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Volumn 376, Issue 1, 2008, Pages 13-24

Analysis of a G protein-coupled receptor for neurotensin by liquid chromatography-electrospray ionization-mass spectrometry

Author keywords

Detergents; Electrospray ionization mass spectrometry (ESI MS); G protein coupled receptor (GPCR); Intact protein; Integral membrane protein; Neurotensin receptor

Indexed keywords

ACTIVATION ANALYSIS; BINDING SITES; CHLORINE COMPOUNDS; DETERGENTS; ELECTRODEPOSITION; LIGANDS; LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; RECOMBINANT PROTEINS; SIZE EXCLUSION CHROMATOGRAPHY; SOAPS (DETERGENTS);

EID: 41549121540     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2007.12.025     Document Type: Article
Times cited : (10)

References (39)
  • 1
    • 0036771038 scopus 로고    scopus 로고
    • Targeting neurotensin receptors with agonists and antagonists for therapeutic purposes
    • Kitabgi P. Targeting neurotensin receptors with agonists and antagonists for therapeutic purposes. Curr. Opin. Drug Disc. Dev. 5 (2002) 764-776
    • (2002) Curr. Opin. Drug Disc. Dev. , vol.5 , pp. 764-776
    • Kitabgi, P.1
  • 2
    • 0034614509 scopus 로고    scopus 로고
    • Identification of residues involved in neurotensin binding and modeling of the agonist binding site in neurotensin receptor 1
    • Barroso S., Richard F., Nicolas-Etheve D., Reversat J.L., Bernassau J.M., Kitabgi P., and Labbe-Jullie C. Identification of residues involved in neurotensin binding and modeling of the agonist binding site in neurotensin receptor 1. J. Biol. Chem. 275 (2000) 328-336
    • (2000) J. Biol. Chem. , vol.275 , pp. 328-336
    • Barroso, S.1    Richard, F.2    Nicolas-Etheve, D.3    Reversat, J.L.4    Bernassau, J.M.5    Kitabgi, P.6    Labbe-Jullie, C.7
  • 3
    • 15844417994 scopus 로고    scopus 로고
    • Proposed ligand binding site of the transmembrane receptor for neurotensin(8-13)
    • Pang Y.P., Cusack B., Groshan K., and Richelson E. Proposed ligand binding site of the transmembrane receptor for neurotensin(8-13). J. Biol. Chem. 271 (1996) 15060-15068
    • (1996) J. Biol. Chem. , vol.271 , pp. 15060-15068
    • Pang, Y.P.1    Cusack, B.2    Groshan, K.3    Richelson, E.4
  • 5
    • 0347286732 scopus 로고    scopus 로고
    • Chemical cross-linking and mass spectrometry for mapping three-dimensional structures of proteins and protein complexes
    • Sinz A. Chemical cross-linking and mass spectrometry for mapping three-dimensional structures of proteins and protein complexes. J. Mass Spectrom. 38 (2003) 1225-1237
    • (2003) J. Mass Spectrom. , vol.38 , pp. 1225-1237
    • Sinz, A.1
  • 6
    • 35348859706 scopus 로고    scopus 로고
    • Investigation of protein-ligand interactions by mass spectrometry
    • Sinz A. Investigation of protein-ligand interactions by mass spectrometry. Chem. Med. Chem. 2 (2007) 425-431
    • (2007) Chem. Med. Chem. , vol.2 , pp. 425-431
    • Sinz, A.1
  • 7
    • 0030330462 scopus 로고    scopus 로고
    • The effect of detergents on proteins analyzed by electrospray ionization
    • Chapman J. (Ed), Humana Press, Totowa, NJ
    • Ogorzalek Loo R.R., Dales N., and Andrews P.C. The effect of detergents on proteins analyzed by electrospray ionization. In: Chapman J. (Ed). Protein and Peptide Analysis by Mass Spectrometry (1996), Humana Press, Totowa, NJ 141-160
    • (1996) Protein and Peptide Analysis by Mass Spectrometry , pp. 141-160
    • Ogorzalek Loo, R.R.1    Dales, N.2    Andrews, P.C.3
  • 9
    • 0035339118 scopus 로고    scopus 로고
    • Mass spectrometric analysis of cyanogen bromide fragments of integral membrane proteins at the picomole level: Application to rhodopsin
    • Kraft P., Mills J., and Dratz E. Mass spectrometric analysis of cyanogen bromide fragments of integral membrane proteins at the picomole level: Application to rhodopsin. Anal. Biochem. 292 (2001) 76-86
    • (2001) Anal. Biochem. , vol.292 , pp. 76-86
