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Volumn 77, Issue 2, 1999, Pages 1024-1035

Spectral tuning in salamander visual pigments studied with dihydroretinal chromophores

Author keywords

[No Author keywords available]

Indexed keywords

11 CIS RETINAL; OPSIN; RETINAL; SCHIFF BASE; VISUAL PIGMENT;

EID: 0032781030     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)76953-5     Document Type: Article
Times cited : (38)

References (90)
  • 1
    • 0029559366 scopus 로고
    • The molecular basis for the green-blue sensitivity shift in the rod visual pigments of the European eel
    • Archer, S., A. Hope, and J. C. Partridge. 1995. The molecular basis for the green-blue sensitivity shift in the rod visual pigments of the European eel. Proc. R. Soc. Lond. B. 262:289-295.
    • (1995) Proc. R. Soc. Lond. B. , vol.262 , pp. 289-295
    • Archer, S.1    Hope, A.2    Partridge, J.C.3
  • 3
    • 0028289475 scopus 로고
    • Molecular determinants of human red/green color discrimination
    • Asenjo, A. B., J. Rim, and D. D. Oprian. 1994. Molecular determinants of human red/green color discrimination. Neuron. 12:1131-1138.
    • (1994) Neuron , vol.12 , pp. 1131-1138
    • Asenjo, A.B.1    Rim, J.2    Oprian, D.D.3
  • 4
    • 0021646399 scopus 로고
    • The photocurrent, noise and spectral sensitivity of rods of the monkey Macaca fascicularis
    • Baylor, D. A., B. J. Nunn, and J. L. Schnapf. 1984. The photocurrent, noise and spectral sensitivity of rods of the monkey Macaca fascicularis. J. Physiol. (Lond.). 357:575-607.
    • (1984) J. Physiol. (Lond.) , vol.357 , pp. 575-607
    • Baylor, D.A.1    Nunn, B.J.2    Schnapf, J.L.3
  • 5
    • 0023232646 scopus 로고
    • Spectral sensitivity of cones of the monkey Macaca fascicularis
    • Baylor, D. A., B. J. Nunn, and J. L. Schnapf. 1987. Spectral sensitivity of cones of the monkey Macaca fascicularis. J. Physiol. (Lond.). 390: 145-160.
    • (1987) J. Physiol. (Lond.) , vol.390 , pp. 145-160
    • Baylor, D.A.1    Nunn, B.J.2    Schnapf, J.L.3
  • 6
    • 0014403593 scopus 로고
    • Synthesis of all-trans-5,6-dihydroretinal, a new visual chromophore
    • Blatz, P. E., P. Balasubramaniyan, and V. Balasubramaniyan. 1968a. Synthesis of all-trans-5,6-dihydroretinal, a new visual chromophore. J. Am. Chem. Soc. 90:3282-3283.
    • (1968) J. Am. Chem. Soc. , vol.90 , pp. 3282-3283
    • Blatz, P.E.1    Balasubramaniyan, P.2    Balasubramaniyan, V.3
  • 7
    • 0014412942 scopus 로고
    • Preparation of a new visual pigment analogue of cattle opsin using 5,6-dihydroretinal
    • Blatz, P. E., P. B. Dewhurst, P. Balasubramaniyan, and V. Balasubramaniyan. 1968b. Preparation of a new visual pigment analogue of cattle opsin using 5,6-dihydroretinal. Nature. 219:169-170.
    • (1968) Nature , vol.219 , pp. 169-170
    • Blatz, P.E.1    Dewhurst, P.B.2    Balasubramaniyan, P.3    Balasubramaniyan, V.4
  • 10
    • 0015528085 scopus 로고
    • Anion-induced wavelength regulation of absorption maxima of Schiff bases of retinal
    • Blatz, P. E., J. H. Mohler, and H. V. Navangul. 1972. Anion-induced wavelength regulation of absorption maxima of Schiff bases of retinal. Biochemistry. 11:848-855.
    • (1972) Biochemistry , vol.11 , pp. 848-855
    • Blatz, P.E.1    Mohler, J.H.2    Navangul, H.V.3
  • 11
    • 0011457788 scopus 로고
    • Ultra-violet light absorption and the structure of organic compounds
    • Braude, E. A. 1945. Ultra-violet light absorption and the structure of organic compounds. Annu. Rep. Prog. Chem. 42:105-130.
