메뉴 건너뛰기




Volumn 9, Issue 11, 2010, Pages 1435-1443

Diversity and functional properties of bistable pigments

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA;

EID: 78049445464     PISSN: 1474905X     EISSN: 14749092     Source Type: Journal    
DOI: 10.1039/c0pp00168f     Document Type: Article
Times cited : (62)

References (83)
  • 2
    • 70349792168 scopus 로고    scopus 로고
    • Phototransduction motifs and variations
    • K. W. Yau R. C. Hardie Phototransduction motifs and variations Cell 2009 139 246 264
    • (2009) Cell , vol.139 , pp. 246-264
    • Yau, K.W.1    Hardie, R.C.2
  • 3
    • 0014428724 scopus 로고
    • The molecular basis of visual excitation
    • G. Wald The molecular basis of visual excitation Nature 1968 219 800 807
    • (1968) Nature , vol.219 , pp. 800-807
    • Wald, G.1
  • 4
    • 0343081370 scopus 로고    scopus 로고
    • X-Ray diffraction analysis of three-dimensional crystals of bovine rhodopsin obtained from mixed micelles
    • T. Okada I. Le Trong B. A. Fox C. A. Behnke R. E. Stenkamp K. Palczewski X-Ray diffraction analysis of three-dimensional crystals of bovine rhodopsin obtained from mixed micelles J. Struct. Biol. 2000 130 73 80
    • (2000) J. Struct. Biol. , vol.130 , pp. 73-80
    • Okada, T.1    Le Trong, I.2    Fox, B.A.3    Behnke, C.A.4    Stenkamp, R.E.5    Palczewski, K.6
  • 6
    • 0037285444 scopus 로고    scopus 로고
    • Rhodopsin structure, dynamics, and activation: A perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking
    • W. L. Hubbell C. Altenbach C. M. Hubbell H. G. Khorana Rhodopsin structure, dynamics, and activation: a perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking Adv. Protein Chem. 2003 63 243 290
    • (2003) Adv. Protein Chem. , vol.63 , pp. 243-290
    • Hubbell, W.L.1    Altenbach, C.2    Hubbell, C.M.3    Khorana, H.G.4
  • 7
    • 0020488317 scopus 로고
    • Complex formation between metarhodopsin II and GTP-binding protein in bovine photoreceptor membranes leads to a shift of the photoproduct equilibrium
    • D. Emeis H. Kuhn J. Reichert K. P. Hofmann Complex formation between metarhodopsin II and GTP-binding protein in bovine photoreceptor membranes leads to a shift of the photoproduct equilibrium FEBS Lett. 1982 143 29 34
    • (1982) FEBS Lett. , vol.143 , pp. 29-34
    • Emeis, D.1    Kuhn, H.2    Reichert, J.3    Hofmann, K.P.4
  • 8
    • 43749109187 scopus 로고    scopus 로고
    • Crystal structure of squid rhodopsin
    • M. Murakami T. Kouyama Crystal structure of squid rhodopsin Nature 2008 453 363 367
    • (2008) Nature , vol.453 , pp. 363-367
    • Murakami, M.1    Kouyama, T.2
  • 11
    • 73249125225 scopus 로고    scopus 로고
    • Identification and characterization of a protostome homologue of peropsin from a jumping spider
    • T. Nagata M. Koyanagi H. Tsukamoto A. Terakita Identification and characterization of a protostome homologue of peropsin from a jumping spider J. Comp. Physiol., A 2010 196 51 59
    • (2010) J. Comp. Physiol., A , vol.196 , pp. 51-59
    • Nagata, T.1    Koyanagi, M.2    Tsukamoto, H.3    Terakita, A.4
  • 13
    • 52149109504 scopus 로고    scopus 로고
    • Gq-coupled rhodopsin subfamily composed of invertebrate visual pigment and melanopsin
