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Volumn 48, Issue 20, 2009, Pages 4294-4304

Modulation of molecular interactions and function by rhodopsin palmitylation

Author keywords

[No Author keywords available]

Indexed keywords

ABSORBANCE SPECTRUM; BINDING POCKETS; CARBOXYL-TERMINAL; CYSTEINE RESIDUES; IN-VITRO; IN-VITRO ASSAYS; IN-VIVO; LIGHT ACTIVATION; MOUSE MODELS; SINGLE MOLECULE FORCE SPECTROSCOPY; TISSUE SAMPLES; TRANSDUCIN; WILD TYPES;

EID: 66149192522     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900417b     Document Type: Article
Times cited : (28)

References (54)
  • 1
    • 0038757730 scopus 로고    scopus 로고
    • Role of palmitoylation/depalmitoylation reactions in G-protein-coupled receptor function
    • DOI 10.1016/S0163-7258(02)00300-5, PII S0163725802003005
    • Qanbar, R., and Bouvier, M. (2003) Role of palmitoylation/ depalmitoylation reactions in G-protein-coupled receptor function. Pharmacol. Ther. 97, 1-33. (Pubitemid 35477802)
    • (2003) Pharmacology and Therapeutics , vol.97 , Issue.1 , pp. 1-33
    • Neve, K.A.1    Qanbar, R.2    Bouvier, M.3
  • 2
    • 33646534202 scopus 로고    scopus 로고
    • Co-ordinated covalent modification of G-protein coupled receptors
    • Torrecilla, I., and Tobin, A. B. (2006) Co-ordinated covalent modification of G-protein coupled receptors. Curr. Pharm. Des. 12, 1797-1808.
    • (2006) Curr. Pharm. Des. , vol.12 , pp. 1797-1808
    • Torrecilla, I.1    Tobin, A.B.2
  • 3
    • 34248215318 scopus 로고    scopus 로고
    • Visual rhodopsin sees the light: Structure and mechanism of g protein signaling
    • Ridge, K. D., and Palczewski, K. (2007) Visual rhodopsin sees the light: structure and mechanism of g protein signaling. J. Biol. Chem. 282, 9297-9301.
    • (2007) J. Biol. Chem. , vol.282 , pp. 9297-9301
    • Ridge, K.D.1    Palczewski, K.2
  • 4
    • 33645535034 scopus 로고    scopus 로고
    • G protein-coupled receptor rhodopsin
    • DOI 10.1146/annurev.biochem.75.103004.142743
    • Palczewski, K. (2006) G protein-coupled receptor rhodopsin. Annu. Rev. Biochem. 75, 743-767. (Pubitemid 44118051)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 743-767
    • Palczewski, K.1
  • 5
    • 0034105642 scopus 로고    scopus 로고
    • Diffusible ligand all-trans-retinal activates opsin via a palmitoylation-dependent mechanism
    • DOI 10.1074/jbc.275.9.6189
    • Sachs, K., Maretzki, D., Meyer, C. K., and Hofmann, K. P. (2000) Diffusible ligand all-trans-retinal activates opsin via a palmitoylation- dependent mechanism. J. Biol. Chem. 275, 6189-6194. (Pubitemid 30129905)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.9 , pp. 6189-6194
    • Sachs, K.1    Maretzki, D.2    Meyer, C.K.3    Hofmann, K.P.4
  • 6
    • 0028287095 scopus 로고
    • Effects of depalmitoylation on physicochemical properties of rhodopsin
    • Traxler, K. W., and Dewey, T. G. (1994) Effects of depalmitoylation on physicochemical properties of rhodopsin. Biochemistry 33, 1718-1723. (Pubitemid 24089698)
    • (1994) Biochemistry , vol.33 , Issue.7 , pp. 1718-1723
    • Traxler, K.W.1    Dewey, T.G.2
  • 7
    • 0034695476 scopus 로고    scopus 로고
    • The amino terminus of the fourth cytoplasmic loop of rhodopsin modulates rhodopsin-transducin interaction
    • DOI 10.1074/jbc.275.3.1930
    • Marin, E. P., Krishna, A. G., Zvyaga, T. A., Isele, J., Siebert, F., and Sakmar, T. P. (2000) The amino terminus of the fourth cytoplasmic loop of rhodopsin modulates rhodopsin-transducin interaction. J. Biol. Chem. 275, 1930-1936. (Pubitemid 30060818)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.3 , pp. 1930-1936