    • (1945) Annu. Rep. Prog. Chem. , vol.42 , pp. 105-130
    • Braude, E.A.1
  • 12
    • 0014090782 scopus 로고
    • Spectroscopic properties of porphyropsins
    • Bridges, C. D. B. 1967. Spectroscopic properties of porphyropsins. Vis. Res. 7:349-369.
    • (1967) Vis. Res. , vol.7 , pp. 349-369
    • Bridges, C.D.B.1
  • 13
    • 0022412616 scopus 로고
    • All-trans-retinoids and dihydroretinoids as probes of the role of chromophore structure in rhodopsin activation
    • Calhoon, R. D., and R. R. Rando. 1985. All-trans-retinoids and dihydroretinoids as probes of the role of chromophore structure in rhodopsin activation. Biochemistry. 24:6446-6452.
    • (1985) Biochemistry , vol.24 , pp. 6446-6452
    • Calhoon, R.D.1    Rando, R.R.2
  • 14
    • 0029261817 scopus 로고
    • Opsin phylogeny and evolution: A model for blue shifts in wavelength regulation
    • Chang, B. S. W., K. A. Crandall, J. P. Carulli, and D. L. Hartl. 1995. Opsin phylogeny and evolution: a model for blue shifts in wavelength regulation. Mol. Phylogenet. Evol. 4:31-43.
    • (1995) Mol. Phylogenet. Evol. , vol.4 , pp. 31-43
    • Chang, B.S.W.1    Crandall, K.A.2    Carulli, J.P.3    Hartl, D.L.4
  • 17
    • 0028178611 scopus 로고
    • Murine and bovine blue cone pigment genes: Cloning and characterization of two new members of the S family of visual pigments
    • Chiu, M. I., D. J. Zack, Y. Wang, and J. Nathans. 1994. Murine and bovine blue cone pigment genes: cloning and characterization of two new members of the S family of visual pigments. Genomics. 21:440-443.
    • (1994) Genomics , vol.21 , pp. 440-443
    • Chiu, M.I.1    Zack, D.J.2    Wang, Y.3    Nathans, J.4
  • 18
    • 0021683714 scopus 로고
    • Absorptance and spectral sensitivity measurements of rod photoreceptors of the tiger salamander, Ambystoma tigrinum
    • Cornwall, M. C., E. F. MacNichol, Jr., and A. Fein. 1984. Absorptance and spectral sensitivity measurements of rod photoreceptors of the tiger salamander, Ambystoma tigrinum. Vis. Res. 24:1651-1659.
    • (1984) Vis. Res. , vol.24 , pp. 1651-1659
    • Cornwall, M.C.1    MacNichol E.F., Jr.2    Fein, A.3
  • 20
    • 0019501897 scopus 로고
    • Polynomial expressions of pigment nomograms
    • Dawis, S. M. 1981. Polynomial expressions of pigment nomograms. Vis. Res. 21:1427-1430.
    • (1981) Vis. Res. , vol.21 , pp. 1427-1430
    • Dawis, S.M.1
  • 22
    • 0017330517 scopus 로고
    • New wavelength dependent visual pigment nomograms
    • Ebrey, T. G., and B. Honig. 1977. New wavelength dependent visual pigment nomograms. Vis. Res. 17:147-151.
    • (1977) Vis. Res. , vol.17 , pp. 147-151
    • Ebrey, T.G.1    Honig, B.2
  • 23
    • 0018625675 scopus 로고
    • Halide control of color of the chicken cone pigment iodopsin
    • Fager, L. Y., and R. S. Fager. 1979. Halide control of color of the chicken cone pigment iodopsin. Exp. Eye Res. 29:401-408.
    • (1979) Exp. Eye Res. , vol.29 , pp. 401-408
    • Fager, L.Y.1    Fager, R.S.2
  • 24
    • 0032126133 scopus 로고    scopus 로고
    • The visual pigments of the bottlenose dolphin (Tursiops truncatus)
    • Fasick, J. I., T. W. Cronin, D. M. Hunt, and P. R. Robinson. 1998. The visual pigments of the bottlenose dolphin (Tursiops truncatus). Vis. Neurosci. 15:643-651.
