메뉴 건너뛰기




Volumn 5, Issue , 2015, Pages

Production of monoclonal antibodies against GPCR using cell-free synthesized GPCR antigen and biotinylated liposome-based interaction assay

Author keywords

[No Author keywords available]

Indexed keywords

DOPAMINE 1 RECEPTOR; DRD1 PROTEIN, HUMAN; EPITOPE; G PROTEIN COUPLED RECEPTOR; GHRELIN RECEPTOR; LIPOSOME; MONOCLONAL ANTIBODY; PROSTAGLANDIN E RECEPTOR 1; PTGER1 PROTEIN, HUMAN; RECOMBINANT PROTEIN; TASTE RECEPTORS, TYPE 1;

EID: 84935844853     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep11333     Document Type: Article
Times cited : (58)

References (40)
  • 1
    • 79953900818 scopus 로고    scopus 로고
    • Overcoming barriers to membrane protein structure determination
    • Bill, R. M. et al. Overcoming barriers to membrane protein structure determination. Nat Biotechnol 29, 335-340 (2011).
    • (2011) Nat Biotechnol , vol.29 , pp. 335-340
    • Bill, R.M.1
  • 2
    • 84873685831 scopus 로고    scopus 로고
    • Molecular signatures of G-protein-coupled receptors
    • Venkatakrishnan, A. J. et al. Molecular signatures of G-protein-coupled receptors. Nature 494, 185-194 (2013).
    • (2013) Nature , vol.494 , pp. 185-194
    • Venkatakrishnan, A.J.1
  • 4
    • 78649681781 scopus 로고    scopus 로고
    • Therapeutic antibodies directed at G protein-coupled receptors
    • Hutchings, C. J., Koglin, M. & Marshall, F. H. Therapeutic antibodies directed at G protein-coupled receptors. MAbs 2, 594-606 (2010).
    • (2010) MAbs , vol.2 , pp. 594-606
    • Hutchings, C.J.1    Koglin, M.2    Marshall, F.H.3
  • 5
    • 78651411166 scopus 로고    scopus 로고
    • Structure of a nanobody-stabilized active state of the β(2) adrenoceptor
    • Rasmussen, S. G. F. et al. Structure of a nanobody-stabilized active state of the β(2) adrenoceptor. Nature 469, 175-180 (2011).
    • (2011) Nature , vol.469 , pp. 175-180
    • Rasmussen, S.G.F.1
  • 6
    • 84862776818 scopus 로고    scopus 로고
    • G-protein-coupled receptor inactivation by an allosteric inverse-agonist antibody
    • Hino, T. et al. G-protein-coupled receptor inactivation by an allosteric inverse-agonist antibody. Nature 482, 237-240 (2012).
    • (2012) Nature , vol.482 , pp. 237-240
    • Hino, T.1
  • 8
    • 34548158514 scopus 로고    scopus 로고
    • Neurotensin receptor type 1: Escherichia coli expression, purification, characterization and biophysical study
    • Harding, P. J. et al. Neurotensin receptor type 1: Escherichia coli expression, purification, characterization and biophysical study. Biochem Soc Trans 35, 760-763 (2007).
    • (2007) Biochem Soc Trans , vol.35 , pp. 760-763
    • Harding, P.J.1
  • 9
    • 77951092731 scopus 로고    scopus 로고
    • Mammalian G protein-coupled receptor expression in Escherichia coli: II. Refolding and biophysical characterization of mouse cannabinoid receptor 1 and human parathyroid hormone receptor 1
    • Michalke, K. et al. Mammalian G protein-coupled receptor expression in Escherichia coli: II. Refolding and biophysical characterization of mouse cannabinoid receptor 1 and human parathyroid hormone receptor 1. Anal Biochem 401, 74-80 (2010).
    • (2010) Anal Biochem , vol.401 , pp. 74-80
    • Michalke, K.1
  • 10
    • 79955033084 scopus 로고    scopus 로고
    • Evaluation of the Pichia pastoris expression system for the production of GPCRs for structural analysis
    • Asada, H. et al. Evaluation of the Pichia pastoris expression system for the production of GPCRs for structural analysis. Microb Cell Fact 10, 24 (2011).
    • (2011) Microb Cell Fact , vol.10 , pp. 24
    • Asada, H.1
  • 11
    • 36448995359 scopus 로고    scopus 로고
    • High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor
    • Cherezov, V. et al. High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor. Science 318, 1258-1265 (2007).
    • (2007) Science , vol.318 , pp. 1258-1265
    • Cherezov, V.1
  • 12
    • 31044446490 scopus 로고    scopus 로고
    • Semliki Forest virus vectors for overexpression of 101 G protein-coupled receptors in mammalian host cells