    • Marin, E.P.1    Krishna, A.G.2    Zvyaga, T.A.3    Isele, J.4    Siebert, F.5    Sakmar, T.P.6
  • 9
    • 0025885547 scopus 로고
    • Depalmitylation with hydroxylamine alters the functional properties of rhodopsin
    • Morrison, D. F., O'Brien, P. J., and Pepperberg, D. R. (1991) Depalmitylation with hydroxylamine alters the functional properties of rhodopsin. J. Biol. Chem. 266, 20118-20123. (Pubitemid 21908434)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.30 , pp. 20118-20123
    • Morrison, D.F.1    O'Brien, P.J.2    Pepperberg, D.R.3
  • 10
    • 21644447832 scopus 로고    scopus 로고
    • Enhanced shutoff of phototransduction in transgenic mice expressing palmitoylation-deficient rhodopsin
    • DOI 10.1074/jbc.M502588200
    • Wang, Z., Wen, X. H., Ablonczy, Z., Crouch, R. K., Makino, C. L., and Lem, J. (2005) Enhanced shutoff of phototrans duction in transgenic mice expressing palmitoylation-deficient rhodopsin. J. Biol. Chem. 280, 24293-24300. (Pubitemid 40934510)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.26 , pp. 24293-24300
    • Wang, Z.1    Wen, X.-H.2    Ablonczy, Z.3    Crouch, R.K.4    Makino, C.L.5    Lem, J.6
  • 11
    • 34249884786 scopus 로고    scopus 로고
    • Three-dimensional architecture of murine rod outer segments determined by cryoelectron tomography
    • DOI 10.1083/jcb.200612010
    • Nickell, S., Park, P. S., Baumeister, W., and Palczewski, K. (2007) Three-dimensional architecture of murine rod outer segments determined by cryoelectron tomography. J. Cell Biol. 177, 917-925. (Pubitemid 46873096)
    • (2007) Journal of Cell Biology , vol.177 , Issue.5 , pp. 917-925
    • Nickell, S.1    Park, P.S.-H.2    Baumeister, W.3    Palczewski, K.4
  • 12
    • 0000073823 scopus 로고
    • The molar extinction of rhodopsin
    • Wald, G., and Brown, P. K. (1953) The molar extinction of rhodopsin. J. Gen. Physiol. 37, 189-200.
    • (1953) J. Gen. Physiol. , vol.37 , pp. 189-200
    • Wald, G.1    Brown, P.K.2
  • 13
    • 0020713543 scopus 로고
    • Monoclonal antibodies to rhodopsin: Characterization, cross-reactivity, and application as structural probes
    • Molday, R. S., and MacKenzie, D. (1983) Monoclonal antibodies to rhodopsin: characterization, cross-reactivity, and application as structural probes. Biochemistry 22, 653-660.
    • (1983) Biochemistry , vol.22 , pp. 653-660
    • Molday, R.S.1    MacKenzie, D.2
  • 16
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • DOI 10.1126/science.276.5315.1109
    • Rief, M., Gautel, M., Oesterhelt, F., Fernandez, J. M., and Gaub, H. E. (1997) Reversible unfolding of individual titin immunoglobulin domains by AFM. Science 276, 1109-1112. (Pubitemid 27218118)
    • (1997) Science , vol.276 , Issue.5315 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 17
    • 0028957661 scopus 로고
    • Structure and function in rhodopsin. Measurement of the rate of metarhodopsin II decay by fluorescence spectroscopy
    • Farrens, D. L., and Khorana, H. G. (1995) Structure and function in rhodopsin. Measurement of the rate of metarhodopsin II decay by fluorescence spectroscopy. J. Biol. Chem. 270, 5073-5076.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5073-5076
    • Farrens, D.L.1    Khorana, H.G.2
  • 19
    • 0023708657 scopus 로고
    • The intrinsic fluorescence of the alpha subunit of transducin. Measurement of receptor-dependent guanine nucleotide exchange
    • Phillips, W. J., and Cerione, R. A. (1988) The intrinsic fluorescence of the alpha subunit of transducin. Measurement of receptor-dependent guanine nucleotide exchange. J. Biol. Chem. 263, 15498-15505.
