메뉴 건너뛰기




Volumn 587, Issue 13, 2013, Pages 2060-2066

A physiological role for the supramolecular organization of rhodopsin and transducin in rod photoreceptors

Author keywords

Phototransduction Transducin Rhodopsin Systems biology Precoupling Rod cell

Indexed keywords

DIMER; RHODOPSIN; TRANSDUCIN;

EID: 84878896615     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2013.05.017     Document Type: Review
Times cited : (25)

References (61)
  • 1
    • 33646178523 scopus 로고    scopus 로고
    • The vertebrate phototransduction cascade: Amplificationand termination mechanisms
    • C.K. Chen The vertebrate phototransduction cascade: amplificationand termination mechanisms Rev. Physiol. Biochem. Pharmacol. 154 2005 101 121
    • (2005) Rev. Physiol. Biochem. Pharmacol. , vol.154 , pp. 101-121
    • Chen, C.K.1
  • 2
    • 33846596863 scopus 로고    scopus 로고
    • Phototransduction, dark adaptation, and rhodopsin regeneration the proctor lecture
    • T.D. Lamb, and E.N. Pugh Jr. Phototransduction, dark adaptation, and rhodopsin regeneration the proctor lecture Invest. Ophthalmol. Vis. Sci. 47 2006 5137 5152
    • (2006) Invest. Ophthalmol. Vis. Sci. , vol.47 , pp. 5137-5152
    • Lamb, T.D.1    Pugh, Jr.E.N.2
  • 4
    • 0021415158 scopus 로고
    • A barrier to lateral diffusion of porphyropsin in Necturus rod outer segment disks
    • R.E. Drzymala, H.L. Weiner, C.A. Dearry, and P.A. Liebman A barrier to lateral diffusion of porphyropsin in Necturus rod outer segment disks Biophys. J. 45 1984 683 692
    • (1984) Biophys. J. , vol.45 , pp. 683-692
    • Drzymala, R.E.1    Weiner, H.L.2    Dearry, C.A.3    Liebman, P.A.4
  • 5
    • 0025114611 scopus 로고
    • Lateral diffusion of visual pigments in toad (Bufo marinus) rods and in catfish (Ictalurus punctatus) cones
    • B.D. Gupta, and T.P. Williams Lateral diffusion of visual pigments in toad (Bufo marinus) rods and in catfish (Ictalurus punctatus) cones J. Physiol. 430 1990 483 496
    • (1990) J. Physiol. , vol.430 , pp. 483-496
    • Gupta, B.D.1    Williams, T.P.2
  • 6
    • 0021243519 scopus 로고
    • Rhodopsin lateral diffusion as a function of rod outer segment disk membrane axial position
    • M.W. Kaplan Rhodopsin lateral diffusion as a function of rod outer segment disk membrane axial position Biophys. J. 45 1984 851 853
    • (1984) Biophys. J. , vol.45 , pp. 851-853
    • Kaplan, M.W.1
  • 7
    • 0016187426 scopus 로고
    • Lateral diffusion of visual pigment in photorecptor disk membranes
    • P.A. Liebman, and G. Entine Lateral diffusion of visual pigment in photorecptor disk membranes Science 185 1974 457 459
    • (1974) Science , vol.185 , pp. 457-459
    • Liebman, P.A.1    Entine, G.2
  • 8
    • 0020008445 scopus 로고
    • Lateral diffusion of visual pigment in rod disk membranes
    • P.A. Liebman, H.L. Weiner, and R.E. Drzymala Lateral diffusion of visual pigment in rod disk membranes Methods Enzymol. 81 1982 660 668
    • (1982) Methods Enzymol. , vol.81 , pp. 660-668
    • Liebman, P.A.1    Weiner, H.L.2    Drzymala, R.E.3
  • 9
    • 0346015887 scopus 로고
    • Lateral diffusion of rhodopsin in the visual receptor membrane
    • M. Poo, and R.A. Cone Lateral diffusion of rhodopsin in the visual receptor membrane J. Supramol. Struct. 1 1973 354
    • (1973) J. Supramol. Struct. , vol.1 , pp. 354
    • Poo, M.1    Cone, R.A.2
  • 10
    • 0016146318 scopus 로고
