메뉴 건너뛰기




Volumn 107, Issue 5, 2014, Pages 1042-1053

Explicit spatiotemporal simulation of receptor-G protein coupling in rod cell disk membranes

Author keywords

[No Author keywords available]

Indexed keywords

RHODOPSIN; TRANSDUCIN;

EID: 84908157267     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2014.05.050     Document Type: Article
Times cited : (42)

References (89)
  • 1
    • 84889564886 scopus 로고    scopus 로고
    • Activation and allosteric modulation of a muscarinic acetylcholine receptor
    • A.C. Kruse, and A.M. Ring B.K. Kobilka Activation and allosteric modulation of a muscarinic acetylcholine receptor Nature 504 2013 101 106
    • (2013) Nature , vol.504 , pp. 101-106
    • Kruse, A.C.1    Ring, A.M.2    Kobilka, B.K.3
  • 2
    • 70350362562 scopus 로고    scopus 로고
    • A G protein-coupled receptor at work: The rhodopsin model
    • K.P. Hofmann, and P. Scheerer O.P. Ernst A G protein-coupled receptor at work: the rhodopsin model Trends Biochem. Sci. 34 2009 540 552
    • (2009) Trends Biochem. Sci. , vol.34 , pp. 540-552
    • Hofmann, K.P.1    Scheerer, P.2    Ernst, O.P.3
  • 3
    • 84883072253 scopus 로고    scopus 로고
    • Precision vs. Flexibility in GPCR signaling
    • M. Elgeti, and A.S. Rose M. Heck Precision vs. flexibility in GPCR signaling J. Am. Chem. Soc. 135 2013 12305 12312
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 12305-12312
    • Elgeti, M.1    Rose, A.S.2    Heck, M.3
  • 4
    • 33747802375 scopus 로고    scopus 로고
    • Building functional modules from molecular interactions
    • K.P. Hofmann, and C.M. Spahn U. Heinemann Building functional modules from molecular interactions Trends Biochem. Sci. 31 2006 497 508
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 497-508
    • Hofmann, K.P.1    Spahn, C.M.2    Heinemann, U.3
  • 5
    • 0016231987 scopus 로고
    • The electrical response of turtle cones to flashes and steps of light
    • D.A. Baylor, A.L. Hodgkin, and T.D. Lamb The electrical response of turtle cones to flashes and steps of light J. Physiol. 242 1974 685 727
    • (1974) J. Physiol. , vol.242 , pp. 685-727
    • Baylor, D.A.1    Hodgkin, A.L.2    Lamb, T.D.3
  • 6
    • 0030034961 scopus 로고    scopus 로고
    • Gain and kinetics of activation in the G-protein cascade of phototransduction
    • T.D. Lamb Gain and kinetics of activation in the G-protein cascade of phototransduction Proc. Natl. Acad. Sci. USA 93 1996 566 570
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 566-570
    • Lamb, T.D.1
  • 7
    • 32544449658 scopus 로고    scopus 로고
    • Toward a unified model of vertebrate rod phototransduction
    • R. Hamer, S. Nicholas, and D. Tranchina J. Jarvinen Toward a unified model of vertebrate rod phototransduction Vis. Neurosci. 22 2005 417 436
    • (2005) Vis. Neurosci. , vol.22 , pp. 417-436
    • Hamer, R.1    Nicholas, S.2    Tranchina, D.3    Jarvinen, J.4
  • 8
    • 84900321553 scopus 로고    scopus 로고
    • A comprehensive model of the phototransduction cascade in mouse rod cells
    • B.M. Invergo, and D. Dell'Orco J. Bertranpetit A comprehensive model of the phototransduction cascade in mouse rod cells Mol. Biosyst. 10 2014 1481 1489
    • (2014) Mol. Biosyst. , vol.10 , pp. 1481-1489
    • Invergo, B.M.1    Dell'Orco, D.2    Bertranpetit, J.3
  • 9
    • 0028085969 scopus 로고
    • Stochastic simulation of activation in the G-protein cascade of phototransduction
    • T.D. Lamb Stochastic simulation of activation in the G-protein cascade of phototransduction Biophys. J. 67 1994 1439 1454
    • (1994) Biophys. J. , vol.67 , pp. 1439-1454
    • Lamb, T.D.1
  • 10
    • 0029731740 scopus 로고    scopus 로고
    • Stochastic simulation of the transducin GTPase cycle
    • S. Felber, and H.P. Breuer K.P. Hofmann Stochastic simulation of the transducin GTPase cycle Biophys. J. 71 1996 3051 3063
    • (1996) Biophys. J. , vol.71 , pp. 3051-3063
    • Felber, S.1    Breuer, H.P.2    Hofmann, K.P.3
  • 11
    • 0042322531 scopus 로고    scopus 로고
    • Mathematical model of the spatio-temporal dynamics of second messengers in visual transduction
