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Volumn 84, Issue 4, 2008, Pages 889-894

Alpha-retinals as rhodopsin chromophores-preference for the 9-Z configuration and partial agonist activity

Author keywords

[No Author keywords available]

Indexed keywords

BOVINAE; VERTEBRATA;

EID: 52149111837     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1751-1097.2008.00321.x     Document Type: Conference Paper
Times cited : (5)

References (53)
  • 1
    • 0014428724 scopus 로고
    • The molecular basis of visual excitation
    • Wald, G. (1968) The molecular basis of visual excitation. Nature 219, 800-807.
    • (1968) Nature , vol.219 , pp. 800-807
    • Wald, G.1
  • 2
    • 70349536422 scopus 로고    scopus 로고
    • Mathies, R. A. and J. Lugtenburg (2000) The primary photoreaction of rhodopsin. In Handbook of Biological Physics, 3. Molecular Mechanisms in Visual Transduction (Edited by D. G. Stavenga, W. J. DeGrip and E. N. Pugh Jr), pp. 55-90. Elsevier Science Pub., Amsterdam.
    • Mathies, R. A. and J. Lugtenburg (2000) The primary photoreaction of rhodopsin. In Handbook of Biological Physics, Vol. 3. Molecular Mechanisms in Visual Transduction (Edited by D. G. Stavenga, W. J. DeGrip and E. N. Pugh Jr), pp. 55-90. Elsevier Science Pub., Amsterdam.
  • 3
    • 77956785528 scopus 로고    scopus 로고
    • Hofmann, K. P. (2000) Late photoproducts and signaling states of bovine rhodopsin. In Handbook of Biological Physics, 3. Molecular Mechanisms in Visual Transduction (Edited by D. G. Stavenga, W. J. DeGrip and E. N. Pugh Jr), pp. 91-142. Elsevier Science Pub., Amsterdam.
    • Hofmann, K. P. (2000) Late photoproducts and signaling states of bovine rhodopsin. In Handbook of Biological Physics, Vol. 3. Molecular Mechanisms in Visual Transduction (Edited by D. G. Stavenga, W. J. DeGrip and E. N. Pugh Jr), pp. 91-142. Elsevier Science Pub., Amsterdam.
  • 5
    • 4344581120 scopus 로고    scopus 로고
    • The retinal conformation and its environment in rhodopsin in light of a new 2.2 Å crystal structure
    • Okada, T., M. Sugihara, A.-N. Bondar, M. Elstner, P. Entel and V. Buss (2004) The retinal conformation and its environment in rhodopsin in light of a new 2.2 Å crystal structure. J. Mol. Biol. 342, 571-583.
    • (2004) J. Mol. Biol , vol.342 , pp. 571-583
    • Okada, T.1    Sugihara, M.2    Bondar, A.-N.3    Elstner, M.4    Entel, P.5    Buss, V.6
  • 7
    • 33746321096 scopus 로고    scopus 로고
    • Crystallographic analysis of primary visual photochemistry
    • Nakamichi, H. and T. Okada (2006) Crystallographic analysis of primary visual photochemistry. Angew. Chem. Int. Ed. Engl. 45, 4270-4273.
    • (2006) Angew. Chem. Int. Ed. Engl , vol.45 , pp. 4270-4273
    • Nakamichi, H.1    Okada, T.2
  • 8
    • 33748079137 scopus 로고    scopus 로고
    • Local peptide movement in the photoreaction intermediate of rhodopsin
    • Nakamichi, H. and T. Okada (2006) Local peptide movement in the photoreaction intermediate of rhodopsin. Proc. Natl Acad. Sci. USA 103, 12729-12734.
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 12729-12734
    • Nakamichi, H.1    Okada, T.2
  • 9
    • 5044235587 scopus 로고    scopus 로고
    • Electron crystallography reveals the structure of metarhodopsin I
    • Ruprecht, J. J., T. Mielke, R. Vogel, C. Villa and G. F. X. Schertler (2004) Electron crystallography reveals the structure of metarhodopsin I. EMBO J. 23, 3609-3620.
