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Volumn 1837, Issue 5, 2014, Pages 664-673

Cone visual pigments

Author keywords

Color vision; G protein coupled receptors; Molecular evolution; Opsin family; Retina; Rhodopsin

Indexed keywords

11 CIS RETINAL; CIS TRANS ISOMERASE; CONE VISUAL PIGMENT; COUNTERION; G PROTEIN COUPLED RECEPTOR; GUANINE NUCLEOTIDE BINDING PROTEIN; RHODOPSIN; UNCLASSIFIED DRUG; VISUAL PIGMENT;

EID: 84897114888     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2013.08.009     Document Type: Review
Times cited : (65)

References (105)
  • 1
    • 0014411230 scopus 로고
    • Molecular basis of visual excitation
    • G. Wald Molecular basis of visual excitation Science 162 1968 230 239
    • (1968) Science , vol.162 , pp. 230-239
    • Wald, G.1
  • 2
    • 0001964739 scopus 로고
    • Visual pigments in human and monkey retinas
    • P.K. Brown, and G. Wald Visual pigments in human and monkey retinas Nature 200 1963 37 43
    • (1963) Nature , vol.200 , pp. 37-43
    • Brown, P.K.1    Wald, G.2
  • 3
    • 0000655941 scopus 로고
    • Visual pigments of single primate cones
    • W.B. Marks, W.H. Dobelle, and E.F. Macnichol Jr. Visual pigments of single primate cones Science 143 1964 1181 1183
    • (1964) Science , vol.143 , pp. 1181-1183
    • Marks, W.B.1    Dobelle, W.H.2    Macnichol, Jr.E.F.3
  • 4
    • 0014111617 scopus 로고
    • Spectral response curves of single cones in the carp
    • T. Tomita, A. Kaneko, M. Murakami, and E.L. Pautler Spectral response curves of single cones in the carp Vision Res. 7 1967 519 531
    • (1967) Vision Res. , vol.7 , pp. 519-531
    • Tomita, T.1    Kaneko, A.2    Murakami, M.3    Pautler, E.L.4
  • 5
    • 0024452437 scopus 로고
    • Purification of cone visual pigments from chicken retina
    • T. Okano, Y. Fukada, I.D. Artamonov, and T. Yoshizawa Purification of cone visual pigments from chicken retina Biochemistry 28 1989 8848 8856 (Pubitemid 19278546)
    • (1989) Biochemistry , vol.28 , Issue.22 , pp. 8848-8856
    • Okano, T.1    Fukada, Y.2    Artamonov, I.D.3    Yoshizawa, T.4
  • 7
    • 0027484909 scopus 로고
    • Nanosecond laser photolysis of iodopsin, a chicken red-sensitive cone visual pigment
    • DOI 10.1021/bi00091a039
    • Y. Shichida, T. Okada, H. Kandori, Y. Fukada, and T. Yoshizawa Nanosecond laser photolysis of iodopsin, a chicken red-sensitive cone visual pigment Biochemistry 32 1993 10832 10838 (Pubitemid 23327821)
    • (1993) Biochemistry , vol.32 , Issue.40 , pp. 10832-10838
    • Shichida, Y.1    Okada, T.2    Kandori, H.3    Fukada, Y.4    Yoshizawa, T.5
  • 10
    • 0026665777 scopus 로고
    • Primary structures of chicken cone visual pigments: Vertebrate rhodopsins have evolved out of cone visual pigments
    • T. Okano, D. Kojima, Y. Fukada, Y. Shichida, and T. Yoshizawa Primary structures of chicken cone visual pigments: vertebrate rhodopsins have evolved out of cone visual pigments Proc. Natl. Acad. Sci. U. S. A. 89 1992 5932 5936
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 5932-5936
    • Okano, T.1    Kojima, D.2    Fukada, Y.3    Shichida, Y.4    Yoshizawa, T.5
  • 11
    • 0004155427 scopus 로고
    • 3rd ed. W. H. Freeman New York
    • L. Stryer Biochemistry 3rd ed. 1988 W. H. Freeman New York
    • (1988) Biochemistry
    • Stryer, L.1
  • 12
    • 0028143702 scopus 로고
    • Pinopsin is a chicken pineal photoreceptive molecule
    • DOI 10.1038/372094a0
    • T. Okano, T. Yoshizawa, and Y. Fukada Pinopsin is a chicken pineal photoreceptive molecule Nature 372 1994 94 97 (Pubitemid 24339489)
    • (1994) Nature , vol.372 , Issue.6501 , pp. 94-97
    • Okano, T.1    Yoshizawa, T.2    Fukada, Y.3
  • 13
    • 0030728953 scopus 로고    scopus 로고
    • Parapinopsin, a novel catfish opsin localized to the parapineal organ, defines a new gene family