    • Lateral diffusion of rhodopsin in the photoreceptor membrane
    • M. Poo, and R.A. Cone Lateral diffusion of rhodopsin in the photoreceptor membrane Nature 247 1974 438 441
    • (1974) Nature , vol.247 , pp. 438-441
    • Poo, M.1    Cone, R.A.2
  • 11
    • 0015934996 scopus 로고
    • Lateral diffusion of phodopsin in Necturusrods
    • M.M. Poo, and R.A. Cone Lateral diffusion of phodopsin in Necturusrods Exp. Eye Res. 17 1973 503 510
    • (1973) Exp. Eye Res. , vol.17 , pp. 503-510
    • Poo, M.M.1    Cone, R.A.2
  • 12
    • 0019378228 scopus 로고
    • Lateral diffusion of rhodopsin in photoreceptor cells measured by fluorescence photobleaching and recovery
    • C.L. Wey, R.A. Cone, and M.A. Edidin Lateral diffusion of rhodopsin in photoreceptor cells measured by fluorescence photobleaching and recovery Biophys. J. 33 1981 225 232
    • (1981) Biophys. J. , vol.33 , pp. 225-232
    • Wey, C.L.1    Cone, R.A.2    Edidin, M.A.3
  • 13
    • 0034604451 scopus 로고    scopus 로고
    • Crystal structure of rhodopsin: A G protein-coupled receptor
    • K. Palczewski Crystal structure of rhodopsin: a G protein-coupled receptor Science 289 2000 739 745
    • (2000) Science , vol.289 , pp. 739-745
    • Palczewski, K.1
  • 14
    • 83755178196 scopus 로고    scopus 로고
    • Update 1 of: Computational modeling approaches to structure-function analysis of G protein-coupled receptors
    • F. Fanelli, and P.G. De Benedetti Update 1 of: computational modeling approaches to structure-function analysis of G protein-coupled receptors Chem. Rev. 111 2011 PR438 535
    • (2011) Chem. Rev. , vol.111 , pp. 438-535
    • Fanelli, F.1    De Benedetti, P.G.2
  • 17
    • 0038159530 scopus 로고    scopus 로고
    • Organization of the G protein-coupled receptors rhodopsin and opsin in native membranes
    • Y. Liang, D. Fotiadis, S. Filipek, D.A. Saperstein, K. Palczewski, and A. Engel 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
  • 18
    • 67650046654 scopus 로고    scopus 로고
    • Aggregation of frog rhodopsin to oligomers and their dissociation to monomer: Application of BN- and SDS-PAGE
    • S.A. Shukolyukov Aggregation of frog rhodopsin to oligomers and their dissociation to monomer: application of BN- and SDS-PAGE Biochemistry (Mosc.) 74 2009 599 604
    • (2009) Biochemistry (Mosc.) , vol.74 , pp. 599-604
    • Shukolyukov, S.A.1
  • 19
    • 11144301981 scopus 로고    scopus 로고
    • The supramolecular structure of the GPCR rhodopsin in solution and native disc membranes
    • K. Suda, S. Filipek, K. Palczewski, A. Engel, and D. Fotiadis The supramolecular structure of the GPCR rhodopsin in solution and native disc membranes Mol. Membr. Biol. 21 2004 435 446
    • (2004) Mol. Membr. Biol. , vol.21 , pp. 435-446
    • Suda, K.1    Filipek, S.2    Palczewski, K.3    Engel, A.4    Fotiadis, D.5
  • 20
    • 69949119573 scopus 로고    scopus 로고
    • Lateral diffusion of rhodopsin in photoreceptor membrane: A reappraisal
    • V.I. Govardovskii, D.A. Korenyak, S.A. Shukolyukov, and L.V. Zueva Lateral diffusion of rhodopsin in photoreceptor membrane: a reappraisal Mol. Vis. 15 2009 1717 1729
    • (2009) Mol. Vis. , vol.15 , pp. 1717-1729
    • Govardovskii, V.I.1    Korenyak, D.A.2    Shukolyukov, S.A.3    Zueva, L.V.4
  • 21
    • 0242581698 scopus 로고    scopus 로고
    • Biophysics: Is rhodopsin dimeric in native retinal rods?