    • (1998) Vis. Neurosci. , vol.15 , pp. 643-651
    • Fasick, J.I.1    Cronin, T.W.2    Hunt, D.M.3    Robinson, P.R.4
  • 25
    • 0032512420 scopus 로고    scopus 로고
    • Mechanism of spectral tuning in the dolphin visual pigments
    • Fasick, J. I., and P. R. Robinson. 1998. Mechanism of spectral tuning in the dolphin visual pigments. Biochemistry. 37:433-438.
    • (1998) Biochemistry , vol.37 , pp. 433-438
    • Fasick, J.I.1    Robinson, P.R.2
  • 26
    • 0025273351 scopus 로고
    • Comparative study on the chromophore binding sites of rod and red-sensitive cone visual pigments by use of synthetic retinal isomers and analogues
    • Fukada, Y., T. Okano, Y. Shichida, T. Yoshizawa, A. Trehan, D. Mead, M. Denny, A. E. Asato, and R. S. H. Liu. 1990. Comparative study on the chromophore binding sites of rod and red-sensitive cone visual pigments by use of synthetic retinal isomers and analogues. Biochemistry. 29: 3133-3140.
    • (1990) Biochemistry , vol.29 , pp. 3133-3140
    • Fukada, Y.1    Okano, T.2    Shichida, Y.3    Yoshizawa, T.4    Trehan, A.5    Mead, D.6    Denny, M.7    Asato, A.E.8    Liu, R.S.H.9
  • 27
    • 0020373644 scopus 로고
    • Activation of phosphodiesterase in frog rod outer segment by rhodopsin analogues
    • Fukada, Y., T. Yoshizawa, M. Ito, and K. Tsukida. 1982. Activation of phosphodiesterase in frog rod outer segment by rhodopsin analogues. Biochim. Biophys. Acta. 708:112-117.
    • (1982) Biochim. Biophys. Acta , vol.708 , pp. 112-117
    • Fukada, Y.1    Yoshizawa, T.2    Ito, M.3    Tsukida, K.4
  • 31
    • 0016809405 scopus 로고
    • Absorption spectra and linear dichroism of some amphibian photoreceptors
    • Harosi, F. I. 1975. Absorption spectra and linear dichroism of some amphibian photoreceptors. J. Gen. Physiol. 66:357-382.
    • (1975) J. Gen. Physiol. , vol.66 , pp. 357-382
    • Harosi, F.I.1
  • 32
    • 0017116047 scopus 로고
    • Spectral relations of cone pigments in goldfish
    • Harosi, F. I. 1976. Spectral relations of cone pigments in goldfish. J. Gen. Physiol. 68:65-80.
    • (1976) J. Gen. Physiol. , vol.68 , pp. 65-80
    • Harosi, F.I.1
  • 34
    • 0027960310 scopus 로고
    • Phylogenetic relationships among vertebrate visual pigments
    • Hisatomi, O., S. Kayada, Y. Aoki, T. Iwasa, and F. Tokunaga. 1994. Phylogenetic relationships among vertebrate visual pigments. Vis. Res. 34:3097-3102.
    • (1994) Vis. Res. , vol.34 , pp. 3097-3102
    • Hisatomi, O.1    Kayada, S.2    Aoki, Y.3    Iwasa, T.4    Tokunaga, F.5
  • 35
    • 0030808817 scopus 로고    scopus 로고
    • The primary structure and distribution of killifish visual pigments
    • Hisatomi, O., T. Satoh, and F. Tokunaga. 1997. The primary structure and distribution of killifish visual pigments. Vis. Res. 37:3089-3096.
    • (1997) Vis. Res. , vol.37 , pp. 3089-3096
    • Hisatomi, O.1    Satoh, T.2    Tokunaga, F.3
  • 37
    • 0031052579 scopus 로고    scopus 로고
    • Mechanisms of wavelength tuning in the rod opsins of deep-sea fishes
    • Hope, A. J., J. C. Partridge, K. S. Dulai, and D. M. Hunt. 1997. Mechanisms of wavelength tuning in the rod opsins of deep-sea fishes. Proc. R. Soc. Lond. B. 264:155-163.
