Ames JB et al. (1997). Molecular mechanics of calcium-myristoyl switches. Nature. 389 [PubMed]

Aton BR, Litman BJ, Jackson ML. (1984). Isolation and identification of the phosphorylated species of rhodopsin. Biochemistry. 23 [PubMed]

Baylor DA, Hodgkin AL, Lamb TD. (1974). The electrical response of turtle cones to flashes and steps of light. The Journal of physiology. 242 [PubMed]

Baylor DA, Lamb TD, Yau KW. (1979). Responses of retinal rods to single photons. The Journal of physiology. 288 [PubMed]

Baylor DA, Rieke F. (1998). Single photon detection by rod cells of theretina Reviews Of Modern Physics. 70

Buczyłko J, Gutmann C, Palczewski K. (1991). Regulation of rhodopsin kinase by autophosphorylation. Proceedings of the National Academy of Sciences of the United States of America. 88 [PubMed]

Burns ME, Mendez A, Chen J, Baylor DA. (2002). Dynamics of cyclic GMP synthesis in retinal rods. Neuron. 36 [PubMed]

Chen CK et al. (2000). Slowed recovery of rod photoresponse in mice lacking the GTPase accelerating protein RGS9-1. Nature. 403 [PubMed]

Chen CK et al. (1999). Abnormal photoresponses and light-induced apoptosis in rods lacking rhodopsin kinase. Proceedings of the National Academy of Sciences of the United States of America. 96 [PubMed]

Chen CK, Inglese J, Lefkowitz RJ, Hurley JB. (1995). Ca(2+)-dependent interaction of recoverin with rhodopsin kinase. The Journal of biological chemistry. 270 [PubMed]

Cone RA, Cobbs WH. (1969). Rhodopsin cycle in the living eye of the rat. Nature. 221 [PubMed]

Cornwall MC, Fain GL. (1994). Bleached pigment activates transduction in isolated rods of the salamander retina. The Journal of physiology. 480 ( Pt 2) [PubMed]

Cornwall MC, Jones GJ, Kefalov VJ, Fain GL, Matthews HR. (2000). Electrophysiological methods for measurement of activation of phototransduction by bleached visual pigment in salamander photoreceptors. Methods in enzymology. 316 [PubMed]

Cornwall MC, Matthews HR, Crouch RK, Fain GL. (1995). Bleached pigment activates transduction in salamander cones. The Journal of general physiology. 106 [PubMed]

DEL CASTILLO J, KATZ B. (1954). Quantal components of the end-plate potential. The Journal of physiology. 124 [PubMed]

Dodd RL. (1998). The role of arrestin and recoverin in signal transduction by retinal rod photoreceptors Thesis.

Ebrey TG. (1968). The thermal decay of the intermediates of rhodopsin in situ. Vision research. 8 [PubMed]

Fain GL, Lamb TD, Matthews HR, Murphy RL. (1989). Cytoplasmic calcium as the messenger for light adaptation in salamander rods. The Journal of physiology. 416 [PubMed]

Fain GL, Lisman JE. (1993). Photoreceptor degeneration in vitamin A deprivation and retinitis pigmentosa: the equivalent light hypothesis. Experimental eye research. 57 [PubMed]

Fain GL, Matthews HR, Cornwall MC, Koutalos Y. (2001). Adaptation in vertebrate photoreceptors. Physiological reviews. 81 [PubMed]

Felber S, Breuer HP, Petruccione F, Honerkamp J, Hofmann KP. (1996). Stochastic simulation of the transducin GTPase cycle. Biophysical journal. 71 [PubMed]

Field GD, Rieke F. (2002). Mechanisms regulating variability of the single photon responses of mammalian rod photoreceptors. Neuron. 35 [PubMed]

Findlay JB et al. (1984). The structure of mammalian rod opsins. Vision research. 24 [PubMed]

Firsov ML, Kolesnikov AV, Golobokova EY, Govardovskii VI. (2005). Two realms of dark adaptation. Vision research. 45 [PubMed]

Forti S, Menini A, Rispoli G, Torre V. (1989). Kinetics of phototransduction in retinal rods of the newt Triturus cristatus. The Journal of physiology. 419 [PubMed]

Gibson SK, Parkes JH, Liebman PA. (2000). Phosphorylation modulates the affinity of light-activated rhodopsin for G protein and arrestin. Biochemistry. 39

Gillespie DT. (1976). A General method for numerically simulating the stochastic time evolution of coupledchemical reactions J Comput Phys. 22

Gillespie DT. (1977). Exact stochastic simulation of coupled chemical reactions. Journal Of Physical Chemistry. 81

Gorczyca WA, Gray-Keller MP, Detwiler PB, Palczewski K. (1994). Purification and physiological evaluation of a guanylate cyclase activating protein from retinal rods. Proceedings of the National Academy of Sciences of the United States of America. 91 [PubMed]

