메뉴 건너뛰기




Volumn 564, Issue 3, 2004, Pages 269-273

Heavier-than-air flying machines are impossible

Author keywords

Alignment; Bacteriorhodopsin; Bovine rhodopsin; GPCR; Modelling; Superposition

Indexed keywords

BACTERIORHODOPSIN; G PROTEIN COUPLED RECEPTOR; RHODOPSIN;

EID: 1942532331     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(04)00320-5     Document Type: Conference Paper
Times cited : (53)

References (47)
  • 3
    • 0008600208 scopus 로고    scopus 로고
    • TinyGRAP database: A bioinformatics tool to mine G protein-coupled receptor mutant data
    • Beukers M.W., Kristiansen I., IJzerman A.P., Edvardsen O. TinyGRAP database: a bioinformatics tool to mine G protein-coupled receptor mutant data. Trends Pharmacol. Sci. 20:1999;475-477.
    • (1999) Trends Pharmacol. Sci. , vol.20 , pp. 475-477
    • Beukers, M.W.1    Kristiansen, I.2    Ijzerman, A.P.3    Edvardsen, O.4
  • 4
    • 0030864048 scopus 로고    scopus 로고
    • X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipid cubic phases
    • Pebay-Peyroula E., Rummel G., Rosenbusch J.P., Landau E.M. X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipid cubic phases. Science. 277:1997;1676-1681.
    • (1997) Science , vol.277 , pp. 1676-1681
    • Pebay-Peyroula, E.1    Rummel, G.2    Rosenbusch, J.P.3    Landau, E.M.4
  • 5
    • 0032546920 scopus 로고    scopus 로고
    • Proton transfer pathways in bacteriorhodopsin at 2.3 Ångstrom resolution
    • Luecke H., Richter H.T., Lanyi J.K. Proton transfer pathways in bacteriorhodopsin at 2.3 Ångstrom resolution. Science. 280:1998;1934-1937.
    • (1998) Science , vol.280 , pp. 1934-1937
    • Luecke, H.1    Richter, H.T.2    Lanyi, J.K.3
  • 6
    • 0032561127 scopus 로고    scopus 로고
    • A novel three-dimensional crystal of bacteriorhodopsin obtained by successive fusion of the vesicular assemblies
    • Takeda K., Sato H., Hino T., Kono M., Fukuda K., Sakurai I., Okada T., Kouyama T. A novel three-dimensional crystal of bacteriorhodopsin obtained by successive fusion of the vesicular assemblies. J. Mol. Biol. 283:1998;463-474.
    • (1998) J. Mol. Biol. , vol.283 , pp. 463-474
    • Takeda, K.1    Sato, H.2    Hino, T.3    Kono, M.4    Fukuda, K.5    Sakurai, I.6    Okada, T.7    Kouyama, T.8
  • 7
    • 0025716272 scopus 로고
    • The structure of bacteriorhodopsin and its relevance to the visual opsins and other seven-helix G protein-coupled receptors
    • Henderson R., Schertler G.F.X. The structure of bacteriorhodopsin and its relevance to the visual opsins and other seven-helix G protein-coupled receptors. Phil. Trans. R. Soc. Lond. B Biol. Sci. 326:1990;379-389.
    • (1990) Phil. Trans. R. Soc. Lond. B Biol. Sci. , vol.326 , pp. 379-389
    • Henderson, R.1    Schertler, G.F.X.2
  • 9
    • 0027506471 scopus 로고
    • The probable arrangement of the helices in G protein-coupled receptors
    • Baldwin J.M. The probable arrangement of the helices in G protein-coupled receptors. EMBO J. 12:1993;1693-1703.
    • (1993) EMBO J. , vol.12 , pp. 1693-1703
    • Baldwin, J.M.1
  • 10
    • 0028962270 scopus 로고
    • Low resolution structure of bovine rhodopsin determined by electron cryo-microscopy
    • Unger V.M., Schertler G.F.X. Low resolution structure of bovine rhodopsin determined by electron cryo-microscopy. Biophys. J. 68:1995;1776-1786.
    • (1995) Biophys. J. , vol.68 , pp. 1776-1786
    • Unger, V.M.1    Schertler, G.F.X.2
  • 11
    • 0027190359 scopus 로고
    • Projection structure of rhodopsin
    • Schertler G.F., Villa C., Henderson R. Projection structure of rhodopsin. Nature. 362:1993;770-772.
