Technol. Cancer Res. Treat. 3, 467-477.
    • (2004) Technol. Cancer Res. Treat. , vol.3 , pp. 467-477
    • Lundstrom, K.1
  • 57
    • 2942532491 scopus 로고    scopus 로고
    • Transient overexpression of kappa and mu opioid receptors using recombinant adenovirus vectors
    • Zhen, Z., Bradel-Tretheway, B. G., Drewhurst, S. and Bidlack, J. M. (2004) Transient overexpression of kappa and mu opioid receptors using recombinant adenovirus vectors. J. Neurosci. Methods 136, 133-139.
    • (2004) J. Neurosci. Methods , vol.136 , pp. 133-139
    • Zhen, Z.1    Bradel-Tretheway, B.G.2    Drewhurst, S.3    Bidlack, J.M.4
  • 58
    • 0031018004 scopus 로고    scopus 로고
    • Potentiation of beta-adrenergic signaling by adenoviral-mediated gene transfer in adult rabbit ventricular myocytes
    • Drazner, M. H., Peppel, K. C., Dyer, S., Grant, A. O., Koch, W. J. and Lefkowitz, R. J. (1997) Potentiation of beta-adrenergic signaling by adenoviral-mediated gene transfer in adult rabbit ventricular myocytes. J. Clin. Invest. 99, 288-296.
    • (1997) J. Clin. Invest. , vol.99 , pp. 288-296
    • Drazner, M.H.1    Peppel, K.C.2    Dyer, S.3    Grant, A.O.4    Koch, W.J.5    Lefkowitz, R.J.6
  • 61
    • 0029996147 scopus 로고    scopus 로고
    • In vivo gene delivery and stable transduction of nondividing cells by a lentiviral vector
    • Naldini, L., Blomer, U., Gallay, P., Ory, D., Mulligan, R., Gage, F. H., Verma, I. M. and Trono, D. (1996) In vivo gene delivery and stable transduction of nondividing cells by a lentiviral vector. Science 272, 263-267.
    • (1996) Science , vol.272 , pp. 263-267
    • Naldini, L.1    Blomer, U.2    Gallay, P.3    Ory, D.4    Mulligan, R.5    Gage, F.H.6    Verma, I.M.7    Trono, D.8
  • 62
  • 63
    • 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
  • 64
    • 0037305599 scopus 로고    scopus 로고
    • Protein expression systems for structural genomics and proteomics
    • Yokoyama, S. (2003) Protein expression systems for structural genomics and proteomics. Curr. Opin. Chem. Biol. 7, 39-43.
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 39-43
    • Yokoyama, S.1
  • 66
    • 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
  • 67
    • 0035815078 scopus 로고    scopus 로고
    • Receptor-G fusion proteins as a tool for ligand screening
    • Guo, Z. D., Suga, H., Okamura, M., Takeda, S. and Haga, T. (2001) Receptor-G fusion proteins as a tool for ligand screening. Life Sci. 68, 2319-2327.
    • (2001) Life Sci. , vol.68 , pp. 2319-2327
    • Guo, Z.D.1    Suga, H.2    Okamura, M.3    Takeda, S.4    Haga, T.5
  • 68
    • 0033631386 scopus 로고    scopus 로고
    • Expression of functional M2 muscarinic acetylcholine receptor in Escherichia coli
    • Furukawa, H. and Haga, T. (2000) Expression of functional M2 muscarinic acetylcholine receptor in Escherichia coli. J. Biochem. 127, 151-161.
    • (2000) J. Biochem. , vol.127 , pp. 151-161
    • Furukawa, H.1    Haga, T.2
  • 69
    • 0035984890 scopus 로고    scopus 로고
    • Functional reconstitution of purified metabotropic glutamate receptor expressed in the fly eye
    • Eroglu, C., Cronet, P., Panneels, P., 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. , vol.3 , pp. 491-496
    • Eroglu, C.1    Cronet, P.2    Panneels, P.3    Beaufils, P.4    Sinning, I.5
  • 70
    • 27644550921 scopus 로고    scopus 로고
    • Expression of functional G protein-coupled receptors in photoreceptors of transgenic Xenopus laevis
    • Zhang, L., Salom, D., He, J., Okun, A., Ballesteros, J., Palczewski, K. and Li, N. (2005) Expression of functional G protein-coupled receptors in photoreceptors of transgenic Xenopus laevis. Biochemistry 44, 14509-14518.
