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Volumn 63, Issue 10, 2006, Pages 1149-1164

Erratum: Recombinant G protein-coupled receptors from expression to renaturation: a challenge towards structure, (Cellular and Molecular Life Sciences CMLS, (2006), 63, 10, (1149-1164), 10.1007/s00018-005-5557-6);Recombinant G protein-coupled receptors from expression to renaturation: A challenge towards structure

Author keywords

GPCR; Membrane protein; Purification; Recombinant; Solubilization; Structure

Indexed keywords

G PROTEIN COUPLED RECEPTOR; MEMBRANE PROTEIN; RECOMBINANT RECEPTOR; RHODOPSIN;

EID: 33745293916     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-006-0001-0     Document Type: Erratum
Times cited : (84)

References (108)
  • 1
    • 0033118334 scopus 로고    scopus 로고
    • Molecular tinkering of G protein-coupled receptors: An evolutionary success
    • Bockaert J. and Pin J. P. (1999) Molecular tinkering of G protein-coupled receptors: an evolutionary success. EMBO J. 18: 1723-1729
    • (1999) EMBO J. , vol.18 , pp. 1723-1729
    • Bockaert, J.1    Pin, J.P.2
  • 4
    • 0041876269 scopus 로고    scopus 로고
    • Heterologous expression of G-protein-coupled receptors: Comparison of expression systems 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 systems from 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
  • 6
    • 0034718925 scopus 로고    scopus 로고
    • Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor
    • Kunishima N., Shimada Y., Tsuji Y., Sato T., Yamamoto M., Kumasaka et al. (2000) Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor. Nature 407: 971-977
    • (2000) Nature , vol.407 , pp. 971-977
    • Kunishima, N.1    Shimada, Y.2    Tsuji, Y.3    Sato, T.4    Yamamoto, M.5    Kumasaka6
  • 9
    • 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
  • 10
    • 0033392364 scopus 로고    scopus 로고
    • Refolding of G-protein-coupled receptors from inclusion bodies produced in Escherichia coli
    • Kiefer H., Maier K. and Vogel R. (1999) Refolding of G-protein-coupled receptors from inclusion bodies produced in Escherichia coli. Biochem. Soc. Trans. 27: 908-912
    • (1999) Biochem. Soc. Trans. , vol.27 , pp. 908-912
    • Kiefer, H.1    Maier, K.2    Vogel, R.3
  • 11
    • 0038392702 scopus 로고    scopus 로고
    • Structure-based analysis of GPCR function: Evidence for a novel pentameric assembly between the dimeric leukotriene B4 receptor BLT1 and the G-protein
    • Baneres J. L. and Parello J. (2003) Structure-based analysis of GPCR function: evidence for a novel pentameric assembly between the dimeric leukotriene B4 receptor BLT1 and the G-protein. J. Mol. Biol. 329: 815-829
    • (2003) J. Mol. Biol. , vol.329 , pp. 815-829
    • Baneres, J.L.1    Parello, J.2
  • 12
    • 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
  • 13
    • 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
  • 14
    • 0037071906 scopus 로고    scopus 로고
    • Construction and deconstruction of bacterial inclusion bodies
    • Carrio M. M. and Villaverde A. (2002) Construction and deconstruction of bacterial inclusion bodies. J. Biotechnol. 96: 3-12
    • (2002) J. Biotechnol. , vol.96 , pp. 3-12
    • Carrio, M.M.1    Villaverde, A.2
  • 15
    • 0034707086 scopus 로고    scopus 로고
    • Interaction of membrane proteins and lipids with solubilizing detergents
    • Maire M. le, Champeil P. and Moller J. V. (2000) Interaction of membrane proteins and lipids with solubilizing detergents. Biochim. Biophys. Acta 1508: 86-111
    • (2000) Biochim. Biophys. Acta , vol.1508 , pp. 86-111
    • Le Maire, M.1    Champeil, P.2    Moller, J.V.3
  • 16
    • 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
  • 17
    • 0016657917 scopus 로고
    • Solubilization of membranes by detergents
    • Helenius A. and Simons K. (1975) Solubilization of membranes by detergents. Biochim. Biophys. Acta 415: 29-79
    • (1975) Biochim. Biophys. Acta , vol.415 , pp. 29-79
    • Helenius, A.1    Simons, K.2
  • 19
    • 0031241608 scopus 로고    scopus 로고
    • Degradative covalent reactions important to protein stability
    • Volkin D. B., Mach H. and Middaugh C. R. (1997) Degradative covalent reactions important to protein stability. Mol. Biotechnol. 8: 105-122
    • (1997) Mol. Biotechnol. , vol.8 , pp. 105-122
    • Volkin, D.B.1    Mach, H.2    Middaugh, C.R.3
  • 20
    • 0031010621 scopus 로고    scopus 로고
    • A method for assessing the stability of a membrane protein
    • Lau F. W. and Bowie J. U. (1997) A method for assessing the stability of a membrane protein. Biochemistry 36: 5884-5892
    • (1997) Biochemistry , vol.36 , pp. 5884-5892
    • Lau, F.W.1    Bowie, J.U.2
  • 21
    • 0027301940 scopus 로고
    • Pigments induce folding of light-harvesting chlorophyll a/b-binding protein