    • (1993) Nature , vol.362 , pp. 770-772
    • Schertler, G.F.1    Villa, C.2    Henderson, R.3
  • 13
    • 0029556994 scopus 로고
    • Projection structure of frog rhodopsin in two crystal forms
    • Schertler G.F.X., Hargrave P.A. Projection structure of frog rhodopsin in two crystal forms. Proc. Natl. Acad. Sci. USA. 92:1995;11578-11582.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11578-11582
    • Schertler, G.F.X.1    Hargrave, P.A.2
  • 14
    • 0032011940 scopus 로고    scopus 로고
    • BUNDLE: A program for building the transmembrane domains of G protein-coupled receptors
    • Filizola M., Perez J.J., Carteni-Farina M. BUNDLE: A program for building the transmembrane domains of G protein-coupled receptors. J. Comput.-Aid. Mol. Des. 12:1998;111-118.
    • (1998) J. Comput.-Aid. Mol. Des. , vol.12 , pp. 111-118
    • Filizola, M.1    Perez, J.J.2    Carteni-Farina, M.3
  • 15
    • 0031251817 scopus 로고    scopus 로고
    • Modelling of the three-dimensional structure of the human melanocortin 1 receptor, using an automated method and docking of a rigid cyclic melanocyte-stimulating hormone core peptide
    • Prusis P., Schiöth H.B., Muceniece R., Herzyk P., Afshar M., Hubbard R.E., Wikberg J.E.S. Modelling of the three-dimensional structure of the human melanocortin 1 receptor, using an automated method and docking of a rigid cyclic melanocyte-stimulating hormone core peptide. J. Mol. Graph. Mod. 15:1997;307-315.
    • (1997) J. Mol. Graph. Mod. , vol.15 , pp. 307-315
    • Prusis, P.1    Schiöth, H.B.2    Muceniece, R.3    Herzyk, P.4    Afshar, M.5    Hubbard, R.E.6    Wikberg, J.E.S.7
  • 16
    • 0029078977 scopus 로고
    • Construction of a 3D model of the cannabinoid CB1 receptor: Determination of helix ends and helix orientation
    • Bramblett R.D., Panu A.M., Ballesteros J.A., Reggio P.H. Construction of a 3D model of the cannabinoid CB1 receptor: determination of helix ends and helix orientation. Life Sci. 56:1995;1971-1982.
    • (1995) Life Sci. , vol.56 , pp. 1971-1982
    • Bramblett, R.D.1    Panu, A.M.2    Ballesteros, J.A.3    Reggio, P.H.4
  • 17
    • 0027497369 scopus 로고
    • Modelling alpha-helical transmembrane domains: The calculation and use of substitution tables for lipid-facing residues
    • Donnelly D., Overington J.P., Ruffle S.V., Nugent J.H., Blundell T.L. Modelling alpha-helical transmembrane domains: the calculation and use of substitution tables for lipid-facing residues. Protein Sci. 2:1993;55-70.
    • (1993) Protein Sci. , vol.2 , pp. 55-70
    • Donnelly, D.1    Overington, J.P.2    Ruffle, S.V.3    Nugent, J.H.4    Blundell, T.L.5
  • 18
    • 0026517309 scopus 로고
    • On the use of the transmembrane domain of bacteriorhodopsin as a template for modeling the three-dimensional structure of guanine nucleotide-binding regulatory protein-coupled receptors
    • Pardo L., Ballesteros J.A., Osman R., Weinstein H. On the use of the transmembrane domain of bacteriorhodopsin as a template for modeling the three-dimensional structure of guanine nucleotide-binding regulatory protein-coupled receptors. Proc. Natl. Acad. Sci. USA. 89:1992;4009-4012.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4009-4012
    • Pardo, L.1    Ballesteros, J.A.2    Osman, R.3    Weinstein, H.4
  • 19
    • 0032575763 scopus 로고    scopus 로고
    • Combined biophysical and biochemical information confirms arrangement of transmembrane helices visible from the three-dimensional map of frog rhodopsin
    • Herzyk P., Hubbard R.E. Combined biophysical and biochemical information confirms arrangement of transmembrane helices visible from the three-dimensional map of frog rhodopsin. J. Mol. Biol. 281:1998;741-754.