    • Hassaine, G. et al. Semliki Forest virus vectors for overexpression of 101 G protein-coupled receptors in mammalian host cells. Protein Expr Purif 45, 343-351 (2006).
    • (2006) Protein Expr Purif , vol.45 , pp. 343-351
    • Hassaine, G.1
  • 13
    • 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, P. J., Rajbhandary, U. L. & Khorana, H. G. The synthesis and high-level expression of a beta2-adrenergic receptor gene in a tetracycline-inducible stable mammalian cell line. Protein Sci 15, 1433-1440 (2006).
    • (2006) Protein Sci , vol.15 , pp. 1433-1440
    • Chelikani, P.1    Reeves, P.J.2    Rajbhandary, U.L.3    Khorana, H.G.4
  • 14
    • 84893954062 scopus 로고    scopus 로고
    • Molecular control of δ-opioid receptor signalling
    • Fenalti, G. et al. Molecular control of δ-opioid receptor signalling. Nature 506, 191-196 (2014).
    • (2014) Nature , vol.506 , pp. 191-196
    • Fenalti, G.1
  • 15
    • 79953802067 scopus 로고    scopus 로고
    • Production and partial purification of membrane proteins using a liposome-supplemented wheat cell-free translation system
    • Nozawa, A. et al. Production and partial purification of membrane proteins using a liposome-supplemented wheat cell-free translation system. BMC Biotechnol 11, 35 (2011).
    • (2011) BMC Biotechnol , vol.11 , pp. 35
    • Nozawa, A.1
  • 16
    • 34447630299 scopus 로고    scopus 로고
    • Functional cell-free synthesis of a seven helix membrane protein: In situ insertion of bacteriorhodopsin into liposomes
    • Kalmbach, R. et al. Functional cell-free synthesis of a seven helix membrane protein: in situ insertion of bacteriorhodopsin into liposomes. J Mol Biol 371, 639-648 (2007).
    • (2007) J Mol Biol , vol.371 , pp. 639-648
    • Kalmbach, R.1
  • 17
    • 84872742965 scopus 로고    scopus 로고
    • Function of Shaker potassium channels produced by cell-free translation upon injection into Xenopus oocytes
    • Jarecki, B. W., Makino, S., Beebe, E. T., Fox, B. G. & Chanda, B. Function of Shaker potassium channels produced by cell-free translation upon injection into Xenopus oocytes. Sci Rep 3, 1040 (2013).
    • (2013) Sci Rep , vol.3 , pp. 1040
    • Jarecki, B.W.1    Makino, S.2    Beebe, E.T.3    Fox, B.G.4    Chanda, B.5
  • 18
    • 34248572721 scopus 로고    scopus 로고
    • Cell-free production of G protein-coupled receptors for functional and structural studies
    • Klammt, C. et al. Cell-free production of G protein-coupled receptors for functional and structural studies. J Struct Biol 158, 482-493 (2007).
    • (2007) J Struct Biol , vol.158 , pp. 482-493
    • Klammt, C.1
  • 19
    • 57349119057 scopus 로고    scopus 로고
    • Efficient cell-free production of olfactory receptors: Detergent optimization, structure, and ligand binding analyses
    • Kaiser, L. et al. Efficient cell-free production of olfactory receptors: detergent optimization, structure, and ligand binding analyses. Proc Natl Acad Sci U S A 105, 15726-15731 (2008).
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 15726-15731
    • Kaiser, L.1
  • 20
    • 84921632535 scopus 로고    scopus 로고
    • High-throughput synthesis of stable isotope-labeled transmembrane proteins for targeted transmembrane proteomics using a wheat germ cell-free protein synthesis system
    • Takemori, N. et al. High-throughput synthesis of stable isotope-labeled transmembrane proteins for targeted transmembrane proteomics using a wheat germ cell-free protein synthesis system. Mol BioSyst 11, 361-365 (2015).
    • (2015) Mol BioSyst , vol.11 , pp. 361-365
    • Takemori, N.1
  • 21
    • 71549135217 scopus 로고    scopus 로고
    • Cell-free translation of integral membrane proteins into unilamelar liposomes
    • Goren, M. A., Nozawa, A., Makino, S.-i., Wrobel, R. L. & Fox, B. G. Cell-free translation of integral membrane proteins into unilamelar liposomes. Methods Enzymol. 463, 647-673 (2009).
    • (2009) Methods Enzymol. , vol.463 , pp. 647-673
    • Goren, M.A.1    Nozawa, A.2    Makino, S.-I.3    Wrobel, R.L.4    Fox, B.G.5
  • 22
    • 0028276006 scopus 로고