    • (1997) Proc. R. Soc. Lond. B , vol.264 , pp. 155-163
    • Hope, A.J.1    Partridge, J.C.2    Dulai, K.S.3    Hunt, D.M.4
  • 38
    • 0001575530 scopus 로고
    • Cis-trans isomers of vitamin A and retinene in the rhodopsin system
    • Hubbard, R., and G. Wald. 1952. Cis-trans isomers of vitamin A and retinene in the rhodopsin system. J. Gen. Physiol. 36:269-315.
    • (1952) J. Gen. Physiol. , vol.36 , pp. 269-315
    • Hubbard, R.1    Wald, G.2
  • 39
    • 0029922071 scopus 로고    scopus 로고
    • Spectral tuning and molecular evolution of rod visual pigments in the species flock of cottoid fish in Lake Baikal
    • Hunt, D. M., J. Fitzgibbon, S. J. Slobodyanyuk, and J. K. Bowmaker. 1996. Spectral tuning and molecular evolution of rod visual pigments in the species flock of cottoid fish in Lake Baikal. Vis. Res. 36:1217-1224.
    • (1996) Vis. Res. , vol.36 , pp. 1217-1224
    • Hunt, D.M.1    Fitzgibbon, J.2    Slobodyanyuk, S.J.3    Bowmaker, J.K.4
  • 41
    • 0024357993 scopus 로고
    • Retinoid requirements for recovery of sensitivity after visual-pigment bleaching in isolated photoreceptors
    • Jones, G. J., R. K. Crouch, B. Wiggert, M. C. Cornwall, and G. J. Chader. 1989. Retinoid requirements for recovery of sensitivity after visual-pigment bleaching in isolated photoreceptors. Proc. Natl. Acad. Sci. USA. 86:9606-9610.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9606-9610
    • Jones, G.J.1    Crouch, R.K.2    Wiggert, B.3    Cornwall, M.C.4    Chader, G.J.5
  • 42
    • 0027441825 scopus 로고
    • Visual pigment bleaching in isolated salamander retinal cones. Microspectrophotometry and light adaptation
    • Jones, G. J., A. Fein, E. F. MacNichol, Jr., and M. C. Cornwall. 1993. Visual pigment bleaching in isolated salamander retinal cones. Microspectrophotometry and light adaptation. J. Gen. Physiol. 102: 483-502.
    • (1993) J. Gen. Physiol. , vol.102 , pp. 483-502
    • Jones, G.J.1    Fein, A.2    MacNichol E.F., Jr.3    Cornwall, M.C.4
  • 43
    • 0032897613 scopus 로고    scopus 로고
    • Occupancy of the chromophore binding site of opsin activates visual transduction in rod photoreceptors
    • Kefalov, V. J., M. C. Cornwall, and R. K. Crouch. 1999. Occupancy of the chromophore binding site of opsin activates visual transduction in rod photoreceptors. J. Gen. Physiol. 113:491-503.
    • (1999) J. Gen. Physiol. , vol.113 , pp. 491-503
    • Kefalov, V.J.1    Cornwall, M.C.2    Crouch, R.K.3
  • 44
    • 0026686815 scopus 로고
    • Anion sensitivity and spectral tuning of cone visual pigments in situ
    • Kleinschmidt, J., and F. I. Harosi. 1992. Anion sensitivity and spectral tuning of cone visual pigments in situ. Proc. Natl. Acad. Sci. USA. 89:9181-9185.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 9181-9185
    • Kleinschmidt, J.1    Harosi, F.I.2
  • 45
    • 0018839748 scopus 로고
    • The chloride effect in chicken red cone receptors
    • Knowles, A. 1980. The chloride effect in chicken red cone receptors. Vis. Res. 20:475-483.
    • (1980) Vis. Res. , vol.20 , pp. 475-483
    • Knowles, A.1
  • 46
    • 0030970581 scopus 로고    scopus 로고
    • Resonance Raman examination of the wavelength regulation mechanism in human visual pigments
    • Kochendoerfer, G. G., Z. Wang, D. D. Oprian, and R. A. Mathies. 1997. Resonance Raman examination of the wavelength regulation mechanism in human visual pigments. Biochemistry. 36:6577-6587.