Gorodovikova EN, Philippov PP. (1993). The presence of a calcium-sensitive p26-containing complex in bovine retina rod cells. FEBS letters. 335 [PubMed]

Granzin J et al. (1998). X-ray crystal structure of arrestin from bovine rod outer segments. Nature. 391 [PubMed]

Gray-Keller MP, Detwiler PB. (1994). The calcium feedback signal in the phototransduction cascade of vertebrate rods. Neuron. 13 [PubMed]

Hamer RD. (2000). Analysis of Ca++-dependent gain changes in PDE activation in vertebrate rod phototransduction. Molecular vision. 6 [PubMed]

Hamer RD. (2000). Computational analysis of vertebrate phototransduction: combined quantitative and qualitative modeling of dark- and light-adapted responses in amphibian rods. Visual neuroscience. 17 [PubMed]

Hamer RD, Nicholas SC, Tranchina D, Liebman PA, Lamb TD. (2003). Multiple steps of phosphorylation of activated rhodopsin can account for the reproducibility of vertebrate rod single-photon responses. The Journal of general physiology. 122 [PubMed]

Hamm HE, Bownds MD. (1986). Protein complement of rod outer segments of frog retina. Biochemistry. 25 [PubMed]

He W, Wensel TG. (2002). RGS function in visual signal transduction. Methods in enzymology. 344 [PubMed]

Hirsch JA, Schubert C, Gurevich VV, Sigler PB. (1999). The 2.8 A crystal structure of visual arrestin: a model for arrestin's regulation. Cell. 97 [PubMed]

Hsu YT, Molday RS. (1993). Modulation of the cGMP-gated channel of rod photoreceptor cells by calmodulin. Nature. 361 [PubMed]

Kawamura S. (1993). Rhodopsin phosphorylation as a mechanism of cyclic GMP phosphodiesterase regulation by S-modulin. Nature. 362 [PubMed]

Kawamura S, Hisatomi O, Kayada S, Tokunaga F, Kuo CH. (1993). Recoverin has S-modulin activity in frog rods. The Journal of biological chemistry. 268 [PubMed]

Kawamura S, Murakami M. (1991). Calcium-dependent regulation of cyclic GMP phosphodiesterase by a protein from frog retinal rods. Nature. 349 [PubMed]

Kennedy MJ et al. (2001). Multiple phosphorylation of rhodopsin and the in vivo chemistry underlying rod photoreceptor dark adaptation. Neuron. 31 [PubMed]

Keresztes G et al. (2004). Absence of the RGS9.Gbeta5 GTPase-activating complex in photoreceptors of the R9AP knockout mouse. The Journal of biological chemistry. 279 [PubMed]

Klenchin VA, Calvert PD, Bownds MD. (1995). Inhibition of rhodopsin kinase by recoverin. Further evidence for a negative feedback system in phototransduction. The Journal of biological chemistry. 270 [PubMed]

Koch KW, Stryer L. (1988). Highly cooperative feedback control of retinal rod guanylate cyclase by calcium ions. Nature. 334 [PubMed]

Korenbrot JI, Miller DL. (1989). Cytoplasmic free calcium concentration in dark-adapted retinal rod outer segments. Vision research. 29 [PubMed]

Koutalos Y, Nakatani K, Yau KW. (1995). The cGMP-phosphodiesterase and its contribution to sensitivity regulation in retinal rods. The Journal of general physiology. 106 [PubMed]

Krispel CM, Chen CK, Simon MI, Burns ME. (2003). Prolonged photoresponses and defective adaptation in rods of Gbeta5-/- mice. The Journal of neuroscience : the official journal of the Society for Neuroscience. 23 [PubMed]

Krupnick JG, Gurevich VV, Benovic JL. (1997). Mechanism of quenching of phototransduction. Binding competition between arrestin and transducin for phosphorhodopsin. The Journal of biological chemistry. 272 [PubMed]

Kühn H, Wilden U. (1982). Assay of phosphorylation of rhodopsin in vitro and in vivo. Methods in enzymology. 81 [PubMed]

Lagnado L, Cervetto L, McNaughton PA. (1992). Calcium homeostasis in the outer segments of retinal rods from the tiger salamander. The Journal of physiology. 455 [PubMed]

Lamb TD. (1981). The involvement of rod photoreceptors in dark adaptation. Vision research. 21 [PubMed]

Lamb TD, Matthews HR, Torre V. (1986). Incorporation of calcium buffers into salamander retinal rods: a rejection of the calcium hypothesis of phototransduction. The Journal of physiology. 372 [PubMed]