    • S. Blackshaw, and S.H. Snyder Parapinopsin, a novel catfish opsin localized to the parapineal organ, defines a new gene family J. Neurosci. 17 1997 8083 8092 (Pubitemid 27461033)
    • (1997) Journal of Neuroscience , vol.17 , Issue.21 , pp. 8083-8092
    • Blackshaw, S.1    Snyder, S.H.2
  • 14
    • 0031001703 scopus 로고    scopus 로고
    • A novel and ancient vertebrate opsin
    • DOI 10.1016/S0014-5793(97)00287-1, PII S0014579397002871
    • B.G. Soni, and R.G. Foster A novel and ancient vertebrate opsin FEBS Lett. 406 1997 279 283 (Pubitemid 27166311)
    • (1997) FEBS Letters , vol.406 , Issue.3 , pp. 279-283
    • Soni, B.G.1    Foster, R.G.2
  • 16
    • 0034687783 scopus 로고    scopus 로고
    • Highly conserved glutamic acid in the extracellular IV-V loop in rhodopsins acts as the counterion in retinochrome, a member of the rhodopsin family
    • DOI 10.1073/pnas.260349597
    • A. Terakita, T. Yamashita, and Y. Shichida Highly conserved glutamic acid in the extracellular IV-V loop in rhodopsins acts as the counterion in retinochrome, a member of the rhodopsin family Proc. Natl. Acad. Sci. U. S. A. 97 2000 14263 14267 (Pubitemid 32016565)
    • (2000) Proceedings of the National Academy of Sciences of the United States of America , vol.97 , Issue.26 , pp. 14263-14267
    • Terakita, A.1    Yamashita, T.2    Shichida, Y.3
  • 22
    • 82455219019 scopus 로고    scopus 로고
    • Vertebrate ancient-long opsin has molecular properties intermediate between those of vertebrate and invertebrate visual pigments
    • K. Sato, T. Yamashita, H. Ohuchi, and Y. Shichida Vertebrate ancient-long opsin has molecular properties intermediate between those of vertebrate and invertebrate visual pigments Biochemistry 50 2011 10484 10490
    • (2011) Biochemistry , vol.50 , pp. 10484-10490
    • Sato, K.1    Yamashita, T.2    Ohuchi, H.3    Shichida, Y.4
  • 23
    • 34247228082 scopus 로고    scopus 로고
    • Coupling of protonation switches during rhodopsin activation
    • DOI 10.1562/2006-06-19-IR-937
    • R. Vogel, T.P. Sakmar, M. Sheves, and F. Siebert Coupling of protonation switches during rhodopsin activation Photochem. Photobiol. 83 2007 286 292 (Pubitemid 46623067)
    • (2007) Photochemistry and Photobiology , vol.83 , Issue.2 , pp. 286-292
    • Vogel, R.1    Sakmar, T.P.2    Sheves, M.3    Siebert, F.4
  • 25
    • 84861607531 scopus 로고    scopus 로고
    • Comparative studies on the late bleaching processes of four kinds of cone visual pigments and rod visual pigment
    • K. Sato, T. Yamashita, Y. Imamoto, and Y. Shichida Comparative studies on the late bleaching processes of four kinds of cone visual pigments and rod visual pigment Biochemistry 51 2012 4300 4308
    • (2012) Biochemistry , vol.51 , pp. 4300-4308
    • Sato, K.1    Yamashita, T.2    Imamoto, Y.3    Shichida, Y.4
  • 27
    • 0028027080 scopus 로고
    • Is chicken green-sensitive cone visual pigment a rhodopsin-like pigment? A comparative study of the molecular properties between chicken green and rhodopsin
    • Y. Shichida, H. Imai, Y. Imamoto, Y. Fukada, and T. Yoshizawa Is chicken green-sensitive cone visual pigment a rhodopsin-like pigment? A comparative study of the molecular properties between chicken green and rhodopsin Biochemistry 33 1994 9040 9044 (Pubitemid 24272850)
    • (1994) Biochemistry , vol.33 , Issue.31 , pp. 9040-9044
    • Shichida, Y.1    Imai, H.2    Imamoto, Y.3    Fukada, Y.4    Yoshizawa, T.5
  • 28
    • 0029128883 scopus 로고
    • Difference in molecular properties between chicken green and rhodopsin as related to the functional difference between cone and rod photoreceptor cells
    • H. Imai, Y. Imamoto, T. Yoshizawa, and Y. Shichida Difference in molecular properties between chicken green and rhodopsin as related to the functional difference between cone and rod photoreceptor cells Biochemistry 34 1995 10525 10531
    • (1995) Biochemistry , vol.34 , pp. 10525-10531
    • Imai, H.1    Imamoto, Y.2    Yoshizawa, T.3    Shichida, Y.4