    • (1988) J. Biol. Chem. , vol.263 , pp. 15498-15505
    • Phillips, W.J.1    Cerione, R.A.2
  • 20
    • 0027270898 scopus 로고
    • Regulation of the rhodopsin-transducin interaction by a highly conserved carboxylic acid group
    • Fahmy, K., and Sakmar, T. P. (1993) Regulation of the rhodopsin-transducin interaction by a highly conserved carboxylic acid group. Biochemistry 32, 7229-7236. (Pubitemid 23223127)
    • (1993) Biochemistry , vol.32 , Issue.28 , pp. 7229-7236
    • Fahmy, K.1    Sakmar, T.P.2
  • 21
    • 0001354986 scopus 로고
    • Expression of opsin genes in COS cells
    • Oprian, D. D. (1993) Expression of opsin genes in COS cells. Methods Neurosci. 15, 301-306.
    • (1993) Methods Neurosci. , vol.15 , pp. 301-306
    • Oprian, D.D.1
  • 22
    • 0034089337 scopus 로고    scopus 로고
    • Assays for detection of constitutively active opsins
    • Robinson, P. R. (2000) Assays for detection of constitutively active opsins. Methods Enzymol. 315, 207-218. (Pubitemid 30123293)
    • (2000) Methods in Enzymology , vol.315 , pp. 207-218
    • Robinson, P.R.1
  • 23
    • 29344435298 scopus 로고    scopus 로고
    • Constitutive activity of a UV cone opsin
    • DOI 10.1016/j.febslet.2005.12.002, PII S0014579305014584
    • Kono, M. (2006) Constitutive activity of a UV cone opsin. FEBS Lett. 580, 229-232. (Pubitemid 43005341)
    • (2006) FEBS Letters , vol.580 , Issue.1 , pp. 229-232
    • Kono, M.1
  • 25
    • 84986512474 scopus 로고
    • CHARMM: A program for macromolecular energy, minimization, and dynamics calculations
    • Brooks, B. R., Olafson, R. E. B., States, D. J., Swaminathan, S, and Karplus, Martin (1983) CHARMM: A program for macromolecular energy, minimization, and dynamics calculations. J. Comput. Chem. 4, 187-217.
    • (1983) J. Comput. Chem. , vol.4 , pp. 187-217
    • Brooks, B.R.1    Olafson, R.E.B.2    States, D.J.3    Swaminathan, S.4    Karplus, M.5
  • 26
    • 0000036869 scopus 로고    scopus 로고
    • Simulation of activation free energies in molecular systems
    • Neria, E., Fischer, S., and Karplus, M. (1996) Simulation of activation free energies in molecular systems. J. Chem. Phys. 105, 1902-1921. (Pubitemid 126612899)
    • (1996) Journal of Chemical Physics , vol.105 , Issue.5 , pp. 1902-1921
    • Neria, E.1    Fischer, S.2    Karplus, M.3
  • 27
    • 0038675609 scopus 로고    scopus 로고
    • Effective energy function for proteins in lipid membranes
    • DOI 10.1002/prot.10410
    • Lazaridis, T. (2003) Effective energy function for proteins in lipid membranes. Proteins 52, 176-192. (Pubitemid 36828942)
    • (2003) Proteins: Structure, Function and Genetics , vol.52 , Issue.2 , pp. 176-192
    • Lazaridis, T.1
  • 28
    • 0033135638 scopus 로고    scopus 로고
    • Effective energy function for proteins in solution
    • DOI 10.1002/(SICI)1097-0134(19990501)35:2<133::AID-PROT1>3.0.CO;2-N
    • Lazaridis, T., and Karplus, M. (1999) Effective energy function for proteins in solution. Proteins 35, 133-152. (Pubitemid 29165128)
    • (1999) Proteins: Structure, Function and Genetics , vol.35 , Issue.2 , pp. 133-152
    • Lazaridis, T.1    Karplus, M.2
  • 29
    • 4344581120 scopus 로고    scopus 로고
    • The retinal conformation and its environment in rhodopsin in light of a new 2.2 Å crystal structure
    • Okada, T., Sugihara, M., Bondar, A. N., Elstner, M., Entel, P., and Buss, V. (2004) The retinal conformation and its environment in rhodopsin in light of a new 2.2 Å crystal structure. J. Mol. Biol. 342, 571-583.
