메뉴 건너뛰기




Volumn 159, Issue 8, 1997, Pages 4045-4054

The Ligand Binding Site of the Formyl Peptide Receptor Maps in the Transmembrane Region

Author keywords

[No Author keywords available]

Indexed keywords

FORMYLMETHIONYLLEUCYLPHENYLALANINE; FORMYLPEPTIDE RECEPTOR; GUANINE NUCLEOTIDE BINDING PROTEIN; IMMUNOGLOBULIN RECEPTOR; LIGAND; RECEPTOR;

EID: 0031572524     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (57)

References (67)
  • 1
    • 0026548156 scopus 로고
    • In vitro mutagenesis and the search for structure-function relationships among G protein-coupled receptors
    • Savarese, T. M., and C. M. Fraser. 1992. In vitro mutagenesis and the search for structure-function relationships among G protein-coupled receptors. Biochem. J. 283:1.
    • (1992) Biochem. J. , vol.283 , pp. 1
    • Savarese, T.M.1    Fraser, C.M.2
  • 3
    • 0027506471 scopus 로고
    • The probable arrangement of the helices in G protein-coupled receptors
    • Baldwin, J. M. 1993. The probable arrangement of the helices in G protein-coupled receptors. EMBO J. 12:1693.
    • (1993) EMBO J. , vol.12 , pp. 1693
    • Baldwin, J.M.1
  • 4
    • 0019141401 scopus 로고
    • Site of attachment of 11-cis-retinal in bovine rhodopsin
    • Wang, J. K., J. H. McDowell, and P. A. Hargrave. 1980. Site of attachment of 11-cis-retinal in bovine rhodopsin. Biochemistry 19:5111.
    • (1980) Biochemistry , vol.19 , pp. 5111
    • Wang, J.K.1    McDowell, J.H.2    Hargrave, P.A.3
  • 5
    • 0025050478 scopus 로고
    • Orientation of retinal in bovine rhodopsin determined by cross-linking using a photoactivatable analog of 11-cis-retinal
    • Nakayama, T. A., and H. G. Khorana. 1990. Orientation of retinal in bovine rhodopsin determined by cross-linking using a photoactivatable analog of 11-cis-retinal. J. Biol. Chem. 265:15762.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15762
    • Nakayama, T.A.1    Khorana, H.G.2
  • 6
    • 0025761854 scopus 로고
    • Mapping of the amino acids in membrane-embedded helices that interact with the retinal chromophore in bovine rhodopsin
    • Nakayama, T. A., and H. G. Khorana. 1991. Mapping of the amino acids in membrane-embedded helices that interact with the retinal chromophore in bovine rhodopsin. J. Biol. Chem. 266:4269.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4269
    • Nakayama, T.A.1    Khorana, H.G.2
  • 7
    • 0021333230 scopus 로고
    • Purification and identification of formyl-methionyl-leucyl-phenylalanine as the major peptide neutrophil chemotactic factor produced by Escherichia coli
    • Marasco, W. A., S. H. Phan, H. Krutzsch, H. J. Showell, D. E. Feltner, R. Nairn, E. L. Becker, and P. A. Ward. 1984. Purification and identification of formyl-methionyl-leucyl-phenylalanine as the major peptide neutrophil chemotactic factor produced by Escherichia coli. J. Biol. Chem. 259:5430.
    • (1984) J. Biol. Chem. , vol.259 , pp. 5430
    • Marasco, W.A.1    Phan, S.H.2    Krutzsch, H.3    Showell, H.J.4    Feltner, D.E.5    Nairn, R.6    Becker, E.L.7    Ward, P.A.8
  • 8
    • 0027955201 scopus 로고
    • Continuous spectrofluorometric analysis of formyl peptide receptor ternary complex interactions
    • Posner, R. G., S. P. Fay, M. D. Domalewski, and L. A. Sklar. 1994. Continuous spectrofluorometric analysis of formyl peptide receptor ternary complex interactions. Mol. Pharmacol. 45:65.
