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Volumn 11, Issue 2, 2007, Pages 224-238

Structural genomics and drug discovery: Molecular Pharmacology

Author keywords

Drug discovery; Electron microscopy; Nuclear magnetic resonance; Protein purification; Recombinant protein expression; Structural genomics; Structure determination; Structure based drug design; X ray crystallography

Indexed keywords

PROTEIN; RECOMBINANT PROTEIN;

EID: 34247893770     PISSN: 15821838     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1582-4934.2007.00028.x     Document Type: Review
Times cited : (70)

References (112)
  • 1
    • 6444234760 scopus 로고    scopus 로고
    • The role of the medicinal chemistry in drug discovery - Then and now
    • Lombardino JG, Love III. JA. The role of the medicinal chemistry in drug discovery - then and now. Nat Rev Drug Discov. 2004 3 : 853 62.
    • (2004) Nat Rev Drug Discov. , vol.3 , pp. 853-62
    • Lombardino, J.G.1    Loveiii., J.A.2
  • 2
    • 34247849961 scopus 로고    scopus 로고
    • Michel H. http://www.mpibp-frankfurt.mpg.de/michel/ public/memprotstruct. html.
    • Michel, H.1
  • 3
    • 28044444551 scopus 로고    scopus 로고
    • The future of G protein-coupled receptors as targets in drug discovery
    • Lundstrom K. The future of G protein-coupled receptors as targets in drug discovery. Idrugs. 2005 8 : 909 13.
    • (2005) Idrugs. , vol.8 , pp. 909-13
    • Lundstrom, K.1
  • 4
    • 0016657917 scopus 로고
    • Solubilization of membranes by detergents
    • Helenius A, Simons K. Solubilization of membranes by detergents. Biochim Biophys Acta. 1975 415 : 29 79.
    • (1975) Biochim Biophys Acta. , vol.415 , pp. 29-79
    • Helenius, A.1    Simons, K.2
  • 5
    • 0037391134 scopus 로고    scopus 로고
    • Membrane protein structural biology: The high throughput challenge
    • Loll PJ. Membrane protein structural biology: the high throughput challenge. J Struct Biol. 2003 142 : 144 53.
    • (2003) J Struct Biol. , vol.142 , pp. 144-53
    • Loll, P.J.1
  • 7
    • 0030574268 scopus 로고    scopus 로고
    • Structure-based drug design
    • Blundell TL. Structure-based drug design. Nature. 1996 : 384S : 23 6.
    • (1996) Nature. , vol.384 , pp. 23-6
    • Blundell, T.L.1
  • 8
    • 0033787344 scopus 로고    scopus 로고
    • Science, art and drug discovery: A personal perspective
    • Campbell SF. Science, art and drug discovery: a personal perspective. Clin Sci. 2000 99 : 255 60.
    • (2000) Clin Sci. , vol.99 , pp. 255-60
    • Campbell, S.F.1
  • 9
    • 15944394229 scopus 로고    scopus 로고
    • High-throughput X-ray crystal-lography for drug discovery
    • Blundell TL, Patel S. High-throughput X-ray crystal-lography for drug discovery. Curr Opin Pharmacol. 2004 4 : 490 6.
    • (2004) Curr Opin Pharmacol. , vol.4 , pp. 490-6
    • Blundell, T.L.1    Patel, S.2
  • 11
    • 0036051992 scopus 로고    scopus 로고
    • High throughput crystallography for lead discovery in drug design
    • Blundell TL, Jhoti H, Abell C. High throughput crystallography for lead discovery in drug design. Nat Rev Drug Discov. 2002 1 : 45 54.
    • (2002) Nat Rev Drug Discov. , vol.1 , pp. 45-54
    • Blundell, T.L.1    Jhoti, H.2    Abell, C.3
  • 15
    • 0348227698 scopus 로고    scopus 로고
    • The impact of structure-guided drug design on clinical agents
    • Hardy LW, Malikayil A. The impact of structure-guided drug design on clinical agents. Curr Drug Discov. 2003 3 : 15 20.
    • (2003) Curr Drug Discov. , vol.3 , pp. 15-20
    • Hardy, L.W.1    Malikayil, A.2
  • 17
    • 0032996584 scopus 로고    scopus 로고
    • Development of neuroaminidase inhibitors as anti-influenza virus drugs
    • Varghese JN. Development of neuroaminidase inhibitors as anti-influenza virus drugs. Drug Dev Res. 1999 46 : 176 96.
