메뉴 건너뛰기




Volumn 91, Issue 12, 2006, Pages 4464-4477

Curvature and Hydrophobic forces drive oligomerization and modulate activity of rhodopsin in membranes

Author keywords

[No Author keywords available]

Indexed keywords

G PROTEIN COUPLED RECEPTOR; RHODOPSIN;

EID: 33845505655     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.106.082776     Document Type: Article
Times cited : (238)

References (103)
  • 2
    • 21844441860 scopus 로고    scopus 로고
    • Monomeric G-protein-coupled receptor as a functional unit
    • Chabre, M., and M. le Maire. 2005. Monomeric G-protein-coupled receptor as a functional unit. Biochemistry. 44:9395-9403.
    • (2005) Biochemistry , vol.44 , pp. 9395-9403
    • Chabre, M.1    Le Maire, M.2
  • 4
    • 0037285444 scopus 로고    scopus 로고
    • Rhodopsin structure, dynamics, and activation: A perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking
    • Hubbell, W. L., C. Altenbach, C. M. Hubbell, and H. G. Khorana. 2003. Rhodopsin structure, dynamics, and activation: a perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking. Adv. Prot. Chem. 63:243-290.
    • (2003) Adv. Prot. Chem. , vol.63 , pp. 243-290
    • Hubbell, W.L.1    Altenbach, C.2    Hubbell, C.M.3    Khorana, H.G.4
  • 5
    • 0036780743 scopus 로고    scopus 로고
    • G-protein-coupled receptor oligomerization and its potential for drug discovery
    • George, S. R., B. F. O'Dowd, and S. R. Lee. 2002. G-protein-coupled receptor oligomerization and its potential for drug discovery. Nat. Rev. Drug Disc. 1:808-820.
    • (2002) Nat. Rev. Drug Disc. , vol.1 , pp. 808-820
    • George, S.R.1    O'Dowd, B.F.2    Lee, S.R.3
  • 6
    • 0035318509 scopus 로고    scopus 로고
    • Oligomerization of G-protein-coupled transmitter receptors
    • Bouvier, M. 2001. Oligomerization of G-protein-coupled transmitter receptors. Nat. Rev. Neurosci. 2:274-286.
    • (2001) Nat. Rev. Neurosci. , vol.2 , pp. 274-286
    • Bouvier, M.1
  • 8
    • 10844255797 scopus 로고    scopus 로고
    • Oligomerization of G protein-coupled receptors: Past, present, and future
    • Park, P. S.-H., S. Filipek, J. W. Wells, and K. Palczewski. 2004. Oligomerization of G protein-coupled receptors: past, present, and future. Biochemistry. 43:15643-15656.
    • (2004) Biochemistry , vol.43 , pp. 15643-15656
    • Park, P.S.-H.1    Filipek, S.2    Wells, J.W.3    Palczewski, K.4
  • 10
    • 0037959071 scopus 로고    scopus 로고
    • The state of lipid rafts: From model membranes to cells
    • Edidin, M. 2003. The state of lipid rafts: from model membranes to cells. Annu. Rev. Biophys. Biomol. Struct. 32:257-283.
    • (2003) Annu. Rev. Biophys. Biomol. Struct. , vol.32 , pp. 257-283
    • Edidin, M.1
  • 14
    • 1942519744 scopus 로고    scopus 로고
    • Membrane model for the GPCR prototype rhodopsin: Hydrophobic interface and dynamical structure
    • Huber, T., A. V. Botelho, K. Beyer, and M. F. Brown. 2004. Membrane model for the GPCR prototype rhodopsin: hydrophobic interface and dynamical structure. Biophys. J. 86:2078-2100.
    • (2004) Biophys. J. , vol.86 , pp. 2078-2100
    • Huber, T.1    Botelho, A.V.2    Beyer, K.3    Brown, M.F.4
  • 18
    • 5044235587 scopus 로고    scopus 로고
    • Electron crystallography reveals the structure of metarhodopsin I
    • Ruprecht, J. J., T. Mielke, R. Vogel, C. Villa, and G. F. X. Schertler. 2004. Electron crystallography reveals the structure of metarhodopsin I. EMBO J. 23:3609-3620.
    • (2004) EMBO J. , vol.23 , pp. 3609-3620
    • Ruprecht, J.J.1    Mielke, T.2    Vogel, R.3    Villa, C.4    Schertler, G.F.X.5
  • 20
    • 0034705612 scopus 로고    scopus 로고
    • Movement of retinal along the visual transduction path
    • Borhan, B., M. L. Souto, H. Imai, Y. Shichida, and K. Nakanishi. 2000. Movement of retinal along the visual transduction path. Science. 288:2209-2212.