    • Paulsen H., Finkenzeller B. and Kuhlein N. (1993) Pigments induce folding of light-harvesting chlorophyll a/b-binding protein. Eur. J. Biochem. 215: 809-816
    • (1993) Eur. J. Biochem. , vol.215 , pp. 809-816
    • Paulsen, H.1    Finkenzeller, B.2    Kuhlein, N.3
  • 22
    • 0030000359 scopus 로고    scopus 로고
    • Assembly of light-harvesting chlorophyll a/b complex in vitro: Time-resolved fluorescence measurements
    • Booth P. J. and Paulsen H. (1996) Assembly of light-harvesting chlorophyll a/b complex in vitro: time-resolved fluorescence measurements. Biochemistry 35: 5103-5108
    • (1996) Biochemistry , vol.35 , pp. 5103-5108
    • Booth, P.J.1    Paulsen, H.2
  • 24
    • 0025316316 scopus 로고
    • A systematic study of liposome and proteoliposome reconstitution involving Bio-Bead-mediated Triton X-100 removal
    • Levy D., Bluzat A., Seigneuret M. and Rigaud J. L. (1990) A systematic study of liposome and proteoliposome reconstitution involving Bio-Bead-mediated Triton X-100 removal. Biochim. Biophys. Acta 1025: 179-190
    • (1990) Biochim. Biophys. Acta , vol.1025 , pp. 179-190
    • Levy, D.1    Bluzat, A.2    Seigneuret, M.3    Rigaud, J.L.4
  • 26
    • 0842267080 scopus 로고    scopus 로고
    • Purification and characterization of the recombinant human dopamine D2S receptor from Pichia pastoris
    • Jong L. A. de, Grunewald S., Franke J. P., Uges D. R. and Bischoff R. (2004) Purification and characterization of the recombinant human dopamine D2S receptor from Pichia pastoris. Protein Expr. Purif. 33: 176-184
    • (2004) Protein Expr. Purif. , vol.33 , pp. 176-184
    • De Jong, L.A.1    Grunewald, S.2    Franke, J.P.3    Uges, D.R.4    Bischoff, R.5
  • 27
    • 0029945739 scopus 로고    scopus 로고
    • Overexpression solubilization and purification of rat and human olfactory receptors
    • Nekrasova E., Sosinskaya A., Natochin M., Lancet D., and Gat U. (1996) Overexpression solubilization and purification of rat and human olfactory receptors. Eur. J. Biochem. 238: 28-37
    • (1996) Eur. J. Biochem. , vol.238 , pp. 28-37
    • Nekrasova, E.1    Sosinskaya, A.2    Natochin, M.3    Lancet, D.4    Gat, U.5
  • 28
    • 3042802392 scopus 로고    scopus 로고
    • Large-scale overproduction functional purification and ligand affinities of the His-tagged human histamine H1 receptor
    • Ratnala V. R., Swarts H. G., VanOostrum J., Leurs R. DeGroot H. J., Bakker R. A. et al. (2004) Large-scale overproduction functional purification and ligand affinities of the His-tagged human histamine H1 receptor. Eur. J. Biochem. 271: 2636-2646
    • (2004) Eur. J. Biochem. , vol.271 , pp. 2636-2646
    • Ratnala, V.R.1    Swarts, H.G.2    VanOostrum, J.3    Leurs, R.4    DeGroot, H.J.5    Bakker, R.A.6
  • 29
    • 0035671430 scopus 로고    scopus 로고
    • Solubilization and purification of the human ETB endothelin receptor produced by high-level fermentation in Pichia pastoris
    • Schiller H., Molsberger E., Janssen P., Michel H. and Reilander H. (2001) Solubilization and purification of the human ETB endothelin receptor produced by high-level fermentation in Pichia pastoris. Receptors Channels 7: 453-469
    • (2001) Receptors Channels , vol.7 , pp. 453-469
    • Schiller, H.1    Molsberger, E.2    Janssen, P.3    Michel, H.4    Reilander, H.5
  • 30
    • 32944474906 scopus 로고    scopus 로고
    • Solubilization purification and mass spectrometry analysis of the human mu-opioid receptor expressed in Pichia pastoris
    • Sarramegna V., Muller I., Mousseau G., Froment C., Monsarrat B., Milon A. et al. (2005) Solubilization purification and mass spectrometry analysis of the human mu-opioid receptor expressed in Pichia pastoris. Protein Expr. Purif. 43: 85-93
    • (2005) Protein Expr. Purif. , vol.43 , pp. 85-93
    • Sarramegna, V.1    Muller, I.2    Mousseau, G.3    Froment, C.4    Monsarrat, B.5    Milon, A.6
  • 31
    • 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
  • 32
    • 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
  • 33
    • 0033214480 scopus 로고    scopus 로고
    • Enhanced expression native purification and characterization of CCR5 a principal HIV-1 coreceptor
    • Mirzabekov T., Bannert N., Farzan M., Hofmann W., Kolchinsky P., Wu L. et al. (1999) Enhanced expression native purification and characterization of CCR5 a principal HIV-1 coreceptor. J. Biol. Chem. 274: 28745-28750
    • (1999) J. Biol. Chem. , vol.274 , pp. 28745-28750
    • Mirzabekov, T.1    Bannert, N.2    Farzan, M.3    Hofmann, W.4    Kolchinsky, P.5    Wu, L.6
  • 34
    • 0032968755 scopus 로고    scopus 로고
    • Surfactants in membrane solubilisation
    • Jones M. N. (1999) Surfactants in membrane solubilisation. Int. J. Pharm. 177: 137-159
    • (1999) Int. J. Pharm. , vol.177 , pp. 137-159