    • (1999) Drug Dev Res. , vol.46 , pp. 176-96
    • Varghese, J.N.1
  • 19
    • 27844553839 scopus 로고    scopus 로고
    • AKT crystal structure and AKT-specific inhibitors
    • Kumar CC, Madison V. AKT crystal structure and AKT-specific inhibitors. Oncogene. 2005 24 : 7493 501.
    • (2005) Oncogene. , vol.24 , pp. 7493-501
    • Kumar, C.C.1    Madison, V.2
  • 20
    • 0033522211 scopus 로고    scopus 로고
    • Tissue distribution of phosphodiesterase families and the effects of sildenafil on tissue cyclic nucleotides, platelet function, and the contractile responses of trabeculae carneae and aortic rings in vitro
    • Wallis RM, Corbin JD, Francis SH, Ellis P. Tissue distribution of phosphodiesterase families and the effects of sildenafil on tissue cyclic nucleotides, platelet function, and the contractile responses of trabeculae carneae and aortic rings in vitro. Am J Cardiol. 1999 83 : 3C 12C.
    • (1999) Am J Cardiol. , vol.83
    • Wallis, R.M.1    Corbin, J.D.2    Francis, S.H.3    Ellis, P.4
  • 21
    • 13944274948 scopus 로고    scopus 로고
    • The past, present and future of cell-free protein synthesis
    • Katzen F, Chang G, Kudlicki W. The past, present and future of cell-free protein synthesis. Trends Biotechnol. 2005 23 : 150 6.
    • (2005) Trends Biotechnol. , vol.23 , pp. 150-6
    • Katzen, F.1    Chang, G.2    Kudlicki, W.3
  • 22
    • 0037305599 scopus 로고    scopus 로고
    • Protein expression systems for structural genomics and proteomics
    • Yokoyama S. Protein expression systems for structural genomics and proteomics. Curr Opin Chem Biol. 2003 7 : 39 43.
    • (2003) Curr Opin Chem Biol. , vol.7 , pp. 39-43
    • Yokoyama, S.1
  • 24
    • 15744391469 scopus 로고    scopus 로고
    • Expression of G protein coupled receptors in a cell-free translational system using detergents and thioredoxinfusion vectors
    • Ishihara G, Goto M, Saeki M, Ito K, Hori T, Kigawa T, Shirouzu M, Yokoyama S. Expression of G protein coupled receptors in a cell-free translational system using detergents and thioredoxinfusion vectors. Prot Expr Purif. 2005 41 : 27 37.
    • (2005) Prot 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
  • 25
    • 29344450131 scopus 로고    scopus 로고
    • X-ray structure of the EmrE multidrug transporter in complex with a substrate
    • Pornillos O, Chen YJ, Chen AP, Chang G. X-ray structure of the EmrE multidrug transporter in complex with a substrate. Science. 2005 310 : 1950 3.
    • (2005) Science. , vol.310 , pp. 1950-3
    • Pornillos, O.1    Chen, Y.J.2    Chen, A.P.3    Chang, G.4
  • 26
    • 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, Walker JE. 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. 1996 260 : 289 98.
    • (1996) J Mol Biol. , vol.260 , pp. 289-98
    • Miroux, B.1    Walker, J.E.2
  • 28
    • 0029838532 scopus 로고    scopus 로고
    • Purification of a rat neurotensin receptor expressed in Escherichia coli
    • Tucker J, Grisshammer R. Purification of a rat neurotensin receptor expressed in Escherichia coli. Biochem J. 1996 317 : 891 9.
    • (1996) Biochem J. , vol.317 , pp. 891-9
    • Tucker, J.1    Grisshammer, R.2
  • 29
    • 12244292640 scopus 로고    scopus 로고
    • Purification and characterization of the human adenosine A(2a) receptor functionally expressed in Escherichia coli
    • Weiss HM, Grisshammer R. Purification and characterization of the human adenosine A(2a) receptor functionally expressed in Escherichia coli. Eur J Biochem. 2002 269 : 82 92.
    • (2002) Eur J Biochem. , vol.269 , pp. 82-92
    • Weiss, H.M.1    Grisshammer, R.2
  • 30
    • 33746813576 scopus 로고    scopus 로고
    • Understanding recombinant expression of membrane proteins
    • Grisshammer R. Understanding recombinant expression of membrane proteins. Curr Opin Biotechnol. 2006 17 : 337 40.
    • (2006) Curr Opin Biotechnol. , vol.17 , pp. 337-40
    • Grisshammer, R.1
  • 31
    • 0037450517 scopus 로고    scopus 로고
    • In vitro folding of alpha-helical membrane proteins
    • Kiefer H. In vitro folding of alpha-helical membrane proteins. Biochim Biophys Acta. 2003 1610 : 57 62.