    • (1994) Mol. Pharmacol. , vol.45 , pp. 65
    • Posner, R.G.1    Fay, S.P.2    Domalewski, M.D.3    Sklar, L.A.4
  • 10
    • 0027184065 scopus 로고
    • Multiple domains of the M-formyl peptide receptor are required for high-affinity ligand binding
    • Quehenberger, O., E. R. Prossnitz, S. L. Cavanagh, C. G. Cochrane, and R. D. Ye. 1993. Multiple domains of the M-formyl peptide receptor are required for high-affinity ligand binding. J. Biol. Chem. 268:18167.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18167
    • Quehenberger, O.1    Prossnitz, E.R.2    Cavanagh, S.L.3    Cochrane, C.G.4    Ye, R.D.5
  • 11
    • 0025766609 scopus 로고
    • Real-Time Analysis of the Assembly of Ligand, Receptor, and G Protein by quantitative fluorescence flow cytometry
    • Fay, S. P., R. G. Posner, W. N. Swann, and L. A. Sklar. 1991. Real-Time Analysis of the Assembly of Ligand, Receptor, and G Protein by quantitative fluorescence flow cytometry. Biochemistry 30:5066.
    • (1991) Biochemistry , vol.30 , pp. 5066
    • Fay, S.P.1    Posner, R.G.2    Swann, W.N.3    Sklar, L.A.4
  • 12
    • 0020644805 scopus 로고
    • Characterization of the rat neutrophil formyl peptide chemotaxis receptor
    • Marasco, W. A., J. C. Fantone, R. J. Freer, and P. A. Ward. 1983. Characterization of the rat neutrophil formyl peptide chemotaxis receptor. Am. J. Pathol. 111:273.
    • (1983) Am. J. Pathol. , vol.111 , pp. 273
    • Marasco, W.A.1    Fantone, J.C.2    Freer, R.J.3    Ward, P.A.4
  • 13
    • 0021257625 scopus 로고
    • Regulatory mechanisms of a chemoattractant receptor on leukocytes
    • Snyderman, R. 1984. Regulatory mechanisms of a chemoattractant receptor on leukocytes. Fed. Proc. 42:2743.
    • (1984) Fed. Proc. , vol.42 , pp. 2743
    • Snyderman, R.1
  • 16
    • 0026644385 scopus 로고
    • A structural homologue of the N-formyl peptide receptor: Characterization and chromosome mapping of a peptide chemoattractant receptor family
    • Murphy, P. M., T. Özçelik, R. T. Kenney, H. L. Tiffany, D. McDermott, and U. Francke. 1992. A structural homologue of the N-formyl peptide receptor: characterization and chromosome mapping of a peptide chemoattractant receptor family. J. Biol. Chem. 267:7637.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7637
    • Murphy, P.M.1    Özçelik, T.2    Kenney, R.T.3    Tiffany, H.L.4    McDermott, D.5    Francke, U.6
  • 17
    • 0026784058 scopus 로고
    • Cloning of a cDNA encoding a receptor related to the formyl peptide receptor of human neutrophils
    • Perez, H. D., R. Holmes, E. Kelly, J. McClary, and W. H. Andrews. 1992. Cloning of a cDNA encoding a receptor related to the formyl peptide receptor of human neutrophils. Gene 118:303.
    • (1992) Gene , vol.118 , pp. 303
    • Perez, H.D.1    Holmes, R.2    Kelly, E.3    McClary, J.4    Andrews, W.H.5
  • 18
    • 0025890276 scopus 로고
    • Expression cloning of a receptor for C5a anaphylatoxin on differentiated HL-60 cells
    • Boulay, F., L. Mery, M. Tardif, L. Brouchon, and P. Vignais. 1991. Expression cloning of a receptor for C5a anaphylatoxin on differentiated HL-60 cells. Biochemistry 30:2993.
    • (1991) Biochemistry , vol.30 , pp. 2993
    • Boulay, F.1    Mery, L.2    Tardif, M.3    Brouchon, L.4    Vignais, P.5
  • 19
    • 0029094253 scopus 로고
    • Quality control in the secretory pathway
    • Hammond, C., and A. Helenius. 1995. Quality control in the secretory pathway. Curr. Opin. Cell Biol. 7:523.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 523
    • Hammond, C.1    Helenius, A.2
  • 20
    • 0026659680 scopus 로고
    • The endoplasmic reticulum as a protein-folding compartment
    • Helenius, A., T. Marquardt, and I. Braakman. 1992. The endoplasmic reticulum as a protein-folding compartment. Trends Cell Biol. 2:227.