    • D. Andreucci, and P. Bisegna E. DiBenedetto Mathematical model of the spatio-temporal dynamics of second messengers in visual transduction Biophys. J. 85 2003 1358 1376
    • (2003) Biophys. J. , vol.85 , pp. 1358-1376
    • Andreucci, D.1    Bisegna, P.2    Dibenedetto, E.3
  • 12
    • 27244449903 scopus 로고    scopus 로고
    • Mathematical and computational modelling of spatio-temporal signalling in rod phototransduction
    • G. Caruso, and H. Khanal E. DiBenedetto et al. Mathematical and computational modelling of spatio-temporal signalling in rod phototransduction Syst. Biol. 152 2005 119 137
    • (2005) Syst. Biol. , vol.152 , pp. 119-137
    • Caruso, G.1    Khanal, H.2    Dibenedetto, E.3
  • 13
    • 33746790751 scopus 로고    scopus 로고
    • Modeling the role of incisures in vertebrate phototransduction
    • G. Caruso, and P. Bisegna E. DiBenedetto Modeling the role of incisures in vertebrate phototransduction Biophys. J. 91 2006 1192 1212
    • (2006) Biophys. J. , vol.91 , pp. 1192-1212
    • Caruso, G.1    Bisegna, P.2    Dibenedetto, E.3
  • 14
    • 67649390956 scopus 로고    scopus 로고
    • An asymptotic analysis of intracellular signaling gradients arising from multiple small compartments
    • R. Straube, and M.J. Ward An asymptotic analysis of intracellular signaling gradients arising from multiple small compartments SIAM J. Appl. Math. 70 2009 248 269
    • (2009) SIAM J. Appl. Math. , vol.70 , pp. 248-269
    • Straube, R.1    Ward, M.J.2
  • 15
    • 72049111861 scopus 로고    scopus 로고
    • Diffusion on a sphere with localized traps: Mean first passage time, eigenvalue asymptotics, and Fekete points
    • D. Coombs, R. Straube, and M. Ward Diffusion on a sphere with localized traps: mean first passage time, eigenvalue asymptotics, and Fekete points SIAM J. Appl. Math. 70 2009 302 332
    • (2009) SIAM J. Appl. Math. , vol.70 , pp. 302-332
    • Coombs, D.1    Straube, R.2    Ward, M.3
  • 16
    • 77951907993 scopus 로고    scopus 로고
    • An asymptotic analysis of the mean first passage time for narrow escape problems: Part I: Two-dimensional domains
    • S. Pillay, and M.J. Ward T. Kolokolnikov An asymptotic analysis of the mean first passage time for narrow escape problems: Part I: Two-dimensional domains Multiscale Model. Simul. 8 2009 803 835
    • (2009) Multiscale Model. Simul. , vol.8 , pp. 803-835
    • Pillay, S.1    Ward, M.J.2    Kolokolnikov, T.3
  • 17
    • 77951899892 scopus 로고    scopus 로고
    • An asymptotic analysis of the mean first passage time for narrow escape problems: Part II: The sphere
    • A.F. Cheviakov, M.J. Ward, and R. Straube An asymptotic analysis of the mean first passage time for narrow escape problems: Part II: The sphere Multiscale Model. Simul. 8 2009 836 870
    • (2009) Multiscale Model. Simul. , vol.8 , pp. 836-870
    • Cheviakov, A.F.1    Ward, M.J.2    Straube, R.3
  • 18
    • 79955122406 scopus 로고    scopus 로고
    • Rhodopsin is spatially heterogeneously distributed in rod outer segment disk membranes
    • N. Buzhynskyy, C. Salesse, and S. Scheuring Rhodopsin is spatially heterogeneously distributed in rod outer segment disk membranes J. Mol. Recognit. 24 2011 483 489
    • (2011) J. Mol. Recognit. , vol.24 , pp. 483-489
    • Buzhynskyy, N.1    Salesse, C.2    Scheuring, S.3
  • 19
    • 69949119573 scopus 로고    scopus 로고
    • Lateral diffusion of rhodopsin in photoreceptor membrane: A reappraisal
    • V.I. Govardovskii, and D.A. Korenyak 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    Zueva, L.V.3
  • 20
    • 0037426865 scopus 로고    scopus 로고
    • Atomic-force microscopy: Rhodopsin dimers in native disc membranes
    • D. Fotiadis, and Y. Liang K. Palczewski Atomic-force microscopy: rhodopsin dimers in native disc membranes Nature 421 2003 127 128
    • (2003) Nature , vol.421 , pp. 127-128
    • Fotiadis, D.1    Liang, Y.2    Palczewski, K.3
  • 21
    • 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
  • 22
    • 77956394404 scopus 로고    scopus 로고
    • Cellular dynamic simulator: An event driven molecular simulation environment for cellular physiology