    • discussion 31
    • M. Chabre, R. Cone, and H. Saibil Biophysics: is rhodopsin dimeric in native retinal rods? Nature 426 2003 30 31 discussion 31
    • (2003) Nature , vol.426 , pp. 30-31
    • Chabre, M.1    Cone, R.2    Saibil, H.3
  • 22
    • 21844441860 scopus 로고    scopus 로고
    • Monomeric G-protein-coupled receptor as a functional unit
    • M. Chabre, and M. le Maire Monomeric G-protein-coupled receptor as a functional unit Biochemistry 44 2005 9395 9403
    • (2005) Biochemistry , vol.44 , pp. 9395-9403
    • Chabre, M.1    Le Maire, M.2
  • 23
    • 62949087122 scopus 로고    scopus 로고
    • The apparent cooperativity of some GPCRs does not necessarily imply dimerization
    • M. Chabre, P. Deterre, and B. Antonny The apparent cooperativity of some GPCRs does not necessarily imply dimerization Trends Pharmacol. Sci. 30 2009 182 187
    • (2009) Trends Pharmacol. Sci. , vol.30 , pp. 182-187
    • Chabre, M.1    Deterre, P.2    Antonny, B.3
  • 24
    • 77958152523 scopus 로고    scopus 로고
    • Class A GPCR heterodimers: Evidence from binding studies
    • N.J. Birdsall Class A GPCR heterodimers: evidence from binding studies Trends Pharmacol. Sci. 31 2010 499 508
    • (2010) Trends Pharmacol. Sci. , vol.31 , pp. 499-508
    • Birdsall, N.J.1
  • 25
    • 0036780743 scopus 로고    scopus 로고
    • G-protein-coupled receptor oligomerization and its potential for drug discovery
    • S.R. George, B.F. O'Dowd, and S.P. Lee G-protein-coupled receptor oligomerization and its potential for drug discovery Nat. Rev. Drug Discov. 1 2002 808 820
    • (2002) Nat. Rev. Drug Discov. , vol.1 , pp. 808-820
    • George, S.R.1    O'Dowd, B.F.2    Lee, S.P.3
  • 26
    • 25444444202 scopus 로고    scopus 로고
    • Computational modeling approaches to structure-function analysis of G protein-coupled receptors
    • F. Fanelli, and P.G. De Benedetti Computational modeling approaches to structure-function analysis of G protein-coupled receptors Chem. Rev. 105 2005 3297 3351
    • (2005) Chem. Rev. , vol.105 , pp. 3297-3351
    • Fanelli, F.1    De Benedetti, P.G.2
  • 27
    • 0031581813 scopus 로고    scopus 로고
    • Mechanistic model of G-protein signal transduction. Determinants of efficacy and effect of precoupled receptors
    • L. Shea, and J.J. Linderman Mechanistic model of G-protein signal transduction. Determinants of efficacy and effect of precoupled receptors Biochem. Pharmacol. 53 1997 519 530
    • (1997) Biochem. Pharmacol. , vol.53 , pp. 519-530
    • Shea, L.1    Linderman, J.J.2
  • 28
    • 29444446964 scopus 로고    scopus 로고
    • Heterotrimeric G proteins precouple with G protein-coupled receptors in living cells
    • M. Nobles, A. Benians, and A. Tinker Heterotrimeric G proteins precouple with G protein-coupled receptors in living cells Proc. Natl. Acad. Sci. USA 102 2005 18706 18711
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 18706-18711
    • Nobles, M.1    Benians, A.2    Tinker, A.3
  • 30
    • 0023645290 scopus 로고
    • Mechanism of action of monoclonal antibodies that block the light activation of the guanyl nucleotide-binding protein, transducin
    • H.E. Hamm, D. Deretic, K.P. Hofmann, A. Schleicher, and B. Kohl Mechanism of action of monoclonal antibodies that block the light activation of the guanyl nucleotide-binding protein, transducin J. Biol. Chem. 262 1987 10831 10838
    • (1987) J. Biol. Chem. , vol.262 , pp. 10831-10838
    • Hamm, H.E.1    Deretic, D.2    Hofmann, K.P.3    Schleicher, A.4    Kohl, B.5
  • 31
    • 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
    • I.D. Alves, G.F. Salgado, Z. Salamon, M.F. Brown, G. Tollin, and V.J. Hruby Phosphatidylethanolamine enhances rhodopsin photoactivation and transducin binding in a solid supported lipid bilayer as determined using plasmon-waveguide resonance spectroscopy Biophys. J. 88 2005 198 210