    • (2004) J. Mol. Biol. , vol.342 , pp. 571-583
    • Okada, T.1    Sugihara, M.2    Bondar, A.N.3    Elstner, M.4    Entel, P.5    Buss, V.6
  • 30
    • 33644861214 scopus 로고    scopus 로고
    • OPM: Orientations of proteins in membranes database
    • DOI 10.1093/bioinformatics/btk023
    • Lomize, M. A., Lomize, A. L., Pogozheva, I. D., and Mosberg, H. I. (2006) OPM: orientations of proteins in membranes database. Bioinformatics 22, 623-625. (Pubitemid 43372827)
    • (2006) Bioinformatics , vol.22 , Issue.5 , pp. 623-625
    • Lomize, M.A.1    Lomize, A.L.2    Pogozheva, I.D.3    Mosberg, H.I.4
  • 31
    • 0000543569 scopus 로고    scopus 로고
    • Influence of the methyl groups on the structure, charge distribution, and proton affinity of the retinal Schiff base
    • Tajkhorshid, E., and Suhai, S. (1999) Influence of the methyl groups on the structure, charge distribution, and proton affinity of the retinal schiff base. J. Phys. Chem. B 103, 5581-5590. (Pubitemid 129702784)
    • (1999) Journal of Physical Chemistry B , vol.103 , Issue.26 , pp. 5581-5590
    • Tajkhorshid, E.1    Suhai, S.2
  • 32
    • 0034128699 scopus 로고    scopus 로고
    • Molecular dynamics study of the nature and origin of retinal's twisted structure in bacteriorhodopsin
    • Tajkhorshid, E., Baudry, J., Schulten, K., and Suhai, S. (2000) Molecular dynamics study of the nature and origin of retinal's twisted structure in bacteriorhodopsin. Biophys. J. 78, 683-693.
    • (2000) Biophys. J. , vol.78 , pp. 683-693
    • Tajkhorshid, E.1    Baudry, J.2    Schulten, K.3    Suhai, S.4
  • 33
    • 0028835990 scopus 로고
    • Functional interactions in bacteriorhodopsin: A theoretical analysis of retinal hydrogen bonding with water
    • Nina, M., Roux, B., and Smith, J. C. (1995) Functional interactions in bacteriorhodopsin: a theoretical analysis of retinal hydrogen bonding with water. Biophys. J. 68, 25-39.
    • (1995) Biophys. J. , vol.68 , pp. 25-39
    • Nina, M.1    Roux, B.2    Smith, J.C.3
  • 35
    • 0031549614 scopus 로고    scopus 로고
    • Conformational effects on the proton affinity of the schiff base in bacteriorhodopsin: A density functional study
    • Tajkhorshid, E., Paizs, B., and Suhai, S. (1997) Conformational effects on the proton affinity of the schiff base in bacteriorhodopsin: A density functional study. J. Phys. Chem. B 101, 8021-8028.