  • 29
    • 0030717668 scopus 로고    scopus 로고
    • Photochemical and biochemical properties of chicken blue-sensitive cone visual pigment
    • DOI 10.1021/bi970809x
    • H. Imai, A. Terakita, S. Tachibanaki, Y. Imamoto, T. Yoshizawa, and Y. Shichida Photochemical and biochemical properties of chicken blue-sensitive cone visual pigment Biochemistry 36 1997 12773 12779 (Pubitemid 27465387)
    • (1997) Biochemistry , vol.36 , Issue.42 , pp. 12773-12779
    • Imai, H.1    Terakita, A.2    Tachibanaki, S.3    Imamoto, Y.4    Yoshizawa, T.5    Shichida, Y.6
  • 30
    • 0141894860 scopus 로고    scopus 로고
    • Role of visual pigment properties in rod and cone phototransduction
    • DOI 10.1038/nature01992
    • V. Kefalov, Y. Fu, N. Marsh-Armstrong, and K.W. Yau Role of visual pigment properties in rod and cone phototransduction Nature 425 2003 526 531 (Pubitemid 37237049)
    • (2003) Nature , vol.425 , Issue.6957 , pp. 526-531
    • Kefalov, V.1    Fu, Y.2    Marsh-Amstrong, N.3    Yau, K.-W.4
  • 31
    • 34548822133 scopus 로고    scopus 로고
    • Signaling properties of a short-wave cone visual pigment and its role in phototransduction
    • DOI 10.1523/JNEUROSCI.2211-07.2007
    • G. Shi, K.W. Yau, J. Chen, and V.J. Kefalov Signaling properties of a short-wave cone visual pigment and its role in phototransduction J. Neurosci. 27 2007 10084 10093 (Pubitemid 47450451)
    • (2007) Journal of Neuroscience , vol.27 , Issue.38 , pp. 10084-10093
    • Shi, G.1    Yau, K.-W.2    Chen, J.3    Kefalov, V.J.4
  • 36
    • 0021748638 scopus 로고
    • Light-induced binding of 48-kDa protein to photoreceptor membranes is highly enhanced by phosphorylation of rhodopsin
    • DOI 10.1016/0014-5793(84)81221-1
    • H. Kühn, S.W. Hall, and U. Wilden Light-induced binding of 48-kDa protein to photoreceptor membranes is highly enhanced by phosphorylation of rhodopsin FEBS Lett. 176 1984 473 478 (Pubitemid 15208287)
    • (1984) FEBS Letters , vol.176 , Issue.2 , pp. 473-478
    • Kuhn, H.1    Hall, S.W.2    Wilden, U.3
  • 38
    • 0015837429 scopus 로고
    • Phosphorylation of rhodopsin in bovine photoreceptor membranes. A dark reaction after illumination
    • H. Kühn, J.H. Cook, and W.J. Dreyer Phosphorylation of rhodopsin in bovine photoreceptor membranes. A dark reaction after illumination Biochemistry 12 1973 2495 2502
    • (1973) Biochemistry , vol.12 , pp. 2495-2502
    • Kühn, H.1    Cook, J.H.2    Dreyer, W.J.3
  • 40
    • 0014194175 scopus 로고
    • Photochemistry of iodopsin
    • T. Yoshizawa, and G. Wald Photochemistry of iodopsin Nature 214 1967 566 571
    • (1967) Nature , vol.214 , pp. 566-571
    • Yoshizawa, T.1    Wald, G.2
  • 42
    • 0028316890 scopus 로고
    • What makes red visual pigments red? A resonance raman microprobe study of retinal chromophore structure in iodopsin
    • S.W. Lin, Y. Imamoto, Y. Fukada, Y. Shichida, T. Yoshizawa, and R.A. Mathies What makes red visual pigments red? A resonance Raman microprobe study of retinal chromophore structure in iodopsin Biochemistry 33 1994 2151 2160 (Pubitemid 24099612)
    • (1994) Biochemistry , vol.33 , Issue.8 , pp. 2151-2160
    • Lin, S.W.1    Imamoto, Y.2    Fukada, Y.3    Shichida, Y.4    Yoshizawa, T.5    Mathies, R.A.6
  • 43
    • 37049065785 scopus 로고
    • Pre-lumirhodopsin and the bleaching of visual pigments
    • T. Yoshizawa, and G. Wald Pre-lumirhodopsin and the bleaching of visual pigments Nature 197 1963 1279 1286
    • (1963) Nature , vol.197 , pp. 1279-1286
    • Yoshizawa, T.1    Wald, G.2
  • 44
    • 0030461341 scopus 로고    scopus 로고
    • Chromophore configuration of iodopsin and its photoproducts formed at low temperatures
    • DOI 10.1021/bi9614850
    • Y. Imamoto, T. Yoshizawa, and Y. Shichida Chromophore configuration of iodopsin and its photoproducts formed at low temperatures Biochemistry 35 1996 14599 14607 (Pubitemid 26423720)