    • Kraft, P.1    Mills, J.2    Dratz, E.3
  • 10
    • 0035886674 scopus 로고    scopus 로고
    • Mass spectrometric analysis of integral membrane proteins at the subnanomolar level: Application to recombinant photopigments
    • Ablonczy Z., Kono M., Crouch R.K., and Knapp D.R. Mass spectrometric analysis of integral membrane proteins at the subnanomolar level: Application to recombinant photopigments. Anal. Chem. 73 (2001) 4774-4779
    • (2001) Anal. Chem. , vol.73 , pp. 4774-4779
    • Ablonczy, Z.1    Kono, M.2    Crouch, R.K.3    Knapp, D.R.4
  • 11
    • 26444447986 scopus 로고    scopus 로고
    • Mass spectrometric analysis of integral membrane proteins at the subpicomolar level: Application to rhodopsin
    • Ablonczy Z., Crouch R.K., and Knapp D.R. Mass spectrometric analysis of integral membrane proteins at the subpicomolar level: Application to rhodopsin. J. Chromatogr. B 825 (2005) 169-175
    • (2005) J. Chromatogr. B , vol.825 , pp. 169-175
    • Ablonczy, Z.1    Crouch, R.K.2    Knapp, D.R.3
  • 12
    • 17644390240 scopus 로고    scopus 로고
    • Mass spectrometric analysis of agonist effects on posttranslational modifications of the β-2 adrenoceptor in mammalian cells
    • Trester-Zedlitz M., Burlingame A., Kobilka B., and von Zastrow M. Mass spectrometric analysis of agonist effects on posttranslational modifications of the β-2 adrenoceptor in mammalian cells. Biochemistry 44 (2005) 6133-6143
    • (2005) Biochemistry , vol.44 , pp. 6133-6143
    • Trester-Zedlitz, M.1    Burlingame, A.2    Kobilka, B.3    von Zastrow, M.4
  • 13
    • 0031964241 scopus 로고    scopus 로고
    • Post-translational modifications of endothelin receptor B from bovine lungs analyzed by mass spectrometry
    • Roos M., Soskic V., Poznanovic S., and Grodovac-Zimmermann J. Post-translational modifications of endothelin receptor B from bovine lungs analyzed by mass spectrometry. J. Biol. Chem. 273 (1998) 924-931
    • (1998) J. Biol. Chem. , vol.273 , pp. 924-931
    • Roos, M.1    Soskic, V.2    Poznanovic, S.3    Grodovac-Zimmermann, J.4
  • 15
    • 0141922921 scopus 로고    scopus 로고
    • Purification and mass spectrometric analysis of the δ opioid receptor
    • Christoffers K.H., Li H., Keenan S.A., and Howells R.D. Purification and mass spectrometric analysis of the δ opioid receptor. Mol. Brain Res. 118 (2003) 119-131
    • (2003) Mol. Brain Res. , vol.118 , pp. 119-131
    • Christoffers, K.H.1    Li, H.2    Keenan, S.A.3    Howells, R.D.4
  • 16
    • 18944378413 scopus 로고    scopus 로고
    • Purification and mass spectrometric analysis of the δ opioid receptor
    • Christoffers K.H., Li H., and Howells R.D. Purification and mass spectrometric analysis of the δ opioid receptor. Mol. Brain Res. 136 (2005) 54-64
    • (2005) Mol. Brain Res. , vol.136 , pp. 54-64
    • Christoffers, K.H.1    Li, H.2    Howells, R.D.3
  • 17
    • 33947415352 scopus 로고    scopus 로고
    • Analysis of an intact G-protein coupled receptor by MALDI-TOF mass spectrometry: Molecular heterogeneity of the tachykinin NK-1 receptor
    • Alves I.D., Sachon E., Bolbach G., Millstine L., Lavielle S., and Sagan S. Analysis of an intact G-protein coupled receptor by MALDI-TOF mass spectrometry: Molecular heterogeneity of the tachykinin NK-1 receptor. Anal. Chem. 79 (2007) 2189-2198
    • (2007) Anal. Chem. , vol.79 , pp. 2189-2198
    • Alves, I.D.1    Sachon, E.2    Bolbach, G.3    Millstine, L.4    Lavielle, S.5    Sagan, S.6
  • 18
    • 0031004233 scopus 로고    scopus 로고
    • Identification of transmembrane tryptic peptides of rhodopsin using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Barnidge D.R., Dratz E.A., Sunner J., and Jesaitis A.J. Identification of transmembrane tryptic peptides of rhodopsin using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Protein Sci. 6 (1997) 816-824
    • (1997) Protein Sci. , vol.6 , pp. 816-824
    • Barnidge, D.R.1    Dratz, E.A.2    Sunner, J.3    Jesaitis, A.J.4
  • 19
    • 0036127198 scopus 로고    scopus 로고