    • M.J. Byrne, M.N. Waxham, and Y. Kubota Cellular dynamic simulator: an event driven molecular simulation environment for cellular physiology Neuroinformatics 8 2010 63 82
    • (2010) Neuroinformatics , vol.8 , pp. 63-82
    • Byrne, M.J.1    Waxham, M.N.2    Kubota, Y.3
  • 23
    • 33751377585 scopus 로고    scopus 로고
    • Cell++ - Simulating biochemical pathways
    • C. Sanford, and M.L. Yip J. Parkinson Cell++ - simulating biochemical pathways Bioinformatics 22 2006 2918 2925
    • (2006) Bioinformatics , vol.22 , pp. 2918-2925
    • Sanford, C.1    Yip, M.L.2    Parkinson, J.3
  • 24
    • 77249093066 scopus 로고    scopus 로고
    • Spatio-temporal correlations can drastically change the response of a MAPK pathway
    • K. Takahashi, S. Tanase-Nicola, and P.R. ten Wolde Spatio-temporal correlations can drastically change the response of a MAPK pathway Proc. Natl. Acad. Sci. USA 107 2010 2473 2478
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 2473-2478
    • Takahashi, K.1    Tanase-Nicola, S.2    Ten Wolde, P.R.3
  • 25
    • 29244454300 scopus 로고    scopus 로고
    • Green's-function reaction dynamics: A particle-based approach for simulating biochemical networks in time and space
    • J.S. van Zon, and P.R. ten Wolde Green's-function reaction dynamics: a particle-based approach for simulating biochemical networks in time and space J. Chem. Phys. 123 2005 234910
    • (2005) J. Chem. Phys. , vol.123 , pp. 234910
    • Van Zon, J.S.1    Ten Wolde, P.R.2
  • 26
    • 18244404300 scopus 로고    scopus 로고
    • Simulating biochemical networks at the particle level and in time and space: Green's function reaction dynamics
    • J.S.J. van Zon, and P.R.P. ten Wolde Simulating biochemical networks at the particle level and in time and space: Green's function reaction dynamics Phys. Rev. Lett. 94 2005 128103
    • (2005) Phys. Rev. Lett. , vol.94 , pp. 128103
    • Van Zon, J.S.J.1    Ten Wolde, P.R.P.2
  • 27
    • 77955396527 scopus 로고    scopus 로고
    • A metabolic model of human erythrocytes: Practical application of the E-Cell Simulation Environment
    • A. Yachie-Kinoshita, and T. Nishino M. Tomita A metabolic model of human erythrocytes: practical application of the E-Cell Simulation Environment J. Biomed. Biotechnol. 2010 2010 642420
    • (2010) J. Biomed. Biotechnol. , vol.2010 , pp. 642420
    • Yachie-Kinoshita, A.1    Nishino, T.2    Tomita, M.3
  • 28
    • 79955815642 scopus 로고    scopus 로고
    • Agent-based simulation of reactions in the crowded and structured intracellular environment: Influence of mobility and location of the reactants
    • M.T. Klann, A. Lapin, and M. Reuss Agent-based simulation of reactions in the crowded and structured intracellular environment: influence of mobility and location of the reactants BMC Syst. Biol. 5 2011 71
    • (2011) BMC Syst. Biol. , vol.5 , pp. 71
    • Klann, M.T.1    Lapin, A.2    Reuss, M.3
  • 29
    • 84855773380 scopus 로고    scopus 로고
    • Spatial modeling of vesicle transport and the cytoskeleton: The challenge of hitting the right road
    • M. Klann, H. Koeppl, and M. Reuss Spatial modeling of vesicle transport and the cytoskeleton: the challenge of hitting the right road PLoS ONE 7 2012 e29645
    • (2012) PLoS ONE , vol.7 , pp. 29645
    • Klann, M.1    Koeppl, H.2    Reuss, M.3
  • 30
    • 0029904436 scopus 로고    scopus 로고
    • Miniature endplate current rise times less than 100 microseconds from improved dual recordings can be modeled with passive acetylcholine diffusion from a synaptic vesicle
    • J.R. Stiles, and D. Van Helden M.M. Salpeter Miniature endplate current rise times less than 100 microseconds from improved dual recordings can be modeled with passive acetylcholine diffusion from a synaptic vesicle Proc. Natl. Acad. Sci. USA 93 1996 5747 5752
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5747-5752
    • Stiles, J.R.1    Van Helden, D.2    Salpeter, M.M.3
  • 31
    • 55149086309 scopus 로고    scopus 로고
    • Fast Monte Carlo simulation methods for biological reaction-diffusion systems in solution and on surfaces