    • (2004) EMBO J , vol.23 , pp. 3609-3620
    • Ruprecht, J.J.1    Mielke, T.2    Vogel, R.3    Villa, C.4    Schertler, G.F.X.5
  • 10
    • 0344392142 scopus 로고    scopus 로고
    • Isorhodopsin rather than rhodopsin mediates rod function in RPE65 knock-out mice
    • Fan, J., B. Rohrer, G. Moiseyev, J.-X. Ma and R. K. Crouch (2003) Isorhodopsin rather than rhodopsin mediates rod function in RPE65 knock-out mice. Proc. Natl Acad. Sci. USA 100, 13662-13667.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 13662-13667
    • Fan, J.1    Rohrer, B.2    Moiseyev, G.3    Ma, J.-X.4    Crouch, R.K.5
  • 11
    • 0001560191 scopus 로고
    • Synthetic analogs of retinal, bacteriorhodopsin and bovine rhodopsin
    • Balogh-Nair, V. and K. Nakanishi (1982) Synthetic analogs of retinal, bacteriorhodopsin and bovine rhodopsin. Methods Enzymol. 88, 496-506.
    • (1982) Methods Enzymol , vol.88 , pp. 496-506
    • Balogh-Nair, V.1    Nakanishi, K.2
  • 12
    • 0039227396 scopus 로고
    • The binding site of opsin based on analog studies with isomeric, fluorinated, alkylated, and other modified retinals
    • Edited by M. I. Dawson and W. H. Okamura, pp, CRC Press, Boca Raton, FL
    • Liu, R. S. H. and A. E. Asato (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 (Edited by M. I. Dawson and W. H. Okamura), 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
  • 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
    • 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., B.-W. Zhang, M. Denny, T. Mirzadegan, K. Seff and R. S. H. Liu (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
  • 15
    • 0025737465 scopus 로고
    • Spectroscopic study of the batho-to-lumi transition during the photobleaching of rhodopsin using ring-modified retinal analogues
    • Okada, T., H. Kandori, Y. Shichida, T. Yoshizawa, M. Denny, B.-W. Zhang, A. E. Asato and R. S. H. Liu (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
  • 16
    • 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., P. H. M. Bovee-Geurts, J. VanOostrum, M. D. Portier, P. J. E. Verdegem, J. Lugtenburg and W. J. DeGrip (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
  • 17
    • 0034006772 scopus 로고    scopus 로고
    • Synthetic retinals: Convenient probes of rhodopsin and visual transduction process
    • Lou, J. H., Q. Tan, E. N. Karnaukhova, N. Berova, K. Nakanishi and R. K. Crouch (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
  • 18
    • 0040141552 scopus 로고    scopus 로고
    • Signaling states of rhodopsin-Retinal provides a scaffold for activating proton transfer switches
    • Meyer, C. K., M. Böhme, A. Ockenfels, W. Gärtner, K. P. Hofmann and O. P. Ernst (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
  • 19
    • 0034792629 scopus 로고    scopus 로고
    • Use of retinal analogues for the study of visual pigment function
    • Crouch, R. K., V. J. Kefalov, W. Gä rtner and M. C. Cornwall (2002) Use of retinal analogues for the study of visual pigment function. Methods Enzymol. 343, 29-48.
    • (2002) Methods Enzymol , vol.343 , pp. 29-48
    • Crouch, R.K.1    Kefalov, V.J.2    Gä rtner, W.3    Cornwall, M.C.4
  • 20
    • 0242438630 scopus 로고    scopus 로고
    • Retinoid cycle in the vertebrate retina: Experimental approaches and mechanisms of isomerization
    • Kuksa, V., Y. Imanishi, M. Batten, K. Palczewski and A. R. Moise (2003) Retinoid cycle in the vertebrate retina: Experimental approaches and mechanisms of isomerization. Vision Res. 43, 2959-2981.
    • (2003) Vision Res , vol.43 , pp. 2959-2981
    • Kuksa, V.1    Imanishi, Y.2    Batten, M.3    Palczewski, K.4    Moise, A.R.5
  • 21
    • 24344507257 scopus 로고    scopus 로고
    • Agonists and partial agonists of rhodopsin: Retinals with ring modifications
    • Vogel, R., F. Siebert, S. Lüdeke, A. Hirshfeld and M. Sheves (2005) Agonists and partial agonists of rhodopsin: Retinals with ring modifications. Biochemistry 44, 11684-11699.
    • (2005) Biochemistry , vol.44 , pp. 11684-11699
    • Vogel, R.1    Siebert, F.2    Lüdeke, S.3    Hirshfeld, A.4    Sheves, M.5
  • 22
    • 26644452318 scopus 로고    scopus 로고
    • Partial agonism in a G protein-coupled receptor-Role of the retinal ring structure in rhodopsin activation
    • Bartl, F. J., O. Fritze, E. Ritter, R. Herrmann, V. Kuksa, K. Palczewski, K. P. Hofmann and O. P. Ernst (2005) Partial agonism in a G protein-coupled receptor-Role of the retinal ring structure in rhodopsin activation. J. Biol. Chem. 280, 34259-34267.