    • Jones, M.N.1
  • 35
    • 0025211780 scopus 로고
    • Detergents: An overview
    • Neugebauer J. M. (1990) Detergents: an overview. Methods Enzymol. 182: 239-253
    • (1990) Methods Enzymol. , vol.182 , pp. 239-253
    • Neugebauer, J.M.1
  • 36
    • 0035914438 scopus 로고    scopus 로고
    • Ligand binding characteristics of CXCR4 incorporated into paramagnetic proteoliposomes
    • Babcock G. J., Mirzabekov T., Wojtowicz W. and Sodroski J. (2001) Ligand binding characteristics of CXCR4 incorporated into paramagnetic proteoliposomes. J. Biol. Chem. 276: 38433-38440
    • (2001) J. Biol. Chem. , vol.276 , pp. 38433-38440
    • Babcock, G.J.1    Mirzabekov, T.2    Wojtowicz, W.3    Sodroski, J.4
  • 38
    • 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
  • 39
    • 0034966097 scopus 로고    scopus 로고
    • Immunoaffinity purification and reconstitution of human alpha(2)-adrenergic receptor subtype C2 into phospholipid vesicles
    • Liitti S., Matikainen M. T., Scheinin M., Glumoff T. and Goldman A. (2001) Immunoaffinity purification and reconstitution of human alpha(2)-adrenergic receptor subtype C2 into phospholipid vesicles. Protein Expr. Purif. 22: 1-10
    • (2001) Protein Expr. Purif. , vol.22 , pp. 1-10
    • Liitti, S.1    Matikainen, M.T.2    Scheinin, M.3    Glumoff, T.4    Goldman, A.5
  • 40
    • 0028876894 scopus 로고
    • Characterization of the rat m3 muscarinic acetylcholine receptor produced in insect cells infected with recombinant baculovirus
    • Vasudevan S., Hulme E. C., Bach M., Haase W., Pavia J. and Reilander H. (1995) Characterization of the rat m3 muscarinic acetylcholine receptor produced in insect cells infected with recombinant baculovirus. Eur. J. Biochem. 227: 466-475
    • (1995) Eur. J. Biochem. , vol.227 , pp. 466-475
    • Vasudevan, S.1    Hulme, E.C.2    Bach, M.3    Haase, W.4    Pavia, J.5    Reilander, H.6
  • 41
    • 0028129840 scopus 로고
    • Solubilization of muscarinic receptor subtypes from baculovirus infected Sf9 insect cells
    • Rinken A., Kameyama K., Haga T. and Engstrom L. (1994) Solubilization of muscarinic receptor subtypes from baculovirus infected Sf9 insect cells. Biochem. Pharmacol. 48: 1245-1251
    • (1994) Biochem. Pharmacol. , vol.48 , pp. 1245-1251
    • Rinken, A.1    Kameyama, K.2    Haga, T.3    Engstrom, L.4
  • 42
    • 12244292640 scopus 로고    scopus 로고
    • Purification and characterization of the human adenosine A2a receptor functionally expressed in Escherichia coli
    • Weiss H. M. and Grisshammer R. (2002) Purification and characterization of the human adenosine A2a 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
  • 43
    • 0242424107 scopus 로고    scopus 로고
    • Monomers and oligomers of the M2 muscarinic cholinergic receptor purified from Sf9 cells
    • Park P. S. and Wells J. W. (2003) Monomers and oligomers of the M2 muscarinic cholinergic receptor purified from Sf9 cells. Biochemistry 42: 12960-12971
    • (2003) Biochemistry , vol.42 , pp. 12960-12971
    • Park, P.S.1    Wells, J.W.2
  • 45
    • 0035811492 scopus 로고    scopus 로고
    • Insights into Wnt binding and signalling from the structures of two Frizzled cysteine-rich domains
    • Dann C. E., Hsieh J. C., Rattner A., Sharma D., Nathans J. and Leahy D. J. (2001) Insights into Wnt binding and signalling from the structures of two Frizzled cysteine-rich domains. Nature 412: 86-90
    • (2001) Nature , vol.412 , pp. 86-90
    • Dann, C.E.1    Hsieh, J.C.2    Rattner, A.3    Sharma, D.4    Nathans, J.5    Leahy, D.J.6
  • 46
    • 0026086012 scopus 로고
    • Reconstitutively active G protein-coupled receptors purified from baculovirus-infected insect cells
    • Parker E. M., Kameyama K., Higashijima T. and Ross E. M. (1991) Reconstitutively active G protein-coupled receptors purified from baculovirus-infected insect cells. J. Biol. Chem. 266: 519-527
    • (1991) J. Biol. Chem. , vol.266 , pp. 519-527
    • Parker, E.M.1    Kameyama, K.2    Higashijima, T.3    Ross, E.M.4
  • 47
    • 18944378413 scopus 로고    scopus 로고
    • Purification and mass spectrometric analysis of the delta opioid receptor
    • Christoffers K. H. Li H. and Howells R. D. (2005) Purification and mass spectrometric analysis of the delta opioid receptor. Brain Res. Mol. Brain Res. 136: 54-64
    • (2005) Brain Res. Mol. Brain Res. , vol.136 , pp. 54-64
    • Christoffers, K.H.1    Li, H.2    Howells, R.D.3
  • 49
    • 0025728196 scopus 로고
    • Purification and functional characterization of the human beta 2-adrenergic receptor produced in baculovirus-infected insect cells
    • Reilander H., Boege F., Vasudevan S., Maul G., Hekman M., Dees C. et al. (1991) Purification and functional characterization of the human beta 2-adrenergic receptor produced in baculovirus-infected insect cells. FEBS. Lett. 282: 441-444