    • (1997) Biochemistry , vol.36 , pp. 6577-6587
    • Kochendoerfer, G.G.1    Wang, Z.2    Oprian, D.D.3    Mathies, R.A.4
  • 48
    • 0000388260 scopus 로고
    • The mechanism of bleaching rhodopsin
    • Kropf, A., and R. Hubbard. 1958. The mechanism of bleaching rhodopsin. Ann. N.Y. Acad. Sci. 74:266-280.
    • (1958) Ann. N.Y. Acad. Sci. , vol.74 , pp. 266-280
    • Kropf, A.1    Hubbard, R.2
  • 49
    • 0028828383 scopus 로고
    • Photoreceptor spectral sensitivities: Common shape in the long-wavelength region
    • Lamb, T. D. 1995. Photoreceptor spectral sensitivities: common shape in the long-wavelength region. Vis. Res. 35:3083-3091.
    • (1995) Vis. Res. , vol.35 , pp. 3083-3091
    • Lamb, T.D.1
  • 50
    • 0028316890 scopus 로고
    • What makes red visual pigments red? A resonance Raman microprobe study of retinal chromophore structure in iodopsin
    • Lin, S. W., Y. Imamoto, Y. Fukada, Y. Shichida, T. Yosnizawa, and R. A. Mathies. 1994. What makes red visual pigments red? A resonance Raman microprobe study of retinal chromophore structure in iodopsin. Biochemistry. 33:2151-2160.
    • (1994) Biochemistry , vol.33 , pp. 2151-2160
    • Lin, S.W.1    Imamoto, Y.2    Fukada, Y.3    Shichida, Y.4    Yosnizawa, T.5    Mathies, R.A.6
  • 51
    • 0032544345 scopus 로고    scopus 로고
    • Mechanisms of spectral tuning in blue cone visual pigments. Visible and Raman spectroscopy of blue-shifted rhodopsin mutants
    • Lin, S. W., G. G. Kochendoerfer, K. S. Carroll, D. Wang, R. A. Mathies, and T. P. Sakmar. 1998. Mechanisms of spectral tuning in blue cone visual pigments. Visible and Raman spectroscopy of blue-shifted rhodopsin mutants. J. Biol. Chem. 273:24583-24591.
    • (1998) J. Biol. Chem. , vol.273 , pp. 24583-24591
    • Lin, S.W.1    Kochendoerfer, G.G.2    Carroll, K.S.3    Wang, D.4    Mathies, R.A.5    Sakmar, T.P.6
  • 52
    • 0024592918 scopus 로고
    • Why are blue visual pigments blue? A resonance Raman microprobe study
    • Loppnow, G. R., B. A. Barry, and R. A. Mathies. 1989. Why are blue visual pigments blue? A resonance Raman microprobe study. Proc. Natl. Acad. Sci. USA. 86:1515-1518.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 1515-1518
    • Loppnow, G.R.1    Barry, B.A.2    Mathies, R.A.3
  • 54
    • 0022451582 scopus 로고
    • A unifying presentation of photopigment spectra
    • MacNichol, E. F., Jr. 1986. A unifying presentation of photopigment spectra. Vis. Res 26:1543-1556.
    • (1986) Vis. Res , vol.26 , pp. 1543-1556
    • MacNichol E.F., Jr.1
  • 55
    • 0030008653 scopus 로고    scopus 로고
    • Multiple visual pigments in a photoreceptor of the salamander retina
    • Makino, C. L., and R. L. Dodd. 1996. Multiple visual pigments in a photoreceptor of the salamander retina. J. Gen. Physiol. 108:27-34.
    • (1996) J. Gen. Physiol. , vol.108 , pp. 27-34
    • Makino, C.L.1    Dodd, R.L.2
  • 58
    • 0025953032 scopus 로고
    • Rapid charge movements and photosensitivity of visual pigments in salamander rods and cones
    • Makino, C. L., W. R Taylor, and D. A. Baylor. 1991. Rapid charge movements and photosensitivity of visual pigments in salamander rods and cones. J. Physiol. (Lond.). 442:761-780.