    • (2000) Science , vol.288 , pp. 2209-2212
    • Borhan, B.1    Souto, M.L.2    Imai, H.3    Shichida, Y.4    Nakanishi, K.5
  • 22
    • 3843115666 scopus 로고    scopus 로고
    • Reduced G protein-coupled signaling efficiency in retinal rod outer segments in response to n-3 fatty acid deficiency
    • Niu, S.-L., D. C. Mitchell, S.-Y. Lim, Z.-M. Wen, H.-Y. Kim, N. Salem, Jr., and B. J. Litman. 2004. Reduced G protein-coupled signaling efficiency in retinal rod outer segments in response to n-3 fatty acid deficiency. J. Biol. Chem. 279:31098-31104.
    • (2004) J. Biol. Chem. , vol.279 , pp. 31098-31104
    • Niu, S.-L.1    Mitchell, D.C.2    Lim, S.-Y.3    Wen, Z.-M.4    Kim, H.-Y.5    Salem Jr., N.6    Litman, B.J.7
  • 23
    • 0034075971 scopus 로고    scopus 로고
    • High-resolution FRET microscopy of cholera toxin B-subunit and GPI-anchored proteins in cell plasma membranes
    • Kenworthy, A. K., N. Petranova, and M. Edidin. 2000. High-resolution FRET microscopy of cholera toxin B-subunit and GPI-anchored proteins in cell plasma membranes. Mol. Biol. Cell. 11:1645-1655.
    • (2000) Mol. Biol. Cell. , vol.11 , pp. 1645-1655
    • Kenworthy, A.K.1    Petranova, N.2    Edidin, M.3
  • 24
    • 0020455954 scopus 로고
    • Spin-label saturation-transfer electron spin resonance detection of transient association of rhodopsin in reconstituted membranes
    • Kusumi, A., and J. S. Hyde. 1982. Spin-label saturation-transfer electron spin resonance detection of transient association of rhodopsin in reconstituted membranes. Biochemistry. 21:5978-5983.
    • (1982) Biochemistry , vol.21 , pp. 5978-5983
    • Kusumi, A.1    Hyde, J.S.2
  • 25
    • 0026795003 scopus 로고
    • Protein rotational diffusion and lipid/protein interactions in recombinants of bovine rhodopsin with saturated diacylphosphatidylcholines of different chain lengths studied by conventional and saturation-transfer electron spin resonance
    • Ryba, N. J. P., and D. Marsh. 1992. Protein rotational diffusion and lipid/protein interactions in recombinants of bovine rhodopsin with saturated diacylphosphatidylcholines of different chain lengths studied by conventional and saturation-transfer electron spin resonance. Biochemistry. 31:7511-7518.
    • (1992) Biochemistry , vol.31 , pp. 7511-7518
    • Ryba, N.J.P.1    Marsh, D.2
  • 26
    • 84943997802 scopus 로고
    • Elastic properties of lipid bilayers. Theory and possible experiments. Z
    • Helfrich, W. 1973. Elastic properties of lipid bilayers. Theory and possible experiments. Z. Naturforsch. 28c:693-703.
    • (1973) Naturforsch. , vol.28 C , pp. 693-703
    • Helfrich, W.1
  • 27
    • 0028124422 scopus 로고
    • Modulation of rhodopsin function by properties of the membrane bilayer
    • Brown, M. F. 1994. Modulation of rhodopsin function by properties of the membrane bilayer. Chem. Phys. Lipids. 73:159-180.
    • (1994) Chem. Phys. Lipids , vol.73 , pp. 159-180
    • Brown, M.F.1
  • 28
    • 33845484750 scopus 로고    scopus 로고
    • Flexible surface model for lipid-rhodopsin interactions: Further analysis
    • (Abstr.)
    • Botelho, A. V., T. Huber, and M. F. Brown. 2003. Flexible surface model for lipid-rhodopsin interactions: further analysis. Biophys. J. 84:55A (Abstr.).
    • (2003) Biophys. J. , vol.84
    • Botelho, A.V.1    Huber, T.2    Brown, M.F.3
  • 29
    • 85030597355 scopus 로고    scopus 로고
    • Direct effect of membrane stress on lipid-rhodopsin organzation and function
    • (Abstr.)
    • Botelho, A. V., T. Huber, T. P. Sakmar, and M. F. Brown. 2005. Direct effect of membrane stress on lipid-rhodopsin organzation and function. Biophys. J. 88:579A (Abstr.).
    • (2005) Biophys. J. , vol.88
    • Botelho, A.V.1    Huber, T.2    Sakmar, T.P.3    Brown, M.F.4
  • 30
    • 85030596759 scopus 로고    scopus 로고
    • Curvature and hydrophobic mismatch drive non-ideal mixing and activation of rhodopsin in membranes
    • (Abstr.)
