메뉴 건너뛰기




Volumn 43, Issue 46, 2004, Pages 14802-14810

Constraints of the 9-methyl group binding pocket of the rhodopsin chromophore probed by 9-halogeno substitution

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; FOURIER TRANSFORM INFRARED SPECTROSCOPY; MATHEMATICAL MODELS; PHOTOCHEMICAL REACTIONS; PHOTOSENSITIVITY;

EID: 8744236234     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi048404h     Document Type: Article
Times cited : (8)

References (56)
  • 1
    • 0020488317 scopus 로고
    • Complex formation between metarhodopsin II and GTP-binding protein in bovine photoreceptor membranes leads to a shift of the photoproduct equilibrium
    • Emeis, D., Kühn, H., Reichert, J., and Hofmann, K. P. (1982) Complex formation between metarhodopsin II and GTP-binding protein in bovine photoreceptor membranes leads to a shift of the photoproduct equilibrium, FEBS Lett. 143, 29-34.
    • (1982) FEBS Lett. , vol.143 , pp. 29-34
    • Emeis, D.1    Kühn, H.2    Reichert, J.3    Hofmann, K.P.4
  • 3
    • 77956785528 scopus 로고    scopus 로고
    • Late photoproducts and signaling states of bovine rhodopsin
    • Stavenga, D. G., DeGrip, W. J., and Pugh, E. N., Jr., Eds. Elsevier Science Pub., Amsterdam, The Netherlands
    • Hofmann, K. P. (2000) Late photoproducts and signaling states of bovine rhodopsin, in Molecular Mechanisms in Visual Transduction (Stavenga, D. G., DeGrip, W. J., and Pugh, E. N., Jr., Eds.) pp 91-142, Elsevier Science Pub., Amsterdam, The Netherlands.
    • (2000) Molecular Mechanisms in Visual Transduction , pp. 91-142
    • Hofmann, K.P.1
  • 4
    • 77957112451 scopus 로고    scopus 로고
    • Structure and mechanism of vertebrate visual pigments
    • Stavenga, D. G., DeGrip, W. J., and Pugh, E. N., Jr., Eds, Elsevier Science Pub., Amsterdam, The Netherlands
    • DeGrip, W. J., and Rothschild, K. J. (2000) Structure and mechanism of vertebrate visual pigments, in Molecular Mechanisms in Visual Transduction (Stavenga, D. G., DeGrip, W. J., and Pugh, E. N., Jr., Eds,) pp 1-54, Elsevier Science Pub., Amsterdam, The Netherlands.
    • (2000) Molecular Mechanisms in Visual Transduction , pp. 1-54
    • DeGrip, W.J.1    Rothschild, K.J.2
  • 5
    • 70349536422 scopus 로고    scopus 로고
    • The primary photoreaction of rhodopsin
    • Stavenga, D. G., DeGrip, W. J., and Pugh, E. N., Jr., Eds. Elsevier Science Pub., Amsterdam, The Netherlands
    • Mathies, R. A., and Lugtenburg, J. (2000) The primary photoreaction of rhodopsin, in Molecular Mechanisms in Visual Transduction (Stavenga, D. G., DeGrip, W. J., and Pugh, E. N., Jr., Eds.) pp 55-90, Elsevier Science Pub., Amsterdam, The Netherlands.
    • (2000) Molecular Mechanisms in Visual Transduction , pp. 55-90
    • Mathies, R.A.1    Lugtenburg, J.2
  • 6
    • 0026316828 scopus 로고
    • Probing the visual pigment rhodopsin and its analogs by molecular modeling analysis and computer graphics
    • Mirzadegan, T., and Liu, R. S. H. (1991) Probing the visual pigment rhodopsin and its analogs by molecular modeling analysis and computer graphics, Prog. Retinal Eye Res. 11, 57-74.