    • (2003) Biochim Biophys Acta. , vol.1610 , pp. 57-62
    • Kiefer, H.1
  • 32
    • 0037518197 scopus 로고    scopus 로고
    • The isolated N-terminal domain of the glucagon-like peptide-1 (GLP-1) receptor binds expending peptides with much higher affinity than GLP-1
    • Lopez de Maturana R, Willshaw A, Kuntzsch A, Rudolph R, Donnelly D. The isolated N-terminal domain of the glucagon-like peptide-1 (GLP-1) receptor binds expending peptides with much higher affinity than GLP-1. J Biol Chem. 2003 278 : 10195 200.
    • (2003) J Biol Chem. , vol.278 , pp. 10195-200
    • Lopez De Maturana, R.1    Willshaw, A.2    Kuntzsch, A.3    Rudolph, R.4    Donnelly, D.5
  • 33
    • 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 JL, Martin A, Hullot P, Girard JP, Rossi JC, Parello J. Structure-based analysis of GPCR function: conformational adaptation of both agonist and receptor upon leukotriene B4 binding to recombinant BLT1. J Mol Biol. 2003 329 : 801 14.
    • (2003) J Mol Biol. , vol.329 , pp. 801-14
    • Baneres, J.L.1    Martin, A.2    Hullot, P.3    Girard, J.P.4    Rossi, J.C.5    Parello, J.6
  • 34
    • 20144385917 scopus 로고    scopus 로고
    • Molecular characterization of a purified 5-HT4 receptor: A structural basis for drug efficacy
    • Baneres JL, Mesnier D, Martin A, Joubert L, Dumuis A, Bockaert J. Molecular characterization of a purified 5-HT4 receptor: a structural basis for drug efficacy. J Biol Chem. 2005 280 : 20253 60.
    • (2005) J Biol Chem. , vol.280 , pp. 20253-60
    • Baneres, J.L.1    Mesnier, D.2    Martin, A.3    Joubert, L.4    Dumuis, A.5    Bockaert, J.6
  • 35
    • 0037450575 scopus 로고    scopus 로고
    • Lactococcus lactis as host for overproduction of functional membrane proteins
    • Kunji ER, Slotboom DJ, Poolman B. Lactococcus lactis as host for overproduction of functional membrane proteins. Biochim Biophys Acta. 2003 1610 : 97 108.
    • (2003) Biochim Biophys Acta. , vol.1610 , pp. 97-108
    • Kunji, E.R.1    Slotboom, D.J.2    Poolman, B.3
  • 36
    • 0029757175 scopus 로고    scopus 로고
    • Controlled gene expression systems for Lactococcus lactis with the food-grade inducer nisin
    • de Ruyter PG, Kuipers OP, de Vos WM. Controlled gene expression systems for Lactococcus lactis with the food-grade inducer nisin. Appl Environ Microbiol. 1996 62 : 3662 7.
    • (1996) Appl Environ Microbiol. , vol.62 , pp. 3662-7
    • De Ruyter, P.G.1    Kuipers, O.P.2    De Vos, W.M.3
  • 37
    • 28844468525 scopus 로고    scopus 로고
    • Functional expression of eukaryotic membrane proteins in Lactococcus lactis
    • Monne M, Chan KW, Slotboom DJ, Kunji ER. Functional expression of eukaryotic membrane proteins in Lactococcus lactis. Protein Sci. 2005 14 : 3048 56.
    • (2005) Protein Sci. , vol.14 , pp. 3048-56
    • Monne, M.1    Chan, K.W.2    Slotboom, D.J.3    Kunji, E.R.4
  • 44
    • 0019985965 scopus 로고
    • Synthesis and assembly of hepatitis B virus surface antigen particles in yeast
    • Valenzuela P, Medina A, Rutter WJ, Ammerer G, Hall BD. Synthesis and assembly of hepatitis B virus surface antigen particles in yeast. Nature. 1982 298 : 347 50.
    • (1982) Nature. , vol.298 , pp. 347-50
    • Valenzuela, P.1    Medina, A.2    Rutter, W.J.3    Ammerer, G.4    Hall, B.D.5
  • 45
    • 0021733769 scopus 로고
    • Expression of human alpha 1-antitrypsin cDNA in the yeast Saccharomyces cerevisiae
    • Cabezon T, De Wilde M, Herion P, Loriau R, Bollen A. Expression of human alpha 1-antitrypsin cDNA in the yeast Saccharomyces cerevisiae. Proc Natl Acad Sci USA. 1984 81 : 6594 8.