    • R.A. Kerr, and T.M. Bartol J.R. Stiles Fast Monte Carlo simulation methods for biological reaction-diffusion systems in solution and on surfaces SIAM J. Sci. Comput. 30 2008 3126
    • (2008) SIAM J. Sci. Comput. , vol.30 , pp. 3126
    • Kerr, R.A.1    Bartol, T.M.2    Stiles, J.R.3
  • 32
    • 43849103490 scopus 로고    scopus 로고
    • Coarse-grained molecular simulation of diffusion and reaction kinetics in a crowded virtual cytoplasm
    • D. Ridgway, and G. Broderick M.J. Ellison Coarse-grained molecular simulation of diffusion and reaction kinetics in a crowded virtual cytoplasm Biophys. J. 94 2008 3748 3759
    • (2008) Biophys. J. , vol.94 , pp. 3748-3759
    • Ridgway, D.1    Broderick, G.2    Ellison, M.J.3
  • 33
    • 33748520215 scopus 로고    scopus 로고
    • Stochastic simulation of chemical reactions with spatial resolution and single molecule detail
    • S.S. Andrews, and D. Bray Stochastic simulation of chemical reactions with spatial resolution and single molecule detail Phys. Biol. 1 2004 137 151
    • (2004) Phys. Biol. , vol.1 , pp. 137-151
    • Andrews, S.S.1    Bray, D.2
  • 34
    • 77950833499 scopus 로고    scopus 로고
    • Detailed simulations of cell biology with smoldyn 2.1
    • S. Andrews, N. Addy, and R. Brent Detailed simulations of cell biology with smoldyn 2.1 PLoS Computational Biol. 6 2010 e1000705
    • (2010) PLoS Computational Biol. , vol.6 , pp. 1000705
    • Andrews, S.1    Addy, N.2    Brent, R.3
  • 35
    • 77953064219 scopus 로고    scopus 로고
    • Rule-based spatial modeling with diffusing, geometrically constrained molecules
    • G. Gruenert, and B. Ibrahim P. Dittrich Rule-based spatial modeling with diffusing, geometrically constrained molecules BMC Bioinformatics 11 2010 307
    • (2010) BMC Bioinformatics , vol.11 , pp. 307
    • Gruenert, G.1    Ibrahim, B.2    Dittrich, P.3
  • 36
    • 84901730756 scopus 로고    scopus 로고
    • ReaDDy - A software for particle-based reaction-diffusion dynamics in crowded cellular environments
    • J. Schöneberg, and F. Noé ReaDDy - a software for particle-based reaction-diffusion dynamics in crowded cellular environments PLoS ONE 8 2013 e74261
    • (2013) PLoS ONE , vol.8 , pp. 74261
    • Schöneberg, J.1    Noé, F.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
    • 0035971240 scopus 로고    scopus 로고
    • Maximal rate and nucleotide dependence of rhodopsin-catalyzed transducin activation: Initial rate analysis based on a double displacement mechanism
    • M. Heck, and K.P. Hofmann Maximal rate and nucleotide dependence of rhodopsin-catalyzed transducin activation: initial rate analysis based on a double displacement mechanism J. Biol. Chem. 276 2001 10000 10009
    • (2001) J. Biol. Chem. , vol.276 , pp. 10000-10009
    • Heck, M.1    Hofmann, K.P.2
  • 39
    • 4344581120 scopus 로고    scopus 로고
    • The retinal conformation and its environment in rhodopsin in light of a new 2.2 Å crystal structure
    • T. Okada, and M. Sugihara V. Buss The retinal conformation and its environment in rhodopsin in light of a new 2.2 Å crystal structure J. Mol. Biol. 342 2004 571 583
    • (2004) J. Mol. Biol. , vol.342 , pp. 571-583
    • Okada, T.1    Sugihara, M.2    Buss, V.3
  • 40
    • 79953234218 scopus 로고    scopus 로고
    • Crystal structure of metarhodopsin II
    • H.-W. Choe, and Y.J. Kim O.P. Ernst Crystal structure of metarhodopsin II Nature 471 2011 651 655
    • (2011) Nature , vol.471 , pp. 651-655
    • Choe, H.-W.1    Kim, Y.J.2    Ernst, O.P.3
  • 41
    • 0029664589 scopus 로고    scopus 로고
    • The 2.0 Å crystal structure of a heterotrimeric G protein
    • D.G. Lambright, and J. Sondek P.B. Sigler The 2.0 Å crystal structure of a heterotrimeric G protein Nature 379 1996 311 319
    • (1996) Nature , vol.379 , pp. 311-319
    • Lambright, D.G.1    Sondek, J.2    Sigler, P.B.3
  • 42
    • 80051658642 scopus 로고    scopus 로고
    • Crystal structure of the β2 adrenergic receptor-Gs protein complex
    • S.G.F. Rasmussen, and B.T. DeVree B.K. Kobilka Crystal structure of the β2 adrenergic receptor-Gs protein complex Nature 477 2011 549 555