    • Mass spectrometric analysis of the kinetics of in vivo rhodopsin phosphorylation
    • Lee K.A., Craven K.B., Niemi G.A., and Hurley J.B. Mass spectrometric analysis of the kinetics of in vivo rhodopsin phosphorylation. Protein Sci. 11 (2002) 862-874
    • (2002) Protein Sci. , vol.11 , pp. 862-874
    • Lee, K.A.1    Craven, K.B.2    Niemi, G.A.3    Hurley, J.B.4
  • 20
    • 0027223209 scopus 로고
    • Mass spectrometric identification of phosphorylation sites in bleached bovine rhodopsin
    • Papac D.I., Oatis J.E., Crouch R.K., and Knapp D.R. Mass spectrometric identification of phosphorylation sites in bleached bovine rhodopsin. Biochemistry 32 (1993) 5930-5934
    • (1993) Biochemistry , vol.32 , pp. 5930-5934
    • Papac, D.I.1    Oatis, J.E.2    Crouch, R.K.3    Knapp, D.R.4
  • 21
    • 0026793047 scopus 로고
    • Palmitylation of a G-protein coupled receptor: Direct analysis by tandem mass spectrometry
    • Papac D.I., Thornburg K.R., Bullesbach E.E., Crouch R.K., and Knapp D.R. Palmitylation of a G-protein coupled receptor: Direct analysis by tandem mass spectrometry. J. Biol. Chem. 267 (1992) 16889-16894
    • (1992) J. Biol. Chem. , vol.267 , pp. 16889-16894
    • Papac, D.I.1    Thornburg, K.R.2    Bullesbach, E.E.3    Crouch, R.K.4    Knapp, D.R.5
  • 22
    • 4444382102 scopus 로고    scopus 로고
    • Probing rhodopsin-transducin interactions by surface modification and mass spectrometry
    • Wang X., Kim S.H., Ablonczy Z., Crouch R.K., and Knapp D.R. Probing rhodopsin-transducin interactions by surface modification and mass spectrometry. Biochemistry 43 (2004) 11153-11162
    • (2004) Biochemistry , vol.43 , pp. 11153-11162
    • Wang, X.1    Kim, S.H.2    Ablonczy, Z.3    Crouch, R.K.4    Knapp, D.R.5
  • 24
    • 0031776931 scopus 로고    scopus 로고
    • Electrospray ionization-mass spectrometry of intact intrinsic membrane proteins
    • Whitelegge J.P., Gundersen C.B., and Faull K.F. Electrospray ionization-mass spectrometry of intact intrinsic membrane proteins. Protein Sci. 7 (1998) 1423-1430
    • (1998) Protein Sci. , vol.7 , pp. 1423-1430
    • Whitelegge, J.P.1    Gundersen, C.B.2    Faull, K.F.3
  • 25
    • 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. Automated large-scale purification of a G protein-coupled receptor for neurotensin. FEBS Lett. 564 (2004) 289-293
    • (2004) FEBS Lett. , vol.564 , pp. 289-293
    • White, J.F.1    Trinh, L.B.2    Shiloach, J.3    Grisshammer, R.4
  • 26
    • 26444581283 scopus 로고    scopus 로고
    • Large-scale expression and purification of a G-protein-coupled receptor for structure determination: An overview
    • Grisshammer R., White J.F., Trinh L.B., and Shiloach J. Large-scale expression and purification of a G-protein-coupled receptor for structure determination: An overview. J. Struct. Funct. Genom. 6 (2005) 159-163
    • (2005) J. Struct. Funct. Genom. , vol.6 , pp. 159-163
    • Grisshammer, R.1    White, J.F.2    Trinh, L.B.3    Shiloach, J.4
  • 27
    • 0030561197 scopus 로고    scopus 로고
    • Electrospray ionization mass spectrometry of genetically and chemically modified bacteriorhodopsins
    • Hufnagel P., Schweiger U., Eckerskorn C., and Oesterhelt D. Electrospray ionization mass spectrometry of genetically and chemically modified bacteriorhodopsins. Anal. Biochem. 243 (1996) 46-54
    • (1996) Anal. Biochem. , vol.243 , pp. 46-54
    • Hufnagel, P.1    Schweiger, U.2    Eckerskorn, C.3    Oesterhelt, D.4
  • 28
    • 0033541651 scopus 로고    scopus 로고
    • Extraction method for analysis of detergent-solubilized bacteriorhodopsin and hydrophobic peptides by electrospray ionization mass spectrometry
    • Barnidge D.R., Dratz E.A., Jesaitis A.J., and Sunner J. Extraction method for analysis of detergent-solubilized bacteriorhodopsin and hydrophobic peptides by electrospray ionization mass spectrometry. Anal. Biochem. 269 (1999) 1-9
    • (1999) Anal. Biochem. , vol.269 , pp. 1-9