    • (1991) FEBS. Lett. , vol.282 , pp. 441-444
    • Reilander, H.1    Boege, F.2    Vasudevan, S.3    Maul, G.4    Hekman, M.5    Dees, C.6
  • 50
    • 0020368287 scopus 로고
    • Fractionation of asparagine-linked oligosaccharides by serial lectin-agarose affinity chromatography: A rapid sensitive and specific technique
    • Cummings R. D. and Kornfeld S. (1982) Fractionation of asparagine-linked oligosaccharides by serial lectin-agarose affinity chromatography: a rapid sensitive and specific technique. J. Biol. Chem. 257: 11235-11240
    • (1982) J. Biol. Chem. , vol.257 , pp. 11235-11240
    • Cummings, R.D.1    Kornfeld, S.2
  • 51
    • 0032547082 scopus 로고    scopus 로고
    • Expression purification and reconstitution of receptor for pituitary adenylate cyclase-activating polypeptide: Large-scale purification of a functionally active G protein-coupled receptor produced in Sf9 insect cells
    • Ohtaki T., Ogi K., Masuda Y., Mitsuoka K., Fujiyoshi Y., Kitada C. et al. (1998) Expression purification and reconstitution of receptor for pituitary adenylate cyclase-activating polypeptide: large-scale purification of a functionally active G protein-coupled receptor produced in Sf9 insect cells. J. Biol. Chem. 273: 15464-15473
    • (1998) J. Biol. Chem. , vol.273 , pp. 15464-15473
    • Ohtaki, T.1    Ogi, K.2    Masuda, Y.3    Mitsuoka, K.4    Fujiyoshi, Y.5    Kitada, C.6
  • 52
    • 0023920896 scopus 로고
    • Large-scale chromatography of recombinant proteins
    • Hochuli E. (1988) Large-scale chromatography of recombinant proteins. J. Chromatogr. 444: 293-302
    • (1988) J. Chromatogr. , vol.444 , pp. 293-302
    • Hochuli, E.1
  • 53
    • 0025946803 scopus 로고
    • Rapid and efficient purification of native histidine-tagged protein expressed by recombinant vaccinia virus
    • USA
    • Janknecht R., Martynoff G. de, Lou J., Hipskind R. A., Nordheim A. and Stunnenberg H. G. (1991) Rapid and efficient purification of native histidine-tagged protein expressed by recombinant vaccinia virus. Proc. Natl. Acad. Sci. USA 88: 8972-8976
    • (1991) Proc. Natl. Acad. Sci. , vol.88 , pp. 8972-8976
    • Janknecht, R.1    De Martynoff, G.2    Lou, J.3    Hipskind, R.A.4    Nordheim, A.5    Stunnenberg, H.G.6
  • 54
    • 0029858001 scopus 로고    scopus 로고
    • Crystallization and identification of an assembly defect of recombinant antenna complexes produced in transgenic tobacco plants
    • USA
    • Flachmann R. and Kuhlbrandt W. (1996) Crystallization and identification of an assembly defect of recombinant antenna complexes produced in transgenic tobacco plants. Proc. Natl. Acad. Sci. USA 93: 14966-14971
    • (1996) Proc. Natl. Acad. Sci. , vol.93 , pp. 14966-14971
    • Flachmann, R.1    Kuhlbrandt, W.2
  • 55
    • 0029073041 scopus 로고
    • Histidine tagging both allows convenient single-step purification of bovine rhodopsin and exerts ionic strength-dependent effects on its photochemistry
    • Janssen J. J., Bovee-Geurts P. H., Merkx M. and DeGrip W. J. (1995) Histidine tagging both allows convenient single-step purification of bovine rhodopsin and exerts ionic strength-dependent effects on its photochemistry. J. Biol. Chem. 270: 11222-11229
    • (1995) J. Biol. Chem. , vol.270 , pp. 11222-11229
    • Janssen, J.J.1    Bovee-Geurts, P.H.2    Merkx, M.3    DeGrip, W.J.4
  • 56
    • 0029445538 scopus 로고
    • Rapid high-yield purification and liposome reconstitution of polyhistidine-tagged sensory rhodopsin I
    • Krebs M. P., Spudich E. N. and Spudich J. L. (1995) Rapid high-yield purification and liposome reconstitution of polyhistidine-tagged sensory rhodopsin I. Protein Expr. Purif. 6: 780-788
    • (1995) Protein Expr. Purif. , vol.6 , pp. 780-788
    • Krebs, M.P.1    Spudich, E.N.2    Spudich, J.L.3
  • 58
    • 0031260369 scopus 로고    scopus 로고
    • Quantitative evaluation of neurotensin receptor purification by immobilized metal affinity chromatography
    • Grisshammer R. and Tucker J. (1997) Quantitative evaluation of neurotensin receptor purification by immobilized metal affinity chromatography. Protein Expr. Purif. 11: 53-60
    • (1997) Protein Expr. Purif. , vol.11 , pp. 53-60
    • Grisshammer, R.1    Tucker, J.2
  • 59
    • 0032575513 scopus 로고    scopus 로고
    • Expression characterization and purification of C-terminally hexahistidine-tagged thromboxane A2 receptors
    • Pawate S., Schey K. L., Meier G. P., Ullian M. E., Mais D. E. and Halushka P. V. (1998) Expression characterization and purification of C-terminally hexahistidine-tagged thromboxane A2 receptors. J. Biol. Chem. 273: 22753-22760
    • (1998) J. Biol. Chem. , vol.273 , pp. 22753-22760
    • Pawate, S.1    Schey, K.L.2    Meier, G.P.3    Ullian, M.E.4    Mais, D.E.5    Halushka, P.V.6