    • Huber, T., A. V. Botelho, T. P. Sakmar, and M. F. Brown. 2006. Curvature and hydrophobic mismatch drive non-ideal mixing and activation of rhodopsin in membranes. Biophys. J. 90:15A (Abstr.).
    • (2006) Biophys. J. , vol.90
    • Huber, T.1    Botelho, A.V.2    Sakmar, T.P.3    Brown, M.F.4
  • 31
    • 0037150089 scopus 로고    scopus 로고
    • Conformational energetics of rhodopsin modulated by nonlamellar forming lipids
    • Botelho, A. V., N. J. Gibson, Y. Wang, R. L. Thurmond, and M. F. Brown. 2002. Conformational energetics of rhodopsin modulated by nonlamellar forming lipids. Biochemistry. 41:6354-6368.
    • (2002) Biochemistry , vol.41 , pp. 6354-6368
    • Botelho, A.V.1    Gibson, N.J.2    Wang, Y.3    Thurmond, R.L.4    Brown, M.F.5
  • 32
    • 0020664920 scopus 로고
    • Rhodopsin in reconstituted phospholipid vesicles. 1. Structural parameters and light-induced conformational changes detected by resonance energy transfer and fluorescence quenching
    • Borochov-Neori, H., and M. Montal. 1983. Rhodopsin in reconstituted phospholipid vesicles. 1. Structural parameters and light-induced conformational changes detected by resonance energy transfer and fluorescence quenching. Biochemistry. 22:197-205.
    • (1983) Biochemistry , vol.22 , pp. 197-205
    • Borochov-Neori, H.1    Montal, M.2
  • 33
    • 0020663426 scopus 로고
    • Rhodopsin in reconstituted phospholipid vesicles. 2. Rhodopsin-rhodopsin interactions detected by resonance energy transfer
    • Borochov-Neori, H., P. A. G. Fortes, and M. Montal. 1983. Rhodopsin in reconstituted phospholipid vesicles. 2. Rhodopsin-rhodopsin interactions detected by resonance energy transfer. Biochemistry. 22:206-213.
    • (1983) Biochemistry , vol.22 , pp. 206-213
    • Borochov-Neori, H.1    Fortes, P.A.G.2    Montal, M.3
  • 34
    • 12544250742 scopus 로고    scopus 로고
    • Suppression of wild-type rhodopsin maturation by mutants linked to autosomal dominant retinitis pigmentosa
    • Rajan, R. S., and R. R. Kopito. 2005. Suppression of wild-type rhodopsin maturation by mutants linked to autosomal dominant retinitis pigmentosa. J. Biol. Chem. 280:1284-1291.
    • (2005) J. Biol. Chem. , vol.280 , pp. 1284-1291
    • Rajan, R.S.1    Kopito, R.R.2
  • 35
    • 0024536280 scopus 로고
    • Rhodopsin-G-protein interactions monitored by resonance energy transfer
    • Borochov-Neori, H., and M. Montal. 1989. Rhodopsin-G-protein interactions monitored by resonance energy transfer. Biochemistry. 28:1711-1718.
    • (1989) Biochemistry , vol.28 , pp. 1711-1718
    • Borochov-Neori, H.1    Montal, M.2
  • 37
    • 0018650688 scopus 로고
    • An analytic solution to the Förster energy transfer problem in two dimensions
    • Wolber, P. K., and B. S. Hudson. 1979. An analytic solution to the Förster energy transfer problem in two dimensions. Biophys. J. 28:197-210.
    • (1979) Biophys. J. , vol.28 , pp. 197-210
    • Wolber, P.K.1    Hudson, B.S.2
  • 38
    • 33845495068 scopus 로고
    • Characterization of rhodopsin in synthetic systems
    • Hubbell, W. L. 1975. Characterization of rhodopsin in synthetic systems. Acc. Chem. Res. 8:85-91.
    • (1975) Acc. Chem. Res. , vol.8 , pp. 85-91
    • Hubbell, W.L.1
  • 39
    • 0021882555 scopus 로고
    • Effects of lipid environment on the light-induced conformational changes of rhodopsin. 2. Roles of lipid chain length, unsaturation, and phase state
    • Baldwin, P. A., and W. L. Hubbell. 1985. Effects of lipid environment on the light-induced conformational changes of rhodopsin. 2. Roles of lipid chain length, unsaturation, and phase state. Biochemistry. 24:2633-2639.
    • (1985) Biochemistry , vol.24 , pp. 2633-2639
    • Baldwin, P.A.1    Hubbell, W.L.2
  • 40
    • 0020589093 scopus 로고
    • Pair distribution-functions of bacteriorhodopsin and rhodopsin in model bilayers
    • Pearson, L. T., S. I. Chan, B. A. Lewis, and D. M. Engelman. 1983. Pair distribution-functions of bacteriorhodopsin and rhodopsin in model bilayers. Biophys. J. 43:167-174.