    • (1991) Prog. Retinal Eye Res. , vol.11 , pp. 57-74
    • Mirzadegan, T.1    Liu, R.S.H.2
  • 9
    • 0024102514 scopus 로고
    • Photoexcitation of rhodopsin: Conformation changes in the chromophore, protein, and associated lipid, as determined by FTIR difference spectroscopy
    • DeGrip, W. J., Gray, D., Gillespie, J., Bovee-Geurts, P. H. M., VanDenBerg, E. M. M., Lugtenburg, J., and Rothschild, K. J. (1988) Photoexcitation of rhodopsin: Conformation changes in the chromophore, protein, and associated lipid, as determined by FTIR difference spectroscopy, Photochem. Photobiol. 48, 497-504.
    • (1988) Photochem. Photobiol. , vol.48 , pp. 497-504
    • DeGrip, W.J.1    Gray, D.2    Gillespie, J.3    Bovee-Geurts, P.H.M.4    VanDenBerg, E.M.M.5    Lugtenburg, J.6    Rothschild, K.J.7
  • 10
    • 85005746610 scopus 로고
    • Application of FTIR spectroscopy to the investigation of dark structures and photoreactions of visual pigments
    • Siebert, F. (1995) Application of FTIR spectroscopy to the investigation of dark structures and photoreactions of visual pigments, Isr. J. Chem. 35, 309-323.
    • (1995) Isr. J. Chem. , vol.35 , pp. 309-323
    • Siebert, F.1
  • 11
    • 0019333910 scopus 로고
    • Interpretation of the resonance Raman spectrum of bathorhodopsin based on visual pigment analogues
    • Eyring, G., Curry, B., Mathies, R. A., Fransen, R., Palings, I., and Lugtenburg, J. (1980) Interpretation of the resonance Raman spectrum of bathorhodopsin based on visual pigment analogues, Biochemistry 19, 2410-2418.
    • (1980) Biochemistry , vol.19 , pp. 2410-2418
    • Eyring, G.1    Curry, B.2    Mathies, R.A.3    Fransen, R.4    Palings, I.5    Lugtenburg, J.6
  • 12
    • 0020486598 scopus 로고
    • Assignment and interpretation of hydrogen out-of-plane vibrations in the resonance Raman spectra of rhodopsin and bathorhodopsin
    • Eyring, G., Curry, B., Broek, A., Lugtenburg, J., and Mathies, R. A. (1982) Assignment and interpretation of hydrogen out-of-plane vibrations in the resonance Raman spectra of rhodopsin and bathorhodopsin, Biochemistry 21, 384-393.
    • (1982) Biochemistry , vol.21 , pp. 384-393
    • Eyring, G.1    Curry, B.2    Broek, A.3    Lugtenburg, J.4    Mathies, R.A.5
  • 13
    • 0024550169 scopus 로고
    • Complete assignment of the hydrogen out-of-plane wagging vibrations of bathorhodopsin: Chromophore structure and energy storage in the primary photoproduct of vision
    • Palings, I., VanDenBerg, E. M. M., Lugtenburg, J., and Mathies, R. A. (1989) Complete assignment of the hydrogen out-of-plane wagging vibrations of bathorhodopsin: Chromophore structure and energy storage in the primary photoproduct of vision, Biochemistry 28, 1498-1507.
    • (1989) Biochemistry , vol.28 , pp. 1498-1507
    • Palings, I.1    VanDenBerg, E.M.M.2    Lugtenburg, J.3    Mathies, R.A.4
  • 14
    • 33845554105 scopus 로고
    • Energy storage and reaction pathways in the first step of the vision process
    • Warshel, A., and Barboy, N. (1982) Energy storage and reaction pathways in the first step of the vision process, J. Am. Chem. Soc. 104, 1469-1476.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 1469-1476
    • Warshel, A.1    Barboy, N.2
  • 15
    • 0023845290 scopus 로고
    • The nature of the primary photochemical events in rhodopsin and isorhodopsin
    • Birge, R. R., Einterz, C. M., Knapp, H. M., and Murray, L. P. (1988) The nature of the primary photochemical events in rhodopsin and isorhodopsin, Biophys. J. 53, 367-385.