    • (2011) Nature , vol.477 , pp. 549-555
    • Rasmussen, S.G.F.1    Devree, B.T.2    Kobilka, B.K.3
  • 43
    • 0023492928 scopus 로고
    • Lateral diffusion in an archipelago. The effect of mobile obstacles
    • M.J. Saxton Lateral diffusion in an archipelago. The effect of mobile obstacles Biophys. J. 52 1987 989 997
    • (1987) Biophys. J. , vol.52 , pp. 989-997
    • Saxton, M.J.1
  • 44
    • 0024723988 scopus 로고
    • Lateral diffusion in an archipelago. Distance dependence of the diffusion coefficient
    • M.J. Saxton Lateral diffusion in an archipelago. Distance dependence of the diffusion coefficient Biophys. J. 56 1989 615 622
    • (1989) Biophys. J. , vol.56 , pp. 615-622
    • Saxton, M.J.1
  • 45
    • 0025084901 scopus 로고
    • Lateral diffusion in a mixture of mobile and immobile particles. A Monte Carlo study
    • M.J. Saxton Lateral diffusion in a mixture of mobile and immobile particles. A Monte Carlo study Biophys. J. 58 1990 1303 1306
    • (1990) Biophys. J. , vol.58 , pp. 1303-1306
    • Saxton, M.J.1
  • 46
    • 0027163092 scopus 로고
    • Lateral diffusion in an archipelago. Dependence on tracer size
    • M.J. Saxton Lateral diffusion in an archipelago. Dependence on tracer size Biophys. J. 64 1993 1053 1062
    • (1993) Biophys. J. , vol.64 , pp. 1053-1062
    • Saxton, M.J.1
  • 47
    • 0036828936 scopus 로고    scopus 로고
    • Space-and time-fractional diffusion and wave equations, fractional Fokker-Planck equations, and physical motivation
    • R. Metzler, and T.F. Nonnenmacher Space-and time-fractional diffusion and wave equations, fractional Fokker-Planck equations, and physical motivation Chem. Phys. 284 2002 67 90
    • (2002) Chem. Phys. , vol.284 , pp. 67-90
    • Metzler, R.1    Nonnenmacher, T.F.2
  • 48
    • 33846844797 scopus 로고    scopus 로고
    • A biological interpretation of transient anomalous subdiffusion. I. Qualitative model
    • M.J. Saxton A biological interpretation of transient anomalous subdiffusion. I. Qualitative model Biophys. J. 92 2007 1178 1191
    • (2007) Biophys. J. , vol.92 , pp. 1178-1191
    • Saxton, M.J.1
  • 49
    • 0027407602 scopus 로고
    • Amplification and kinetics of the activation steps in phototransduction
    • E.N. Pugh Jr., and T.D. Lamb Amplification and kinetics of the activation steps in phototransduction Biochim. Biophys. Acta 1141 1993 111 149
    • (1993) Biochim. Biophys. Acta , vol.1141 , pp. 111-149
    • Pugh, Jr.E.N.1    Lamb, T.D.2
  • 50
    • 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
  • 51
    • 0019842511 scopus 로고
    • Lateral diffusion of photopigments in photoreceptor disk membrane vesicles by the dynamic Kerr effect
    • H. Takezoe, and H. Yu Lateral diffusion of photopigments in photoreceptor disk membrane vesicles by the dynamic Kerr effect Biochemistry 20 1981 5275 5281
    • (1981) Biochemistry , vol.20 , pp. 5275-5281
    • Takezoe, H.1    Yu, H.2
  • 52
    • 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
  • 53
    • 57649223688 scopus 로고    scopus 로고
    • Activation-dependent hindrance of photoreceptor G protein diffusion by lipid microdomains
    • Q. Wang, and X. Zhang 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    Wensel, T.G.3
  • 54
    • 84866315927 scopus 로고    scopus 로고
    • Impact of signaling microcompartment geometry on GPCR dynamics in live retinal photoreceptors
    • M. Najafi, and M. Haeri P. Calvert Impact of signaling microcompartment geometry on GPCR dynamics in live retinal photoreceptors J. Gen. Physiol. 140 2012 249 266
    • (2012) J. Gen. Physiol. , vol.140 , pp. 249-266
    • Najafi, M.1    Haeri, M.2    Calvert, P.3
  • 55
    • 33750836895 scopus 로고    scopus 로고
    • Crystal structure of a photoactivated deprotonated intermediate of rhodopsin
    • D. Salom, and D.T. Lodowski K. Palczewski Crystal structure of a photoactivated deprotonated intermediate of rhodopsin Proc. Natl. Acad. Sci. USA 103 2006 16123 16128
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 16123-16128
    • Salom, D.1    Lodowski, D.T.2    Palczewski, K.3