    • (1997) J. Phys. Chem. B , vol.101 , pp. 8021-8028
    • Tajkhorshid, E.1    Paizs, B.2    Suhai, S.3
  • 36
    • 41149137801 scopus 로고    scopus 로고
    • Activation of G protein-coupled receptors: Beyond two-state models and tertiary conformational changes
    • Park, P. S., Lodowski, D. T., and Palczewski, K. (2008) Activation of G protein-coupled receptors: beyond two-state models and tertiary conformational changes. Annu. Rev. Pharmacol. Toxicol. 48, 107-141.
    • (2008) Annu. Rev. Pharmacol. Toxicol. , vol.48 , pp. 107-141
    • Park, P.S.1    Lodowski, D.T.2    Palczewski, K.3
  • 37
    • 33847021802 scopus 로고    scopus 로고
    • Diseases caused by defects in the visual cycle: Retinoids as potential therapeutic agents
    • Travis, G. H., Golczak, M., Moise, A. R., and Palczewski, K. (2007) Diseases caused by defects in the visual cycle: retinoids as potential therapeutic agents. Annu. Rev. Pharmacol. Toxicol. 47, 469-512.
    • (2007) Annu. Rev. Pharmacol. Toxicol. , vol.47 , pp. 469-512
    • Travis, G.H.1    Golczak, M.2    Moise, A.R.3    Palczewski, K.4
  • 38
    • 34347259478 scopus 로고    scopus 로고
    • Deciphering molecular interactions of native membrane proteins by single-molecule force spectroscopy
    • DOI 10.1146/annurev.biophys.36.040306.132640
    • Kedrov, A., Janovjak, H., Sapra, K. T., and Muller, D. J. (2007) Deciphering molecular interactions of native membrane proteins by single-molecule force spectroscopy. Annu. Rev. Biophys. Biomol. Struct. 36, 233-260. (Pubitemid 46998118)
    • (2007) Annual Review of Biophysics and Biomolecular Structure , vol.36 , pp. 233-260
    • Kedrov, A.1    Janovjak, H.2    Sapra, K.T.3    Muller, D.J.4
  • 40
    • 15944387765 scopus 로고    scopus 로고
    • Dual role of interactions between membranous and soluble portions of helical membrane receptors for folding and signaling
    • DOI 10.1016/j.tips.2005.02.009
    • Klein-Seetharaman, J. (2005) Dual role of interactions between membranous and soluble portions of helical membrane receptors for folding and signaling. Trends Pharmacol. Sci. 26, 183-189. (Pubitemid 40432653)
    • (2005) Trends in Pharmacological Sciences , vol.26 , Issue.4 , pp. 183-189
    • Klein-Seetharaman, J.1
  • 41
    • 0030931599 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: Packing of the helices in the transmembrane domain and folding to a tertiary structure in the intradiscal domain are coupled
    • Hwa, J., Garriga, P., Liu, X., and Khorana, H. G. (1997) Structure and function in rhodopsin: packing of the helices in the transmembrane domain and folding to a tertiary structure in the intradiscal domain are coupled. Proc. Natl. Acad. Sci. U. S. A. 94, 10571-10576.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 10571-10576
    • Hwa, J.1    Garriga, P.2    Liu, X.3    Khorana, H.G.4
  • 42
    • 0035942215 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: Mass spectrometric identification of the abnormal intradiscal disulfide bond in misfolded retinitis pigmentosa mutants
    • Hwa, J., Klein-Seetharaman, J., and Khorana, H. G. (2001) Structure and function in rhodopsin: Mass spectrometric identification of the abnormal intradiscal disulfide bond in misfolded retinitis pigmentosa mutants. Proc. Natl. Acad. Sci. U. S. A. 98, 4872-4876.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 4872-4876
    • Hwa, J.1    Klein-Seetharaman, J.2    Khorana, H.G.3
  • 43
    • 0031569809 scopus 로고    scopus 로고
    • Palmitoylation of muscarinic acetylcholine receptor m2 subtypes: Reduction in their ability to activate G proteins by mutation of a putative palmitoylation site, cysteine 457, in the carboxyl-terminal tail
    • Hayashi, M. K., and Haga, T. (1997) Palmitoylation of muscarinic acetylcholine receptor m2 subtypes: reduction in their ability to activate G proteins by mutation of a putative palmitoylation site, cysteine 457, in the carboxyl-terminal tail. Arch. Biochem. Biophys. 340, 376-382.