    • (1988) Biophys. J. , vol.53 , pp. 367-385
    • Birge, R.R.1    Einterz, C.M.2    Knapp, H.M.3    Murray, L.P.4
  • 16
    • 0030139354 scopus 로고    scopus 로고
    • Physiological activity of retinoids in natural and artificial visual pigments
    • Corson, D. W., and Crouch, R. K. (1996) Physiological activity of retinoids in natural and artificial visual pigments, Photochem. Photobiol. 63, 595-600.
    • (1996) Photochem. Photobiol. , vol.63 , pp. 595-600
    • Corson, D.W.1    Crouch, R.K.2
  • 17
    • 0030471282 scopus 로고    scopus 로고
    • Retinal analog study of the role of steric interactions in the excited-state isomerization dynamics of rhodopsin
    • Kochendoerfer, G. G., Verdegem, P. J. E., VanDerHoef, I., Lugtenburg, J., and Mathies, R. A. (1996) Retinal analog study of the role of steric interactions in the excited-state isomerization dynamics of rhodopsin, Biochemistry 35, 16230-16240.
    • (1996) Biochemistry , vol.35 , pp. 16230-16240
    • Kochendoerfer, G.G.1    Verdegem, P.J.E.2    VanDerHoef, I.3    Lugtenburg, J.4    Mathies, R.A.5
  • 18
    • 0001612847 scopus 로고    scopus 로고
    • Femtosecond spectroscopy of a 13-demethylrhodopsin visual pigment analogue: The role of non-bonded interactions in the isomerization process
    • Wang, Q., Kochendoerfer, G. G., Schoenlein, R. W., Verdegem, P. J. E., Lugtenburg, J., Mathies, R. A., and Shank, C. V. (1996) Femtosecond spectroscopy of a 13-demethylrhodopsin visual pigment analogue: The role of non-bonded interactions in the isomerization process, J. Phys. Chem. B 100, 17388-17394.
    • (1996) J. Phys. Chem. B , vol.100 , pp. 17388-17394
    • Wang, Q.1    Kochendoerfer, G.G.2    Schoenlein, R.W.3    Verdegem, P.J.E.4    Lugtenburg, J.5    Mathies, R.A.6    Shank, C.V.7
  • 19
    • 0034006772 scopus 로고    scopus 로고
    • Synthetic retinals: Convenient probes of rhodopsin and visual transduction process
    • Lou, J. H., Tan, Q., Karnaukhova, E. N., Berova, N., Nakanishi, K., and Crouch, R. K. (2000) Synthetic retinals: Convenient probes of rhodopsin and visual transduction process, Methods Enzymol. 315, 219-237.
    • (2000) Methods Enzymol. , vol.315 , pp. 219-237
    • Lou, J.H.1    Tan, Q.2    Karnaukhova, E.N.3    Berova, N.4    Nakanishi, K.5    Crouch, R.K.6
  • 20
    • 0036570054 scopus 로고    scopus 로고
    • Time-resolved resonance Raman analysis of chromophore structural changes in the formation and decay of rhodopsin's BSI intermediate
    • Pan, D. H., Ganim, Z., Kim, J. E., Verhoeven, M. A., Lugtenburg, J., and Mathies, R. A. (2002) Time-resolved resonance Raman analysis of chromophore structural changes in the formation and decay of rhodopsin's BSI intermediate, J. Am. Chem. Soc. 124, 4857-4864.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 4857-4864
    • Pan, D.H.1    Ganim, Z.2    Kim, J.E.3    Verhoeven, M.A.4    Lugtenburg, J.5    Mathies, R.A.6
  • 24
    • 0024341576 scopus 로고
    • Removal of the 9-methyl group of retinal inhibits signal transduction in the visual process. A Fourier transform infrared and biochemical investigation
    • Ganter, U. M., Schmid, E. D., Perez-Sala, D., Rando, R. R., and Siebert, F. (1989) Removal of the 9-methyl group of retinal inhibits signal transduction in the visual process. A Fourier transform infrared and biochemical investigation, Biochemistry 28, 5954-5962.