  • 56
    • 0028140412 scopus 로고
    • Anomalous diffusion due to obstacles: A Monte Carlo study
    • M.J. Saxton Anomalous diffusion due to obstacles: a Monte Carlo study Biophys. J. 66 1994 394 401
    • (1994) Biophys. J. , vol.66 , pp. 394-401
    • Saxton, M.J.1
  • 57
    • 84876909902 scopus 로고    scopus 로고
    • Anomalous and normal diffusion of proteins and lipids in crowded lipid membranes
    • discussion 419-459
    • M. Javanainen, and H. Hammaren I. Vattulainen Anomalous and normal diffusion of proteins and lipids in crowded lipid membranes Faraday Discuss. 161 2013 397 417 discussion 419-459
    • (2013) Faraday Discuss. , vol.161 , pp. 397-417
    • Javanainen, M.1    Hammaren, H.2    Vattulainen, I.3
  • 58
    • 78651247184 scopus 로고    scopus 로고
    • Near-critical fluctuations and cytoskeleton-assisted phase separation lead to subdiffusion in cell membranes
    • J. Ehrig, E.P. Petrov, and P. Schwille Near-critical fluctuations and cytoskeleton-assisted phase separation lead to subdiffusion in cell membranes Biophys. J. 100 2011 80 89
    • (2011) Biophys. J. , vol.100 , pp. 80-89
    • Ehrig, J.1    Petrov, E.P.2    Schwille, P.3
  • 59
    • 84896947293 scopus 로고    scopus 로고
    • Anomalous diffusion due to hindering by mobile obstacles undergoing Brownian motion or Orstein-Ulhenbeck processes
    • H. Berry, and H. Chaté Anomalous diffusion due to hindering by mobile obstacles undergoing Brownian motion or Orstein-Ulhenbeck processes Phys. Rev. E Stat. Nonlin. Soft Matter Phys. 89 2014 022708
    • (2014) Phys. Rev. e Stat. Nonlin. Soft Matter Phys. , vol.89 , pp. 022708
    • Berry, H.1    Chaté, H.2
  • 60
    • 23744452794 scopus 로고    scopus 로고
    • Anomalous diffusion spreads its wings
    • AUGUST
    • J. Klafter, and I.M. Sokolov Anomalous diffusion spreads its wings Physics world. August 2005 29 32
    • (2005) Physics World. , pp. 29-32
    • Klafter, J.1    Sokolov, I.M.2
  • 61
    • 0024496187 scopus 로고
    • Concentration effects on reactions in membranes: Rhodopsin and transducin
    • M.J. Saxton, and J.C. Owicki Concentration effects on reactions in membranes: rhodopsin and transducin Biochim. Biophys. Acta 979 1989 27 34
    • (1989) Biochim. Biophys. Acta , vol.979 , pp. 27-34
    • Saxton, M.J.1    Owicki, J.C.2
  • 62
    • 34547157646 scopus 로고    scopus 로고
    • Receptor-mediated activation of heterotrimeric G-proteins: Current structural insights
    • C.A. Johnston, and D.P. Siderovski Receptor-mediated activation of heterotrimeric G-proteins: current structural insights Mol. Pharmacol. 72 2007 219 230
    • (2007) Mol. Pharmacol. , vol.72 , pp. 219-230
    • Johnston, C.A.1    Siderovski, D.P.2
  • 63
    • 0026505707 scopus 로고
    • A quantitative account of the activation steps involved in phototransduction in amphibian photoreceptors
    • T.D. Lamb, and E.N. Pugh Jr. A quantitative account of the activation steps involved in phototransduction in amphibian photoreceptors J. Physiol. 449 1992 719 758
    • (1992) J. Physiol. , vol.449 , pp. 719-758
    • Lamb, T.D.1    Pugh, Jr.E.N.2
  • 64
    • 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, and G.F.J. Salgado 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.J.2    Hruby, V.J.3
  • 65
    • 84878896615 scopus 로고    scopus 로고
    • A physiological role for the supramolecular organization of rhodopsin and transducin in rod photoreceptors
    • D. Dell'Orco A physiological role for the supramolecular organization of rhodopsin and transducin in rod photoreceptors FEBS Lett. 587 2013 2060 2066
    • (2013) FEBS Lett. , vol.587 , pp. 2060-2066
    • Dell'Orco, D.1
  • 66
    • 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
  • 67
    • 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
  • 68
    • 0023645290 scopus 로고
    • Mechanism of action of monoclonal antibodies that block the light activation of the guanyl nucleotide-binding protein, transducin
    • H.E. Hamm, and D. Deretic 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    Kohl, B.3
  • 69
    • 66149122990 scopus 로고    scopus 로고