    • (1984) Proc Natl Acad Sci USA. , vol.81 , pp. 6594-8
    • Cabezon, T.1    De Wilde, M.2    Herion, P.3    Loriau, R.4    Bollen, A.5
  • 47
    • 0024040372 scopus 로고
    • Isolation and characterization of mutants which show an oversecretion phenotype in Saccharomyces cerevisiae
    • Sakai A, Shimizu Y, Hishinuma F. Isolation and characterization of mutants which show an oversecretion phenotype in Saccharomyces cerevisiae. Genetics. 1988 119 : 499 506.
    • (1988) Genetics. , vol.119 , pp. 499-506
    • Sakai, A.1    Shimizu, Y.2    Hishinuma, F.3
  • 48
    • 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 NE, Gee M, Andersen B, Naider F, Thorner J, Stevens RC. Expression and purification of the Saccharomyces cerevisiae alpha-factor receptor (Ste2p), a 7-transmembrane-segment G protein-coupled receptor. J Biol Chem. 1997 272 : 15553 61.
    • (1997) J Biol Chem. , vol.272 , pp. 15553-61
    • David, N.E.1    Gee, M.2    Andersen, B.3    Naider, F.4    Thorner, J.5    Stevens, R.C.6
  • 49
    • 0032081297 scopus 로고    scopus 로고
    • The human D1A dopamine receptor: Heterologous expression in Saccharomyces cerevisiae and purification of the functional receptor
    • Andersen B, Stevens RC. The human D1A dopamine receptor: heterologous expression in Saccharomyces cerevisiae and purification of the functional receptor. Prot Expr Purif. 1998 13 : 111 9.
    • (1998) Prot Expr Purif. , vol.13 , pp. 111-9
    • Andersen, B.1    Stevens, R.C.2
  • 52
    • 0024964627 scopus 로고
    • New expression vectors for the fission yeast Schizosaccharomyces pombe
    • Broker M, Bauml, O. New expression vectors for the fission yeast Schizosaccharomyces pombe. FEBS Lett. 1989 248 : 105 10.
    • (1989) FEBS Lett. , vol.248 , pp. 105-10
    • Broker, M.1    Bauml, O.2
  • 53
    • 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, Michel H. Constitutive expression of the human D2S-dopamine receptor in the unicellular yeast Saccharomyces cerevisiae. Biochim Biophys Acta. 1994 1193 : 255 62.
    • (1994) Biochim Biophys Acta. , vol.1193 , pp. 255-62
    • Sander, P.1    Grunewald, S.2    Maul, G.3    Reilander, H.4    Michel, H.5
  • 54
    • 0032148392 scopus 로고    scopus 로고
    • Pharmacological characterization of the D2 dopamine receptor expressed in the yeast Schizosaccharomyces pombe
    • Presland J, Strange PG. Pharmacological characterization of the D2 dopamine receptor expressed in the yeast Schizosaccharomyces pombe. Biochem Pharmacol. 1998 56 : 577 82.
    • (1998) Biochem Pharmacol. , vol.56 , pp. 577-82
    • Presland, J.1    Strange, P.G.2
  • 55
    • 17244363998 scopus 로고    scopus 로고
    • Heterologous protein production using the Pichia pastoris expression system
    • Macauley-Patrick S, Fazenda ML, McNeil B, Harvey LM. Heterologous protein production using the Pichia pastoris expression system. Yeast. 2005 22 : 249 70.
    • (2005) Yeast. , vol.22 , pp. 249-70
    • MacAuley-Patrick, S.1    Fazenda, M.L.2    McNeil, B.3    Harvey, L.M.4
  • 56
    • 0033955337 scopus 로고    scopus 로고
    • Heterologous protein expression in the methylotrophic yeast Pichia pastoris
    • Cereghino JL, Cregg JM. Heterologous protein expression in the methylotrophic yeast Pichia pastoris. FEMS Microbiol Rev. 2000 24 : 45 66.
    • (2000) FEMS Microbiol Rev. , vol.24 , pp. 45-66
    • Cereghino, J.L.1    Cregg, J.M.2
  • 57
    • 0032052515 scopus 로고    scopus 로고
    • Cloning of clustered Streptomyces viridosporus T7A lignocellulose catabolism genes encoding peroxidase and endoglucanase and their extracellular expression in Pichia pastoris
    • Thomas L, Crawford, DL. Cloning of clustered Streptomyces viridosporus T7A lignocellulose catabolism genes encoding peroxidase and endoglucanase and their extracellular expression in Pichia pastoris. Can J Microbiol. 1998 44 : 364 72.