    • (1997) Arch. Biochem. Biophys. , vol.340 , pp. 376-382
    • Hayashi, M.K.1    Haga, T.2
  • 44
    • 0024544232 scopus 로고
    • Palmitoylation of the human beta 2-adrenergic receptor. Mutation of Cys341 in the carboxyl tail leads to an uncoupled nonpalmitoylated form of the receptor
    • O'Dowd, B. F., Hnatowich, M., Caron, M. G., Lefkowitz, R. J., and Bouvier, M. (1989) Palmitoylation of the human beta 2-adrenergic receptor. Mutation of Cys341 in the carboxyl tail leads to an uncoupled nonpalmitoylated form of the receptor. J. Biol. Chem. 264, 7564-7569.
    • (1989) J. Biol. Chem. , vol.264 , pp. 7564-7569
    • O'Dowd, B.F.1    Hnatowich, M.2    Caron, M.G.3    Lefkowitz, R.J.4    Bouvier, M.5
  • 45
    • 34548303255 scopus 로고    scopus 로고
    • 1A receptor in lipid microdomains depends on its palmitoylation and is involved in receptor-mediated signaling
    • DOI 10.1124/mol.107.037085
    • Renner, U., Glebov, K., Lang, T., Papusheva, E., Balakrishnan, S., Keller, B., Richter, D. W., Jahn, R., and Ponimaskin, E. (2007) Localization of the mouse 5-hydroxytryptamine (1A) receptor in lipid microdomains depends on its palmitoylation and is involved in receptor-mediated signaling. Mol. Pharmacol. 72, 502-513. (Pubitemid 47347285)
    • (2007) Molecular Pharmacology , vol.72 , Issue.3 , pp. 502-513
    • Renner, U.1    Glebov, K.2    Lang, T.3    Papusheva, E.4    Balakrishnan, S.5    Keller, B.6    Richter, D.W.7    Jahn, R.8    Ponimaskin, E.9
  • 46
    • 0942298112 scopus 로고    scopus 로고
    • The 5-hydroxytryptamine (1A) receptor is stably palmitoylated, and acylation is critical for communication of receptor with Gi protein
    • Papoucheva, E., Dumuis, A., Sebben, M., Richter, D. W., and Ponimaskin, E. G. (2004) The 5-hydroxytryptamine (1A) receptor is stably palmitoylated, and acylation is critical for communication of receptor with Gi protein. J. Biol. Chem. 279, 3280-3291.
    • (2004) J. Biol. Chem. , vol.279 , pp. 3280-3291
    • Papoucheva, E.1    Dumuis, A.2    Sebben, M.3    Richter, D.W.4    Ponimaskin, E.G.5
  • 47
    • 0031564603 scopus 로고    scopus 로고
    • 1 receptor does not affect receptor-G protein interaction
    • DOI 10.1016/S0014-2999(97)00059-9, PII S0014299997000599
    • Jin, H., Zastawny, R., George, S. R., and O'Dowd, B. F. (1997) Elimination of palmitoylation sites in the human dopamine D1 receptor does not affect receptor-G protein interaction. Eur. J. Pharmacol. 324, 109-116. (Pubitemid 27160915)
    • (1997) European Journal of Pharmacology , vol.324 , Issue.1 , pp. 109-116
    • Jin, H.1    Zastawny, R.2    George, S.R.3    O'Dowd, B.F.4
  • 48
    • 0027401994 scopus 로고
    • Mutations of the α(2A)-adrenergic receptor that eliminate detectable palmitoylation do not perturb receptor-G-protein coupling
    • Kennedy, M. E., and Limbird, L. E. (1993) Mutations of the alpha 2A-adrenergic receptor that eliminate detectable palmitoylation do not perturb receptor-G-protein coupling. J. Biol. Chem. 268, 8003-8011. (Pubitemid 23120381)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.11 , pp. 8003-8011
    • Kennedy, M.E.1    Limbird, L.E.2
  • 49
    • 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., and Albert, A. D. (1996) Structure determination of the fourth cytoplasmic loop and carboxyl terminal domain of bovine rhodopsin. Mol. Vis. 2, 12.