    • (1983) Biophys. J. , vol.43 , pp. 167-174
    • Pearson, L.T.1    Chan, S.I.2    Lewis, B.A.3    Engelman, D.M.4
  • 41
    • 0021104115 scopus 로고
    • Bacteriorhodopsin remains dispersed in fluid phospholipid bilayers over a wide range of bilayer thickness
    • Lewis, B. A., and D. M. Engelman. 1983. Bacteriorhodopsin remains dispersed in fluid phospholipid bilayers over a wide range of bilayer thickness. J. Mol. Biol. 166:203-210.
    • (1983) J. Mol. Biol. , vol.166 , pp. 203-210
    • Lewis, B.A.1    Engelman, D.M.2
  • 42
    • 7044241302 scopus 로고    scopus 로고
    • How lipids affect the activities of integral membrane proteins
    • Lee, A. G. 2004. How lipids affect the activities of integral membrane proteins. Biochim. Biophys. Acta. 1666:62-87.
    • (2004) Biochim. Biophys. Acta. , vol.1666 , pp. 62-87
    • Lee, A.G.1
  • 43
    • 0036725152 scopus 로고    scopus 로고
    • Physical principles underlying the transduction of bilayer deformation forces during mechanosensitive channel gating
    • Perozo, E., A. Kloda, D. M. Cortes, and B. Martinac. 2002. Physical principles underlying the transduction of bilayer deformation forces during mechanosensitive channel gating. Nat. Struct. Biol. 9:696-703.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 696-703
    • Perozo, E.1    Kloda, A.2    Cortes, D.M.3    Martinac, B.4
  • 44
    • 7244244196 scopus 로고    scopus 로고
    • Lipids do influence protein function-the hydrophobic matching hypothesis revisited
    • Jensen, M. Ø., and O. G. Mouritsen. 2004. Lipids do influence protein function-the hydrophobic matching hypothesis revisited. Biochim. Biophys. Acta. 1666:205-226.
    • (2004) Biochim. Biophys. Acta , vol.1666 , pp. 205-226
    • Jensen, M.Ø.1    Mouritsen, O.G.2
  • 46
    • 0033737385 scopus 로고    scopus 로고
    • Inclusion-induced bilayer deformations: Effects of monolayer equililbrium curvature
    • Nielsen, C., and O. S. Andersen. 2000. Inclusion-induced bilayer deformations: effects of monolayer equililbrium curvature. Biophys. J. 79:2583-2604.
    • (2000) Biophys. J. , vol.79 , pp. 2583-2604
    • Nielsen, C.1    Andersen, O.S.2
  • 47
    • 0033038093 scopus 로고    scopus 로고
    • Theoretical analysis of hydrophobic matching and membrane-mediated interactions in lipid bilayers containing gramicidin
    • Harroun, T. A., W. T. Heller, T. M. Weiss, L. Yang, and H. W. Huang. 1999. Theoretical analysis of hydrophobic matching and membrane-mediated interactions in lipid bilayers containing gramicidin. Biophys. J. 76:3176-3185.
    • (1999) Biophys. J. , vol.76 , pp. 3176-3185
    • Harroun, T.A.1    Heller, W.T.2    Weiss, T.M.3    Yang, L.4    Huang, H.W.5
  • 48
    • 0021758996 scopus 로고
    • Temperature and pH dependence of the metarhodopsin I-metarhodopsin II kinetics and equilibria in bovine rod diskmembrane suspensions
    • Parkes, J. H., and P. A. Liebman. 1984. Temperature and pH dependence of the metarhodopsin I-metarhodopsin II kinetics and equilibria in bovine rod diskmembrane suspensions. Biochemistry. 23:5054-5061.
    • (1984) Biochemistry , vol.23 , pp. 5054-5061
    • Parkes, J.H.1    Liebman, P.A.2
  • 49
    • 0038729667 scopus 로고    scopus 로고
    • Signaling states of rhodopsin. Formation of the storage form, metarhodopsin III, from active metarhodopsin II
    • Heck, M., S. A. Schädel, D. Maretzki, F. J. Bartl, E. Ritter, K. Palczewski, and K. P. Hofmann. 2003. Signaling states of rhodopsin. Formation of the storage form, metarhodopsin III, from active metarhodopsin II. J. Biol. Chem. 278:3162-3169.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3162-3169
    • Heck, M.1    Schädel, S.A.2    Maretzki, D.3    Bartl, F.J.4    Ritter, E.5    Palczewski, K.6    Hofmann, K.P.7
  • 50
    • 0018145219 scopus 로고
    • Biochemical aspects of the visual process. XXXVIII. Effects of lateral aggregation on rhodopsin in phospholipase C-treated photoreceptor membranes
    • van Breugel, P. J. G. M., P. H. M. Geurts, F. J. M. Daemen, and S. L. Bonting. 1978. Biochemical aspects of the visual process. XXXVIII. Effects of lateral aggregation on rhodopsin in phospholipase C-treated photoreceptor membranes. Biochim. Biophys. Acta. 509:136-147.