    • (1992) Trends Cell Biol. , vol.2 , pp. 227
    • Helenius, A.1    Marquardt, T.2    Braakman, I.3
  • 21
    • 0026047192 scopus 로고
    • Transmembrane signalling by the N-formyl peptide receptor in stably transfected fibroblasts
    • Prossnitz, E. R., O. Quehenberger, C. G. Cochrane, and R. D. Ye. 1991. Transmembrane signalling by the N-formyl peptide receptor in stably transfected fibroblasts. Biochem. Biophys. Res. Commun. 179:471.
    • (1991) Biochem. Biophys. Res. Commun. , vol.179 , pp. 471
    • Prossnitz, E.R.1    Quehenberger, O.2    Cochrane, C.G.3    Ye, R.D.4
  • 22
    • 0020491290 scopus 로고
    • Oligonucleotide-directed mutagenesis using M13-derived vectors: An efficient and general procedure for the production of point mutations in any fragment
    • Zoller, M. J., and M. Smith. 1982. Oligonucleotide-directed mutagenesis using M13-derived vectors: an efficient and general procedure for the production of point mutations in any fragment. Nucleic Acids Res. 10:6487.
    • (1982) Nucleic Acids Res. , vol.10 , pp. 6487
    • Zoller, M.J.1    Smith, M.2
  • 23
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A., J. D. Roberts, and R. A. Zakour. 1987. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154:367.
    • (1987) Methods Enzymol. , vol.154 , pp. 367
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 25
    • 0029421657 scopus 로고
    • Cell surface accumulation of over-expressed hamster lysosomal membrane glycoproteins
    • Uthayakumar, S., and B. L. Granger. 1995. Cell surface accumulation of over-expressed hamster lysosomal membrane glycoproteins. Cell. Mol. Biol. Res. 41: 405.
    • (1995) Cell. Mol. Biol. Res. , vol.41 , pp. 405
    • Uthayakumar, S.1    Granger, B.L.2
  • 26
    • 0023850352 scopus 로고
    • SRα promoter: An efficient and versatile mammalian cDNA expression system composed of the simian virus 40 early promoter and the R-U5 segment of human T-cell leukemia virus type 1 long terminal repeat
    • Takebe, Y., M. Seiki, J.-I. Fujisawa, P. Hoy, K. Yokota, K.-I. Arai, M. Yoshida, and N. Arai. 1988. SRα promoter: an efficient and versatile mammalian cDNA expression system composed of the simian virus 40 early promoter and the R-U5 segment of human T-cell leukemia virus type 1 long terminal repeat. Mol. Cell. Biol. 8:466.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 466
    • Takebe, Y.1    Seiki, M.2    Fujisawa, J.-I.3    Hoy, P.4    Yokota, K.5    Arai, K.-I.6    Yoshida, M.7    Arai, N.8
  • 27
    • 0025868356 scopus 로고
    • A new cationic liposome reagent mediating nearly quantitative transfection of animal cells
    • Rose, J. K., L. Buonocore, and M. A. Whitt. 1991. A new cationic liposome reagent mediating nearly quantitative transfection of animal cells. Biotechniques 10:520.
    • (1991) Biotechniques , vol.10 , pp. 520
    • Rose, J.K.1    Buonocore, L.2    Whitt, M.A.3
  • 28
    • 0021101284 scopus 로고
    • Expression of recombinant plasmids in mammalian cells is enhanced by sodium butyrate
    • Gorman, C. M., B. H. Howard, and R. Reeves. 1983. Expression of recombinant plasmids in mammalian cells is enhanced by sodium butyrate. Nucleic Acids Res. 11:7631.