    • Monitoring the interaction of a single G-protein key binding site with rhodopsin disk membranes upon light activation
    • T.Y. Kim, and H. Uji-i U. Alexiev Monitoring the interaction of a single G-protein key binding site with rhodopsin disk membranes upon light activation Biochemistry 48 2009 3801 3803
    • (2009) Biochemistry , vol.48 , pp. 3801-3803
    • Kim, T.Y.1    Uji-I, H.2    Alexiev, U.3
  • 70
    • 38549161544 scopus 로고    scopus 로고
    • A biological interpretation of transient anomalous subdiffusion. II. Reaction kinetics
    • M.J. Saxton A biological interpretation of transient anomalous subdiffusion. II. Reaction kinetics Biophys. J. 94 2008 760 771
    • (2008) Biophys. J. , vol.94 , pp. 760-771
    • Saxton, M.J.1
  • 71
    • 84887396922 scopus 로고    scopus 로고
    • Anomalous versus slowed-down Brownian diffusion in the ligand-binding equilibrium
    • H. Soula, and B. Caré H. Berry Anomalous versus slowed-down Brownian diffusion in the ligand-binding equilibrium Biophys. J. 105 2013 2064 2073
    • (2013) Biophys. J. , vol.105 , pp. 2064-2073
    • Soula, H.1    Caré, B.2    Berry, H.3
  • 72
    • 77957937199 scopus 로고    scopus 로고
    • Atomic-level characterization of the structural dynamics of proteins
    • D.E. Shaw, and P. Maragakis W. Wriggers Atomic-level characterization of the structural dynamics of proteins Science 330 2010 341 346
    • (2010) Science , vol.330 , pp. 341-346
    • Shaw, D.E.1    Maragakis, P.2    Wriggers, W.3
  • 73
    • 0034623787 scopus 로고    scopus 로고
    • COMPUTING: Screen savers of the world unite!
    • M. Shirts, and V.S. Pande COMPUTING: screen savers of the world unite! Science 290 2000 1903 1904
    • (2000) Science , vol.290 , pp. 1903-1904
    • Shirts, M.1    Pande, V.S.2
  • 74
    • 67650099787 scopus 로고    scopus 로고
    • ACEMD: Accelerating biomolecular dynamics in the microsecond time scale
    • M.J. Harvey, G. Giupponi, and G.D. Fabritiis ACEMD: accelerating biomolecular dynamics in the microsecond time scale J. Chem. Theory Comput. 5 2009 1632 1639
    • (2009) J. Chem. Theory Comput. , vol.5 , pp. 1632-1639
    • Harvey, M.J.1    Giupponi, G.2    Fabritiis, G.D.3
  • 75
    • 84872152631 scopus 로고    scopus 로고
    • OpenMM 4: A reusable, extensible, hardware independent library for high performance molecular simulation
    • P. Eastman, and M.S. Friedrichs V.S. Pande OpenMM 4: a reusable, extensible, hardware independent library for high performance molecular simulation J. Chem. Theory Comput. 9 2012 461 469
    • (2012) J. Chem. Theory Comput. , vol.9 , pp. 461-469
    • Eastman, P.1    Friedrichs, M.S.2    Pande, V.S.3
  • 76
    • 2942567954 scopus 로고    scopus 로고
    • Describing protein folding kinetics by molecular dynamics simulations: 1. Theory
    • W.C. Swope, J.W. Pitera, and F. Suits Describing protein folding kinetics by molecular dynamics simulations: 1. Theory J. Phys. Chem. B 108 2004 6571 6581
    • (2004) J. Phys. Chem. B , vol.108 , pp. 6571-6581
    • Swope, W.C.1    Pitera, J.W.2    Suits, F.3
  • 77
    • 0000573002 scopus 로고    scopus 로고
    • A direct approach to conformational dynamics based on hybrid Monte Carlo
    • C. Schütte, and A. Fischer P. Deuflhard A direct approach to conformational dynamics based on hybrid Monte Carlo J. Comput. Phys. 151 1999 146 168
    • (1999) J. Comput. Phys. , vol.151 , pp. 146-168
    • Schütte, C.1    Fischer, A.2    Deuflhard, P.3
  • 78
    • 34247339716 scopus 로고    scopus 로고
    • Hierarchical analysis of conformational dynamics in biomolecules: Transition networks of metastable states
    • F. Noé, and I. Horenko J.C. Smith Hierarchical analysis of conformational dynamics in biomolecules: transition networks of metastable states J. Chem. Phys. 126 2007 155102
    • (2007) J. Chem. Phys. , vol.126 , pp. 155102
    • Noé, F.1    Horenko, I.2    Smith, J.C.3
  • 79
    • 70450255797 scopus 로고    scopus 로고
    • Constructing the equilibrium ensemble of folding pathways from short off-equilibrium simulations