    • (1978) Biochim. Biophys. Acta , vol.509 , pp. 136-147
    • Van Breugel, P.J.G.M.1    Geurts, P.H.M.2    Daemen, F.J.M.3    Bonting, S.L.4
  • 51
    • 0020503982 scopus 로고
    • Reversible modulation of rhodopsin photolysis in pure phosphatidylserine membranes
    • DeGrip, W. J., J. Olive, and P. H. M. Bovee-Geurts. 1983. Reversible modulation of rhodopsin photolysis in pure phosphatidylserine membranes. Biochim. Biophys. Acta. 734:168-179.
    • (1983) Biochim. Biophys. Acta , vol.734 , pp. 168-179
    • Degrip, W.J.1    Olive, J.2    Bovee-Geurts, P.H.M.3
  • 52
    • 0035818444 scopus 로고    scopus 로고
    • Anions stabilize a metarhodopsin II-like photoproduct with a protonated Schiff base
    • Vogel, R., G. B. Fan, F. Siebert, and M. Sheves. 2001. Anions stabilize a metarhodopsin II-like photoproduct with a protonated Schiff base. Biochemistry. 40:13342-13352.
    • (2001) Biochemistry , vol.40 , pp. 13342-13352
    • Vogel, R.1    Fan, G.B.2    Siebert, F.3    Sheves, M.4
  • 54
    • 0034730097 scopus 로고    scopus 로고
    • Transducin-dependent protonation of glutamic acid 134 in rhodopsin
    • Fahmy, K., T. P. Sakmar, and F. Siebert. 2000. Transducin-dependent protonation of glutamic acid 134 in rhodopsin. Biochemistry. 39:10607-10612.
    • (2000) Biochemistry , vol.39 , pp. 10607-10612
    • Fahmy, K.1    Sakmar, T.P.2    Siebert, F.3
  • 55
    • 0027518957 scopus 로고
    • Lipid headgroup and acyl chain composition modulate the MI-MII equilibrium of rhodopsin in recombinant membranes
    • Gibson, N. J., and M. F. Brown. 1993. Lipid headgroup and acyl chain composition modulate the MI-MII equilibrium of rhodopsin in recombinant membranes. Biochemistry. 32:2438-2454.
    • (1993) Biochemistry , vol.32 , pp. 2438-2454
    • Gibson, N.J.1    Brown, M.F.2
  • 56
    • 0027317273 scopus 로고
    • Two different forms of metarhodopsin II: Schiff base deprotonation precedes proton uptake and signaling state
    • Arnis, S., and K. P. Hofmann. 1993. Two different forms of metarhodopsin II: Schiff base deprotonation precedes proton uptake and signaling state. Proc. Natl. Acad. Sci. USA. 90:7849-7853.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7849-7853
    • Arnis, S.1    Hofmann, K.P.2
  • 57
    • 0025074536 scopus 로고
    • Interconversion of metarhodopsins I and II: A branched photointermediate decay model
    • Straume, M., D. C. Mitchell, J. L. Miller, and B. J. Litman. 1990. Interconversion of metarhodopsins I and II: a branched photointermediate decay model. Biochemistry. 29:9135-9142.
    • (1990) Biochemistry , vol.29 , pp. 9135-9142
    • Straume, M.1    Mitchell, D.C.2    Miller, J.L.3    Litman, B.J.4
  • 58
    • 0021474573 scopus 로고
    • Mattress model of lipid-protein interactions in membranes
    • Mouritsen, O. G., and M. Bloom. 1984. Mattress model of lipid-protein interactions in membranes. Biophys. J. 46:141-153.
    • (1984) Biophys. J. , vol.46 , pp. 141-153
    • Mouritsen, O.G.1    Bloom, M.2
  • 60
    • 0027757062 scopus 로고
    • Effects of temperature on rhodopsin photointermediates from lumirhodopsin to metarhodopsin-II
    • Thorgeirsson, T. E., J. W. Lewis, S. E. Wallace-Williams, and D. S. Kliger. 1993. Effects of temperature on rhodopsin photointermediates from lumirhodopsin to metarhodopsin-II. Biochemistry. 32:13861-13872.
    • (1993) Biochemistry , vol.32 , pp. 13861-13872
    • Thorgeirsson, T.E.1    Lewis, J.W.2    Wallace-Williams, S.E.3    Kliger, D.S.4
  • 61
    • 33645705346 scopus 로고
    • Membrane-induced interactions between inclusions
    • Dan, N., P. Pincus, and S. A. Safran. 1993. Membrane-induced interactions between inclusions. Langmuir. 9:2768-2771.