    • (2005) Biochemistry , vol.44 , pp. 14509-14518
    • Zhang, L.1    Salom, D.2    He, J.3    Okun, A.4    Ballesteros, J.5    Palczewski, K.6    Li, N.7
  • 71
    • 0031740283 scopus 로고    scopus 로고
    • How lipids interact with an intrinsic membrane protein: The case of the calcium pump
    • Lee, A. G. (1998) How lipids interact with an intrinsic membrane protein: the case of the calcium pump. Biochim. Biophys. Acta 1376, 381-390.
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 381-390
    • Lee, A.G.1
  • 73
    • 33751293464 scopus 로고    scopus 로고
    • Solubilization and purification of membrane proteins
    • (Lundstrom, K., Ed.), CRC, Boca Raton
    • Byrne, B. and Jormakka, M. (2006) Solubilization and purification of membrane proteins. In: Structural Genomics on Membrane Proteins (Lundstrom, K., Ed.), pp. 179-198. CRC, Boca Raton.
    • (2006) Structural Genomics on Membrane Proteins , pp. 179-198
    • Byrne, B.1    Jormakka, M.2
  • 74
    • 0342378077 scopus 로고    scopus 로고
    • One-step purification of histidine-tagged cytochrome bo3 from Escherichia coli and demonstration that associated quinone is not required for the structural integrity of the oxidase
    • Rumbley, J. N., Furlong Nickels, E. and Gennis, R. B. (1997) One-step purification of histidine-tagged cytochrome bo3 from Escherichia coli and demonstration that associated quinone is not required for the structural integrity of the oxidase. Biochim. Biophys. Acta 1340, 131-142.
    • (1997) Biochim. Biophys. Acta , vol.1340 , pp. 131-142
    • Rumbley, J.N.1    Furlong Nickels, E.2    Gennis, R.B.3
  • 76
    • 33751291577 scopus 로고    scopus 로고
    • Membrane protein NMR
    • (Lundstrom, K., Ed.), CRC, Boca Raton
    • Xie, X.-Q. (2006) Membrane protein NMR. In: Structural Genomics on Membrane Proteins (Lundstrom, K., Ed.), pp. 211-259. CRC, Boca Raton.
    • (2006) Structural Genomics on Membrane Proteins , pp. 211-259
    • Xie, X.-Q.1
  • 77
    • 47049102965 scopus 로고    scopus 로고
    • Toward crystallization of G protein-coupled receptors
    • (Lundstrom, K. and Chiu, M.L., Eds), CRC, Boca Raton
    • Chiu, M. L. and MacWilliams, M. P. (2006) Toward crystallization of G protein-coupled receptors. In: G Protein-Coupled Receptors in Drug Discovery (Lundstrom, K. and Chiu, M.L., Eds), pp. 271-296. CRC, Boca Raton.
    • (2006) G Protein-Coupled Receptors in Drug Discovery , pp. 271-296
    • Chiu, M.L.1    MacWilliams, M.P.2
  • 78
    • 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
  • 79
    • 0027686674 scopus 로고
    • Structure at 2.5 A of a designed peptide that maintains solubility of membrane proteins
    • Schafmeister, C. E., Miercke, L. J. and Stroud, R. M. (1993) Structure at 2.5 A of a designed peptide that maintains solubility of membrane proteins. Science 262, 734-738.