    • F. Noé, and C. Schütte T.R. Weikl Constructing the equilibrium ensemble of folding pathways from short off-equilibrium simulations Proc. Natl. Acad. Sci. USA 106 2009 19011 19016
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 19011-19016
    • Noé, F.1    Schütte, C.2    Weikl, T.R.3
  • 80
    • 0035799692 scopus 로고    scopus 로고
    • Membrane protein diffusion sets the speed of rod phototransduction
    • P.D. Calvert, and V.I. Govardovskii C.L. Makino Membrane protein diffusion sets the speed of rod phototransduction Nature 411 2001 90 94
    • (2001) Nature , vol.411 , pp. 90-94
    • Calvert, P.D.1    Govardovskii, V.I.2    Makino, C.L.3
  • 81
    • 0019631401 scopus 로고
    • Lateral mobility of erythrocyte membrane proteins studied by the fluorescence photobleaching recovery technique
    • C.H. Chang, and H. Takeuchi S. Ohnishi Lateral mobility of erythrocyte membrane proteins studied by the fluorescence photobleaching recovery technique J. Biochem. 90 1981 997 1004
    • (1981) J. Biochem. , vol.90 , pp. 997-1004
    • Chang, C.H.1    Takeuchi, H.2    Ohnishi, S.3
  • 83
    • 0242613637 scopus 로고
    • Interactions between photoexcited rhodopsin and GTP-binding protein: Kinetic and stoichiometric analyses from light-scattering changes
    • H. Kühn, and N. Bennett M. Chabre Interactions between photoexcited rhodopsin and GTP-binding protein: kinetic and stoichiometric analyses from light-scattering changes Proc. Natl. Acad. Sci. USA 78 1981 6873 6877
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 6873-6877
    • Kühn, H.1    Bennett, N.2    Chabre, M.3
  • 84
    • 0034049644 scopus 로고    scopus 로고
    • Light scattering methods to monitor interactions between rhodopsin-containing membranes and soluble proteins
    • M. Heck, A. Pulvermüller, and K.P. Hofmann Light scattering methods to monitor interactions between rhodopsin-containing membranes and soluble proteins Methods Enzymol. 315 2000 329 347
    • (2000) Methods Enzymol. , vol.315 , pp. 329-347
    • Heck, M.1    Pulvermüller, A.2    Hofmann, K.P.3
  • 85
    • 0021758996 scopus 로고
    • Temperature and pH dependence of the metarhodopsin I-metarhodopsin II kinetics and equilibria in bovine rod disk membrane suspensions
    • J.H. Parkes, and P.A. Liebman Temperature and pH dependence of the metarhodopsin I-metarhodopsin II kinetics and equilibria in bovine rod disk membrane suspensions Biochemistry 23 1984 5054 5061
    • (1984) Biochemistry , vol.23 , pp. 5054-5061
    • Parkes, J.H.1    Liebman, P.A.2
  • 86
    • 0038822850 scopus 로고    scopus 로고
    • Effects of pH on rhodopsin photointermediates from lumirhodopsin to metarhodopsin II
    • S. Jäger, and I. Szundi D.S. Kliger Effects of pH on rhodopsin photointermediates from lumirhodopsin to metarhodopsin II Biochemistry 37 1998 6998 7005
    • (1998) Biochemistry , vol.37 , pp. 6998-7005
    • Jäger, S.1    Szundi, I.2    Kliger, D.S.3
  • 87
    • 0033594815 scopus 로고    scopus 로고
    • Molecular determinants of the reversible membrane anchorage of the G-protein transducin
    • H.R. Seitz, and M. Heck A. Seelig Molecular determinants of the reversible membrane anchorage of the G-protein transducin Biochemistry 38 1999 7950 7960
    • (1999) Biochemistry , vol.38 , pp. 7950-7960
    • Seitz, H.R.1    Heck, M.2    Seelig, A.3
  • 88
    • 33845374715 scopus 로고
    • Microviscosity measurements of phospholipid bilayers using fluorescent dyes that undergo torsional relaxation
    • C.E. Kung, and J.K. Reed Microviscosity measurements of phospholipid bilayers using fluorescent dyes that undergo torsional relaxation Biochemistry 25 1986 6114 6121
    • (1986) Biochemistry , vol.25 , pp. 6114-6121
    • Kung, C.E.1    Reed, J.K.2
  • 89
    • 70350729439 scopus 로고    scopus 로고
    • Stochastic modelling of reaction-diffusion processes: Algorithms for bimolecular reactions
    • R. Erban, and S.J. Chapman Stochastic modelling of reaction-diffusion processes: algorithms for bimolecular reactions Phys. Biol. 6 2009 046001
    • (2009) Phys. Biol. , vol.6 , pp. 046001
    • Erban, R.1    Chapman, S.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.