    • (1996) Biochemistry , vol.35 , Issue.46 , pp. 14599-14607
    • Imamoto, Y.1    Yoshizawa, T.2    Shichida, Y.3
  • 45
    • 84859166126 scopus 로고    scopus 로고
    • Schiff base protonation changes in Siberian hamster ultraviolet cone pigment photointermediates
    • V.L. Mooney, I. Szundi, J.W. Lewis, E.C. Yan, and D.S. Kliger Schiff base protonation changes in Siberian hamster ultraviolet cone pigment photointermediates Biochemistry 51 2012 2630 2637
    • (2012) Biochemistry , vol.51 , pp. 2630-2637
    • Mooney, V.L.1    Szundi, I.2    Lewis, J.W.3    Yan, E.C.4    Kliger, D.S.5
  • 46
    • 0024350856 scopus 로고
    • Effect of chloride ion on the thermal decay process of the batho intermediate of iodopsin at low temperature
    • DOI 10.1021/bi00450a025
    • Y. Imamoto, H. Kandori, T. Okano, Y. Fukada, Y. Shichida, and T. Yoshizawa Effect of chloride ion on the thermal decay process of the batho intermediate of iodopsin at low temperature Biochemistry 28 1989 9412 9416 (Pubitemid 20000716)
    • (1989) Biochemistry , vol.28 , Issue.24 , pp. 9412-9416
    • Imamoto, Y.1    Kandori, H.2    Okano, T.3    Fukada, Y.4    Shichida, Y.5    Yoshizawa, T.6
  • 47
    • 0027944844 scopus 로고
    • Thermal recovery of iodopsin from its meta I-intermediate
    • DOI 10.1016/0014-5793(94)01112-5
    • Y. Imamoto, H. Imai, T. Yoshizawa, and Y. Shichida Thermal recovery of iodopsin from its meta I-intermediate FEBS Lett. 354 1994 165 168 (Pubitemid 24335499)
    • (1994) FEBS Letters , vol.354 , Issue.2 , pp. 165-168
    • Shichida, Y.1
  • 48
    • 52149119639 scopus 로고    scopus 로고
    • Thermal recovery of iodopsin from photobleaching intermediates
    • Y. Imamoto, and Y. Shichida Thermal recovery of iodopsin from photobleaching intermediates Photochem. Photobiol. 84 2008 941 948
    • (2008) Photochem. Photobiol. , vol.84 , pp. 941-948
    • Imamoto, Y.1    Shichida, Y.2
  • 50
    • 33746321096 scopus 로고    scopus 로고
    • Crystallographic analysis of primary visual photochemistry
    • DOI 10.1002/anie.200600595
    • H. Nakamichi, and T. Okada Crystallographic analysis of primary visual photochemistry Angew. Chem. Int. Ed. Engl. 45 2006 4270 4273 (Pubitemid 44105630)
    • (2006) Angewandte Chemie - International Edition , vol.45 , Issue.26 , pp. 4270-4273
    • Nakamichi, H.1    Okada, T.2
  • 52
    • 84861354678 scopus 로고    scopus 로고
    • Rapid release of retinal from a cone visual pigment following photoactivation
    • M.H. Chen, C. Kuemmel, R.R. Birge, and B.E. Knox Rapid release of retinal from a cone visual pigment following photoactivation Biochemistry 51 2012 4117 4125
    • (2012) Biochemistry , vol.51 , pp. 4117-4125
    • Chen, M.H.1    Kuemmel, C.2    Birge, R.R.3    Knox, B.E.4
  • 53
    • 84877028283 scopus 로고    scopus 로고
    • Efficiencies of activation of transducin by cone and rod visual pigments
    • Y. Imamoto, I. Seki, T. Yamashita, and Y. Shichida Efficiencies of activation of transducin by cone and rod visual pigments Biochemistry 52 2013 3010 3018
    • (2013) Biochemistry , vol.52 , pp. 3010-3018
    • Imamoto, Y.1    Seki, I.2    Yamashita, T.3    Shichida, Y.4
  • 55
    • 0027992847 scopus 로고
    • Direct observation of the thermal equilibria among lumirhodopsin, metarhodopsin I, and metarhodopsin II in chicken rhodopsin
    • DOI 10.1021/bi00251a049
    • H. Imai, T. Mizukami, Y. Imamoto, and Y. Shichida Direct observation of the thermal equilibria among lumirhodopsin, metarhodopsin I, and metarhodopsin II in chicken rhodopsin Biochemistry 33 1994 14351 14358 (Pubitemid 24382383)
    • (1994) Biochemistry , vol.33 , Issue.47 , pp. 14351-14358
    • Imai, H.1    Mizukami, T.2    Imamoto, Y.3    Shichida, Y.4
  • 56
    • 75149166607 scopus 로고    scopus 로고
    • Direct observation of the pH-dependent equilibrium between metarhodopsins i and II and the pH-independent interaction of metarhodopsin II with transducin C-terminal peptide