    • (2005) J. Biol. Chem , vol.280 , pp. 34259-34267
    • Bartl, F.J.1    Fritze, O.2    Ritter, E.3    Herrmann, R.4    Kuksa, V.5    Palczewski, K.6    Hofmann, K.P.7    Ernst, O.P.8
  • 23
    • 33748787144 scopus 로고    scopus 로고
    • Methyl substituents at the 11- or 12-position of retinal profoundly and differentially affect photochemistry and signalling activity of rhodopsin
    • Verhoeven, M. A., P. H. M. Bovee-Geurts, H. J. M. de Groot, J. Lugtenburg and W. J. DeGrip (2006) Methyl substituents at the 11- or 12-position of retinal profoundly and differentially affect photochemistry and signalling activity of rhodopsin. J. Mol. Biol. 363, 98-113.
    • (2006) J. Mol. Biol , vol.363 , pp. 98-113
    • Verhoeven, M.A.1    Bovee-Geurts, P.H.M.2    de Groot, H.J.M.3    Lugtenburg, J.4    DeGrip, W.J.5
  • 25
    • 32344443931 scopus 로고    scopus 로고
    • Agonists and partial agonists of rhodopsin: Retinal polyene methylation affects receptor activation
    • Vogel, R., S. Lüdeke, F. Siebert, T. P. Sakmar, A. Hirshfeld and M. Sheves (2006) Agonists and partial agonists of rhodopsin: Retinal polyene methylation affects receptor activation. Biochemistry 45, 1640-1652.
    • (2006) Biochemistry , vol.45 , pp. 1640-1652
    • Vogel, R.1    Lüdeke, S.2    Siebert, F.3    Sakmar, T.P.4    Hirshfeld, A.5    Sheves, M.6
  • 26
    • 0024081391 scopus 로고
    • The visual process: Photophysics and photoisomerization of model visual pigments and the primary reaction
    • Becker, R. S. (1988) The visual process: Photophysics and photoisomerization of model visual pigments and the primary reaction. Photochem. Photobiol. 48, 369-399.
    • (1988) Photochem. Photobiol , vol.48 , pp. 369-399
    • Becker, R.S.1
  • 27
    • 0000687281 scopus 로고    scopus 로고
    • Charge localization and dynamics in rhodopsin
    • Buda, F., H. J. M. de Groot and A. Bifone (1996) Charge localization and dynamics in rhodopsin. Phys. Rev. Lett. 77, 4474-4477.
    • (1996) Phys. Rev. Lett , vol.77 , pp. 4474-4477
    • Buda, F.1    de Groot, H.J.M.2    Bifone, A.3
  • 28
    • 0037047148 scopus 로고    scopus 로고
    • 1H and 13C MAS NMR evidence for pronounced ligand-protein interactions involving the ionone ring of the retinylidene chromophore in rhodopsin
    • Creemers, A. F. L., S. R. Kiihne, P. H. M. Bovee-Geurts, W. J. DeGrip, J. Lugtenburg and H. J. M. de Groot (2002) 1H and 13C MAS NMR evidence for pronounced ligand-protein interactions involving the ionone ring of the retinylidene chromophore in rhodopsin. Proc. Natl Acad. Sci. USA 99, 9101-9106.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 9101-9106
    • Creemers, A.F.L.1    Kiihne, S.R.2    Bovee-Geurts, P.H.M.3    DeGrip, W.J.4    Lugtenburg, J.5    de Groot, H.J.M.6
  • 29
    • 35848955899 scopus 로고    scopus 로고
    • 7,8-Dihydro-retinals outperform the native retinals in conferring photosensitivity to visual opsin
    • DeGrip, W. J., P. H. M. Bovee-Geurts, I. Van der Hoef and J. Lugtenburg (2007) 7,8-Dihydro-retinals outperform the native retinals in conferring photosensitivity to visual opsin. J. Am. Chem. Soc. 129, 13265-13269.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 13265-13269
    • DeGrip, W.J.1    Bovee-Geurts, P.H.M.2    Van der Hoef, I.3    Lugtenburg, J.4
  • 31
    • 8744236234 scopus 로고    scopus 로고
    • Constraints of the 9-methyl group binding pocket of the rhodopsin chromophore probed by 9-halogeno substitution
    • Wang, Y.-J., P. H. M. Bovee-Geurts, J. Lugtenburg and W. J. DeGrip (2004) Constraints of the 9-methyl group binding pocket of the rhodopsin chromophore probed by 9-halogeno substitution. Biochemistry 43, 14802-14810.