    • (1983) Nucleic Acids Res. , vol.11 , pp. 7631
    • Gorman, C.M.1    Howard, B.H.2    Reeves, R.3
  • 29
    • 0028916589 scopus 로고
    • Binding of low affinity N-formyl peptide receptors to G protein: Characterization of a novel inactive receptor intermediate
    • Prossnitz, E. R., R. E. Schreiber, G. M. Bokoch, and R. D. Ye. 1995. Binding of low affinity N-formyl peptide receptors to G protein: characterization of a novel inactive receptor intermediate. J. Biol. Chem. 270:10686.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10686
    • Prossnitz, E.R.1    Schreiber, R.E.2    Bokoch, G.M.3    Ye, R.D.4
  • 30
    • 0027370126 scopus 로고
    • Species and subtype variants of the N-formyl peptide chemotactic receptor reveal multiple important functional domains
    • Gao, J.-L., and P. M. Murphy. 1993. Species and subtype variants of the N-formyl peptide chemotactic receptor reveal multiple important functional domains. J. Biol. Chem. 268:25395.
    • (1993) J. Biol. Chem. , vol.268 , pp. 25395
    • Gao, J.-L.1    Murphy, P.M.2
  • 31
    • 0025729153 scopus 로고
    • Spectral tuning of pigments underlying red-green color vision
    • Neitz, M., J. Neitz, and G. H. Jacobs. 1991. Spectral tuning of pigments underlying red-green color vision. Science 252:971.
    • (1991) Science , vol.252 , pp. 971
    • Neitz, M.1    Neitz, J.2    Jacobs, G.H.3
  • 32
    • 0029002999 scopus 로고
    • Arginine 206 of the C5a receptor is critical for ligand recognition and receptor activation by C-terminal hexapeptide by C-terminal hexapeptide analogs
    • DeMartino, J. A., Z. D. Konteatis, S. J. Siciliano, G. Van Riper, D. J. Underwood, P. A. Fischer, and M. S. Springer. 1995. Arginine 206 of the C5a receptor is critical for ligand recognition and receptor activation by C-terminal hexapeptide by C-terminal hexapeptide analogs. J. Biol. Chem. 270:15966.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15966
    • DeMartino, J.A.1    Konteatis, Z.D.2    Siciliano, S.J.3    Van Riper, G.4    Underwood, D.J.5    Fischer, P.A.6    Springer, M.S.7
  • 34
    • 0024344941 scopus 로고
    • Identification of two serine residues involved in agonist activation of the β-adrenergic receptor
    • Strader, C. D., M. R. Candelore, W. S. Hills, I. S. Sigal, and R. A. F. Dixon. 1989. Identification of two serine residues involved in agonist activation of the β-adrenergic receptor. J. Biol. Chem. 264:13572.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13572
    • Strader, C.D.1    Candelore, M.R.2    Hills, W.S.3    Sigal, I.S.4    Dixon, R.A.F.5
  • 35
    • 0026040728 scopus 로고
    • 3 muscarinic receptor: Identification of a series of threonine and tyrosine residues involved in agonist but not antagonist binding
    • 3 muscarinic receptor: identification of a series of threonine and tyrosine residues involved in agonist but not antagonist binding. EMBO J. 10:3729.
    • (1991) EMBO J. , vol.10 , pp. 3729
    • Wess, J.1    Gdula, D.2    Brann, M.R.3
  • 38
    • 0025021022 scopus 로고
    • Fluorescence analysis of the size of a binding pocket of a peptide receptor at natural abundance
    • Sklar, L. A., S. P. Fay, B. E. Seligman, R. J. Freer, N. Muthukumaraswamy, and H. Mueller. 1990. Fluorescence analysis of the size of a binding pocket of a peptide receptor at natural abundance. Biochemistry 29:313.
    • (1990) Biochemistry , vol.29 , pp. 313
    • Sklar, L.A.1    Fay, S.P.2    Seligman, B.E.3    Freer, R.J.4    Muthukumaraswamy, N.5    Mueller, H.6
  • 39
    • 0026783557 scopus 로고
    • i proteins in the Sf9 insect cell: Characterization of the uncoupled recombinant N-formyl peptide receptor
    • i proteins in the Sf9 insect cell: characterization of the uncoupled recombinant N-formyl peptide receptor. J. Biol. Chem. 267:19757.