    • K. Sato, T. Morizumi, T. Yamashita, and Y. Shichida Direct observation of the pH-dependent equilibrium between metarhodopsins I and II and the pH-independent interaction of metarhodopsin II with transducin C-terminal peptide Biochemistry 49 2010 736 741
    • (2010) Biochemistry , vol.49 , pp. 736-741
    • Sato, K.1    Morizumi, T.2    Yamashita, T.3    Shichida, Y.4
  • 57
    • 0029907599 scopus 로고    scopus 로고
    • Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin
    • DOI 10.1126/science.274.5288.768
    • D.L. Farrens, C. Altenbach, K. Yang, W.L. Hubbell, and H.G. Khorana Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin Science 274 1996 768 770 (Pubitemid 26398253)
    • (1996) Science , vol.274 , Issue.5288 , pp. 768-770
    • Farrens, D.L.1    Altenbach, C.2    Yang, K.3    Hubbell, W.L.4    Khorana, H.G.5
  • 60
    • 45849129020 scopus 로고    scopus 로고
    • Rod and cone photoreceptors: Molecular basis of the difference in their physiology
    • S. Kawamura, and S. Tachibanaki Rod and cone photoreceptors: molecular basis of the difference in their physiology Comp. Biochem. Physiol. A Mol. Integr. Physiol. 150 2008 369 377
    • (2008) Comp. Biochem. Physiol. A Mol. Integr. Physiol. , vol.150 , pp. 369-377
    • Kawamura, S.1    Tachibanaki, S.2
  • 63
    • 0037168497 scopus 로고    scopus 로고
    • Conserved proline residue at position 189 in cone visual pigments as a determinant of molecular properties different from rhodopsins
    • DOI 10.1021/bi026444k
    • S. Kuwayama, H. Imai, T. Hirano, A. Terakita, and Y. Shichida Conserved proline residue at position 189 in cone visual pigments as a determinant of molecular properties different from rhodopsins Biochemistry 41 2002 15245 15252 (Pubitemid 36008133)
    • (2002) Biochemistry , vol.41 , Issue.51 , pp. 15245-15252
    • Kuwayama, S.1    Imai, H.2    Hirano, T.3    Terakita, A.4    Shichida, Y.5
  • 64
    • 13544272595 scopus 로고    scopus 로고
    • Amino acid residues responsible for the meta-III decay rates in rod and cone visual pigments
    • DOI 10.1021/bi047994g
    • S. Kuwayama, H. Imai, T. Morizumi, and Y. Shichida Amino acid residues responsible for the meta-III decay rates in rod and cone visual pigments Biochemistry 44 2005 2208 2215 (Pubitemid 40223648)
    • (2005) Biochemistry , vol.44 , Issue.6 , pp. 2208-2215
    • Kuwayama, S.1    Imai, H.2    Morizumi, T.3    Shichida, Y.4
  • 66
    • 0001566840 scopus 로고
    • The biochemistry of vision
    • G. Wald The biochemistry of vision Annu. Rev. Biochem. 22 1953 497 526
    • (1953) Annu. Rev. Biochem. , vol.22 , pp. 497-526
    • Wald, G.1
  • 67
    • 0022696951 scopus 로고
    • Molecular genetics of inherited variation in human color vision
    • J. Nathans, T.P. Piantanida, R.L. Eddy, T.B. Shows, and D.S. Hogness Molecular genetics of inherited variation in human color vision Science 232 1986 203 210 (Pubitemid 16046601)
    • (1986) Science , vol.232 , Issue.4747 , pp. 203-210
    • Nathans, J.1    Piantanida, T.P.2    Eddy, R.L.3
  • 68
    • 0022695490 scopus 로고
    • Molecular genetics of human color vision: The genes encoding blue, green, and red pigments
    • J. Nathans, D. Thomas, and D.S. Hogness Molecular genetics of human color vision: the genes encoding blue, green, and red pigments Science 232 1986 193 202 (Pubitemid 16046600)
    • (1986) Science , vol.232 , Issue.4747 , pp. 193-202
    • Nathans, J.1    Thomas, D.2    Hogness, D.S.3
  • 69
    • 0021686079 scopus 로고
    • Chromatographic resolution of the rod pigment from the four cone pigments of the chicken retina
    • DOI 10.1016/S0042-6989(84)80005-X
    • L. Yen, and R.S. Fager Chromatographic resolution of the rod pigment from the four cone pigments of the chicken retina Vision Res. 24 1984 1555 1562 (Pubitemid 15181712)
    • (1984) Vision Research , vol.24 , Issue.11 , pp. 1555-1562