    • (1996) Mol. Vis. , vol.2 , pp. 12
    • Yeagle, P.L.1    Alderfer, J.L.2    Albert, A.D.3
  • 50
    • 12844283365 scopus 로고    scopus 로고
    • The conformation of the cytoplasmic helix 8 of the CB1 cannabinoid receptor using NMR and circular dichroism
    • DOI 10.1016/j.bbamem.2004.10.011, PII S0005273604002810
    • Choi, G., Guo, J., and Makriyannis, A. (2005) The conformation of the cytoplasmic helix 8 of the CB1 cannabinoid receptor using NMR and circular dichroism. Biochim. Biophys. Acta 1668, 1-9. (Pubitemid 40164727)
    • (2005) Biochimica et Biophysica Acta - Biomembranes , vol.1668 , Issue.1 , pp. 1-9
    • Choi, G.1    Guo, J.2    Makriyannis, A.3
  • 51
    • 0036729440 scopus 로고    scopus 로고
    • The cytoplasmic helix of cannabinoid receptor CB2, a conformational study by circular dichroism and (1)H NMR spectroscopy in aqueous and membrane-like environments
    • Choi, G., Landin, J., and Xie, X. Q. (2002) The cytoplasmic helix of cannabinoid receptor CB2, a conformational study by circular dichroism and (1)H NMR spectroscopy in aqueous and membrane-like environments. J. Pept. Res. 60, 169-177.
    • (2002) J. Pept. Res. , vol.60 , pp. 169-177
    • Choi, G.1    Landin, J.2    Xie, X.Q.3
  • 52
    • 2442456918 scopus 로고    scopus 로고
    • Structural studies of the putative helix 8 in the human beta(2) adrenergic receptor: An NMR study
    • Katragadda, M., Maciejewski, M. W., and Yeagle, P. L. (2004) Structural studies of the putative helix 8 in the human beta(2) adrenergic receptor: an NMR study. Biochim. Biophys. Acta 1663, 74-81.
    • (2004) Biochim. Biophys. Acta , vol.1663 , pp. 74-81
    • Katragadda, M.1    Maciejewski, M.W.2    Yeagle, P.L.3
  • 53
    • 0037064217 scopus 로고    scopus 로고
    • Crystal structure of rhodopsin: A template for cone visual pigments and other G protein-coupled receptors
    • DOI 10.1016/S0005-2736(02)00567-9, PII S0005273602005679
    • Stenkamp, R. E., Filipek, S., Driessen, C. A., Teller, D. C., and Palczewski, K. (2002) Crystal structure of rhodopsin: a template for cone visual pigments and other G protein-coupled receptors. Biochim. Biophys. Acta 1565, 168-182. (Pubitemid 35284473)
    • (2002) Biochimica et Biophysica Acta - Biomembranes , vol.1565 , Issue.2 , pp. 168-182
    • Stenkamp, R.E.1    Filipek, S.2    Driessen, C.A.G.G.3    Teller, D.C.4    Palczewski, K.5
  • 54
    • 0033594926 scopus 로고    scopus 로고
    • Structural features of the C-terminal domain of bovine rhodopsin: A site-directed spin-labeling study
    • Langen, R., Cai, K., Altenbach, C., Khorana, H. G., and Hubbell, W. L. (1999) Structural features of the C-terminal domain of bovine rhodopsin: a site-directed spin-labeling study. Biochemistry 38, 7918-7924. (Pubitemid 129516641)
    • (1999) Biochemistry , vol.38 , Issue.25 , pp. 7918-7924
    • Langen, R.1    Cai, K.2    Altenbach, C.3    Khorana, H.G.4    Hubbell, W.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.