    • (2005) Biophys. J. , vol.88 , pp. 198-210
    • Alves, I.D.1    Salgado, G.F.2    Salamon, Z.3    Brown, M.F.4    Tollin, G.5    Hruby, V.J.6
  • 32
    • 0029922635 scopus 로고    scopus 로고
    • Surface plasmon resonance spectroscopy studies of membrane proteins: Transducin binding and activation by rhodopsin monitored in thin membrane films
    • Z. Salamon, Y. Wang, J.L. Soulages, M.F. Brown, and G. Tollin Surface plasmon resonance spectroscopy studies of membrane proteins: transducin binding and activation by rhodopsin monitored in thin membrane films Biophys. J. 71 1996 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
  • 33
    • 33847098734 scopus 로고    scopus 로고
    • Monomeric dark rhodopsin holds the molecular determinants for transducin recognition: Insights from computational analysis
    • D. Dell'Orco, M. Seeber, and F. Fanelli Monomeric dark rhodopsin holds the molecular determinants for transducin recognition: insights from computational analysis FEBS Lett. 581 2007 944 948
    • (2007) FEBS Lett. , vol.581 , pp. 944-948
    • Dell'Orco, D.1    Seeber, M.2    Fanelli, F.3
  • 34
    • 27744531868 scopus 로고    scopus 로고
    • Rhodopsin activation follows precoupling with transducin: Inferences from computational analysis
    • F. Fanelli, and D. Dell'Orco Rhodopsin activation follows precoupling with transducin: inferences from computational analysis Biochemistry 44 2005 14695 14700
    • (2005) Biochemistry , vol.44 , pp. 14695-14700
    • Fanelli, F.1    Dell'Orco, D.2
  • 35
    • 40349088696 scopus 로고    scopus 로고
    • Dark and photoactivated rhodopsin share common binding modes to transducin
    • F. Fanelli, and D. Dell'Orco Dark and photoactivated rhodopsin share common binding modes to transducin FEBS Lett. 582 2008 991 996
    • (2008) FEBS Lett. , vol.582 , pp. 991-996
    • Fanelli, F.1    Dell'Orco, D.2
  • 36
    • 77950857819 scopus 로고    scopus 로고
    • The membrane complex between transducin and dark-state rhodopsin exhibits large-amplitude interface dynamics on the sub-microsecond timescale: Insights from all-atom MD simulations
    • N.G. Sgourakis, and A.E. Garcia The membrane complex between transducin and dark-state rhodopsin exhibits large-amplitude interface dynamics on the sub-microsecond timescale: insights from all-atom MD simulations J. Mol. Biol. 398 2010 161 173
    • (2010) J. Mol. Biol. , vol.398 , pp. 161-173
    • Sgourakis, N.G.1    Garcia, A.E.2
  • 37
    • 80455132755 scopus 로고    scopus 로고
    • A dynamic scaffolding mechanism for rhodopsin and transducin interaction in vertebrate vision
    • D. Dell'Orco, and K.W. Koch A dynamic scaffolding mechanism for rhodopsin and transducin interaction in vertebrate vision Biochem. J. 440 2011 263 271
    • (2011) Biochem. J. , vol.440 , pp. 263-271
    • Dell'Orco, D.1    Koch, K.W.2
  • 38
    • 77955985486 scopus 로고    scopus 로고
    • On-chip photoactivation of heterologously expressed rhodopsin allows kinetic analysis of G-protein signaling by surface plasmon resonance spectroscopy
    • K.E. Komolov, M. Aguila, D. Toledo, J. Manyosa, P. Garriga, and K.W. Koch On-chip photoactivation of heterologously expressed rhodopsin allows kinetic analysis of G-protein signaling by surface plasmon resonance spectroscopy Anal. Bioanal. Chem. 397 2010 2967 2976
    • (2010) Anal. Bioanal. Chem. , vol.397 , pp. 2967-2976
    • Komolov, K.E.1    Aguila, M.2    Toledo, D.3    Manyosa, J.4    Garriga, P.5    Koch, K.W.6
  • 39
    • 77953245135 scopus 로고    scopus 로고
    • Application of surface plasmon resonance spectroscopy to study G-protein coupled receptor signalling
    • K.E. Komolov, and K.W. Koch Application of surface plasmon resonance spectroscopy to study G-protein coupled receptor signalling Methods Mol. Biol. 627 2010 249 260