    • (1989) Biochemistry , vol.28 , pp. 5954-5962
    • Ganter, U.M.1    Schmid, E.D.2    Perez-Sala, D.3    Rando, R.R.4    Siebert, F.5
  • 26
    • 0028912287 scopus 로고
    • Reduced light-dependent phosphorylation of an analog visual pigment containing 9-demethylretinal as its chromophore
    • Morrison, D. F., Ting, T. D., Vallury, V., Ho, Y.-K., Crouch, R. K., Corson, D. W., Mangini, N. J., and Pepperberg, D. R. (1995) Reduced light-dependent phosphorylation of an analog visual pigment containing 9-demethylretinal as its chromophore, J. Biol. Chem. 270, 6718-6721.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6718-6721
    • Morrison, D.F.1    Ting, T.D.2    Vallury, V.3    Ho, Y.-K.4    Crouch, R.K.5    Corson, D.W.6    Mangini, N.J.7    Pepperberg, D.R.8
  • 27
    • 0032512369 scopus 로고    scopus 로고
    • 9 methyl group in rhodopsin activation: Characterization of mutant opsins with the artificial chromophore 11-cis-9-demethylretinal
    • 9 methyl group in rhodopsin activation: Characterization of mutant opsins with the artificial chromophore 11-cis-9-demethylretinal, Biochemistry 37, 538-545.
    • (1998) Biochemistry , vol.37 , pp. 538-545
    • Han, M.1    Groesbeek, M.2    Smith, S.O.3    Sakmar, T.P.4
  • 28
    • 0040141552 scopus 로고    scopus 로고
    • Signaling states of rhodopsin-Retinal provides a scaffold for activating proton-transfer switches
    • Meyer, C. K., Böhme, M., Ockenfels, A., Gärtner, W., Hofmann, K. P., and Ernst, O. P. (2000) Signaling states of rhodopsin-Retinal provides a scaffold for activating proton-transfer switches, J. Biol. Chem. 275, 19713-19718.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19713-19718
    • Meyer, C.K.1    Böhme, M.2    Ockenfels, A.3    Gärtner, W.4    Hofmann, K.P.5    Ernst, O.P.6
  • 29
    • 0034254233 scopus 로고    scopus 로고
    • The molecular origin of the inhibition of transducin activation in rhodopsin lacking the 9-methyl group of the retinal chromophore: A UV-vis and FTIR spectroscopic study
    • Vogel, R., Fan, G.-B., Sheves, M., and Siebert, F. (2000) The molecular origin of the inhibition of transducin activation in rhodopsin lacking the 9-methyl group of the retinal chromophore: A UV-vis and FTIR spectroscopic study, Biochemistry 39, 8895-8908.
    • (2000) Biochemistry , vol.39 , pp. 8895-8908
    • Vogel, R.1    Fan, G.-B.2    Sheves, M.3    Siebert, F.4
  • 30
    • 84957064283 scopus 로고
    • General and theoretical aspects of the carbon-halogen bond
    • Patai, S., Ed. John Wiley and Sons, London, U.K.
    • Wagnière, G. H. (1973) General and theoretical aspects of the carbon-halogen bond, in The Chemistry of the Carbon Halogen Bond (Patai, S., Ed.) part I, pp 1-47, John Wiley and Sons, London, U.K.
    • (1973) The Chemistry of the Carbon Halogen Bond , Issue.1 PART , pp. 1-47
    • Wagnière, G.H.1
  • 31
    • 4544354236 scopus 로고    scopus 로고
    • 9-Demethyl-9-haloretinals by Wadsworth-Emmons coupling-Easy preparation of pure (all-E), (9Z), and (11Z) isomers
    • Wang, Y.-J., Woo, W. S., VanDerHoef, I., and Lugtenburg, J. (2004) 9-Demethyl-9-haloretinals by Wadsworth-Emmons coupling-Easy preparation of pure (all-E), (9Z), and (11Z) isomers, Eur. J. Org. Chem. 2166-2175.