    • (1991) J. Physiol. (Lond.) , vol.442 , pp. 761-780
    • Makino, C.L.1    Taylor, W.R.2    Baylor, D.A.3
  • 59
    • 0002539819 scopus 로고
    • Primate photoreceptors and cone mechanisms
    • A. Fein and J. S. Levine, editors. A. R. Liss, New York
    • Mansfield, R. J. W. 1985. Primate photoreceptors and cone mechanisms. In The Visual System. A. Fein and J. S. Levine, editors. A. R. Liss, New York. 89-106.
    • (1985) The Visual System , pp. 89-106
    • Mansfield, R.J.W.1
  • 60
    • 0001718556 scopus 로고
    • Retinal has a highly dipolar vertically excited singlet state: Implications for vision
    • Mathies, R., and L. Stryer. 1976. Retinal has a highly dipolar vertically excited singlet state: implications for vision. Proc. Natl. Acad. Sci. USA. 73:2169-2173.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 2169-2173
    • Mathies, R.1    Stryer, L.2
  • 61
    • 0016713274 scopus 로고
    • Existence of a β-ionone ringbinding site in the rhodopsin molecule
    • Matsumoto, H., and T. Yoshizawa. 1975. Existence of a β-ionone ringbinding site in the rhodopsin molecule. Nature. 258:523-526.
    • (1975) Nature , vol.258 , pp. 523-526
    • Matsumoto, H.1    Yoshizawa, T.2
  • 63
    • 33847086348 scopus 로고
    • Opsin shifts in bovine rhodopsin and bacteriorhodopsin. Comparison of two external point-charge models
    • Motto, M. G., M. Sheves, K. Tsujimoto, V. Balogh-Nair, and K. Nakanishi. 1980. Opsin shifts in bovine rhodopsin and bacteriorhodopsin. Comparison of two external point-charge models. J. Am. Chem. Soc. 102: 7947-7949.
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 7947-7949
    • Motto, M.G.1    Sheves, M.2    Tsujimoto, K.3    Balogh-Nair, V.4    Nakanishi, K.5
  • 64
    • 36849140192 scopus 로고
    • Intensities of electronic transitions in molecular spectra. III. Organic molecules with double bonds. Conjugated dienes
    • Mulliken, R. S. 1939. Intensities of electronic transitions in molecular spectra. III. Organic molecules with double bonds. Conjugated dienes. J. Chem. Phys. 7:121-135.
    • (1939) J. Chem. Phys. , vol.7 , pp. 121-135
    • Mulliken, R.S.1
  • 65
    • 0013941208 scopus 로고
    • S-potentials from colour units in the retina of fish (Cyprinidae)
    • Naka, K. I., and W. A. H. Rushton. 1966. S-potentials from colour units in the retina of fish (Cyprinidae). J. Physiol. (Lond.). 185:536-555.
    • (1966) J. Physiol. (Lond.) , vol.185 , pp. 536-555
    • Naka, K.I.1    Rushton, W.A.H.2
  • 66
    • 77957209808 scopus 로고
    • Why 11-cis retinal?
    • Nakanishi, K. 1991. Why 11-cis retinal? Am. Zool. 31:479-489.
    • (1991) Am. Zool. , vol.31 , pp. 479-489
    • Nakanishi, K.1
  • 67
    • 33847086787 scopus 로고
    • An external point-charge model for bacteriorhodopsin to account for its purple color
    • Nakanishi, K., V. Balogh-Nair, M. Arnaboldi, K. Tsujimoto, and B. Honig. 1980. An external point-charge model for bacteriorhodopsin to account for its purple color. J. Am. Chem. Soc. 102:7945-7947.
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 7945-7947
    • Nakanishi, K.1    Balogh-Nair, V.2    Arnaboldi, M.3    Tsujimoto, K.4    Honig, B.5
  • 69
    • 85005558631 scopus 로고
    • Application of artificial pigments to structure determination and study of photoinduced transformations of retinal proteins
    • Nakanishi, K., and R. K. Crouch. 1995. Application of artificial pigments to structure determination and study of photoinduced transformations of retinal proteins. Isr. J. Chem. 35:253-272.