    • (2010) Methods Mol. Biol. , vol.627 , pp. 249-260
    • Komolov, K.E.1    Koch, K.W.2
  • 40
    • 33144482517 scopus 로고    scopus 로고
    • Surface plasmon resonance study of g protein/receptor coupling in a lipid bilayer-free system
    • K.E. Komolov, I.I. Senin, P.P. Philippov, and K.W. Koch Surface plasmon resonance study of g protein/receptor coupling in a lipid bilayer-free system Anal. Chem. 78 2006 1228 1234
    • (2006) Anal. Chem. , vol.78 , pp. 1228-1234
    • Komolov, K.E.1    Senin, I.I.2    Philippov, P.P.3    Koch, K.W.4
  • 41
    • 0023141386 scopus 로고
    • Kinetic study on the equilibrium between membrane-bound and free photoreceptor G-protein
    • A. Schleicher, and K.P. Hofmann Kinetic study on the equilibrium between membrane-bound and free photoreceptor G-protein J. Membr. Biol. 95 1987 271 281
    • (1987) J. Membr. Biol. , vol.95 , pp. 271-281
    • Schleicher, A.1    Hofmann, K.P.2
  • 42
    • 70349339354 scopus 로고    scopus 로고
    • Network-level analysis of light adaptation in rod cells under normal and altered conditions
    • D. Dell'Orco, H. Schmidt, S. Mariani, and F. Fanelli Network-level analysis of light adaptation in rod cells under normal and altered conditions Mol. Biosyst. 5 2009 1232 1246
    • (2009) Mol. Biosyst. , vol.5 , pp. 1232-1246
    • Dell'Orco, D.1    Schmidt, H.2    Mariani, S.3    Fanelli, F.4
  • 44
    • 0032558776 scopus 로고    scopus 로고
    • Assembly of the Drosophila phototransduction cascade into a signalling complex shapes elementary responses
    • K. Scott, and C.S. Zuker Assembly of the Drosophila phototransduction cascade into a signalling complex shapes elementary responses Nature 395 1998 805 808
    • (1998) Nature , vol.395 , pp. 805-808
    • Scott, K.1    Zuker, C.S.2
  • 45
    • 84871720383 scopus 로고    scopus 로고
    • Detecting single photons: A supramolecular matter?
    • L. Cangiano, and D. Dell'Orco Detecting single photons: a supramolecular matter? FEBS Lett. 587 2013 1 4
    • (2013) FEBS Lett. , vol.587 , pp. 1-4
    • Cangiano, L.1    Dell'Orco, D.2
  • 46
    • 0022514971 scopus 로고
    • Rotational diffusion of rhodopsin in the visual receptor membrane: Effects of temperature and bleaching
    • M. Coke, C.J. Restall, CM. Kemp, and D. Chapman Rotational diffusion of rhodopsin in the visual receptor membrane: effects of temperature and bleaching Biochemistry 25 1986 513 518
    • (1986) Biochemistry , vol.25 , pp. 513-518
    • Coke, M.1    Restall, C.J.2    Kemp, C.M.3    Chapman, D.4
  • 47
    • 0025976856 scopus 로고
    • Reaction rate and collisional efficiency of the rhodopsin-transducin system in intact retinal rods
    • M. Kahlert, and K.P. Hofmann Reaction rate and collisional efficiency of the rhodopsin-transducin system in intact retinal rods Biophys. J. 59 1991 375 386
    • (1991) Biophys. J. , vol.59 , pp. 375-386
    • Kahlert, M.1    Hofmann, K.P.2
  • 48
    • 0021287057 scopus 로고
    • Effects of temperature changes on toad rod photocurrents
    • T.D. Lamb Effects of temperature changes on toad rod photocurrents J. Physiol. 346 1984 557 578
    • (1984) J. Physiol. , vol.346 , pp. 557-578
    • Lamb, T.D.1
  • 49
    • 25844514195 scopus 로고    scopus 로고
    • Light responses and light adaptation in rat retinal rods at different temperatures
    • S. Nymark, H. Heikkinen, C. Haldin, K. Donner, and A. Koskelainen Light responses and light adaptation in rat retinal rods at different temperatures J. Physiol. 567 2005 923 938
    • (2005) J. Physiol. , vol.567 , pp. 923-938
    • Nymark, S.1    Heikkinen, H.2    Haldin, C.3    Donner, K.4    Koskelainen, A.5
  • 51
    • 84865620375 scopus 로고    scopus 로고
    • The photovoltage of rods and cones in the dark-adapted mouse retina
    • L. Cangiano, S. Asteriti, L. Cervetto, and C. Gargini The photovoltage of rods and cones in the dark-adapted mouse retina J. Physiol. 590 2012 3841 3855