    • (2004) Eur. J. Org. Chem. , pp. 2166-2175
    • Wang, Y.-J.1    Woo, W.S.2    VanDerHoef, I.3    Lugtenburg, J.4
  • 32
    • 4544288650 scopus 로고    scopus 로고
    • 4,5-Didehydro-9-demethyl-9-halo-5,6-dihydroretinals and their 9-cyclopropyl and 9-isopropyl derivatives-Simple preparation of α-ionone derivatives and pure (all-E)-, (9-Z)-, and (11-Z)-α-retinals
    • Wang, Y.-J., and Lugtenburg, J. (2004) 4,5-Didehydro-9-demethyl-9-halo-5, 6-dihydroretinals and their 9-cyclopropyl and 9-isopropyl derivatives-Simple preparation of α-ionone derivatives and pure (all-E)-, (9-Z)-, and (11-Z)-α-retinals, Eur. J. Org. Chem. 3497-3510.
    • (2004) Eur. J. Org. Chem. , pp. 3497-3510
    • Wang, Y.-J.1    Lugtenburg, J.2
  • 33
    • 0025282408 scopus 로고
    • 10,20-Methanorhodopsins: (7E,9E,13E)-10,20-methanorhodopsin and (7E,9Z,13Z)-10,20-methanorhodopsin- 11-cis-Locked rhodopsin analog pigments with unusual thermal and photo-stability
    • DeGrip, W. J., VanOostrum, J., Bovee-Geurts, P. H. M., VanDer-Steen, R., VanAmsterdam, L. J. P., Groesbeek, M., and Lugtenburg, J. (1990) 10,20-Methanorhodopsins: (7E,9E,13E)-10,20-methanorhodopsin and (7E,9Z,13Z)-10,20-methanorhodopsin- 11-cis-Locked rhodopsin analog pigments with unusual thermal and photo-stability, Eur. J. Biochem. 191, 211-220.
    • (1990) Eur. J. Biochem. , vol.191 , pp. 211-220
    • DeGrip, W.J.1    VanOostrum, J.2    Bovee-Geurts, P.H.M.3    VanDer-Steen, R.4    VanAmsterdam, L.J.P.5    Groesbeek, M.6    Lugtenburg, J.7
  • 34
    • 0032477819 scopus 로고    scopus 로고
    • An additional methyl group at the 10-position of retinal dramatically slows down the kinetics of the rhodopsin photocascade
    • DeLange, F., Bovee-Geurts, P. H. M., VanOostrum, J., Portier, M. D., Verdegem, P. J. E., Lugtenburg, J., and DeGrip, W. J. (1998) An additional methyl group at the 10-position of retinal dramatically slows down the kinetics of the rhodopsin photocascade, Biochemistry 37, 1411-1420.
    • (1998) Biochemistry , vol.37 , pp. 1411-1420
    • DeLange, F.1    Bovee-Geurts, P.H.M.2    VanOostrum, J.3    Portier, M.D.4    Verdegem, P.J.E.5    Lugtenburg, J.6    DeGrip, W.J.7
  • 35
    • 0032032913 scopus 로고    scopus 로고
    • Selective detergent-extraction from mixed detergent/lipid/protein micelles, using cyclodextrin inclusion compounds: A novel generic approach for the preparation of proteoliposomes
    • DeGrip, W. J., VanOostrum, J., and Bovee-Geurts, P. H. M. (1998) Selective detergent-extraction from mixed detergent/lipid/protein micelles, using cyclodextrin inclusion compounds: A novel generic approach for the preparation of proteoliposomes, Biochem. J. 330, 667-674.