    • (1998) Can J Microbiol. , vol.44 , pp. 364-72
    • Thomas, L.1    Crawford, D.L.2
  • 58
    • 0029560973 scopus 로고
    • Expression of functional mouse 5-HT5A serotonin receptor in the methylotrophic yeast Pichia pastoris: Pharmacological characterization and localization
    • Weiss HM, Haase W, Michel H, Reilander H. Expression of functional mouse 5-HT5A serotonin receptor in the methylotrophic yeast Pichia pastoris: pharmacological characterization and localization. FEBS Lett. 1995 377 : 451 6.
    • (1995) FEBS Lett. , vol.377 , pp. 451-6
    • Weiss, H.M.1    Haase, W.2    Michel, H.3    Reilander, H.4
  • 59
    • 33646130717 scopus 로고    scopus 로고
    • Expression of membrane proteins in yeast
    • In: K. Lundstrom, editor. Boca Raton: CRC Press. p.
    • Reinhart C, Kettler C. Expression of membrane proteins in yeast. In : K. Lundstrom, editor. Structural genomics on membrane proteins. Boca Raton : CRC Press 2006. p. 115 52.
    • (2006) Structural Genomics on Membrane Proteins. , pp. 115-52
    • Reinhart, C.1    Kettler, C.2
  • 62
    • 0141457531 scopus 로고    scopus 로고
    • Structural characterisation of neuronal voltage-sensitive K+ channels heterologously expressed in Pichia pastoris
    • Parcej DN, Eckhardt-Strelau L. Structural characterisation of neuronal voltage-sensitive K+ channels heterologously expressed in Pichia pastoris. J Mol Biol. 2003 333 : 103 16.
    • (2003) J Mol Biol. , vol.333 , pp. 103-16
    • Parcej, D.N.1    Eckhardt-Strelau, L.2
  • 63
    • 23244456428 scopus 로고    scopus 로고
    • Crystal structure of a mammalian voltage-dependent Shaker family K+ channel
    • Long SB, Campbell EB, MacKinnon R. Crystal structure of a mammalian voltage-dependent Shaker family K+ channel. Science. 2005 309 : 897 903.
    • (2005) Science. , vol.309 , pp. 897-903
    • Long, S.B.1    Campbell, E.B.2    MacKinnon, R.3
  • 64
    • 0033502881 scopus 로고    scopus 로고
    • Generation of baculovirusex-pression vectors
    • Luque T, O'Reilly DR. Generation of baculovirusex-pression vectors. Mol Biotechnol. 1999 13 : 153 63.
    • (1999) Mol Biotechnol. , vol.13 , pp. 153-63
    • Luque, T.1    O'Reilly, D.R.2
  • 65
    • 0034089238 scopus 로고    scopus 로고
    • Baculovirus expression system for expression and characterization of functional recombinant visual pigments
    • Klaassen CHW, De Grip WJ. Baculovirus expression system for expression and characterization of functional recombinant visual pigments. Meth Enzymol. 2000 315 : 12 29.
    • (2000) Meth Enzymol. , vol.315 , pp. 12-29
    • Klaassen, C.H.W.1    De Grip, W.J.2
  • 66
    • 34247879396 scopus 로고    scopus 로고
    • Expression of functional membrane proteins in the baculovirus-insect cell system: Challenges and developments
    • In: K. Lundstrom, editor. Boca Raton: CRC Press. p.
    • Bosman GJ, De Grip WJ. Expression of functional membrane proteins in the baculovirus-insect cell system: challenges and developments. In : K. Lundstrom, editor. Structural genomics on membrane proteins. Boca Raton : CRC Press 2006. p. 153 67.
    • (2006) Structural Genomics on Membrane Proteins. , pp. 153-67
    • Bosman, G.J.1    De Grip, W.J.2
  • 70
    • 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 BG, Wagner R, Lecat S, Brillet K, Rabut G, Pattus F. 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. Prot Expr Purif. 2003 31 : 123 32.
    • (2003) Prot Expr Purif. , vol.31 , pp. 123-32
    • Perret, B.G.1    Wagner, R.2    Lecat, S.3    Brillet, K.4    Rabut, G.5    Pattus, F.6
  • 71
    • 8844270180 scopus 로고    scopus 로고
    • RTP family members induce functional expression of mammalian odorant receptors
    • Saito H, Kubota M, Roberts RW, Chi Q, Matsunami H. RTP family members induce functional expression of mammalian odorant receptors. Cell. 2004 119 : 679 91.