Lamb TD, McNaughton PA, Yau KW. (1981). Spatial spread of activation and background desensitization in toad rod outer segments. The Journal of physiology. 319 [PubMed]

Lamb TD, Pugh EN. (1992). G-protein cascades: gain and kinetics. Trends in neurosciences. 15 [PubMed]

Lamb TD, Pugh EN. (2000). Phototransduction in vertebrate rods and cones: molecular mechanisms ofamplification, recovery and light adaptation Handbook of Biological Physics, Molecular Mechanisms of Visual Transduction. 3

Leibrock CS, Reuter T, Lamb TD. (1994). Dark adaptation of toad rod photoreceptors following small bleaches. Vision research. 34 [PubMed]

Leibrock CS, Reuter T, Lamb TD. (1998). Molecular basis of dark adaptation in rod photoreceptors. Eye (London, England). 12 ( Pt 3b) [PubMed]

Leskov IB et al. (2000). The gain of rod phototransduction: reconciliation of biochemical and electrophysiological measurements. Neuron. 27 [PubMed]

Lishko PV, Martemyanov KA, Hopp JA, Arshavsky VY. (2002). Specific binding of RGS9-Gbeta 5L to protein anchor in photoreceptor membranes greatly enhances its catalytic activity. The Journal of biological chemistry. 277 [PubMed]

Makino CL et al. (2004). Recoverin regulates light-dependent phosphodiesterase activity in retinal rods. The Journal of general physiology. 123 [PubMed]

Martemyanov KA, Arshavsky VY. (2002). Noncatalytic domains of RGS9-1.Gbeta 5L play a decisive role in establishing its substrate specificity. The Journal of biological chemistry. 277 [PubMed]

Martemyanov KA et al. (2003). The DEP domain determines subcellular targeting of the GTPase activating protein RGS9 in vivo. The Journal of neuroscience : the official journal of the Society for Neuroscience. 23 [PubMed]

Matthews HR. (1991). Incorporation of chelator into guinea-pig rods shows that calcium mediates mammalian photoreceptor light adaptation. The Journal of physiology. 436 [PubMed]

Matthews HR. (1995). Effects of lowered cytoplasmic calcium concentration and light on the responses of salamander rod photoreceptors. J Physiol. 484 ( Pt 2)

Matthews HR. (1996). Static and dynamic actions of cytoplasmic Ca2+ in the adaptation of responses to saturating flashes in salamander rods. The Journal of physiology. 490 ( Pt 1) [PubMed]

Matthews HR, Murphy RL, Fain GL, Lamb TD. (1988). Photoreceptor light adaptation is mediated by cytoplasmic calcium concentration. Nature. 334 [PubMed]

McCarthy ST, Younger JP, Owen WG. (1994). Free calcium concentrations in bullfrog rods determined in the presence of multiple forms of Fura-2. Biophysical journal. 67 [PubMed]

Melia TJ, Cowan CW, Angleson JK, Wensel TG. (1997). A comparison of the efficiency of G protein activation by ligand-free and light-activated forms of rhodopsin. Biophysical journal. 73 [PubMed]

Mendez A et al. (2000). Rapid and reproducible deactivation of rhodopsin requires multiple phosphorylation sites. Neuron. 28 [PubMed]

Miller JL, Dratz EA. (1984). Phosphorylation at sites near rhodopsin's carboxyl-terminus regulates light initiated cGMP hydrolysis. Vision research. 24 [PubMed]

Murnick JG, Lamb TD. (1996). Kinetics of desensitization induced by saturating flashes in toad and salamander rods. The Journal of physiology. 495 ( Pt 1) [PubMed]

Nakatani K, Yau KW. (1988). Calcium and magnesium fluxes across the plasma membrane of the toad rod outer segment. The Journal of physiology. 395 [PubMed]

Nikonov S, Engheta N, Pugh EN. (1998). Kinetics of recovery of the dark-adapted salamander rod photoresponse. The Journal of general physiology. 111 [PubMed]

Nikonov S, Lamb TD, Pugh EN. (2000). The role of steady phosphodiesterase activity in the kinetics and sensitivity of the light-adapted salamander rod photoresponse. The Journal of general physiology. 116 [PubMed]

Ohguro H, Johnson RS, Ericsson LH, Walsh KA, Palczewski K. (1994). Control of rhodopsin multiple phosphorylation. Biochemistry. 33 [PubMed]

Ohguro H, Palczewski K, Ericsson LH, Walsh KA, Johnson RS. (1993). Sequential phosphorylation of rhodopsin at multiple sites. Biochemistry. 32 [PubMed]

Ohguro H et al. (1996). Structural and enzymatic aspects of rhodopsin phosphorylation. The Journal of biological chemistry. 271 [PubMed]

Ohguro H, Van Hooser JP, Milam AH, Palczewski K. (1995). Rhodopsin phosphorylation and dephosphorylation in vivo. The Journal of biological chemistry. 270 [PubMed]