    • (1998) Biochem. J. , vol.330 , pp. 667-674
    • DeGrip, W.J.1    VanOostrum, J.2    Bovee-Geurts, P.H.M.3
  • 36
    • 0020503982 scopus 로고
    • Reversible modulation of rhodopsin photolysis in pure phosphatidylserine membranes
    • DeGrip, W. J., Olive, J., and Bovee-Geurts, P. H. M. (1983) Reversible modulation of rhodopsin photolysis in pure phosphatidylserine membranes, Biochim. Biophys. Acta 734, 168-179.
    • (1983) Biochim. Biophys. Acta , vol.734 , pp. 168-179
    • DeGrip, W.J.1    Olive, J.2    Bovee-Geurts, P.H.M.3
  • 37
    • 0018851718 scopus 로고
    • Surface induced orientation of multilayer membrane arrays: Theoretical analysis and a new method with application to purple membrane fragments
    • Clark, N. A., Rothschild, K. J., Simon, B. A., and Luippold, D. A. (1980) Surface induced orientation of multilayer membrane arrays: Theoretical analysis and a new method with application to purple membrane fragments, Biophys. J. 31, 65-96.
    • (1980) Biophys. J. , vol.31 , pp. 65-96
    • Clark, N.A.1    Rothschild, K.J.2    Simon, B.A.3    Luippold, D.A.4
  • 38
    • 0031029938 scopus 로고    scopus 로고
    • Modulation of the metarhodopsin I/metarhodopsin II equilibrium of bovine rhodopsin by ionic strength - Evidence for a surface charge effect
    • DeLange, F., Merkx, M., Bovee-Geurts, P. H. M., Pistorius, A. M. A., and DeGrip, W. J. (1997) Modulation of the metarhodopsin I/metarhodopsin II equilibrium of bovine rhodopsin by ionic strength - Evidence for a surface charge effect, Eur. J. Biochem. 243, 174-180.
    • (1997) Eur. J. Biochem. , vol.243 , pp. 174-180
    • DeLange, F.1    Merkx, M.2    Bovee-Geurts, P.H.M.3    Pistorius, A.M.A.4    DeGrip, W.J.5
  • 39
    • 0024803054 scopus 로고
    • A study of the binding site requirements of rhodopsin using isomers of α-retinal and 5-substituted α-retinal analogs
    • Asato, A. E., Zhang, B.-W., Denny, M., Mirzadegan, T., Seff, K., and Liu, R. S. H. (1989) A study of the binding site requirements of rhodopsin using isomers of α-retinal and 5-substituted α-retinal analogs, Bioorg. Chem. 17, 410-421.
    • (1989) Bioorg. Chem. , vol.17 , pp. 410-421
    • Asato, A.E.1    Zhang, B.-W.2    Denny, M.3    Mirzadegan, T.4    Seff, K.5    Liu, R.S.H.6
  • 40
    • 0344823697 scopus 로고    scopus 로고
    • Conformational similarities in the β-ionone ring region of the rhodopsin chromophore in its ground state and after photoactivation to the metarhodopsin-I intermediate
    • Spooner, P. J. R., Sharples, J. M., Goodall, S. C., Seedorf, H., Verhoeven, M. A., Lugtenburg, J., Bovee-Geurts, P. H. M., DeGrip, W. J., and Watts, A. (2003) Conformational similarities in the β-ionone ring region of the rhodopsin chromophore in its ground state and after photoactivation to the metarhodopsin-I intermediate. Biochemistry 42, 13371-13378.
    • (2003) Biochemistry , vol.42 , pp. 13371-13378
    • Spooner, P.J.R.1    Sharples, J.M.2    Goodall, S.C.3    Seedorf, H.4    Verhoeven, M.A.5    Lugtenburg, J.6    Bovee-Geurts, P.H.M.7    DeGrip, W.J.8    Watts, A.9
  • 41
    • 0023215761 scopus 로고
    • Assignment of fingerprint vibrations in the resonance Raman spectra of rhodopsin, isorhodopsin, and bathorhodopsin: Implications for chromophore structure and environment
    • Palings, I., Pardoen, J. A., VanDenBerg, E. M. M., Winkel, C., Lugtenburg, J., and Mathies, R. A. (1987) Assignment of fingerprint vibrations in the resonance Raman spectra of rhodopsin, isorhodopsin, and bathorhodopsin: Implications for chromophore structure and environment, Biochemistry 26, 2544-2556.