    • (2012) J. Physiol. , vol.590 , pp. 3841-3855
    • Cangiano, L.1    Asteriti, S.2    Cervetto, L.3    Gargini, C.4
  • 53
    • 0037187644 scopus 로고    scopus 로고
    • Massive light-driven translocation of transducin between the two major compartments of rod cells: A novel mechanism of light adaptation
    • M. Sokolov, A.L. Lyubarsky, K.J. Strissel, A.B. Savchenko, V.I. Govardovskii, E.N. Pugh Jr., and V.Y. Arshavsky Massive light-driven translocation of transducin between the two major compartments of rod cells: a novel mechanism of light adaptation Neuron 34 2002 95 106
    • (2002) Neuron , vol.34 , pp. 95-106
    • Sokolov, M.1    Lyubarsky, A.L.2    Strissel, K.J.3    Savchenko, A.B.4    Govardovskii, V.I.5    Pugh, Jr.E.N.6    Arshavsky, V.Y.7
  • 54
    • 0017770143 scopus 로고
    • Temperature and wavelength effects on the photochemistry of rhodopsin, isorhodopsin, bacteriorhodopsin and their photoproducts
    • J.B. Hurley, T.G. Ebrey, B. Honig, and M. Ottolenghi Temperature and wavelength effects on the photochemistry of rhodopsin, isorhodopsin, bacteriorhodopsin and their photoproducts Nature 270 1977 540 542
    • (1977) Nature , vol.270 , pp. 540-542
    • Hurley, J.B.1    Ebrey, T.G.2    Honig, B.3    Ottolenghi, M.4
  • 55
    • 0033680726 scopus 로고    scopus 로고
    • The gain of rod phototransduction: Reconciliation of biochemical and electrophysiological measurements
    • I.B. Leskov The gain of rod phototransduction: reconciliation of biochemical and electrophysiological measurements Neuron 27 2000 525 537
    • (2000) Neuron , vol.27 , pp. 525-537
    • Leskov, I.B.1
  • 56
    • 33746898592 scopus 로고    scopus 로고
    • RGS expression rate-limits recovery of rod photoresponses
    • CM. Krispel RGS expression rate-limits recovery of rod photoresponses Neuron 51 2006 409 416
    • (2006) Neuron , vol.51 , pp. 409-416
    • Krispel, C.M.1
  • 57
    • 77749324809 scopus 로고    scopus 로고
    • Control of rhodopsin's active lifetime by arrestin-1 expression in mammalian rods
    • O.P. Gross, and M.E. Burns Control of rhodopsin's active lifetime by arrestin-1 expression in mammalian rods J. Neurosci. 30 2010 3450 3457
    • (2010) J. Neurosci. , vol.30 , pp. 3450-3457
    • Gross, O.P.1    Burns, M.E.2
  • 58
    • 84863535732 scopus 로고    scopus 로고
    • Structural determinants of the supramolecular organization of G protein-coupled receptors in bilayers
    • X. Periole, A.M. Knepp, T.P. Sakmar, S.J. Marrink, and T. Huber Structural determinants of the supramolecular organization of G protein-coupled receptors in bilayers J. Am. Chem. Soc. 134 2012 10959 10965
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 10959-10965
    • Periole, X.1    Knepp, A.M.2    Sakmar, T.P.3    Marrink, S.J.4    Huber, T.5
  • 59
    • 57649223688 scopus 로고    scopus 로고
    • Activation-dependent hindrance of photoreceptor G protein diffusion by lipid microdomains
    • Q. Wang, X. Zhang, L. Zhang, F. He, G. Zhang, M. Jamrich, and T.G. Wensel Activation-dependent hindrance of photoreceptor G protein diffusion by lipid microdomains J. Biol. Chem. 283 2008 30015 30024
    • (2008) J. Biol. Chem. , vol.283 , pp. 30015-30024
    • Wang, Q.1    Zhang, X.2    Zhang, L.3    He, F.4    Zhang, G.5    Jamrich, M.6    Wensel, T.G.7
  • 61
    • 46449137096 scopus 로고    scopus 로고
    • Mesoscopic Monte Carlo simulations of stochastic encounters between photoactivated rhodopsin and transducin in disc membranes
    • D. Dell'Orco, and H. Schmidt Mesoscopic Monte Carlo simulations of stochastic encounters between photoactivated rhodopsin and transducin in disc membranes J. Phys. Chem. B 112 2008 4419 4426
    • (2008) J. Phys. Chem. B , vol.112 , pp. 4419-4426
    • Dell'Orco, D.1    Schmidt, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.