  • 60
    • 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
  • 61
    • 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
  • 62
    • 0028809411 scopus 로고
    • Amino and carboxyl terminal modifications to facilitate the production and purification of a G protein-coupled receptor
    • Kobilka B. K. (1995) Amino and carboxyl terminal modifications to facilitate the production and purification of a G protein-coupled receptor. Anal. Biochem. 231: 269-271
    • (1995) Anal. Biochem. , vol.231 , pp. 269-271
    • Kobilka, B.K.1
  • 63
    • 0030465362 scopus 로고    scopus 로고
    • Purification and functional reconstitution with GTP-binding regulatory proteins of hexahistidine-tagged muscarinic acetylcholine receptors (m2 subtype)
    • Tokyo
    • Hayashi M. K. and Haga T. (1996) Purification and functional reconstitution with GTP-binding regulatory proteins of hexahistidine-tagged muscarinic acetylcholine receptors (m2 subtype). J. Biochem. (Tokyo) 120: 1232-1238
    • (1996) J. Biochem. , vol.120 , pp. 1232-1238
    • Hayashi, M.K.1    Haga, T.2
  • 64
    • 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. J. Biotechnol. 77: 219-234
    • (2000) J. Biotechnol. , vol.77 , pp. 219-234
    • Hampe, W.1    Voss, R.H.2    Haase, W.3    Boege, F.4    Michel, H.5    Reilander, H.6
  • 65
    • 0034603147 scopus 로고    scopus 로고
    • The effect of pH on beta(2) adrenoceptor function: Evidence for protonation-dependent activation
    • Ghanouni P., Schambye H., Seifert R., Lee T. W., Rasmussen S. G., Gether U. et al. (2000) The effect of pH on beta(2) adrenoceptor function: evidence for protonation-dependent activation. J. Biol. Chem. 275: 3121-3127
    • (2000) J. Biol. Chem. , vol.275 , pp. 3121-3127
    • Ghanouni, P.1    Schambye, H.2    Seifert, R.3    Lee, T.W.4    Rasmussen, S.G.5    Gether, U.6
  • 67
    • 0033516576 scopus 로고    scopus 로고
    • Identification and molecular characterization of m3 muscarinic receptor dimers
    • Zeng F. Y. and Wess J. (1999) Identification and molecular characterization of m3 muscarinic receptor dimers. J. Biol. Chem. 274: 19487-19497
    • (1999) J. Biol. Chem. , vol.274 , pp. 19487-19497
    • Zeng, F.Y.1    Wess, J.2
  • 69
    • 0035984890 scopus 로고    scopus 로고
    • Functional reconstitution of purified metabotropic glutamate receptor expressed in the fly eye
    • 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. , vol.3 , pp. 491-496
    • Eroglu, C.1    Cronet, P.2    Panneels, V.3    Beaufils, P.4    Sinning, I.5
  • 70
    • 0042354628 scopus 로고    scopus 로고
    • Pharmacological characterization and immunoaffinity purification of metabotropic glutamate receptor from Drosophila overexpressed in Sf9 cells
    • Panneels V., Eroglu C., Cronet P. and Sinning I. (2003) Pharmacological characterization and immunoaffinity purification of metabotropic glutamate receptor from Drosophila overexpressed in Sf9 cells. Protein Expr. Purif. 30: 275-282
    • (2003) Protein Expr. Purif. , vol.30 , pp. 275-282
    • Panneels, V.1    Eroglu, C.2    Cronet, P.3    Sinning, I.4
  • 71
    • 0023515308 scopus 로고
    • Expression of a synthetic bovine rhodopsin gene in monkey kidney cells
    • USA
    • Oprian D. D., Molday R. S., Kaufman R. J. and Khorana H. G. (1987) Expression of a synthetic bovine rhodopsin gene in monkey kidney cells. Proc. Natl. Acad. Sci. USA 84: 8874-8878
    • (1987) Proc. Natl. Acad. Sci. , vol.84 , pp. 8874-8878
    • Oprian, D.D.1    Molday, R.S.2    Kaufman, R.J.3    Khorana, H.G.4
  • 72
    • 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-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line
    • USA
    • 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-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line. Proc. Natl. Acad. Sci. USA 99: 13419-13424
    • (2002) Proc. Natl. Acad. Sci. , vol.99 , pp. 13419-13424
    • Reeves, P.J.1    Callewaert, N.2    Contreras, R.3    Khorana, H.G.4
  • 73
    • 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
    • USA
    • 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. , vol.99 , pp. 13413-13418
    • Reeves, P.J.1    Kim, J.M.2    Khorana, H.G.3
  • 74
    • 0029859488 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: Expression of functional mammalian opsin in Saccharomyces cerevisiae
    • USA
    • Mollaaghababa R., Davidson F. F., Kaiser C. and Khorana H. G. (1996) Structure and function in rhodopsin: expression of functional mammalian opsin in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 93: 11482-11486
    • (1996) Proc. Natl. Acad. Sci. , vol.93 , pp. 11482-11486
    • Mollaaghababa, R.1    Davidson, F.F.2    Kaiser, C.3    Khorana, H.G.4
  • 75
    • 0037199993 scopus 로고    scopus 로고