    • (1998) J. Mol. Biol. , vol.281 , pp. 741-754
    • Herzyk, P.1    Hubbard, R.E.2
  • 20
    • 0030998038 scopus 로고    scopus 로고
    • The transmembrane 7-alpha-bundle of rhodopsin: Distance geometry calculations with hydrogen bonding constraints
    • Pogozheva I.D., Lomize A.L., Mosberg H.I. The transmembrane 7-alpha-bundle of rhodopsin: distance geometry calculations with hydrogen bonding constraints. Biophys. J. 72:1997;1963-1985.
    • (1997) Biophys. J. , vol.72 , pp. 1963-1985
    • Pogozheva, I.D.1    Lomize, A.L.2    Mosberg, H.I.3
  • 21
    • 0027465713 scopus 로고
    • Modelling of transmembrane seven helix bundles
    • Cronet P., Sander C., Vriend G. Modelling of transmembrane seven helix bundles. Protein Eng. 6:1993;59-64.
    • (1993) Protein Eng. , vol.6 , pp. 59-64
    • Cronet, P.1    Sander, C.2    Vriend, G.3
  • 22
    • 1942539860 scopus 로고    scopus 로고
    • http://www.gpcr.org/articles/2003_mod/index.html.
  • 23
    • 0035748996 scopus 로고    scopus 로고
    • Comparison of performance in successive CASP Experiments
    • Venclovas C., Zemla A., Fidelis K., Moult J. Comparison of performance in successive CASP Experiments. Proteins. 5:(Suppl.):2001;163-170.
    • (2001) Proteins , vol.5 , Issue.SUPPL. , pp. 163-170
    • Venclovas, C.1    Zemla, A.2    Fidelis, K.3    Moult, J.4
  • 24
    • 0027410367 scopus 로고
    • --binding site in the human red and green colour vision pigments
    • --binding site in the human red and green colour vision pigments. Biochemistry. 32:1993;2125-2130.
    • (1993) Biochemistry , vol.32 , pp. 2125-2130
    • Wang, Z.1    Asenjo, A.B.2    Oprian, D.D.3
  • 25
    • 0034948696 scopus 로고    scopus 로고
    • Structural mimicry in G protein-coupled receptors: Implications of the high-resolution structure of rhodopsin for structure-function analysis of rhodopsin-like receptors
    • Ballesteros J.A., Shi L., Javitch J.A. Structural mimicry in G protein-coupled receptors: implications of the high-resolution structure of rhodopsin for structure-function analysis of rhodopsin-like receptors. Mol. Pharmacol. 60:2001;1-19.
    • (2001) Mol. Pharmacol. , vol.60 , pp. 1-19
    • Ballesteros, J.A.1    Shi, L.2    Javitch, J.A.3
  • 26
    • 0033638881 scopus 로고    scopus 로고
    • Modelling and docking the endothelin G protein-coupled receptor
    • Orry A.J.W., Wallace B.A. Modelling and docking the endothelin G protein-coupled receptor. Biophys. J. 79:2000;3083-3094.
    • (2000) Biophys. J. , vol.79 , pp. 3083-3094
    • Orry, A.J.W.1    Wallace, B.A.2
  • 27
    • 0035731824 scopus 로고    scopus 로고
    • Computational model of the complex between GR113808 and the 5-HT4 receptor guided by site-directed mutagenesis and the crystal structure of rhodopsin
    • Lopez-Rodriguez M.L., Murcia M., Benhamu B., Olivella M., Campillo M., Pardo L. Computational model of the complex between GR113808 and the 5-HT4 receptor guided by site-directed mutagenesis and the crystal structure of rhodopsin. J. Comput.-Aid. Mol. Des. 15:2001;1025-1033.
    • (2001) J. Comput.-Aid. Mol. Des. , vol.15 , pp. 1025-1033
    • Lopez-Rodriguez, M.L.1    Murcia, M.2    Benhamu, B.3    Olivella, M.4    Campillo, M.5    Pardo, L.6
  • 29
    • 0038119607 scopus 로고    scopus 로고
    • Homology model of the CB1 cannabinoid receptor: Sites critical for nonclassical cannabinoid agonist interaction
    • Shim J.Y., Welsh W.J., Howlett A.C. Homology model of the CB1 cannabinoid receptor: Sites critical for nonclassical cannabinoid agonist interaction. Biopolymers. 71:2003;169-189.