    • (2004) Biochemistry , vol.43 , pp. 14802-14810
    • Wang, Y.-J.1    Bovee-Geurts, P.H.M.2    Lugtenburg, J.3    DeGrip, W.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 a-ionone derivatives and pure (all-E)-, (9-Z)- and (11-Z)-α-retinals
    • Wang, Y.-J. and J. Lugtenburg (2004) 4,5-Didehydro-9-demethyl-9-halo-5,6- dihydroretinals and their 9-cyclopropyl and 9-isopropyl derivatives-Simple preparation of a-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
    • 63849147051 scopus 로고    scopus 로고
    • Dartnall, H. J. A. (ed.) (1972) Photosensitivity. In Photochemistry of Vision, VII/I, pp. 122-145. Springer-Verlag, Berlin.
    • Dartnall, H. J. A. (ed.) (1972) Photosensitivity. In Photochemistry of Vision, Vol. VII/I, pp. 122-145. Springer-Verlag, Berlin.
  • 34
    • 0035923444 scopus 로고    scopus 로고
    • Wavelength dependent cis-trans isomerization in vision
    • Kim, J. E., M. J. Tauber and R. A. Mathies (2001) Wavelength dependent cis-trans isomerization in vision. Biochemistry 40, 13774-13778.
    • (2001) Biochemistry , vol.40 , pp. 13774-13778
    • Kim, J.E.1    Tauber, M.J.2    Mathies, R.A.3
  • 35
    • 11144335976 scopus 로고    scopus 로고
    • Solid-state NMR analysis of ligand-receptor interactions reveals an induced misfit in the binding site of isorhodopsin
    • Creemers, A. F. L., P. H. M. Bovee-Geurts, W. J. DeGrip, J. Lugtenburg and H. J. M. de Groot (2004) Solid-state NMR analysis of ligand-receptor interactions reveals an induced misfit in the binding site of isorhodopsin. Biochemistry 43, 16011-16018.
    • (2004) Biochemistry , vol.43 , pp. 16011-16018
    • Creemers, A.F.L.1    Bovee-Geurts, P.H.M.2    DeGrip, W.J.3    Lugtenburg, J.4    de Groot, H.J.M.5
  • 36
    • 85005675452 scopus 로고
    • Spectral and kinetic characterization of visual pigment photointermediates
    • Kliger, D. S. and J. W. Lewis (1995) Spectral and kinetic characterization of visual pigment photointermediates. Isr. J. Chem. 35, 289-307.
    • (1995) Isr. J. Chem , vol.35 , pp. 289-307
    • Kliger, D.S.1    Lewis, J.W.2
  • 38
    • 0020595783 scopus 로고
    • Fourier transform infrared difference spectra of intermediates in rhodopsin bleaching
    • Rothschild, K. J., W. A. Cantore and H. Marrero (1983) Fourier transform infrared difference spectra of intermediates in rhodopsin bleaching. Science 219, 1333-1335.
    • (1983) Science , vol.219 , pp. 1333-1335
    • Rothschild, K.J.1    Cantore, W.A.2    Marrero, H.3
  • 39
    • 0001461410 scopus 로고
    • FTIR evidence of an altered chromophore protein interaction in the artificial visual pigment cis-5,6-dihydroisorhodopsin and its photoproducts BSI, lumirhodopsin, and metarhodopsin-I
    • Ganter, U. M., T. Kashima, M. Sheves and F. Siebert (1991) FTIR evidence of an altered chromophore protein interaction in the artificial visual pigment cis-5,6-dihydroisorhodopsin and its photoproducts BSI, lumirhodopsin, and metarhodopsin-I. J. Am. Chem. Soc. 113, 4087-4092.
    • (1991) J. Am. Chem. Soc , vol.113 , pp. 4087-4092
    • Ganter, U.M.1    Kashima, T.2    Sheves, M.3    Siebert, F.4
  • 40
    • 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
  • 41
    • 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., G.-B. Fan, M. Sheves and F. Siebert (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
  • 42
    • 77957112451 scopus 로고    scopus 로고
    • DeGrip, W. J. and K. J. Rothschild (2000) Structure and mechanism of vertebrate visual pigments. In Handbook of Biological Physics, 3. Molecular Mechanisms in Visual Transduction (Edited by D. G. Stavenga, W. J. DeGrip and E. N. Pugh Jr), pp. 1-54. Elsevier Science Pub., Amsterdam.