    • Purification and characterization of a receptor for human parathyroid hormone and parathyroid hormone-related peptide
    • Shimada M., Chen X., Cvrk T., Hilfiker H., Parfenova M. and Segre G. V. (2002) Purification and characterization of a receptor for human parathyroid hormone and parathyroid hormone-related peptide. J. Biol. Chem. 277: 31774-31780
    • (2002) J. Biol. Chem. , vol.277 , pp. 31774-31780
    • Shimada, M.1    Chen, X.2    Cvrk, T.3    Hilfiker, H.4    Parfenova, M.5    Segre, G.V.6
  • 76
    • 0031455378 scopus 로고    scopus 로고
    • Functional coupling of a human retinal metabotropic glutamate receptor (hmGluR6) to bovine rod transducin and rat Go in an in vitro reconstitution system
    • Weng K., Lu C., Daggett L. P., Kuhn R., Flor P. J., Johnson E. C. et al. (1997) Functional coupling of a human retinal metabotropic glutamate receptor (hmGluR6) to bovine rod transducin and rat Go in an in vitro reconstitution system. J. Biol. Chem. 272: 33100-33104
    • (1997) J. Biol. Chem. , vol.272 , pp. 33100-33104
    • Weng, K.1    Lu, C.2    Daggett, L.P.3    Kuhn, R.4    Flor, P.J.5    Johnson, E.C.6
  • 77
    • 0036082288 scopus 로고    scopus 로고
    • Biochemistry and pharmacology of epitope-tagged alpha(1)-adrenergic receptor subtypes
    • Vicentic A., Robeva A., Rogge G., Uberti M. and Minneman K. P. (2002) Biochemistry and pharmacology of epitope-tagged alpha(1)-adrenergic receptor subtypes. J. Pharmacol. Exp. Ther. 302: 58-65
    • (2002) J. Pharmacol. Exp. Ther. , vol.302 , pp. 58-65
    • Vicentic, A.1    Robeva, A.2    Rogge, G.3    Uberti, M.4    Minneman, K.P.5
  • 78
    • 0030070457 scopus 로고    scopus 로고
    • Double tagging recombinant A1- and A2A-adenosine receptors with hexahistidine and the FLAG epitope: Development of an efficient generic protein purification procedure
    • Robeva A. S., Woodard R., Luthin D. R., Taylor H. E. and Linden J. (1996) Double tagging recombinant A1- and A2A-adenosine receptors with hexahistidine and the FLAG epitope: development of an efficient generic protein purification procedure. Biochem. Pharmacol. 51: 545-555
    • (1996) Biochem. Pharmacol. , vol.51 , pp. 545-555
    • Robeva, A.S.1    Woodard, R.2    Luthin, D.R.3    Taylor, H.E.4    Linden, J.5
  • 79
    • 0023714467 scopus 로고    scopus 로고
    • A short polypeptide marker sequence useful for recombinant protein identification and purification
    • Hopp W. Prickett K. S. Price V. L. Libby R. T. March C. J. Cerretti et al. (1998) A short polypeptide marker sequence useful for recombinant protein identification and purification. Biotechnology 6: 1204-1210
    • (1998) Biotechnology , vol.6 , pp. 1204-1210
    • Hopp, W.1    Prickett, K.S.2    Price, V.L.3    Libby, R.T.4    March, C.J.5    Cerretti6
  • 80
    • 0034047889 scopus 로고    scopus 로고
    • Paramagnetic proteoliposomes containing a pure native and oriented seven-transmembrane segment protein CCR5
    • Mirzabekov T., Kontos H., Farzan M., Marasco W. and Sodroski J. (2000) Paramagnetic proteoliposomes containing a pure native and oriented seven-transmembrane segment protein CCR5. Nat. Biotechnol. 18: 649-654
    • (2000) Nat. Biotechnol. , vol.18 , pp. 649-654
    • Mirzabekov, T.1    Kontos, H.2    Farzan, M.3    Marasco, W.4    Sodroski, J.5
  • 81
    • 0036211021 scopus 로고    scopus 로고
    • Regulation of dopamine D(1) receptor trafficking by protein kinase A-dependent phosphorylation
    • Mason J. N., Kozell L. B. and Neve K. A. (2002) Regulation of dopamine D(1) receptor trafficking by protein kinase A-dependent phosphorylation. Mol. Pharmacol. 61: 806-816
    • (2002) Mol. Pharmacol. , vol.61 , pp. 806-816
    • Mason, J.N.1    Kozell, L.B.2    Neve, K.A.3
  • 82
    • 0033554397 scopus 로고    scopus 로고
    • Membrane cholesterol modulates galanin-GalR2 interaction
    • Pang L,. Graziano M. and Wang S. (1999) Membrane cholesterol modulates galanin-GalR2 interaction. Biochemistry 38: 12003-12011
    • (1999) Biochemistry , vol.38 , pp. 12003-12011
    • Pang, L.1    Graziano, M.2    Wang, S.3
  • 83
    • 0030582573 scopus 로고    scopus 로고
    • Rhodopsin-cholesterol interactions in bovine rod outer segment disk membranes
    • Albert A. D., Young J. E. and Yeagle P. L. (1996) Rhodopsin-cholesterol interactions in bovine rod outer segment disk membranes. Biochim. Biophys. Acta 1285: 47-55
    • (1996) Biochim. Biophys. Acta , vol.1285 , pp. 47-55
    • Albert, A.D.1    Young, J.E.2    Yeagle, P.L.3
  • 84
    • 0037206131 scopus 로고    scopus 로고
    • Cholesterol as stabilizer of the oxytocin receptor
    • Gimpl G. and Fahrenholz F. (2002) Cholesterol as stabilizer of the oxytocin receptor. Biochim. Biophys. Acta 1564: 384-392
    • (2002) Biochim. Biophys. Acta , vol.1564 , pp. 384-392
    • Gimpl, G.1    Fahrenholz, F.2
  • 85
    • 0029028008 scopus 로고