    • (2004) Cell. , vol.119 , pp. 679-91
    • Saito, H.1    Kubota, M.2    Roberts, R.W.3    Chi, Q.4    Matsunami, H.5
  • 73
    • 33744803544 scopus 로고    scopus 로고
    • Vectors for gene expression in mammalian cells
    • In: S.C. Makrides, editor. Amsterdam: Elsevier Science B.V.
    • Makrides SC. Vectors for gene expression in mammalian cells. In : S.C. Makrides, editor. Gene transfer and expression in mammalian cells. Amsterdam : Elsevier Science B.V. 2003 9 26.
    • (2003) Gene Transfer and Expression in Mammalian Cells. , pp. 9-26
    • Makrides, S.C.1
  • 74
    • 0025766560 scopus 로고
    • Characterization of Chinese hamster ovary cells stably transformed by a plasmid with an inducible APRT gene
    • Walter CA, Humphrey RM, Adair GM, Nairn RS. Characterization of Chinese hamster ovary cells stably transformed by a plasmid with an inducible APRT gene. Plasmid. 1991 25 : 208 16.
    • (1991) Plasmid. , vol.25 , pp. 208-16
    • Walter, C.A.1    Humphrey, R.M.2    Adair, G.M.3    Nairn, R.S.4
  • 75
    • 33744457017 scopus 로고    scopus 로고
    • The synthesis and high-level expression of a beta2-adrenergic receptor gene in a tetracycline-inducible stable mammalian cell line
    • Chelikani P, Reeves PJ, Rajbhandary UL, Khorana HG. The synthesis and high-level expression of a beta2-adrenergic receptor gene in a tetracycline-inducible stable mammalian cell line. Protein Sci. 2006 15 : 1433 40.
    • (2006) Protein Sci. , vol.15 , pp. 1433-40
    • Chelikani, P.1    Reeves, P.J.2    Rajbhandary, U.L.3    Khorana, H.G.4
  • 76
    • 0028986773 scopus 로고
    • Properties of a kappa-opioid receptor expressed in CHO cells: Interaction with multiple G-proteins is not specific for any individual G alpha sub-unit and is similar to that of other opioid receptors
    • Prather PL, McGinn TM, Claude PA, Liu-Chen LY, Loh HH, Law PY. Properties of a kappa-opioid receptor expressed in CHO cells: interaction with multiple G-proteins is not specific for any individual G alpha sub-unit and is similar to that of other opioid receptors. Brain Res Mol Brain Res. 1995 29 : 336 46.
    • (1995) Brain Res Mol Brain Res. , vol.29 , pp. 336-46
    • Prather, P.L.1    McGinn, T.M.2    Claude, P.A.3    Liu-Chen, L.Y.4    Loh, H.H.5    Law, P.Y.6
  • 77
    • 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 PJ, Kim JM, Khorana HG. 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. 2002 99 : 13413 8.
    • (2002) Proc Natl Acad Sci USA. , vol.99 , pp. 13413-8
    • Reeves, P.J.1    Kim, J.M.2    Khorana, H.G.3
  • 78
    • 34247894550 scopus 로고    scopus 로고
    • Expression of membrane proteins in mammalian cells
    • In: K. Lundstrom, editor. Boca Raton: CRC Press. p.
    • Lundstrom K. Expression of membrane proteins in mammalian cells. In : K. Lundstrom, editor. Structural genomics on membrane proteins. Boca Raton : CRC Press 2006. p. 169 78.
    • (2006) Structural Genomics on Membrane Proteins. , pp. 169-78
    • Lundstrom, K.1
  • 79
    • 0026585147 scopus 로고
    • High-level expression of the tick-borne encephalitis virus NS1 protein by using an adenovirus-based vector: Protection elicited in a murine model
    • Jacobs SC, Stephenson JR, Wilkinson GW. High-level expression of the tick-borne encephalitis virus NS1 protein by using an adenovirus-based vector: protection elicited in a murine model. J Virol. 1992 66 : 2086 95.
    • (1992) J Virol. , vol.66 , pp. 2086-95
    • Jacobs, S.C.1    Stephenson, J.R.2    Wilkinson, G.W.3
  • 80
    • 2942532491 scopus 로고    scopus 로고
    • Transient overexpression of kappa and mu opioid receptors using recombinant adenovirus vectors
    • Zhen Z, Bradel-Tretheway BG, Drewhurst S, Bidlack JM. Transient overexpression of kappa and mu opioid receptors using recombinant adenovirus vectors. J Neurosci Methods. 2004 136 : 133 9.