    • Luminescent oxygen channeling immunoassay: Measurement of particle binding kinetics by chemiluminescence
    • Ullman, E. F. et al. Luminescent oxygen channeling immunoassay: measurement of particle binding kinetics by chemiluminescence. Proc Natl Acad Sci USA 91, 5426-5430 (1994).
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 5426-5430
    • Ullman, E.F.1
  • 23
    • 38049057933 scopus 로고    scopus 로고
    • Arabidopsis HY5 protein functions as a DNA-binding tag for purification and functional immobilization of proteins on agarose/DNA microplate
    • Sawasaki, T. et al. Arabidopsis HY5 protein functions as a DNA-binding tag for purification and functional immobilization of proteins on agarose/DNA microplate. FEBS Lett 582, 221-228 (2008).
    • (2008) FEBS Lett , vol.582 , pp. 221-228
    • Sawasaki, T.1
  • 24
    • 76649104730 scopus 로고    scopus 로고
    • Practical cell-free protein synthesis system using purified wheat embryos
    • Takai, K., Sawasaki, T. & Endo, Y. Practical cell-free protein synthesis system using purified wheat embryos. Nat Protoc 5, 227-238 (2010).
    • (2010) Nat Protoc , vol.5 , pp. 227-238
    • Takai, K.1    Sawasaki, T.2    Endo, Y.3
  • 25
    • 84918792765 scopus 로고    scopus 로고
    • The ligand binding ability of dopamine D1 receptors synthesized using a wheat germ cell-free protein synthesis system with liposomes
    • Arimitsu, E. et al. The ligand binding ability of dopamine D1 receptors synthesized using a wheat germ cell-free protein synthesis system with liposomes. Eur J Pharmacol 745, 117-122 (2014).
    • (2014) Eur J Pharmacol , vol.745 , pp. 117-122
    • Arimitsu, E.1
  • 26
    • 0026630139 scopus 로고
    • Serine mutations in transmembrane V of the dopamine D1 receptor affect ligand interactions and receptor activation
    • Pollock, N. J. et al. Serine mutations in transmembrane V of the dopamine D1 receptor affect ligand interactions and receptor activation. J Biol Chem 267, 17780-17786 (1992).
    • (1992) J Biol Chem , vol.267 , pp. 17780-17786
    • Pollock, N.J.1
  • 27
    • 77955458275 scopus 로고    scopus 로고
    • Simple screening method for autoantigen proteins using the N-terminal biotinylated protein library produced by wheat cell-free synthesis
    • Matsuoka, K., Komori, H., Nose, M., Endo, Y. & Sawasaki, T. Simple screening method for autoantigen proteins using the N-terminal biotinylated protein library produced by wheat cell-free synthesis. J Proteome Res 9, 4264-4273 (2010).
    • (2010) J Proteome Res , vol.9 , pp. 4264-4273
    • Matsuoka, K.1    Komori, H.2    Nose, M.3    Endo, Y.4    Sawasaki, T.5
  • 28
    • 34248351200 scopus 로고    scopus 로고
    • Production and characterization of monoclonal antibodies sensitive to conformation in the 5HT2c serotonin receptor
    • Mancia, F. et al. Production and characterization of monoclonal antibodies sensitive to conformation in the 5HT2c serotonin receptor. Proc Natl Acad Sci U S A 104, 4303-4308 (2007).
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 4303-4308
    • Mancia, F.1
  • 29
    • 69949151874 scopus 로고    scopus 로고
    • A rapid and efficient single-cell manipulation method for screening antigen-specific antibody-secreting cells from human peripheral blood
    • Jin, A. et al. A rapid and efficient single-cell manipulation method for screening antigen-specific antibody-secreting cells from human peripheral blood. Nat Med 15, 1088-1092 (2009).
    • (2009) Nat Med , vol.15 , pp. 1088-1092
    • Jin, A.1
  • 30
    • 84871558037 scopus 로고    scopus 로고
    • A novel rabbit immunospot array assay on a chip allows for the rapid generation of rabbit monoclonal antibodies with high affinity
    • Ozawa, T. et al. A novel rabbit immunospot array assay on a chip allows for the rapid generation of rabbit monoclonal antibodies with high affinity. PLoS ONE 7, e52383 (2012).
    • (2012) PLoS ONE , vol.7
    • Ozawa, T.1
  • 31
    • 0021964141 scopus 로고
    • Measurements of the true affinity constant in solution of antigen-antibody complexes by enzyme-linked immunosorbent assay