    • Purification of recombinant porcine m2 muscarinic acetylcholine receptor from Chinese hamster ovary cells: Circular dichroism spectra and ligand binding properties
    • Peterson G. L., Toumadje A., Johnson W. C. Jr and Schimerlik M. I. (1995) Purification of recombinant porcine m2 muscarinic acetylcholine receptor from Chinese hamster ovary cells: circular dichroism spectra and ligand binding properties. J. Biol. Chem. 270: 17808-17814
    • (1995) J. Biol. Chem. , vol.270 , pp. 17808-17814
    • Peterson, G.L.1    Toumadje, A.2    Johnson Jr., W.C.3    Schimerlik, M.I.4
  • 87
    • 0035957435 scopus 로고    scopus 로고
    • Crystal structure of the ectodomain of Methuselah a Drosophila G protein-coupled receptor associated with extended lifespan
    • USA
    • West A. P. Jr, Llamas L. L., Snow P. M., Benzer S. and Bjorkman P. J. (2001) Crystal structure of the ectodomain of Methuselah a Drosophila G protein-coupled receptor associated with extended lifespan. Proc. Natl. Acad. Sci. USA 98: 3744-3749
    • (2001) Proc. Natl. Acad. Sci. , vol.98 , pp. 3744-3749
    • West Jr., A.P.1    Llamas, L.L.2    Snow, P.M.3    Benzer, S.4    Bjorkman, P.J.5
  • 88
    • 12744280744 scopus 로고    scopus 로고
    • Structure of human follicle-stimulating hormone in complex with its receptor
    • Fan Q. R. and Hendrickson W. A. (2005) Structure of human follicle-stimulating hormone in complex with its receptor. Nature 433: 269-277
    • (2005) Nature , vol.433 , pp. 269-277
    • Fan, Q.R.1    Hendrickson, W.A.2
  • 89
    • 4444351153 scopus 로고    scopus 로고
    • NMR structure and peptide hormone binding site of the first extracellular domain of a type B1 G protein-coupled receptor
    • USA
    • Grace C. R., Perrin M. H., DiGruccio M. R., Miller C. L., Rivier J. E., Vale W. W. et al. (2004) NMR structure and peptide hormone binding site of the first extracellular domain of a type B1 G protein-coupled receptor. Proc. Natl. Acad. Sci. USA 101: 12836-12841
    • (2004) Proc. Natl. Acad. Sci. , vol.101 , pp. 12836-12841
    • Grace, C.R.1    Perrin, M.H.2    DiGruccio, M.R.3    Miller, C.L.4    Rivier, J.E.5    Vale, W.W.6
  • 90
    • 12344250438 scopus 로고    scopus 로고
    • Structural genomics of GPCRs
    • Lundstrom K. (2005) Structural genomics of GPCRs. Trends Biotechnol. 23: 103-108
    • (2005) Trends Biotechnol. , vol.23 , pp. 103-108
    • Lundstrom, K.1
  • 91
    • 22844448355 scopus 로고    scopus 로고
    • Structural biology of G protein-coupled receptors
    • Lundstrom K. (2005) Structural biology of G protein-coupled receptors. Bioorg. Med. Chem. Lett. 15: 3654-3657
    • (2005) Bioorg. Med. Chem. Lett. , vol.15 , pp. 3654-3657
    • Lundstrom, K.1
  • 92
    • 0037450576 scopus 로고    scopus 로고
    • Expression and purification of truncated non-glycosylated turkey beta-adrenergic receptors for crystallization
    • Warne T., Chirnside J. and Schertler G. F. (2003) Expression and purification of truncated non-glycosylated turkey beta-adrenergic receptors for crystallization. Biochim. Biophys. Acta 1610: 133-140
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 133-140
    • Warne, T.1    Chirnside, J.2    Schertler, G.F.3
  • 93
    • 0027155189 scopus 로고
    • The substance P receptor which couples to Gq/11 is a substrate of beta-adrenergic receptor kinase 1 and 2
    • Kwatra M. M., Schwinn D. A., Schreurs J., Blank J. L., Kim C. M., Benovic J. L. et al. (1993) The substance P receptor which couples to Gq/11 is a substrate of beta-adrenergic receptor kinase 1 and 2. J. Biol. Chem. 268: 9161-9164
    • (1993) J. Biol. Chem. , vol.268 , pp. 9161-9164
    • Kwatra, M.M.1    Schwinn, D.A.2    Schreurs, J.3    Blank, J.L.4    Kim, C.M.5    Benovic, J.L.6
  • 94
    • 1942468187 scopus 로고    scopus 로고
    • Automated large-scale purification of a G protein-coupled receptor for neurotensin
    • White J. F., Trinh L. B., Shiloach J. and Grisshammer R. (2004) Automated large-scale purification of a G protein-coupled receptor for neurotensin. FEBS. Lett. 564: 289-293
    • (2004) FEBS. Lett. , vol.564 , pp. 289-293
    • White, J.F.1    Trinh, L.B.2    Shiloach, J.3    Grisshammer, R.4
  • 95
    • 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: 369-373
    • (2001) Protein Expr. Purif. , vol.23 , pp. 369-373
    • Busuttil, B.E.1    Turney, K.L.2    Frauman, A.G.3
  • 96
    • 85159987875 scopus 로고    scopus 로고
    • Large-scale purification and characterization of human parathyroid hormone-1 receptor stably expressed in HEK293S GnTI(-) cells
    • in press
    • Gan L., Alexander J. M., Wittelsberger A., Thomas B. and Rosenblatt M. (in press) Large-scale purification and characterization of human parathyroid hormone-1 receptor stably expressed in HEK293S GnTI(-) cells. Protein Expr. Purif.
    • Protein Expr. Purif.