    • (1993) Langmuir. , vol.9 , pp. 2768-2771
    • Dan, N.1    Pincus, P.2    Safran, S.A.3
  • 64
    • 0032857624 scopus 로고    scopus 로고
    • The influence of membrane lateral pressures on simple geometric models of protein conformational equilibria
    • Cantor, R. S. 1999. The influence of membrane lateral pressures on simple geometric models of protein conformational equilibria. Chem. Phys. Lipids. 101:45-56.
    • (1999) Chem. Phys. Lipids , vol.101 , pp. 45-56
    • Cantor, R.S.1
  • 67
    • 0023682325 scopus 로고
    • Lipid-protein interactions mediate the photochemical function of rhodopsin
    • Wiedmann, T. S., R. D. Pates, J. M. Beach, A. Salmon, and M. F. Brown. 1988. Lipid-protein interactions mediate the photochemical function of rhodopsin. Biochemistry. 27:6469-6474.
    • (1988) Biochemistry , vol.27 , pp. 6469-6474
    • Wiedmann, T.S.1    Pates, R.D.2    Beach, J.M.3    Salmon, A.4    Brown, M.F.5
  • 68
    • 1642447757 scopus 로고    scopus 로고
    • Elastic coupling of integral membrane protein stability to lipid bilayer forces
    • Hong, H., and L. K. Tamm. 2004. Elastic coupling of integral membrane protein stability to lipid bilayer forces. Proc. Natl. Acad. Sci. USA. 101:4065-4070.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 4065-4070
    • Hong, H.1    Tamm, L.K.2
  • 69
    • 28444488355 scopus 로고    scopus 로고
    • Solving the membrane protein folding problem
    • Bowie, J. U. 2005. Solving the membrane protein folding problem. Nature (Lond.). 438:581-589.
    • (2005) Nature (Lond.) , vol.438 , pp. 581-589
    • Bowie, J.U.1
  • 70
    • 28444476999 scopus 로고    scopus 로고
    • Membrane curvature and mechanisms of dynamic cell membrane remodelling
    • McMahon, H. T., and J. L. Gallop. 2005. Membrane curvature and mechanisms of dynamic cell membrane remodelling. Nature (Lond.). 438:590-596.
    • (2005) Nature (Lond.) , vol.438 , pp. 590-596
    • McMahon, H.T.1    Gallop, J.L.2
  • 71
    • 23044490778 scopus 로고    scopus 로고
    • Same in the membrane: Designing systems to modulate membrane proteins
    • Booth, P. J. 2005. Same in the membrane: designing systems to modulate membrane proteins. Curr. Opin. Struct. Biol. 15:435-440.
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 435-440
    • Booth, P.J.1
  • 72
    • 33644846421 scopus 로고    scopus 로고
    • How proteins produce cellular membrane curvature
    • Zimmerberg, J., and M. M. Kozlov. 2006. How proteins produce cellular membrane curvature. Nat. Rev. Mol. Cell Biol. 7:9-19.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 9-19
    • Zimmerberg, J.1    Kozlov, M.M.2
  • 73
    • 33845469707 scopus 로고
    • Activation of mannosyltransferase II by nonbilayer phospholipids
    • Jensen, J. W., and J. S. Schutzbach. 1984. Activation of mannosyltransferase II by nonbilayer phospholipids. Biochemistry. 23:1115-1119.
    • (1984) Biochemistry , vol.23 , pp. 1115-1119
    • Jensen, J.W.1    Schutzbach, J.S.2
  • 75
    • 0023052449 scopus 로고
    • Phase equilibria of membrane lipids from Acholeplasma laidlawii. The importance of a single lipid forming nonlamellar phases
    • Lindblom, G., I. Brentel, M. Sjölund, G. Wikander, and Å. Wieslander. 1986. Phase equilibria of membrane lipids from Acholeplasma laidlawii. The importance of a single lipid forming nonlamellar phases. Biochemistry. 25:7502-7510.
    • (1986) Biochemistry , vol.25 , pp. 7502-7510
    • Lindblom, G.1    Brentel, I.2    Sjölund, M.3    Wikander, G.4    Wieslander, Å.5
  • 76
    • 0027291942 scopus 로고
    • Probability of alamethicin conductance states varies with nonlamellar tendency of bilayer phospholipids
    • Keller, S. L., S. M. Bezrukov, S. M. Gruner, M. W. Tate, I. Vodyanoy, and V. A. Parsegian. 1993. Probability of alamethicin conductance states varies with nonlamellar tendency of bilayer phospholipids. Biophys. J. 65:23-27.