    • (2003) Biopolymers , vol.71 , pp. 169-189
    • Shim, J.Y.1    Welsh, W.J.2    Howlett, A.C.3
  • 31
    • 0037151054 scopus 로고    scopus 로고
    • Involvement of the second extracellular loop (E2) of the neurokinin-1 receptor in the binding of substance P. Photoaffinity labeling and modeling studies
    • Lequin O., Bolbach G., Frank F., Convert O., Girault-Lagrange S., Chassaing G., Lavielle S., Sagan S. Involvement of the second extracellular loop (E2) of the neurokinin-1 receptor in the binding of substance P. Photoaffinity labeling and modeling studies. J. Biol. Chem. 277:2002;22386-22394.
    • (2002) J. Biol. Chem. , vol.277 , pp. 22386-22394
    • Lequin, O.1    Bolbach, G.2    Frank, F.3    Convert, O.4    Girault-Lagrange, S.5    Chassaing, G.6    Lavielle, S.7    Sagan, S.8
  • 32
    • 0037133525 scopus 로고    scopus 로고
    • NMR structure of the second intracellular loop of the alpha 2A adrenergic receptor: Evidence for a novel cytoplasmic helix
    • Chung D.A., Zuiderweg E.R., Fowler C.B., Soyer O.S., Mosberg H.I., Neubig R.R. NMR structure of the second intracellular loop of the alpha 2A adrenergic receptor: evidence for a novel cytoplasmic helix. Biochemistry. 41:2002;3596-3604.
    • (2002) Biochemistry , vol.41 , pp. 3596-3604
    • Chung, D.A.1    Zuiderweg, E.R.2    Fowler, C.B.3    Soyer, O.S.4    Mosberg, H.I.5    Neubig, R.R.6
  • 33
    • 0041883731 scopus 로고    scopus 로고
    • Modeling and docking of the three-dimensional structure of the human melanocortin 4 receptor
    • Yang X., Wang Z., Dong W., Ling L., Yang H., Chen R. Modeling and docking of the three-dimensional structure of the human melanocortin 4 receptor. J. Protein Chem. 22:2003;335-344.
    • (2003) J. Protein Chem. , vol.22 , pp. 335-344
    • Yang, X.1    Wang, Z.2    Dong, W.3    Ling, L.4    Yang, H.5    Chen, R.6
  • 34
    • 0038174859 scopus 로고    scopus 로고
    • Key issues in the computational simulation of GPCR function: Representation of loop domains
    • Mehler E.L., Periole X., Hassan S.A., Weinstein H. Key issues in the computational simulation of GPCR function: representation of loop domains. J. Comput.-Aid. Mol. Des. 16:2002;841-853.
    • (2002) J. Comput.-Aid. Mol. Des. , vol.16 , pp. 841-853
    • Mehler, E.L.1    Periole, X.2    Hassan, S.A.3    Weinstein, H.4
  • 35
    • 0035933818 scopus 로고    scopus 로고
    • Molecular characterization of the substance P*neurokinin-1 receptor complex: Development of an experimentally based model
    • Pellegrini M., Bremer A.A., Ulfers A.L., Boyd N.D., Mierke D.F. Molecular characterization of the substance P*neurokinin-1 receptor complex: development of an experimentally based model. J. Biol. Chem. 276:2001;22862-22867.
    • (2001) J. Biol. Chem. , vol.276 , pp. 22862-22867
    • Pellegrini, M.1    Bremer, A.A.2    Ulfers, A.L.3    Boyd, N.D.4    Mierke, D.F.5
  • 36
    • 0036093814 scopus 로고    scopus 로고
    • Molecular modelling and site-directed mutagenesis of human GALR1 galanin receptor defines determinants of receptor subtype specificity
    • Church W.B., Jones K.A., Kuiper D.A., Shine J., Iismaa T.P. Molecular modelling and site-directed mutagenesis of human GALR1 galanin receptor defines determinants of receptor subtype specificity. Protein Eng. 5:2002;313-323.
    • (2002) Protein Eng. , vol.5 , pp. 313-323
    • Church, W.B.1    Jones, K.A.2    Kuiper, D.A.3    Shine, J.4    Iismaa, T.P.5
  • 37
    • 0036169280 scopus 로고    scopus 로고
    • The binding site of aminergic G protein-coupled receptors: The transmembrane segments and second extracellular loop
    • Shi L., Javitch J.A. The binding site of aminergic G protein-coupled receptors: the transmembrane segments and second extracellular loop. Annu. Rev. Pharmacol. Toxicol. 42:2002;437-467.