    • Gan, L.1    Alexander, J.M.2    Wittelsberger, A.3    Thomas, B.4    Rosenblatt, M.5
  • 97
    • 7044264520 scopus 로고    scopus 로고
    • Functional characterization and purification of the secretin receptor expressed in baculovirus-infected insect cells
    • Asmann Y. W., Dong M. and Miller L. J. (2004) Functional characterization and purification of the secretin receptor expressed in baculovirus-infected insect cells. Regul. Pept. 123: 217-223
    • (2004) Regul. Pept. , vol.123 , pp. 217-223
    • Asmann, Y.W.1    Dong, M.2    Miller, L.J.3
  • 98
    • 2142766875 scopus 로고    scopus 로고
    • Different structural states of the proteolipid membrane are produced by ligand binding to the human delta-opioid receptor as shown by plasmon-waveguide resonance spectroscopy
    • Alves I. D., Cowell S. M., Salamon Z,. Devanathan S., Tollin G. and Hruby V. J. (2004) Different structural states of the proteolipid membrane are produced by ligand binding to the human delta-opioid receptor as shown by plasmon-waveguide resonance spectroscopy. Mol. Pharmacol. 65: 1248-1257
    • (2004) Mol. Pharmacol. , vol.65 , pp. 1248-1257
    • Alves, I.D.1    Cowell, S.M.2    Salamon, Z.3    Devanathan, S.4    Tollin, G.5    Hruby, V.J.6
  • 99
    • 13844276949 scopus 로고    scopus 로고
    • Expression and characterization of human CB1 cannabinoid receptor in methylotrophic yeast Pichia pastoris
    • Kim T. K., Zhang R., Feng W., Cai J., Pierce W. and Song Z. H. (2005) Expression and characterization of human CB1 cannabinoid receptor in methylotrophic yeast Pichia pastoris. Protein Expr. Purif. 40: 60-70
    • (2005) Protein Expr. Purif. , vol.40 , pp. 60-70
    • Kim, T.K.1    Zhang, R.2    Feng, W.3    Cai, J.4    Pierce, W.5    Song, Z.H.6
  • 100
    • 0036915216 scopus 로고    scopus 로고
    • Expression of CB2 cannabinoid receptor in Pichia pastoris
    • Feng W, Cai J., Pierce W. M. Jr. and Song Z. H. (2002) Expression of CB2 cannabinoid receptor in Pichia pastoris. Protein Expr. Purif. 26: 496-505
    • (2002) Protein Expr. Purif. , vol.26 , pp. 496-505
    • Feng, W.1    Cai, J.2    Pierce Jr., W.M.3    Song, Z.H.4
  • 101
    • 11144318571 scopus 로고    scopus 로고
    • Purification and mass spectroscopic analysis of human CB2 cannabinoid receptor expressed in the baculovirus system
    • Filppula S., Yaddanapudi S., Mercier R., Xu W,. Pavlopoulos S. and Makriyannis A. (2004) Purification and mass spectroscopic analysis of human CB2 cannabinoid receptor expressed in the baculovirus system. J. Pept. Res. 64: 225-236
    • (2004) J. Pept. Res. , vol.64 , pp. 225-236
    • Filppula, S.1    Yaddanapudi, S.2    Mercier, R.3    Xu, W.4    Pavlopoulos, S.5    Makriyannis, A.6
  • 102
    • 23844504618 scopus 로고    scopus 로고
    • Purification and mass spectroscopic analysis of human CB1 cannabinoid receptor functionally expressed using the baculovirus system
    • Xu W., Filppula S. A., Mercier R., Yaddanapudi S., Pavlopoulos S., Cai J. et al. (2005) Purification and mass spectroscopic analysis of human CB1 cannabinoid receptor functionally expressed using the baculovirus system. J. Pept. Res. 66: 138-150
    • (2005) J. Pept. Res. , vol.66 , pp. 138-150
    • Xu, W.1    Filppula, S.A.2    Mercier, R.3    Yaddanapudi, S.4    Pavlopoulos, S.5    Cai, J.6
  • 103
    • 25844443463 scopus 로고    scopus 로고
    • Expression of human peripheral cannabinoid receptor for structural studies
    • Yeliseev A. A., Wong K. K., Soubias O. and Gawrisch K. (2005) Expression of human peripheral cannabinoid receptor for structural studies. Protein Sci. 14: 2638-2653
    • (2005) Protein Sci. , vol.14 , pp. 2638-2653
    • Yeliseev, A.A.1    Wong, K.K.2    Soubias, O.3    Gawrisch, K.4
  • 104
    • 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: 293-300
    • (1999) Biochem. J. , vol.342 , pp. 293-300
    • Klaassen, C.H.1    Bovee-Geurts, P.H.2    Decaluwe, G.L.3    DeGrip, W.J.4
  • 106
  • 107
    • 28544450037 scopus 로고    scopus 로고
    • Purification and characterization of a recombinant G-protein-coupled receptor Saccharomyces cerevisiae Ste2p transiently expressed in HEK293 EBNA1 cells
    • Shi C., Shin Y. O., Hanson J., Cass B., Loewen M. C. and Durocher Y. (2005) Purification and characterization of a recombinant G-protein-coupled receptor Saccharomyces cerevisiae Ste2p transiently expressed in HEK293 EBNA1 cells. Biochemistry 44: 15705-15714
    • (2005) Biochemistry , vol.44 , pp. 15705-15714
    • Shi, C.1    Shin, Y.O.2    Hanson, J.3    Cass, B.4    Loewen, M.C.5    Durocher, Y.6
  • 108
    • 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. et al. (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


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