    • (1993) Biophys. J. , vol.65 , pp. 23-27
    • Keller, S.L.1    Bezrukov, S.M.2    Gruner, S.M.3    Tate, M.W.4    Vodyanoy, I.5    Parsegian, V.A.6
  • 77
    • 0001065811 scopus 로고
    • Theory of protein-lipid and protein-protein interactions in bilayer membranes
    • Owicki, J. C., and H. M. McConnell. 1979. Theory of protein-lipid and protein-protein interactions in bilayer membranes. Proc. Natl. Acad. Sci. USA. 76:4750-4754.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4750-4754
    • Owicki, J.C.1    McConnell, H.M.2
  • 78
    • 0031740415 scopus 로고    scopus 로고
    • Hydrophobic mismatch between proteins and lipids in membranes
    • Killian, J. A. 1998. Hydrophobic mismatch between proteins and lipids in membranes. Biochim. Biophys. Acta. 1376:401-416.
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 401-416
    • Killian, J.A.1
  • 79
    • 0018594495 scopus 로고
    • Rhodopsin-lipid associations in bovine rod outer segment membranes. Identification of immobilized lipid by spin-labels
    • Watts, A., I. D. Volotovski, and D. Marsh. 1979. Rhodopsin-lipid associations in bovine rod outer segment membranes. Identification of immobilized lipid by spin-labels. Biochemistry. 18:5006-5013.
    • (1979) Biochemistry , vol.18 , pp. 5006-5013
    • Watts, A.1    Volotovski, I.D.2    Marsh, D.3
  • 80
    • 0029778268 scopus 로고    scopus 로고
    • Rhodopsin activation blocked by metal-ion-binding sites linking transmembrane helices C and F
    • Sheikh, S. P., T. A. Zvyaga, O. Lichtarge, T. P. Sakmar, and H. R. Bourne. 1996. Rhodopsin activation blocked by metal-ion-binding sites linking transmembrane helices C and F. Nature (Lond.). 383:347-350.
    • (1996) Nature (Lond.) , vol.383 , pp. 347-350
    • Sheikh, S.P.1    Zvyaga, T.A.2    Lichtarge, O.3    Sakmar, T.P.4    Bourne, H.R.5
  • 86
    • 0008565479 scopus 로고    scopus 로고
    • Plasmon resonance spectroscopy: Probing molecular interactions within membranes
    • Salamon, Z., M. F. Brown, and G. Tollin. 1999. Plasmon resonance spectroscopy: probing molecular interactions within membranes. Trends Biochem. Sci. 24:213-219.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 213-219
    • Salamon, Z.1    Brown, M.F.2    Tollin, G.3
  • 87
    • 0011847313 scopus 로고
    • Stability of lyotropic phases with curved interfaces
    • Gruner, S. M. 1989. Stability of lyotropic phases with curved interfaces. J. Phys. Chem. 93:7562-7570.
    • (1989) J. Phys. Chem. , vol.93 , pp. 7562-7570
    • Gruner, S.M.1
  • 88
    • 0025134135 scopus 로고
    • II) phase, and non-lamellar phase transitions of lipids
    • II) phase, and non-lamellar phase transitions of lipids. Biochim. Biophys. Acta. 1031:1-69.
    • (1990) Biochim. Biophys. Acta , vol.1031 , pp. 1-69
    • Seddon, J.M.1
  • 89
    • 0028415938 scopus 로고
    • Globular and bicontinuous phases of nonionic surfactant films
    • Olsson, U., and H. Wennerström. 1994. Globular and bicontinuous phases of nonionic surfactant films. Adv. Colloid Interface Sci. 49:113-146.
    • (1994) Adv. Colloid Interface Sci. , vol.49 , pp. 113-146
    • Olsson, U.1    Wennerström, H.2
  • 90
    • 0015963426 scopus 로고
    • Effects of detergents and high pressures upon the metarhodopsin I-metarhodopsin II equilibrium
    • Lamola, A. A., T. Yamane, and A. Zipp. 1974. Effects of detergents and high pressures upon the metarhodopsin I-metarhodopsin II equilibrium. Biochemistry. 13:738-745.
    • (1974) Biochemistry , vol.13 , pp. 738-745
    • Lamola, A.A.1    Yamane, T.2    Zipp, A.3
  • 91
    • 24144476925 scopus 로고    scopus 로고
    • Effect of packing density on rhodopsin stability and function in polyunsaturated membranes
    • Niu, S.-L., and D. C. Mitchell. 2005. Effect of packing density on rhodopsin stability and function in polyunsaturated membranes. Biophys. J. 89:1833-1840.
    • (2005) Biophys. J. , vol.89 , pp. 1833-1840
    • Niu, S.-L.1    Mitchell, D.C.2
  • 92
    • 0029922635 scopus 로고    scopus 로고
    • Surface plasmon resonance spectroscopy studies of membrane proteins: Transducin binding and activation by rhodopsin monitored in thin membrane films
    • Salamon, Z., Y. Wang, J. L. Soulages, M. F. Brown, and G. Tollin. 1996. Surface plasmon resonance spectroscopy studies of membrane proteins: transducin binding and activation by rhodopsin monitored in thin membrane films. Biophys. J. 71:283-294.