    • DeGrip, W. J. and K. J. Rothschild (2000) Structure and mechanism of vertebrate visual pigments. In Handbook of Biological Physics, Vol. 3. Molecular Mechanisms in Visual Transduction (Edited by D. G. Stavenga, W. J. DeGrip and E. N. Pugh Jr), pp. 1-54. Elsevier Science Pub., Amsterdam.
  • 43
    • 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., Z. Ganim, J. E. Kim, M. A. Verhoeven, J. Lugtenburg and R. A. Mathies (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
  • 44
    • 3242687856 scopus 로고    scopus 로고
    • Formation of meta III during the decay of activated rhodopsin proceeds via meta I and not via meta II
    • Vogel, R., F. Siebert, X. Y. Zhang, G.-B. Fan and M. Sheves (2004) Formation of meta III during the decay of activated rhodopsin proceeds via meta I and not via meta II. Biochemistry 43, 9457-9466.
    • (2004) Biochemistry , vol.43 , pp. 9457-9466
    • Vogel, R.1    Siebert, F.2    Zhang, X.Y.3    Fan, G.-B.4    Sheves, M.5
  • 45
    • 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., E. D. Schmid, D. Perez-Sala, R. R. Rando and F. Siebert (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
  • 49
    • 3042798261 scopus 로고    scopus 로고
    • Molecular mechanisms of ligand binding, signaling, and regulation within the superfamily of G-proteincoupled receptors: Molecular modeling and mutagenesis approaches to receptor structure and function
    • Kristiansen, K. (2004) Molecular mechanisms of ligand binding, signaling, and regulation within the superfamily of G-proteincoupled receptors: Molecular modeling and mutagenesis approaches to receptor structure and function. Pharmacol. Ther. 103, 21-80.
    • (2004) Pharmacol. Ther , vol.103 , pp. 21-80
    • Kristiansen, K.1
  • 50
    • 20444499405 scopus 로고    scopus 로고
    • Probing the β2 adrenoceptor binding site with catechol reveals differences in binding and activation by agonists and partial agonists
    • Swaminath, G., X. Deupi' , T. W. Lee, W. Zhu, F. S. Thian, T. S. Kobilka and B. K. Kobilka (2005) Probing the β2 adrenoceptor binding site with catechol reveals differences in binding and activation by agonists and partial agonists. J. Biol. Chem. 280, 22165-22171.
    • (2005) J. Biol. Chem , vol.280 , pp. 22165-22171
    • Swaminath, G.1    Deupi', X.2    Lee, T.W.3    Zhu, W.4    Thian, F.S.5    Kobilka, T.S.6    Kobilka, B.K.7
  • 51
    • 33846635151 scopus 로고    scopus 로고
    • Solid-state NMR evidence for a protonation switch in the binding pocket of the H1 receptor upon binding of the agonist histamine
    • Ratnala, V. R. P., S. R. Kiihne, F. Buda, R. Leurs, H. J. M. de Groot and W. J. DeGrip (2007) Solid-state NMR evidence for a protonation switch in the binding pocket of the H1 receptor upon binding of the agonist histamine. J. Am. Chem. Soc. 129, 867-872.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 867-872
    • Ratnala, V.R.P.1    Kiihne, S.R.2    Buda, F.3    Leurs, R.4    de Groot, H.J.M.5    DeGrip, W.J.6
  • 52
    • 33847021802 scopus 로고    scopus 로고
    • Diseases caused by defects in the visual cycle: Retinoids as potential therapeutic agents
    • Travis, G. H., M. Golczak, A. R. Moise and K. Palczewski (2007) Diseases caused by defects in the visual cycle: Retinoids as potential therapeutic agents. Annu. Rev. Pharmacol. Toxicol. 47, 469-512.
    • (2007) Annu. Rev. Pharmacol. Toxicol , vol.47 , pp. 469-512
    • Travis, G.H.1    Golczak, M.2    Moise, A.R.3    Palczewski, K.4
  • 53
    • 34247250194 scopus 로고    scopus 로고
    • Delivery of retinoid-based therapies to target tissues
    • Moise, A. R., N. Noy, K. Palczewski and W. S. Blaner (2007) Delivery of retinoid-based therapies to target tissues. Biochemistry 46, 4449-4458.
    • (2007) Biochemistry , vol.46 , pp. 4449-4458
    • Moise, A.R.1    Noy, N.2    Palczewski, K.3    Blaner, W.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.