    • (1995) Isr. J. Chem. , vol.35 , pp. 253-272
    • Nakanishi, K.1    Crouch, R.K.2
  • 70
    • 0025050478 scopus 로고
    • Orientation of retinal in bovine rhodopsin determined by cross-linking using a photoactivatable analog of 11-cis-retinal
    • Nakayama, T. A., and H. G. Khorana. 1990. Orientation of retinal in bovine rhodopsin determined by cross-linking using a photoactivatable analog of 11-cis-retinal. J. Biol. Chem. 265:15762-15769.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15762-15769
    • Nakayama, T.A.1    Khorana, H.G.2
  • 71
    • 0025761854 scopus 로고
    • Mapping of the amino acids in membrane-embedded helices that interact with the retinal chromophore in bovine rhodopsin
    • Nakayama, T. A., and H. G. Khorana. 1991. Mapping of the amino acids in membrane-embedded helices that interact with the retinal chromophore in bovine rhodopsin. J. Biol. Chem. 266:4269-4275.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4269-4275
    • Nakayama, T.A.1    Khorana, H.G.2
  • 72
    • 0025012994 scopus 로고
    • Determinants of visual pigment absorbance: Role of charged amino acids in the putative transmembrane segments
    • Nathans, J. 1990a. Determinants of visual pigment absorbance: role of charged amino acids in the putative transmembrane segments. Biochemistry. 29:937-942.
    • (1990) Biochemistry , vol.29 , pp. 937-942
    • Nathans, J.1
  • 73
    • 0025162902 scopus 로고
    • Determinants of visual pigment absorbance: Identification of the retinylidene Schiff's base counterion in bovine rhodopsin
    • Nathans, J. 1990b. Determinants of visual pigment absorbance: identification of the retinylidene Schiff's base counterion in bovine rhodopsin. Biochemistry. 29:9746-9752.
    • (1990) Biochemistry , vol.29 , pp. 9746-9752
    • Nathans, J.1
  • 74
    • 0025729153 scopus 로고
    • Spectral tuning of pigments underlying red-green color vision
    • Neitz, M., J. Neitz, and G. H. Jacobs. 1991. Spectral tuning of pigments underlying red-green color vision. Science. 252:971-974.
    • (1991) Science , vol.252 , pp. 971-974
    • Neitz, M.1    Neitz, J.2    Jacobs, G.H.3
  • 75
    • 0024452437 scopus 로고
    • Purification of cone visual pigments from chicken retina
    • Okano, T., Y. Fukada, I. D. Artamonov, and T. Yoshizawa. 1989. Purification of cone visual pigments from chicken retina. Biochemistry. 28: 8848-8856.
    • (1989) Biochemistry , vol.28 , pp. 8848-8856
    • Okano, T.1    Fukada, Y.2    Artamonov, I.D.3    Yoshizawa, T.4
  • 76
    • 0026665777 scopus 로고
    • Primary structures of chicken cone visual pigments: Vertebrate rhodopsins have evolved out of cone visual pigments
    • Okano, T., D. Kojima, Y. Fukada, Y. Shichida, and T. Yoshizawa. 1992a. Primary structures of chicken cone visual pigments: vertebrate rhodopsins have evolved out of cone visual pigments. Proc. Natl. Acad. Sci. USA. 89:5932-5936.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5932-5936
    • Okano, T.1    Kojima, D.2    Fukada, Y.3    Shichida, Y.4    Yoshizawa, T.5
  • 78
    • 0032031426 scopus 로고    scopus 로고
    • Spectral and polarization sensitivity of photocurrents of amphibian rods in the visible and ultraviolet
    • Palacios, A. G., R. Srivastava, and T. H. Goldsmith. 1998. Spectral and polarization sensitivity of photocurrents of amphibian rods in the visible and ultraviolet. Vis. Neurosci. 15:319-331.