    • (1996) Biophys. J. , vol.71 , pp. 283-294
    • Salamon, Z.1    Wang, Y.2    Soulages, J.L.3    Brown, M.F.4    Tollin, G.5
  • 93
    • 11244331442 scopus 로고    scopus 로고
    • Phosphatidylethanolamine enhances rhodopsin photoactivation and transducin binding in a solid supported lipid bilayer as determined using plasmon-waveguide resonance spectroscopy
    • Alves, I. D., G. F. J. Salgado, Z. Salamon, M. F. Brown, G. Tollin, and V. J. Hruby. 2005. Phosphatidylethanolamine enhances rhodopsin photoactivation and transducin binding in a solid supported lipid bilayer as determined using plasmon-waveguide resonance spectroscopy. Biophys. J. 88:198-210.
    • (2005) Biophys. J. , vol.88 , pp. 198-210
    • Alves, I.D.1    Salgado, G.F.J.2    Salamon, Z.3    Brown, M.F.4    Tollin, G.5    Hruby, V.J.6
  • 94
    • 0018567294 scopus 로고
    • Energy uptake in the first step of visual excitation
    • Cooper, A. 1979. Energy uptake in the first step of visual excitation. Nature (Lond.). 282:531-533.
    • (1979) Nature (Lond.) , vol.282 , pp. 531-533
    • Cooper, A.1
  • 95
    • 0023219466 scopus 로고
    • Energy storage in the primary photochemical events of rhodopsin and isorhodopsin
    • Schick, G. A., T. M. Cooper, R. A. Holloway, L. P. Murray, and R. R. Birge. 1987. Energy storage in the primary photochemical events of rhodopsin and isorhodopsin. Biochemistry. 26:2556-2562.
    • (1987) Biochemistry , vol.26 , pp. 2556-2562
    • Schick, G.A.1    Cooper, T.M.2    Holloway, R.A.3    Murray, L.P.4    Birge, R.R.5
  • 96
    • 0021811862 scopus 로고
    • Thermotropic behavior of retinal rod membranes and dispersions of extracted phospholipids
    • Miljanich, G. P., M. F. Brown, S. Mabrey-Gaud, E. A. Dratz, and J. M. Sturtevant. 1985. Thermotropic behavior of retinal rod membranes and dispersions of extracted phospholipids. J. Membr. Biol. 85:79-86.
    • (1985) J. Membr. Biol. , vol.85 , pp. 79-86
    • Miljanich, G.P.1    Brown, M.F.2    Mabrey-Gaud, S.3    Dratz, E.A.4    Sturtevant, J.M.5
  • 98
    • 7044232102 scopus 로고    scopus 로고
    • Nonbilayer lipids affect peripheral and integral membrane proteins via changes in the lateral pressure profile
    • van den Brink-van der Laan, E., J. A. Killian, and B. de Kruijff. 2004. Nonbilayer lipids affect peripheral and integral membrane proteins via changes in the lateral pressure profile. Biochim. Biophys. Acta. 1666:275-288.
    • (2004) Biochim. Biophys. Acta , vol.1666 , pp. 275-288
    • Van Den Brink-van Der Laan, E.1    Killian, J.A.2    De Kruijff, B.3
  • 99
    • 0038159530 scopus 로고    scopus 로고
    • Organization of the G protein-coupled receptors rhodopsin and opsin in native membranes
    • Liang, Y., D. Fotiadis, S. Filipek, D. A. Saperstein, K. Palczewski, and A. Engel. 2003. Organization of the G protein-coupled receptors rhodopsin and opsin in native membranes. J. Biol. Chem. 278:21655-21662.
    • (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
  • 100
    • 21144431897 scopus 로고    scopus 로고
    • Diversifying the repertoire of G protein-coupled receptors through oligomerization
    • Park, P. S.-H., and K. Palczewski. 2005. Diversifying the repertoire of G protein-coupled receptors through oligomerization. Proc. Natl. Acad. Sci. USA. 102:8793-8794.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 8793-8794
    • Park, P.S.-H.1    Palczewski, K.2
  • 101
    • 0242581698 scopus 로고    scopus 로고
    • Is rhodopsin dimeric in native retinal rods?
    • Chabre, M., R. Cone, and H. Saibil. 2003. Is rhodopsin dimeric in native retinal rods? Nature (Lond.). 426:30-31.
    • (2003) Nature (Lond.) , vol.426 , pp. 30-31
    • Chabre, M.1    Cone, R.2    Saibil, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.