    • Barnidge, D.R.1    Dratz, E.A.2    Jesaitis, A.J.3    Sunner, J.4
  • 29
    • 0030900871 scopus 로고    scopus 로고
    • Analysis of hydrophobic proteins and peptides by electrospray ionization mass spectrometry
    • Schaller J., Pellascio B.C., and Schlunegger U.P. Analysis of hydrophobic proteins and peptides by electrospray ionization mass spectrometry. Rapid Commun. Mass Spectrom. 11 (1997) 418-426
    • (1997) Rapid Commun. Mass Spectrom. , vol.11 , pp. 418-426
    • Schaller, J.1    Pellascio, B.C.2    Schlunegger, U.P.3
  • 30
    • 0027166358 scopus 로고
    • Analysis of hydrophobic proteins and peptides by electrospray ionization mass spectrometry
    • Schindler P.A., Vandorsselaer A., and Falick A.M. Analysis of hydrophobic proteins and peptides by electrospray ionization mass spectrometry. Anal. Biochem. 213 (1993) 256-263
    • (1993) Anal. Biochem. , vol.213 , pp. 256-263
    • Schindler, P.A.1    Vandorsselaer, A.2    Falick, A.M.3
  • 34
    • 0036051481 scopus 로고    scopus 로고
    • The chloroplast grana proteome defined by intact mass measurements from liquid chromatography mass spectrometry
    • Gomez S.M., Nishio J.N., Faull K.F., and Whitelegge J.P. The chloroplast grana proteome defined by intact mass measurements from liquid chromatography mass spectrometry. Mol. Cell. Proteomics 1 (2002) 46-59
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 46-59
    • Gomez, S.M.1    Nishio, J.N.2    Faull, K.F.3    Whitelegge, J.P.4
  • 35
    • 0942276251 scopus 로고    scopus 로고
    • A detergent- and cyanogen bromide-free method for integral membrane proteomics: Application to Halobacterium purple membranes and the human epidermal membrane proteome
    • Blonder J., Conrads T.P., Yu L.R., Terunuma A., Janini G.M., Issaq H.J., Vogel J.C., and Veenstra T.D. A detergent- and cyanogen bromide-free method for integral membrane proteomics: Application to Halobacterium purple membranes and the human epidermal membrane proteome. Proteomics 4 (2004) 31-45
    • (2004) Proteomics , vol.4 , pp. 31-45
    • Blonder, J.1    Conrads, T.P.2    Yu, L.R.3    Terunuma, A.4    Janini, G.M.5    Issaq, H.J.6    Vogel, J.C.7    Veenstra, T.D.8
  • 36
    • 33645466243 scopus 로고    scopus 로고
    • Toward the complete membrane proteome: High coverage of integral membrane proteins through transmembrane peptide detection
    • Fischer F., Wolters D., Rogner M., and Poetsch A. Toward the complete membrane proteome: High coverage of integral membrane proteins through transmembrane peptide detection. Mol. Cell. Proteomics 5 (2006) 444-453
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 444-453
    • Fischer, F.1    Wolters, D.2    Rogner, M.3    Poetsch, A.4
  • 37
    • 1842532945 scopus 로고    scopus 로고
    • A complete peptide mapping of membrane proteins: A novel surfactant aiding the enzymatic digestion of bacteriorhodopsin
    • Yu Y.Q., Gilar M., and Gebler J.C. A complete peptide mapping of membrane proteins: A novel surfactant aiding the enzymatic digestion of bacteriorhodopsin. Rapid Commun. Mass Spectrom. 18 (2004) 711-715
    • (2004) Rapid Commun. Mass Spectrom. , vol.18 , pp. 711-715
    • Yu, Y.Q.1    Gilar, M.2    Gebler, J.C.3
  • 38
    • 0016192651 scopus 로고
    • Surface tension of amino acid solutions: Hydrophobicity scale of amino acid residues
    • Bull H.B., and Breese K. Surface tension of amino acid solutions: Hydrophobicity scale of amino acid residues. Arch. Biochem. Biophys. 161 (1974) 665-670
    • (1974) Arch. Biochem. Biophys. , vol.161 , pp. 665-670
    • Bull, H.B.1    Breese, K.2
  • 39
    • 0025345759 scopus 로고
    • Structure and functional expression of the cloned rat neurotensin receptor
    • Tanaka K., Masu M., and Nakanishi S. Structure and functional expression of the cloned rat neurotensin receptor. Neuron 4 (1990) 847-854
    • (1990) Neuron , vol.4 , pp. 847-854
    • Tanaka, K.1    Masu, M.2    Nakanishi, S.3


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