    • (2002) Annu. Rev. Pharmacol. Toxicol. , vol.42 , pp. 437-467
    • Shi, L.1    Javitch, J.A.2
  • 38
    • 0030606345 scopus 로고    scopus 로고
    • Structure determination of the fourth cytoplasmic loop and carboxyl terminal domain of bovine rhodopsin
    • Yeagle P.L., Alderfer J.L., Albert A.D. Structure determination of the fourth cytoplasmic loop and carboxyl terminal domain of bovine rhodopsin. Mol. Vis. 2:1996;12-19.
    • (1996) Mol. Vis. , vol.2 , pp. 12-19
    • Yeagle, P.L.1    Alderfer, J.L.2    Albert, A.D.3
  • 39
    • 0030964858 scopus 로고    scopus 로고
    • The first and second cytoplasmic loops of the G protein-receptor, rhodopsin, independently form beta-turns
    • Yeagle P.L., Alderfer J.L., Salloum A.C., Ali L., Albert A.D. The first and second cytoplasmic loops of the G protein-receptor, rhodopsin, independently form beta-turns. Biochemistry. 36:1997;3864-3869.
    • (1997) Biochemistry , vol.36 , pp. 3864-3869
    • Yeagle, P.L.1    Alderfer, J.L.2    Salloum, A.C.3    Ali, L.4    Albert, A.D.5
  • 40
    • 0028812838 scopus 로고
    • Structure of the third cytoplasmic loop of bovine rhodopsin
    • Yeagle P.L., Alderfer J.L., Albert A.D. Structure of the third cytoplasmic loop of bovine rhodopsin. Biochemistry. 34:1995;14621-14625.
    • (1995) Biochemistry , vol.34 , pp. 14621-14625
    • Yeagle, P.L.1    Alderfer, J.L.2    Albert, A.D.3
  • 42
    • 0025398721 scopus 로고
    • WHAT IF: A molecular modeling and drug design program
    • Vriend G. WHAT IF: A molecular modeling and drug design program. J. Mol. Graph. 8:1990;52-56.
    • (1990) J. Mol. Graph. , vol.8 , pp. 52-56
    • Vriend, G.1
  • 43
    • 0038159530 scopus 로고    scopus 로고
    • Organization of the G protein-coupled receptors rhodopsin and opsin in native membranes
    • Liang Y., Fotiadis D., Filipek S., Saperstein D.A., Palczewski K., Engel A. Organization of the G protein-coupled receptors rhodopsin and opsin in native membranes. J. Biol. Chem. 278:2003;21655-21662.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21655-21662
    • Liang, Y.1    Fotiadis, D.2    Filipek, S.3    Saperstein, D.A.4    Palczewski, K.5    Engel, A.6
  • 44
    • 0001228323 scopus 로고
    • A common motif in G protein-coupled seven transmembrane helix receptors
    • Oliveira L., Paiva A.C.M., Vriend G. A common motif in G protein-coupled seven transmembrane helix receptors. J. Comput.-Aid. Mol. Des. 7:1993;649-658.
    • (1993) J. Comput.-Aid. Mol. Des. , vol.7 , pp. 649-658
    • Oliveira, L.1    Paiva, A.C.M.2    Vriend, G.3
  • 45
    • 0028221558 scopus 로고
    • A model of the serotonin 5-HT1A receptor: Agonist and antagonist binding sites
    • Kuipers W., Van Wijngaarden I., IJzerman A.P. A model of the serotonin 5-HT1A receptor: agonist and antagonist binding sites. Drug Des. Discov. 11:1994;231-249.
    • (1994) Drug Des. Discov. , vol.11 , pp. 231-249
    • Kuipers, W.1    Van Wijngaarden, I.2    Ijzerman, A.P.3
  • 46
    • 0031391387 scopus 로고    scopus 로고
    • Identification of class-determining residues in G protein-coupled receptors by sequence analysis
    • Kuipers W., Oliveira L., Vriend G., IJzerman A.P. Identification of class-determining residues in G protein-coupled receptors by sequence analysis. Receptors Channels. 5:1997;159-174.
    • (1997) Receptors Channels , vol.5 , pp. 159-174
    • Kuipers, W.1    Oliveira, L.2    Vriend, G.3    Ijzerman, A.P.4
  • 47
    • 1942443719 scopus 로고
    • Molecular modelling of serotonin receptors
    • Rippmann F., Bottcher E. Molecular modelling of serotonin receptors. 7TM. 3:1993;1-27.
    • (1993) 7TM , vol.3 , pp. 1-27
    • Rippmann, F.1    Bottcher, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.