    • (2004) J Neurosci Methods. , vol.136 , pp. 133-9
    • Zhen, Z.1    Bradel-Tretheway, B.G.2    Drewhurst, S.3    Bidlack, J.M.4
  • 81
    • 0031018004 scopus 로고    scopus 로고
    • Potentiation of beta-adrenergic signaling by adenoviral-mediated gene transfer in adult rabbit ventricular myocytes
    • Drazner MH, Peppel KC, Dyer S, Grant AO, Koch WJ, Lefkowitz RJ. Potentiation of beta-adrenergic signaling by adenoviral-mediated gene transfer in adult rabbit ventricular myocytes. J Clin Invest. 1997 99 : 288 96.
    • (1997) J Clin Invest. , vol.99 , pp. 288-96
    • Drazner, M.H.1    Peppel, K.C.2    Dyer, S.3    Grant, A.O.4    Koch, W.J.5    Lefkowitz, R.J.6
  • 82
    • 0000233999 scopus 로고
    • Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase
    • Niles EG, Studier FW, Moss B. Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase. Proc Natl Acad Sci USA. 1986 83 : 8122 6.
    • (1986) Proc Natl Acad Sci USA. , vol.83 , pp. 8122-6
    • Niles, E.G.1    Studier, F.W.2    Moss, B.3
  • 83
    • 0005601726 scopus 로고    scopus 로고
    • Mammalian expression systems and vaccination
    • In: Ring, C.J.A., Blair, E.D., editors. Oxford: BIOS Scientific Publishers Ltd. p.
    • Carroll MW, Wilkinson GWG, Lundstrom K. Mammalian expression systems and vaccination. In : Ring C.J.A., Blair E.D., editors. Genetically engineered viruses. Oxford : BIOS Scientific Publishers Ltd 2001. p. 107 57.
    • (2001) Genetically Engineered Viruses. , pp. 107-57
    • Carroll, M.W.1    Wilkinson, G.W.G.2    Lundstrom, K.3
  • 86
    • 36148996186 scopus 로고    scopus 로고
    • Virus-based vectors for gene expression in mammalian cells: Lentiviruses
    • In: Makrides, S.C., editor. Amsterdam: Elsevier Science B.V. p.
    • Gasmi M, Wong-Staal F. Virus-based vectors for gene expression in mammalian cells: lentiviruses. In : Makrides S.C., editor. Gene transfer in mammalian cells. Amsterdam : Elsevier Science B.V. 2003. p. 251 64.
    • (2003) Gene Transfer in Mammalian Cells. , pp. 251-64
    • Gasmi, M.1    Wong-Staal, F.2
  • 88
    • 14744304517 scopus 로고
    • A new generation of animal cell expression vectors based on the Semliki Forest virus replicon
    • Liljestrom P, Garoff H. A new generation of animal cell expression vectors based on the Semliki Forest virus replicon. Biotechnology (N Y). 1991 9 : 1356 61.
    • (1991) Biotechnology (N Y). , vol.9 , pp. 1356-61
    • Liljestrom, P.1    Garoff, H.2
  • 89
    • 0037450521 scopus 로고    scopus 로고
    • Semliki Forest virus vectors for rapid and high-level expression of integral membrane proteins
    • Lundstrom K. Semliki Forest virus vectors for rapid and high-level expression of integral membrane proteins. Biochim Biophys Acta. 2003 1610 : 90 6.
    • (2003) Biochim Biophys Acta. , vol.1610 , pp. 90-6
    • Lundstrom, K.1
  • 92
    • 34247867105 scopus 로고    scopus 로고
    • Semliki Forest virus vectors: Versatile tools for efficient large-scale expression of membrane receptors
    • In: Kühne, S.R., de Groot, H.J.M., editors. Netherlands: Kluwer Academic Publishers. p.
    • Lundstrom K. Semliki Forest virus vectors: versatile tools for efficient large-scale expression of membrane receptors. In : Kühne S.R., de Groot H.J.M., editors. Perspectives on solid state NMR in biology. Netherlands : Kluwer Academic Publishers 2001. p. 131 9.
    • (2001) Perspectives on Solid State NMR in Biology. , pp. 131-9
    • Lundstrom, K.1
  • 93
    • 0031740283 scopus 로고    scopus 로고
    • How lipids interact with an intrinsic membrane protein: The case of the calcium pump
    • Lee AG. How lipids interact with an intrinsic membrane protein: the case of the calcium pump. Biochim Biophys Acta. 1998 1376 : 381 90.