    • (1993) Science , vol.262 , pp. 734-738
    • Schafmeister, C.E.1    Miercke, L.J.2    Stroud, R.M.3
  • 80
    • 0030451437 scopus 로고    scopus 로고
    • Amphipols: Polymers that keep membrane proteins soluble in aqueous solutions
    • Tribet, C., Audebert, R. and Popot, J. L. (1996) Amphipols: polymers that keep membrane proteins soluble in aqueous solutions. Proc. Natl. Acad. Sci. USA 93, 15047-15050.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 15047-15050
    • Tribet, C.1    Audebert, R.2    Popot, J.L.3
  • 82
    • 0029992660 scopus 로고    scopus 로고
    • Lipidic cubic phases: A novel concept for the crystallization of membrane proteins
    • Landau, E. M. and Rosenbusch, J. P. (1996) Lipidic cubic phases: a novel concept for the crystallization of membrane proteins. Proc. Natl. Acad. Sci. USA 93, 14532-14535.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14532-14535
    • Landau, E.M.1    Rosenbusch, J.P.2
  • 85
    • 0029836953 scopus 로고    scopus 로고
    • Discovering high affinity ligands for proteins: SAR by NMR
    • Shuker, S. B., Hajduk, P. J., Meadows, R. P. and Fesik, S. W. (1996) Discovering high affinity ligands for proteins: SAR by NMR. Science 274, 1531-1534.
    • (1996) Science , vol.274 , pp. 1531-1534
    • Shuker, S.B.1    Hajduk, P.J.2    Meadows, R.P.3    Fesik, S.W.4
  • 86
    • 0032710475 scopus 로고    scopus 로고
    • NMR techniques for characterization of ligand binding: Utility for lead generation and optimization in drug discovery
    • Moore, J. M. (1999) NMR techniques for characterization of ligand binding: utility for lead generation and optimization in drug discovery. Biopolymers 51, 221-243.
    • (1999) Biopolymers , vol.51 , pp. 221-243
    • Moore, J.M.1
  • 87
    • 0036365716 scopus 로고    scopus 로고
    • Applications of NMR to structure-based drug design in structural genomics
    • Powers, R. (2002) Applications of NMR to structure-based drug design in structural genomics. J. Struct. Funct. Genom. 2, 113-123.
    • (2002) J. Struct. Funct. Genom. , vol.2 , pp. 113-123
    • Powers, R.1
  • 88
    • 33751266160 scopus 로고    scopus 로고
    • Electron microscopy and atomic force microscopy of reconstituted membrane proteins
    • (Lundstrom, K., Ed.), CRC, Boca Raton
    • Engel, A. (2006) Electron microscopy and atomic force microscopy of reconstituted membrane proteins. In: Structural Genomics on Membrane Proteins (Lundstrom, K., Ed.), pp. 300-320. CRC, Boca Raton.
    • (2006) Structural Genomics on Membrane Proteins , pp. 300-320
    • Engel, A.1
  • 89
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryomicroscopy
    • Henderson, R., Baldwin, J. M., Ceska, T. A., Zemlin, F., Beckmann, E. and Downing, K. H. (1990) Model for the structure of bacteriorhodopsin based on high-resolution electron cryomicroscopy. J. Mol. Biol. 213, 899-929.
    • (1990) J. Mol. Biol. , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckmann, E.5    Downing, K.H.6
  • 93
    • 14844330221 scopus 로고    scopus 로고
    • Structural studies by electron tomography: From cells to molecules
    • Lucic, V., Forster, F. and Baumeister, W. (2005) Structural studies by electron tomography: from cells to molecules. Annu. Rev. Biochem. 74, 833-865.
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 833-865
    • Lucic, V.1    Forster, F.2    Baumeister, W.3
  • 94
    • 22544445550 scopus 로고    scopus 로고
    • High-yield expression, reconstitution and structure of the recombinant, fully functional glutamate transporter GLT-1 from Rattus norvegicus
    • Raunser, S., Haase, W., Bostina, M., Parcej, D. N. and Kuhlbrandt, W. (2005) High-yield expression, reconstitution and structure of the recombinant, fully functional glutamate transporter GLT-1 from Rattus norvegicus. J. Mol. Biol. 351, 598-613.
    • (2005) J. Mol. Biol. , vol.351 , pp. 598-613
    • Raunser, S.1    Haase, W.2    Bostina, M.3    Parcej, D.N.4    Kuhlbrandt, W.5
  • 95
    • 18044397545 scopus 로고    scopus 로고
    • Progress of structural genomics initiatives: An analysis of solved target structures
    • Todd, A. E., Marsden, R. L., Thornton, J. M. and Orengo, C. A. (2005) Progress of structural genomics initiatives: an analysis of solved target structures. J. Mol. Biol. 348, 1235-1260.