    • (1987) Biochemistry , vol.26 , pp. 2544-2556
    • Palings, I.1    Pardoen, J.A.2    VanDenBerg, E.M.M.3    Winkel, C.4    Lugtenburg, J.5    Mathies, R.A.6
  • 42
    • 0002856611 scopus 로고
    • Determination of retinal chromophore structure in rhodopsins
    • Spiro, T. G., Ed. John Wiley and Sons, New York
    • Mathies, R. A., Smith, S. O., and Palings, I. (1987) Determination of retinal chromophore structure in rhodopsins, in Resonance Roman Spectra of Polyenes and Aromatics (Spiro, T. G., Ed.) pp 59-108, John Wiley and Sons, New York.
    • (1987) Resonance Roman Spectra of Polyenes and Aromatics , pp. 59-108
    • Mathies, R.A.1    Smith, S.O.2    Palings, I.3
  • 43
    • 0025737465 scopus 로고
    • Spectroscopic study of the batho-to-lumi transition during the photobleaching of rhodopsin using ring-modified retinal analogues
    • Okada, T., Kandori, H., Shichida, Y., Yoshizawa, T., Denny, M., Zhang, B.-W., Asato, A. E., and Liu, R. S. H. (1991) Spectroscopic study of the batho-to-lumi transition during the photobleaching of rhodopsin using ring-modified retinal analogues, Biochemistry 30, 4796-4802.
    • (1991) Biochemistry , vol.30 , pp. 4796-4802
    • Okada, T.1    Kandori, H.2    Shichida, Y.3    Yoshizawa, T.4    Denny, M.5    Zhang, B.-W.6    Asato, A.E.7    Liu, R.S.H.8
  • 46
    • 0040344173 scopus 로고
    • The stereochemistry of vision
    • Tamm, T., Ed. Elsevier Biomedical Press, Amsterdam, The Netherlands
    • Balogh-Nair, V., and Nakanishi, K. (1982) The stereochemistry of vision, in Stereochemistry (Tamm, T., Ed.) pp 283-334, Elsevier Biomedical Press, Amsterdam, The Netherlands.
    • (1982) Stereochemistry , pp. 283-334
    • Balogh-Nair, V.1    Nakanishi, K.2
  • 47
    • 0039227396 scopus 로고
    • The binding site of opsin based on analog studies with isomeric, fluorinated, alkylated, and other modified retinals
    • Dawson, M. I., and Okamura, W. H., Eds. CRC Press, Boca Raton, FL
    • Liu, R. S. H., and Asato, A. E. (1990) The binding site of opsin based on analog studies with isomeric, fluorinated, alkylated, and other modified retinals, in Chemistry and Biology of Synthetic Retinoids (Dawson, M. I., and Okamura, W. H., Eds.) pp 52-75, CRC Press, Boca Raton, FL.
    • (1990) Chemistry and Biology of Synthetic Retinoids , pp. 52-75
    • Liu, R.S.H.1    Asato, A.E.2
  • 48
    • 0038159530 scopus 로고    scopus 로고
    • Organization of the G protein-coupled receptors rhodopsin and opsin in native membranes
    • Liang, Y., Fotiadis, D., Filipek, S., Saperstein, D. A., Palczewski, K., and Engel, A. (2003) Organization of the G protein-coupled receptors rhodopsin and opsin in native membranes, J. Biol. Chem. 278, 21655-21662.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21655-21662
    • Liang, Y.1    Fotiadis, D.2    Filipek, S.3    Saperstein, D.A.4    Palczewski, K.5    Engel, A.6
  • 49
    • 0242578633 scopus 로고    scopus 로고
    • Secondary binding sites of retinoids in opsin: Characterization and role in regeneration
    • Heck, M., Schädel, S. A., Maretzki, D., and Hofmann, K. P. (2003) Secondary binding sites of retinoids in opsin: Characterization and role in regeneration, Vision Res. 43, 3003-3010.