    • (1998) Biochim Biophys Acta. , vol.1376 , pp. 381-90
    • Lee, A.G.1
  • 95
    • 33751293464 scopus 로고    scopus 로고
    • Solubilization and purification of membrane proteins
    • Lundstrom, K., editor. Boca Raton: CRC Press
    • Byrne B, Jormakka M. Solubilization and purification of membrane proteins, In : Lundstrom K., editor. Structural genomics on membrane proteins. Boca Raton : CRC Press 2006. p. 179 98.
    • (2006) Structural Genomics on Membrane Proteins. , pp. 179-98
    • Byrne, B.1    Jormakka, M.2
  • 98
    • 0029836953 scopus 로고    scopus 로고
    • Discovering high-affinity ligands for proteins: SAR by NMR
    • Shuker SB, Hajduk PJ, Meadows RP, Fesik SW. Discovering high-affinity ligands for proteins: SAR by NMR. Science. 1996 274 : 1531 4.
    • (1996) Science. , vol.274 , pp. 1531-4
    • Shuker, S.B.1    Hajduk, P.J.2    Meadows, R.P.3    Fesik, S.W.4
  • 99
    • 0032710475 scopus 로고    scopus 로고
    • NMR techniques for characterization of ligand binding: Utility for lead generation and optimization in drug discovery
    • Moore JM. NMR techniques for characterization of ligand binding: utility for lead generation and optimization in drug discovery. Biopolymers. 1999 51 : 221 43.
    • (1999) Biopolymers. , vol.51 , pp. 221-43
    • Moore, J.M.1
  • 100
    • 0036365716 scopus 로고    scopus 로고
    • Applications of NMR to structure-based drug design in structural genomics
    • Powers R. Applications of NMR to structure-based drug design in structural genomics. J Struct Funct Genomics. 2002 2 : 113 23.
    • (2002) J Struct Funct Genomics. , vol.2 , pp. 113-23
    • Powers, R.1
  • 101
    • 33751291577 scopus 로고    scopus 로고
    • Membrane protein NMR
    • Lundstrom, K., editor. Boca Raton: CRC Press. p.
    • Xie X-Q. Membrane protein NMR. In : Lundstrom K., editor. Structural genomics on membrane proteins. Boca Raton : CRC Press 2006. p. 211 59.
    • (2006) Structural Genomics on Membrane Proteins. , pp. 211-59
    • Xie, X.-Q.1
  • 102
    • 33751266160 scopus 로고    scopus 로고
    • Electron microscopy and atomic force microscopy of reconstituted membrane proteins
    • In: Lundstrom, K., editor. Boca Raton: CRC Press. p.
    • Engel A. Electron microscopy and atomic force microscopy of reconstituted membrane proteins. In : Lundstrom K., editor. Structural genomics on membrane proteins. Boca Raton : CRC Press 2006. p. 300 20.
    • (2006) Structural Genomics on Membrane Proteins. , pp. 300-20
    • Engel, A.1
  • 103
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • Henderson R, Baldwin JM, Ceska TA, Zemlin F, Beckmann E, Downing KH. Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J Mol Biol. 1990 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
  • 107
    • 0036408584 scopus 로고    scopus 로고
    • Structural genomics of "non-standard" proteins: A chance for membrane proteins?
    • Essen LO. Structural genomics of "non-standard" proteins: a chance for membrane proteins? Gene Funct Dis. 2002 3 : 39 48.
    • (2002) Gene Funct Dis. , vol.3 , pp. 39-48
    • Essen, L.O.1
  • 108
    • 8544275816 scopus 로고    scopus 로고
    • Protein biophysical properties that correlate with crystallization success in Thermotoga maritima: Maximum clustering strategy for structural genomics
    • Canaves JM, Page R, Wilson IA, Stevens RC. Protein biophysical properties that correlate with crystallization success in Thermotoga maritima: maximum clustering strategy for structural genomics. J Mol Biol. 2004 344 : 977 91.
    • (2004) J Mol Biol. , vol.344 , pp. 977-91
    • Canaves, J.M.1    Page, R.2    Wilson, I.A.3    Stevens, R.C.4
  • 111
    • 34247898422 scopus 로고    scopus 로고
    • http://www.spineurope.org
  • 112
    • 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, Reinhart C. Enhancing functional production of G protein-coupled receptors in Pichia pastoris to levels required for structural studies via a single expression screen. Protein Sci. 2006 15 : 1115 26.
    • (2006) Protein Sci. , vol.15 , pp. 1115-26
    • 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


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