    • (2005) J. Mol. Biol. , vol.348 , pp. 1235-1260
    • Todd, A.E.1    Marsden, R.L.2    Thornton, J.M.3    Orengo, C.A.4
  • 96
    • 0033979165 scopus 로고    scopus 로고
    • Engineering of a proteolytically stable human beta 2-adrenergic receptor/maltose-binding protein fusion and production of the chimeric protein in Escherichia coli and baculovirus-infected insect cells
    • Hampe, W., Voss, R. H., Haase, W., Boege, F., Michel, H. and Reilander, H. (2000) Engineering of a proteolytically stable human beta 2-adrenergic receptor/maltose-binding protein fusion and production of the chimeric protein in Escherichia coli and baculovirus-infected insect cells. Biotechnology 77, 219-234.
    • (2000) Biotechnology , vol.77 , pp. 219-234
    • Hampe, W.1    Voss, R.H.2    Haase, W.3    Boege, F.4    Michel, H.5    Reilander, H.6
  • 97
    • 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, 121-133.
    • (1990) Science , vol.250 , pp. 121-133
    • King, K.1    Dohlman, H.G.2    Thorner, J.3    Caron, M.G.4    Lefkowitz, R.J.5
  • 98
    • 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, 1137-1147.
    • (1998) Biochem. J. , vol.330 , pp. 1137-1147
    • Weiss, H.M.1    Haase, W.2    Michel, H.3    Reilander, H.4
  • 100
    • 0348196650 scopus 로고    scopus 로고
    • Functional expression and direct visualization of the human alpha 2B-adrenergic receptor and alpha 2B-AR-green fluorescent fusion protein in mammalian cell using Semliki Forest virus vectors
    • Sen, S., Jaakola, V. P., Heimo, H., Engstrom, M., Larjomaa, P., Scheinin, M., Lundstrom, K. and Goldman, A. (2003) Functional expression and direct visualization of the human alpha 2B-adrenergic receptor and alpha 2B-AR-green fluorescent fusion protein in mammalian cell using Semliki Forest virus vectors. Protein Expr. Purif. 32, 265-275.
    • (2003) Protein Expr. Purif. , vol.32 , pp. 265-275
    • Sen, S.1    Jaakola, V.P.2    Heimo, H.3    Engstrom, M.4    Larjomaa, P.5    Scheinin, M.6    Lundstrom, K.7    Goldman, A.8
  • 101
    • 0028104820 scopus 로고
    • Phosphorylation and palmitoylation of the human D2L dopamine receptor in Sf9 cells
    • Ng, G. Y., O'Dowd, B. F., Caron, M., Dennis, M., Brann, M. R. and George, S. R. (1994) Phosphorylation and palmitoylation of the human D2L dopamine receptor in Sf9 cells. J. Neurochem. 63, 1589-1595.
    • (1994) J. Neurochem. , vol.63 , pp. 1589-1595
    • Ng, G.Y.1    O'Dowd, B.F.2    Caron, M.3    Dennis, M.4    Brann, M.R.5    George, S.R.6
  • 102
    • 0031595788 scopus 로고    scopus 로고
    • Mapping of dopamine D3 receptor binding site by pharmacological characterization of mutants expressed in CHO cells with the Semliki Forest virus system
    • Lundstrom, K., Turpin, M. P., Large, C., Robertson, G., Thomas, P. and Lewell, X. Q. (1998) Mapping of dopamine D3 receptor binding site by pharmacological characterization of mutants expressed in CHO cells with the Semliki Forest virus system. J. Recept. Signal Transduct. Res. 18, 133-150.
    • (1998) J. Recept. Signal Transduct. Res. , vol.18 , pp. 133-150
    • Lundstrom, K.1    Turpin, M.P.2    Large, C.3    Robertson, G.4    Thomas, P.5    Lewell, X.Q.6
  • 103
    • 0028095456 scopus 로고
    • High-level expression of functional glutamate receptor channels in insect cells
    • Keinanen, K., Kohr, G., Seeburg, P. H., Laukkanen, M. L. and Oker-Blom, C. (1994) High-level expression of functional glutamate receptor channels in insect cells. Biotechnology 12, 802-806.