    • (1998) Vis. Neurosci. , vol.15 , pp. 319-331
    • Palacios, A.G.1    Srivastava, R.2    Goldsmith, T.H.3
  • 80
    • 0343177634 scopus 로고
    • Glutamic acid-113 serves as the retinylidene Schiff base counterion in bovine rhodopsin
    • Sakmar, T. P., R. R. Franke, and H. G. Khorana. 1989. Glutamic acid-113 serves as the retinylidene Schiff base counterion in bovine rhodopsin. Proc. Natl. Acad. Sci. USA. 86:8309-8313.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 8309-8313
    • Sakmar, T.P.1    Franke, R.R.2    Khorana, H.G.3
  • 81
    • 0031566429 scopus 로고    scopus 로고
    • The steric trigger in rhodopsin activation
    • Shieh, T., M. Han, T. P. Sakmar, and S. O. Smith. 1997. The steric trigger in rhodopsin activation. J. Mol. Biol. 269:373-384.
    • (1997) J. Mol. Biol. , vol.269 , pp. 373-384
    • Shieh, T.1    Han, M.2    Sakmar, T.P.3    Smith, S.O.4
  • 83
    • 0030786395 scopus 로고    scopus 로고
    • Mechanisms of spectral tuning in the mouse green cone pigment
    • Sun, H., J. P. Macke, and J. Nathans. 1997. Mechanisms of spectral tuning in the mouse green cone pigment. Proc. Natl. Acad. Sci. USA. 94: 8860-8865.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 8860-8865
    • Sun, H.1    Macke, J.P.2    Nathans, J.3
  • 84
    • 0344035075 scopus 로고
    • The structure of 1-acetyl-2-methylcyclohexene: Spectral characteristics of s-cis-α,β-unsaturated ketones
    • Turner, R. B., and D. M. Voitle. 1951. The structure of 1-acetyl-2-methylcyclohexene: spectral characteristics of s-cis-α,β-unsaturated ketones. J. Am. Chem. Soc. 73:1403-1410.
    • (1951) J. Am. Chem. Soc. , vol.73 , pp. 1403-1410
    • Turner, R.B.1    Voitle, D.M.2
  • 85
    • 33845375680 scopus 로고
    • Retinal analogues with locked 6-7 conformations show that bacteriorhodopsin requires the 6-s-trans conformation of the chromophore
    • van der Steen, R., P. L. Biesheuvel, R. A. Mathies, and J. Lugtenburg. 1986. Retinal analogues with locked 6-7 conformations show that bacteriorhodopsin requires the 6-s-trans conformation of the chromophore. J. Am. Chem. Soc. 108:6410-6411.
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 6410-6411
    • Van Der Steen, R.1    Biesheuvel, P.L.2    Mathies, R.A.3    Lugtenburg, J.4
  • 86
    • 0039196399 scopus 로고
    • Vision
    • Wald, G. 1953. Vision. Fed. Proc. 12:606-611.
    • (1953) Fed. Proc. , vol.12 , pp. 606-611
    • Wald, G.1
  • 87
    • 0032527219 scopus 로고    scopus 로고
    • Molecular cloning of the salamander red and blue cone visual pigments
    • Xu, L., E. S. Hazard, III, D. K. Lockman, R. K. Crouch, and J.-X. Ma. 1998. Molecular cloning of the salamander red and blue cone visual pigments. Mol. Vis. 4.
    • (1998) Mol. Vis. , vol.4
    • Xu, L.1    Hazard E.S. III2    Lockman, D.K.3    Crouch, R.K.4    Ma, J.-X.5
  • 88
    • 0020957807 scopus 로고
    • Activation of phosphodiesterase by rhodopsin and its analogues
    • Yoshizawa, T., and Y. Fukada. 1983. Activation of phosphodiesterase by rhodopsin and its analogues. Biophys. Struct. Mech. 9:245-258.
    • (1983) Biophys. Struct. Mech. , vol.9 , pp. 245-258
    • Yoshizawa, T.1    Fukada, Y.2
  • 90
    • 0024362631 scopus 로고
    • Effect of carboxylic acid side chains on the absorption maximum of visual pigments
    • Zhukovsky, E. A., and D. D. Oprian. 1989. Effect of carboxylic acid side chains on the absorption maximum of visual pigments. Science. 246: 928-930.
    • (1989) Science , vol.246 , pp. 928-930
    • Zhukovsky, E.A.1    Oprian, D.D.2


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