    • Friguet, B., Chaffotte, A. F., Djavadi-Ohaniance, L. & Goldberg, M. E. Measurements of the true affinity constant in solution of antigen-antibody complexes by enzyme-linked immunosorbent assay. J Immunol Methods 77, 305-319 (1985).
    • (1985) J Immunol Methods , vol.77 , pp. 305-319
    • Friguet, B.1    Chaffotte, A.F.2    Djavadi-Ohaniance, L.3    Goldberg, M.E.4
  • 32
    • 33751252292 scopus 로고    scopus 로고
    • Direct observation of individual endogenous protein complexes in situ by proximity ligation
    • Söderberg, O. et al. Direct observation of individual endogenous protein complexes in situ by proximity ligation. Nat Methods 3, 995-1000 (2006).
    • (2006) Nat Methods , vol.3 , pp. 995-1000
    • Söderberg, O.1
  • 33
    • 77952964100 scopus 로고    scopus 로고
    • Biotinylated-sortase self-cleavage purification (BISOP) method for cell-free produced proteins
    • Matsunaga, S., Matsuoka, K., Shimizu, K., Endo, Y. & Sawasaki, T. Biotinylated-sortase self-cleavage purification (BISOP) method for cell-free produced proteins. BMC Biotechnol 10, 42 (2010).
    • (2010) BMC Biotechnol , vol.10 , pp. 42
    • Matsunaga, S.1    Matsuoka, K.2    Shimizu, K.3    Endo, Y.4    Sawasaki, T.5
  • 34
    • 0027340692 scopus 로고
    • Localization of D1 and D2 dopamine receptors in brain with subtype-specific antibodies
    • Levey, A. I. et al. Localization of D1 and D2 dopamine receptors in brain with subtype-specific antibodies. Proc Natl Acad Sci USA 90, 8861-8865 (1993).
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 8861-8865
    • Levey, A.I.1
  • 35
    • 33846252240 scopus 로고    scopus 로고
    • Genome-wide atlas of gene expression in the adult mouse brain
    • Lein, E. S. et al. Genome-wide atlas of gene expression in the adult mouse brain. Nature 445, 168 (2007).
    • (2007) Nature , vol.445 , pp. 168
    • Lein, E.S.1
  • 36
    • 33750320548 scopus 로고    scopus 로고
    • Depolarization-induced suppression of inhibition mediated by endocannabinoids at synapses from fast-spiking interneurons to medium spiny neurons in the striatum
    • Narushima, M., Uchigashima, M., Hashimoto, K., Watanabe, M. & Kano, M. Depolarization-induced suppression of inhibition mediated by endocannabinoids at synapses from fast-spiking interneurons to medium spiny neurons in the striatum. Eur J Neurosci 24, 2246-2252 (2006).
    • (2006) Eur J Neurosci , vol.24 , pp. 2246-2252
    • Narushima, M.1    Uchigashima, M.2    Hashimoto, K.3    Watanabe, M.4    Kano, M.5
  • 37
    • 33646572522 scopus 로고    scopus 로고
    • Expression and distribution of JNK/SAPK-associated scaffold protein JSAP1 in developing and adult mouse brain
    • Miura, E. et al. Expression and distribution of JNK/SAPK-associated scaffold protein JSAP1 in developing and adult mouse brain. J. Neurochem. 97, 1431-1446 (2006).
    • (2006) J. Neurochem. , vol.97 , pp. 1431-1446
    • Miura, E.1
  • 38
    • 0037168586 scopus 로고    scopus 로고
    • Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences
    • Strausberg, R. L. et al. Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci USA 99, 16899-16903 (2002).
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 16899-16903
    • Strausberg, R.L.1
  • 39
    • 56049095074 scopus 로고    scopus 로고
    • Exploration of human ORFeome: High-throughput preparation of ORF clones and efficient characterization of their protein products
    • Nagase, T. et al. Exploration of human ORFeome: high-throughput preparation of ORF clones and efficient characterization of their protein products. DNA Res. 15, 137-149 (2008).
    • (2008) DNA Res. , vol.15 , pp. 137-149
    • Nagase, T.1
  • 40
    • 77954069481 scopus 로고    scopus 로고
    • Quantitative electron microscopy for the nanoscale analysis of membrane lipid distribution
    • Fujita, A., Cheng, J. & Fujimoto, T. Quantitative electron microscopy for the nanoscale analysis of membrane lipid distribution. Nat Protoc 5, 661-669 (2010).
    • (2010) Nat Protoc , vol.5 , pp. 661-669
    • Fujita, A.1    Cheng, J.2    Fujimoto, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.