    • (1994) Biotechnology , vol.12 , pp. 802-806
    • Keinanen, K.1    Kohr, G.2    Seeburg, P.H.3    Laukkanen, M.L.4    Oker-Blom, C.5
  • 104
    • 0035860530 scopus 로고    scopus 로고
    • Recombinant Semliki Forest virus for overexpression and pharmacological characterisation of the histamine H(2) receptor in mammalian cells
    • Hoffmann, M., Verzijl, D., Lundstrom, K., Simmen, U., Alewijnse, A. E., Timmerman, H. and Leurs, R. (2001) Recombinant Semliki Forest virus for overexpression and pharmacological characterisation of the histamine H(2) receptor in mammalian cells. Eur. J. Pharmacol. 427, 105-114.
    • (2001) Eur. J. Pharmacol. , vol.427 , pp. 105-114
    • Hoffmann, M.1    Verzijl, D.2    Lundstrom, K.3    Simmen, U.4    Alewijnse, A.E.5    Timmerman, H.6    Leurs, R.7
  • 106
    • 0037048801 scopus 로고    scopus 로고
    • Green fluorescent protein as a reporter of human mu-opioid receptor overexpression and localization in the methylotrophic yeast Pichia pastoris
    • Sarramegna, V., Talmont, F., Seree de Roch, M., Milon, A. and Demange, P. (2002) Green fluorescent protein as a reporter of human mu-opioid receptor overexpression and localization in the methylotrophic yeast Pichia pastoris. J. Biotechnol. 99, 23-39.
    • (2002) J. Biotechnol. , vol.99 , pp. 23-39
    • Sarramegna, V.1    Talmont, F.2    Seree De Roch, M.3    Milon, A.4    Demange, P.5
  • 107
    • 0031610110 scopus 로고    scopus 로고
    • Expression of an integral membrane protein, the 5HT5A receptor
    • Weiss, H. M., Haase, W. and Reilander, H. (1998) Expression of an integral membrane protein, the 5HT5A receptor. Methods Mol. Biol. 103, 227-239
    • (1998) Methods Mol. Biol. , vol.103 , pp. 227-239
    • Weiss, H.M.1    Haase, W.2    Reilander, H.3
  • 108
    • 0028978242 scopus 로고
    • Expression of the human 5-hydroxytryptamine1A receptor in Sf9 cells: Reconstitution of a coupled phenotype by co-expression of mammalian G protein subunits
    • Butkerait, P., Zheng, Y., Hallak, H., Graham, T. E., Miller, H. A., Burris, K. D., Molinoff, P. B. and Manning, D. R. (1995) Expression of the human 5-hydroxytryptamine1A receptor in Sf9 cells: reconstitution of a coupled phenotype by co-expression of mammalian G protein subunits. J. Biol. Chem. 270, 18691-18699.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18691-18699
    • Butkerait, P.1    Zheng, Y.2    Hallak, H.3    Graham, T.E.4    Miller, H.A.5    Burris, K.D.6    Molinoff, P.B.7    Manning, D.R.8
  • 110
    • 0028216257 scopus 로고
    • Expression of thyrotropin-releasing hormone receptors by adenovirus-mediated gene transfer reveals that thyrotropin-releasing hormone desensitization is cell specific
    • Falck-Pedersen, E., Heinflink, M., Alvira, M., Nussenzveig, D. R. and Gershengorn, M. C. (1994) Expression of thyrotropin-releasing hormone receptors by adenovirus-mediated gene transfer reveals that thyrotropin-releasing hormone desensitization is cell specific. Mol. Pharmacol. 45, 684-689.
    • (1994) Mol. Pharmacol. , vol.45 , pp. 684-689
    • Falck-Pedersen, E.1    Heinflink, M.2    Alvira, M.3    Nussenzveig, D.R.4    Gershengorn, M.C.5
  • 111
    • 0035543199 scopus 로고    scopus 로고
    • The expression of soluble, full-length, recombinant human TSH receptor in a prokaryotic system
    • Busuttil, B. E., Turney, K. L. and Frauman, A. G. (2001) The expression of soluble, full-length, recombinant human TSH receptor in a prokaryotic system. Protein Expr. Purif. 23, 369-673.
    • (2001) Protein Expr. Purif. , vol.23 , pp. 369-673
    • Busuttil, B.E.1    Turney, K.L.2    Frauman, A.G.3


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