Ohyama T et al. (2000). Fraction of the dark current carried by Ca(2+) through cGMP-gated ion channels of intact rod and cone photoreceptors. The Journal of general physiology. 116 [PubMed]

Palczewski K, Buczyłko J, Kaplan MW, Polans AS, Crabb JW. (1991). Mechanism of rhodopsin kinase activation. The Journal of biological chemistry. 266 [PubMed]

Pepperberg DR et al. (1992). Light-dependent delay in the falling phase of the retinal rod photoresponse. Visual neuroscience. 8 [PubMed]

Pepperberg DR, Jin J, Jones GJ. (1994). Modulation of transduction gain in light adaptation of retinal rods. Visual neuroscience. 11 [PubMed]

Pfister C, Kühn H, Chabre M. (1983). Interaction between photoexcited rhodopsin and peripheral enzymes in frog retinal rods. Influence on the postmetarhodopsin II decay and phosphorylation rate of rhodopsin. European journal of biochemistry. 136 [PubMed]

Pugh EN. (1999). Variability in single photon responses: a cut in the Gordian knot of rod phototransduction? Neuron. 23 [PubMed]

Pugh EN, Lamb TD. (1990). Cyclic GMP and calcium: the internal messengers of excitation and adaptation in vertebrate photoreceptors. Vision research. 30 [PubMed]

Pugh EN, Lamb TD. (1993). Amplification and kinetics of the activation steps in phototransduction. Biochimica et biophysica acta. 1141 [PubMed]

Pulvermüller A, Palczewski K, Hofmann KP. (1993). Interaction between photoactivated rhodopsin and its kinase: stability and kinetics of complex formation. Biochemistry. 32 [PubMed]

Rieke F, Baylor DA. (1996). Molecular origin of continuous dark noise in rod photoreceptors. Biophysical journal. 71 [PubMed]

Rieke F, Baylor DA. (1998). Origin of reproducibility in the responses of retinal rods to single photons. Biophysical journal. 75 [PubMed]

Rodieck RW. (1998). The first steps in seeing .

Sampath AP, Matthews HR, Cornwall MC, Fain GL. (1998). Bleached pigment produces a maintained decrease in outer segment Ca2+ in salamander rods. The Journal of general physiology. 111 [PubMed]

Schnapf JL. (1983). Dependence of the single photon response on longitudinal position of absorption in toad rod outer segments. The Journal of physiology. 343 [PubMed]

Schneeweis DM, Schnapf JL. (1995). Photovoltage of rods and cones in the macaque retina. Science (New York, N.Y.). 268 [PubMed]

Schröder K, Pulvermüller A, Hofmann KP. (2002). Arrestin and its splice variant Arr1-370A (p44). Mechanism and biological role of their interaction with rhodopsin. The Journal of biological chemistry. 277 [PubMed]

Skiba NP et al. (2001). RGS9-G beta 5 substrate selectivity in photoreceptors. Opposing effects of constituent domains yield high affinity of RGS interaction with the G protein-effector complex. The Journal of biological chemistry. 276 [PubMed]

Stryer L, Tanaka T, Ikura M, Ames JB, Porumb T. (1995). Amino-terminal myristoylation induces cooperative calcium binding to recoverin. J Biol Chem. 270

Tamura T, Nakatani K, Yau KW. (1991). Calcium feedback and sensitivity regulation in primate rods. The Journal of general physiology. 98 [PubMed]

Thompson P, Findlay JB. (1984). Phosphorylation of ovine rhodopsin. Identification of the phosphorylated sites. The Biochemical journal. 220 [PubMed]

Torre V, Matthews HR, Lamb TD. (1986). Role of calcium in regulating the cyclic GMP cascade of phototransduction in retinal rods. Proceedings of the National Academy of Sciences of the United States of America. 83 [PubMed]

Whitlock GG, Lamb TD. (1999). Variability in the time course of single photon responses from toad rods: termination of rhodopsin's activity. Neuron. 23 [PubMed]

Wilden U. (1995). Duration and amplitude of the light-induced cGMP hydrolysis in vertebrate photoreceptors are regulated by multiple phosphorylation of rhodopsin and by arrestin binding. Biochemistry. 34 [PubMed]

Wilden U, Kühn H. (1982). Light-dependent phosphorylation of rhodopsin: number of phosphorylation sites. Biochemistry. 21 [PubMed]

Xu J et al. (1997). Prolonged photoresponses in transgenic mouse rods lacking arrestin. Nature. 389 [PubMed]

Yau KW. (1994). Phototransduction mechanism in retinal rods and cones. The Friedenwald Lecture. Investigative ophthalmology & visual science. 35 [PubMed]