    • Lei Yen1    Fager, R.S.2
  • 70
    • 0020018792 scopus 로고
    • Chromatographic separation of rod and cone pigments from chicken retinas
    • L.Y. Fager, and R.S. Fager Chromatographic separation of rod and cone pigments from chicken retinas Methods Enzymol. 81 1982 160 166
    • (1982) Methods Enzymol. , vol.81 , pp. 160-166
    • Fager, L.Y.1    Fager, R.S.2
  • 73
    • 0001344032 scopus 로고
    • Methodology of vitamin A and visual pigments
    • R. Hubbard, P.K. Brown, and D. Bownds Methodology of vitamin A and visual pigments Methods Enzymol. 18 1971 615 653
    • (1971) Methods Enzymol. , vol.18 , pp. 615-653
    • Hubbard, R.1    Brown, P.K.2    Bownds, D.3
  • 74
    • 0000480719 scopus 로고
    • Synthesis and photochemistry of stereoisomers of retinal
    • R.S.H. Liu, and A.E. Asato Synthesis and photochemistry of stereoisomers of retinal Methods Enzymol. 88 1982 506 516
    • (1982) Methods Enzymol. , vol.88 , pp. 506-516
    • Liu, R.S.H.1    Asato, A.E.2
  • 75
    • 0015528085 scopus 로고
    • Anion-induced wavelength regulation of absorption maxima of Schiff bases of retinal
    • P.E. Blatz, J.H. Mohler, and H.V. Navangul Anion-induced wavelength regulation of absorption maxima of Schiff bases of retinal Biochemistry 11 1972 848 855
    • (1972) Biochemistry , vol.11 , pp. 848-855
    • Blatz, P.E.1    Mohler, J.H.2    Navangul, H.V.3
  • 76
    • 0017171319 scopus 로고
    • Visual-pigment spectra: Implications of the protonation of the retinal Schiff base
    • B. Honig, A.D. Greenberg, U. Dinur, and T.G. Ebrey Visual-pigment spectra: implications of the protonation of the retinal Schiff base Biochemistry 15 1976 4593 4599
    • (1976) Biochemistry , vol.15 , pp. 4593-4599
    • Honig, B.1    Greenberg, A.D.2    Dinur, U.3    Ebrey, T.G.4
  • 77
    • 0027960310 scopus 로고
    • Phylogenetic relationships among vertebrate visual pigments
    • DOI 10.1016/0042-6989(94)90075-2
    • O. Hisatomi, S. Kayada, Y. Aoki, T. Iwasa, and F. Tokunaga Phylogenetic relationships among vertebrate visual pigments Vision Res. 34 1994 3097 3102 (Pubitemid 24325225)
    • (1994) Vision Research , vol.34 , Issue.23 , pp. 3097-3102
    • Hisatomi, O.1    Kayada, S.2    Aoki, Y.3    Iwasa, T.4    Tokunaga, F.5
  • 78
    • 0025729153 scopus 로고
    • Spectral tuning of pigments underlying red-green color vision
    • M. Neitz, J. Neitz, and G.H. Jacobs Spectral tuning of pigments underlying red-green color vision Science 252 1991 971 974 (Pubitemid 21917017)
    • (1991) Science , vol.252 , Issue.5008 , pp. 971-974
    • Neitz, M.1    Neitz, J.2    Jacobs, G.H.3
  • 79
    • 0028289475 scopus 로고
    • Molecular determinants of human red/green color discrimination
    • DOI 10.1016/0896-6273(94)90320-4
    • A.B. Asenjo, J. Rim, and D.D. Oprian Molecular determinants of human red/green color discrimination Neuron 12 1994 1131 1138 (Pubitemid 24178204)
    • (1994) Neuron , vol.12 , Issue.5 , pp. 1131-1138
    • Asenjo, A.B.1    Rim, J.2    Oprian, D.D.3
  • 80
    • 0030970581 scopus 로고    scopus 로고
    • Resonance raman examination of the wavelength regulation mechanism in human visual pigments
    • DOI 10.1021/bi970322o
    • G.G. Kochendoerfer, Z. Wang, D.D. Oprian, and R.A. Mathies Resonance Raman examination of the wavelength regulation mechanism in human visual pigments Biochemistry 36 1997 6577 6587 (Pubitemid 27242315)
    • (1997) Biochemistry , vol.36 , Issue.22 , pp. 6577-6587
    • Kochendoerfer, G.G.1    Wang, Z.2    Oprian, D.D.3    Mathies, R.A.4
  • 81
    • 2642608655 scopus 로고    scopus 로고
    • The 'five-sites' rule and the evolution of red and green color vision in mammals
    • S. Yokoyama, and F.B. Radlwimmer The "five-sites" rule and the evolution of red and green color vision in mammals Mol. Biol. Evol. 15 1998 560 567 (Pubitemid 28194620)
    • (1998) Molecular Biology and Evolution , vol.15 , Issue.5 , pp. 560-567