    • (1992) J. Biol. Chem. , vol.267 , pp. 19757
    • Quehenberger, O.1    Prossnitz, E.R.2    Cochrane, C.G.3    Ye, R.D.4
  • 40
    • 0028038183 scopus 로고
    • Human formyl peptide receptor ligand binding domain(s): Studies using an improved mutagenesis/expression vector reveal a novel mechanism for the regulation of the receptor occupancy
    • Perez, H. D., L. Vilander, W. H. Andrews, and R. Holmes. 1994. Human formyl peptide receptor ligand binding domain(s): studies using an improved mutagenesis/expression vector reveal a novel mechanism for the regulation of the receptor occupancy. J. Biol. Chem. 269:22485.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22485
    • Perez, H.D.1    Vilander, L.2    Andrews, W.H.3    Holmes, R.4
  • 41
    • 0028224016 scopus 로고
    • Structural and functional characterization of the human formyl peptide receptor ligand-binding region
    • Radel, S. J., R. J. Genco, and E. De Nardin. 1994. Structural and functional characterization of the human formyl peptide receptor ligand-binding region. Infect. Immun. 62:1726.
    • (1994) Infect. Immun. , vol.62 , pp. 1726
    • Radel, S.J.1    Genco, R.J.2    De Nardin, E.3
  • 42
    • 0027955272 scopus 로고
    • Generation of chimeric C5a/formyl peptide receptors: Towards the identification of the human C5a receptor binding site
    • Pease, J. E., D. R. Burton, and M. D. Barker. 1994. Generation of chimeric C5a/formyl peptide receptors: towards the identification of the human C5a receptor binding site. Eur. J. Immunol. 24:211.
    • (1994) Eur. J. Immunol. , vol.24 , pp. 211
    • Pease, J.E.1    Burton, D.R.2    Barker, M.D.3
  • 43
    • 0028169697 scopus 로고
    • 2-terminal region of C5aR but not that of FPR is critical for both protein transport and ligand binding
    • 2-terminal region of C5aR but not that of FPR is critical for both protein transport and ligand binding. J. Biol. Chem. 269:3457.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3457
    • Mery, L.1    Boulay, F.2
  • 47
    • 0028334663 scopus 로고
    • The amino terminus of the human C5a receptor is required for high affinity C5a binding and for the receptor activation by C5a but not C5a analogs
    • DeMartino, J. A., G. Van Riper, S. J. Siciliano, C. J. Molineaux, Z. D. Konteatis, H. Rosen, and M. S. Springer. 1994. The amino terminus of the human C5a receptor is required for high affinity C5a binding and for the receptor activation by C5a but not C5a analogs. J. Biol. Chem. 269:14446.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14446
    • DeMartino, J.A.1    Van Riper, G.2    Siciliano, S.J.3    Molineaux, C.J.4    Konteatis, Z.D.5    Rosen, H.6    Springer, M.S.7
  • 49
    • 0028125886 scopus 로고
    • Rhodopsin mutation G90D and a molecular mechanism for congenital night blindness
    • Rao, V. R., G. B. Cohen, and D. D. Oprian. 1994. Rhodopsin mutation G90D and a molecular mechanism for congenital night blindness. Nature 367:639.
    • (1994) Nature , vol.367 , pp. 639
    • Rao, V.R.1    Cohen, G.B.2    Oprian, D.D.3
  • 50
    • 0028920298 scopus 로고
    • 2 receptor by the substituted-cysteine accessibility method
    • 2 receptor by the substituted-cysteine accessibility method. Neuron 14:825.
    • (1995) Neuron , vol.14 , pp. 825
    • Javitch, J.A.1    Fu, D.2    Chen, J.3    Karlin, A.4
  • 51
    • 0028850149 scopus 로고
    • Aspartic acid residue 124 in the third transmembrane domain of the somatostatin receptor subtype 3 is essential for somatostatin-14 binding
    • Nehring, R. B., W. Myerhof, and D. Richter. 1995. Aspartic acid residue 124 in the third transmembrane domain of the somatostatin receptor subtype 3 is essential for somatostatin-14 binding. DNA Cell Biol. 14:939.