    • (2003) Vision Res. , vol.43 , pp. 3003-3010
    • Heck, M.1    Schädel, S.A.2    Maretzki, D.3    Hofmann, K.P.4
  • 50
    • 0042591319 scopus 로고    scopus 로고
    • Ligand channeling within a G-protein-coupled receptor - The entry and exit of retinals in native opsin
    • Schädel, S. A., Heck, M., Maretzki, D., Filipek, S., Teller, D. C., Palczewski, K., and Hofmann, K. P. (2003) Ligand channeling within a G-protein-coupled receptor - The entry and exit of retinals in native opsin, J. Biol. Chem. 278, 24896-24903.
    • (2003) J. Biol. Chem. , vol.278 , pp. 24896-24903
    • Schädel, S.A.1    Heck, M.2    Maretzki, D.3    Filipek, S.4    Teller, D.C.5    Palczewski, K.6    Hofmann, K.P.7
  • 53
    • 0038529723 scopus 로고    scopus 로고
    • Pharmacological chaperone-mediated in vivo folding and stabilization of the P23H-opsin mutant associated with autosomal dominant retinitis pigmentosa
    • Noorwez, S. M., Kuksa, V., Imanishi, Y., Zhu, L., Filipek, S., Palczewski, K., and Kaushal, S. (2003) Pharmacological chaperone-mediated in vivo folding and stabilization of the P23H-opsin mutant associated with autosomal dominant retinitis pigmentosa, J. Biol. Chem. 278, 14442-14450.
    • (2003) J. Biol. Chem. , vol.278 , pp. 14442-14450
    • Noorwez, S.M.1    Kuksa, V.2    Imanishi, Y.3    Zhu, L.4    Filipek, S.5    Palczewski, K.6    Kaushal, S.7
  • 54
    • 0037129946 scopus 로고    scopus 로고
    • Relative orientation between the β-ionone ring and the polyene chain for the chromophore of rhodopsin in native membranes
    • Spooner, P. J. R., Sharples, J. M., Verhoeven, M. A., Lugtenburg, J., Glaubitz, C., and Watts, A. (2002) Relative orientation between the β-ionone ring and the polyene chain for the chromophore of rhodopsin in native membranes, Biochemistry 41, 7549-7555.
    • (2002) Biochemistry , vol.41 , pp. 7549-7555
    • Spooner, P.J.R.1    Sharples, J.M.2    Verhoeven, M.A.3    Lugtenburg, J.4    Glaubitz, C.5    Watts, A.6
  • 55
    • 2442452670 scopus 로고    scopus 로고
    • Role of the 9-methyl group of retinal in cone visual pigments
    • Das, J., Crouch, R. K., Ma, J.-X., Oprian, D. D., and Kono, M. (2004) Role of the 9-methyl group of retinal in cone visual pigments, Biochemistry 43, 5532-5538.
    • (2004) Biochemistry , vol.43 , pp. 5532-5538
    • Das, J.1    Crouch, R.K.2    Ma, J.-X.3    Oprian, D.D.4    Kono, M.5
  • 56
    • 0012347344 scopus 로고    scopus 로고
    • Energy storage in the primary photoproduct of vision
    • Bifone, A., DeGroot, H. J. M., and Buda, F. (1997) Energy storage in the primary photoproduct of vision, J. Phys. Chem. B 101, 2954-2958.
    • (1997) J. Phys. Chem. B , vol.101 , pp. 2954-2958
    • Bifone, A.1    DeGroot, H.J.M.2    Buda, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.