    • Yokoyama, S.1    Bernhard Radlwimmer, F.2
  • 83
    • 0017367128 scopus 로고
    • Ionochromic behavior of Gecko visual pigments
    • F. Crescitelli Ionochromic behavior of Grecko visual pigments Science 195 1977 187 188 (Pubitemid 8012000)
    • (1977) Science , vol.195 , Issue.4274 , pp. 187-188
    • Crescitelli, F.1
  • 84
    • 0019126855 scopus 로고
    • The Gecko visual pigments: The nitrate effect
    • DOI 10.1016/0042-6989(80)90075-9
    • F. Crescitelli The gecko visual pigments: the nitrate effect Vision Res. 20 1980 937 945 (Pubitemid 11232067)
    • (1980) Vision Research , vol.20 , Issue.11 , pp. 937-945
    • Crescitelli, F.1
  • 85
    • 0017088913 scopus 로고
    • The effects of chloride ion upon chicken visual pigments
    • A. Knowles The effects of chloride ion upon chicken visual pigments Biochem. Biophys. Res. Commun. 73 1976 56 62
    • (1976) Biochem. Biophys. Res. Commun. , vol.73 , pp. 56-62
    • Knowles, A.1
  • 86
    • 0018625675 scopus 로고
    • Halide control of color of the chicken cone pigment idopsin
    • DOI 10.1016/0014-4835(79)90056-3
    • L.Y. Fager, and R.S. Fager Halide control of color of the chicken cone pigment iodopsin Exp. Eye Res. 29 1979 401 408 (Pubitemid 10206915)
    • (1979) Experimental Eye Research , vol.29 , Issue.4 , pp. 401-408
    • Fager, L.Y.1    Fager, R.S.2
  • 87
    • 0025368056 scopus 로고
    • Effects of chloride on chicken iodopsin and the chromophore transfer reactions from iodopsin to scotopsin and B-photopsin
    • DOI 10.1021/bi00476a028
    • Y. Shichida, T. Kato, S. Sasayama, Y. Fukada, and T. Yoshizawa Effects of chloride on chicken iodopsin and the chromophore transfer reactions from iodopsin to scotopsin and B-photopsin Biochemistry 29 1990 5843 5848 (Pubitemid 20192458)
    • (1990) Biochemistry , vol.29 , Issue.24 , pp. 5843-5848
    • Shichida, Y.1    Kato, T.2    Sasayama, S.3    Fukada, Y.4    Yoshizawa, T.5
  • 88
    • 0028825022 scopus 로고
    • Effect of chloride on the thermal reverse reaction of intermediates of iodopsin
    • S. Tachibanaki, Y. Imamoto, H. Imai, and Y. Shichida Effect of chloride on the thermal reverse reaction of intermediates of iodopsin Biochemistry 34 1995 13170 13175
    • (1995) Biochemistry , vol.34 , pp. 13170-13175
    • Tachibanaki, S.1    Imamoto, Y.2    Imai, H.3    Shichida, Y.4
  • 89
    • 0027410367 scopus 로고
    • --binding site in the human red and green color vision pigments
    • Z. Wang, A.B. Asenjo, and D.D. Oprian Identification of the Cl-binding site in the human red and green color vision pigments Biochemistry 32 1993 2125 2130 (Pubitemid 23094870)
    • (1993) Biochemistry , vol.32 , Issue.9 , pp. 2125-2130
    • Wang, Z.1    Asenjo, A.B.2    Oprian, D.D.3
  • 90
    • 84871300294 scopus 로고    scopus 로고
    • Spectroscopic analysis of the effect of chloride on the active intermediates of the primate L group cone visual pigment
    • T. Morizumi, K. Sato, and Y. Shichida Spectroscopic analysis of the effect of chloride on the active intermediates of the primate L group cone visual pigment Biochemistry 51 2012 10017 10023
    • (2012) Biochemistry , vol.51 , pp. 10017-10023
    • Morizumi, T.1    Sato, K.2    Shichida, Y.3
  • 91
    • 84874025028 scopus 로고    scopus 로고
    • Chloride-dependent spectral tuning mechanism of L-group cone visual pigments
    • T. Yamashita, S. Nakamura, K. Tsutsui, T. Morizumi, and Y. Shichida Chloride-dependent spectral tuning mechanism of L-group cone visual pigments Biochemistry 52 2013 1192 1197
    • (2013) Biochemistry , vol.52 , pp. 1192-1197
    • Yamashita, T.1    Nakamura, S.2    Tsutsui, K.3    Morizumi, T.4    Shichida, Y.5
  • 93
    • 0035814807 scopus 로고    scopus 로고
    • Chloride effect on iodopsin studied by low-temperature visible and infrared spectroscopies
    • DOI 10.1021/bi001332j