    • (1995) DNA Cell Biol. , vol.14 , pp. 939
    • Nehring, R.B.1    Myerhof, W.2    Richter, D.3
  • 54
    • 0028045051 scopus 로고
    • Hydrogen bonding interaction of thyrotropin-releasing hormone (TRH) with transmembrane tyrosine 106 of the TRH receptor
    • Perlman, J. H., C. N. Thaw, L. Laakkonen, C. Y. Bowers, R. Osman, and M. C. Gershengorn. 1994. Hydrogen bonding interaction of thyrotropin-releasing hormone (TRH) with transmembrane tyrosine 106 of the TRH receptor. J. Biol. Chem. 269:1610.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1610
    • Perlman, J.H.1    Thaw, C.N.2    Laakkonen, L.3    Bowers, C.Y.4    Osman, R.5    Gershengorn, M.C.6
  • 55
    • 0029953735 scopus 로고    scopus 로고
    • A refined model of the thyrotropin-releasing hormone (TRH) receptor binding pocket: Experimental analysis and energy minimization of the complex between TRH and TRH receptor
    • Perlman, J. H., L. Laakkonen, F. Guamieri, R. Osman, and M. C. Gershengorn. 1996. A refined model of the thyrotropin-releasing hormone (TRH) receptor binding pocket: experimental analysis and energy minimization of the complex between TRH and TRH receptor. Biochemistry 35:7643.
    • (1996) Biochemistry , vol.35 , pp. 7643
    • Perlman, J.H.1    Laakkonen, L.2    Guamieri, F.3    Osman, R.4    Gershengorn, M.C.5
  • 56
    • 0029730779 scopus 로고    scopus 로고
    • Functional interaction of transmembrane helices 3 and 6 in rhodopsin: Replacement of phenylalanine 261 by alanine causes reversion of phenotype of a glycine 121 replacement mutant
    • Han, M., S. W. Lin, M. Minkova, S. O. Smith, and T. P. Sakmar. 1996. Functional interaction of transmembrane helices 3 and 6 in rhodopsin: replacement of phenylalanine 261 by alanine causes reversion of phenotype of a glycine 121 replacement mutant. J. Biol. Chem. 271:32337.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32337
    • Han, M.1    Lin, S.W.2    Minkova, M.3    Smith, S.O.4    Sakmar, T.P.5
  • 60
    • 0029957956 scopus 로고    scopus 로고
    • Connectivity and orientation of the seven helical bundle in the tachykinin NK-1 receptor probed by zinc site engineering
    • Elling, C. E., and T. W. Schwanz. 1996. Connectivity and orientation of the seven helical bundle in the tachykinin NK-1 receptor probed by zinc site engineering. EMBO J. 15:6213.
    • (1996) EMBO J. , vol.15 , pp. 6213
    • Elling, C.E.1    Schwanz, T.W.2
  • 62
    • 0028908506 scopus 로고
    • Distinct roles for arginines in transmembrane helices 6 and 7 of the thyrotropin-releasing hormone receptor
    • Perlman, J. H., L. Laakkonen, R. Osman, and M. C. Gershengom. 1995. Distinct roles for arginines in transmembrane helices 6 and 7 of the thyrotropin-releasing hormone receptor. Mol. Pharmacol. 47:480.
    • (1995) Mol. Pharmacol. , vol.47 , pp. 480
    • Perlman, J.H.1    Laakkonen, L.2    Osman, R.3    Gershengom, M.C.4
  • 63
  • 65
    • 0025881062 scopus 로고
    • Three-dimensional models of neurotransmitter G-binding protein-coupled receptors
    • Hibert, M. F., S. Trumpp-Kallmeyer, A. Bruinvels, and J. Hoflack. 1991. Three-dimensional models of neurotransmitter G-binding protein-coupled receptors. Mol. Pharmacol. 40:8.
    • (1991) Mol. Pharmacol. , vol.40 , pp. 8
    • Hibert, M.F.1    Trumpp-Kallmeyer, S.2    Bruinvels, A.3    Hoflack, J.4
  • 67
    • 0343177634 scopus 로고
    • Glutamic acid-113 serves as the retinylidene Schiff base counterion in bovine rhodopsin
    • Sakmar, T. P., R. R. Franke, and H. G. Khorana. 1989. Glutamic acid-113 serves as the retinylidene Schiff base counterion in bovine rhodopsin. Proc. Natl. Acad. Sci. USA 86:8309.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 8309
    • Sakmar, T.P.1    Franke, R.R.2    Khorana, H.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.