    • T. Hirano, H. Imai, H. Kandori, and Y. Shichida Chloride effect on iodopsin studied by low-temperature visible and infrared spectroscopies Biochemistry 40 2001 1385 1392 (Pubitemid 32142900)
    • (2001) Biochemistry , vol.40 , Issue.5 , pp. 1385-1392
    • Hirano, T.1    Imai, H.2    Kandori, H.3    Shichida, Y.4
  • 95
    • 0037202369 scopus 로고    scopus 로고
    • Molecular evolution of color vision in vertebrates
    • DOI 10.1016/S0378-1119(02)00845-4, PII S0378111902008454
    • S. Yokoyama Molecular evolution of color vision in vertebrates Gene 300 2002 69 78 (Pubitemid 35441162)
    • (2002) Gene , vol.300 , Issue.1-2 , pp. 69-78
    • Yokoyama, S.1
  • 96
    • 78649506250 scopus 로고    scopus 로고
    • Photosensitivities of rhodopsin mutants with a displaced counterion
    • K. Tsutsui, and Y. Shichida Photosensitivities of rhodopsin mutants with a displaced counterion Biochemistry 49 2010 10089 10097
    • (2010) Biochemistry , vol.49 , pp. 10089-10097
    • Tsutsui, K.1    Shichida, Y.2
  • 97
    • 34249666129 scopus 로고    scopus 로고
    • Photoisomerization efficiency in UV-absorbing visual pigments: Protein-directed isomerization of an unprotonated retinal Schiff base
    • DOI 10.1021/bi7003763
    • K. Tsutsui, H. Imai, and Y. Shichida Photoisomerization efficiency in UV-absorbing visual pigments: protein-directed isomerization of an unprotonated retinal Schiff base Biochemistry 46 2007 6437 6445 (Pubitemid 46842887)
    • (2007) Biochemistry , vol.46 , Issue.21 , pp. 6437-6445
    • Tsutsui, K.1    Imai, H.2    Shichida, Y.3
  • 98
    • 0033695109 scopus 로고    scopus 로고
    • Origin and functional impact of dark noise in retinal cones
    • F. Rieke, and D.A. Baylor Origin and functional impact of dark noise in retinal cones Neuron 26 2000 181 186
    • (2000) Neuron , vol.26 , pp. 181-186
    • Rieke, F.1    Baylor, D.A.2
  • 99
    • 79958711363 scopus 로고    scopus 로고
    • Activation of visual pigments by light and heat
    • D.G. Luo, W.W. Yue, P. Ala-Laurila, and K.W. Yau Activation of visual pigments by light and heat Science 332 2011 1307 1312
    • (2011) Science , vol.332 , pp. 1307-1312
    • Luo, D.G.1    Yue, W.W.2    Ala-Laurila, P.3    Yau, K.W.4
  • 100
    • 77952572623 scopus 로고    scopus 로고
    • Protein fluctuations as the possible origin of the thermal activation of rod photoreceptors in the dark
    • V.A. Lorenz-Fonfria, Y. Furutani, T. Ota, K. Ido, and H. Kandori Protein fluctuations as the possible origin of the thermal activation of rod photoreceptors in the dark J. Am. Chem. Soc. 132 2010 5693 5703
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 5693-5703
    • Lorenz-Fonfria, V.A.1    Furutani, Y.2    Ota, T.3    Ido, K.4    Kandori, H.5
  • 101
    • 0026352455 scopus 로고
    • Design, chemical synthesis, and expression of genes for the three human color vision pigments
    • D.D. Oprian, A.B. Asenjo, N. Lee, and S.L. Pelletier Design, chemical synthesis, and expression of genes for the three human color vision pigments Biochemistry 30 1991 11367 11372
    • (1991) Biochemistry , vol.30 , pp. 11367-11372
    • Oprian, D.D.1    Asenjo, A.B.2    Lee, N.3    Pelletier, S.L.4
  • 102
    • 0025972460 scopus 로고
    • Response properties of cones from the retina of the tiger salamander
    • R.J. Perry, and P.A. McNaughton Response properties of cones from the retina of the tiger salamander J. Physiol. 433 1991 561 587
    • (1991) J. Physiol. , vol.433 , pp. 561-587
    • Perry, R.J.1    McNaughton, P.A.2
  • 104
    • 0033651036 scopus 로고    scopus 로고
    • Visual pigment reconstitution in intact goldfish retina using synthetic retinaldehyde isomers
    • J.W. Parry, and J.K. Bowmaker Visual pigment reconstitution in intact goldfish retina using synthetic retinaldehyde isomers Vision Res. 40 2000 2241 2247
    • (2000) Vision Res. , vol.40 , pp. 2241-2247
    • Parry, J.W.1    Bowmaker, J.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.