    • M. Koyanagi A. Terakita Gq-coupled rhodopsin subfamily composed of invertebrate visual pigment and melanopsin Photochem. Photobiol. 2008 84 1024 30
    • (2008) Photochem. Photobiol. , vol.84 , pp. 1024-1030
    • Koyanagi, M.1    Terakita, A.2
  • 20
    • 0347926182 scopus 로고    scopus 로고
    • Diminished pupillary light reflex at high irradiances in melanopsin-knockout mice
    • R. J. Lucas S. Hattar M. Takao D. M. Berson R. G. Foster K. W. Yau Diminished pupillary light reflex at high irradiances in melanopsin-knockout mice Science 2003 299 245 247
    • (2003) Science , vol.299 , pp. 245-247
    • Lucas, R.J.1    Hattar, S.2    Takao, M.3    Berson, D.M.4    Foster, R.G.5    Yau, K.W.6
  • 22
    • 20144378876 scopus 로고    scopus 로고
    • Cephalochordate melanopsin: Evolutionary linkage between invertebrate visual cells and vertebrate photosensitive retinal ganglion cells
    • M. Koyanagi K. Kubokawa H. Tsukamoto Y. Shichida A. Terakita Cephalochordate melanopsin: evolutionary linkage between invertebrate visual cells and vertebrate photosensitive retinal ganglion cells Curr. Biol. 2005 15 1065 1069
    • (2005) Curr. Biol. , vol.15 , pp. 1065-1069
    • Koyanagi, M.1    Kubokawa, K.2    Tsukamoto, H.3    Shichida, Y.4    Terakita, A.5
  • 23
    • 67049119906 scopus 로고    scopus 로고
    • Light-transduction in melanopsin-expressing photoreceptors of Amphioxus
    • P. Gomez Mdel J. M. Angueyra E. Nasi Light-transduction in melanopsin-expressing photoreceptors of Amphioxus Proc. Natl. Acad. Sci. U. S. A. 2009 106 9081 9086
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 9081-9086
    • Gomez Mdel, P.1    Angueyra, J.M.2    Nasi, E.3
  • 24
    • 0005918232 scopus 로고
    • Lumi- and meta-rhodopsins of squid and octopus
    • A. Kropf P. K. Brown R. Hubbard Lumi- and meta-rhodopsins of squid and octopus Nature 1959 183 446 448
    • (1959) Nature , vol.183 , pp. 446-448
    • Kropf, A.1    Brown, P.K.2    Hubbard, R.3
  • 25
    • 0027259284 scopus 로고
    • Interaction of GTP-binding protein Gq with photoactivated rhodopsin in the photoreceptor membranes of crayfish
    • A. Terakita T. Hariyama Y. Tsukahara Y. Katsukura H. Tashiro Interaction of GTP-binding protein Gq with photoactivated rhodopsin in the photoreceptor membranes of crayfish FEBS Lett. 1993 330 197 200
    • (1993) FEBS Lett. , vol.330 , pp. 197-200
    • Terakita, A.1    Hariyama, T.2    Tsukahara, Y.3    Katsukura, Y.4    Tashiro, H.5
  • 26
    • 0032515077 scopus 로고    scopus 로고
    • Selective activation of G-protein subtypes by vertebrate and invertebrate rhodopsins
    • A. Terakita T. Yamashita S. Tachibanaki Y. Shichida Selective activation of G-protein subtypes by vertebrate and invertebrate rhodopsins FEBS Lett. 1998 439 110 114
    • (1998) FEBS Lett. , vol.439 , pp. 110-114
    • Terakita, A.1    Yamashita, T.2    Tachibanaki, S.3    Shichida, Y.4
  • 27
    • 0029730789 scopus 로고    scopus 로고
    • Simple purification and functional reconstitution of octopus photoreceptor Gq, which couples rhodopsin to phospholipase C
    • S. Kikkawa K. Tominaga M. Nakagawa T. Iwasa M. Tsuda Simple purification and functional reconstitution of octopus photoreceptor Gq, which couples rhodopsin to phospholipase C Biochemistry 1996 35 15857 15864
    • (1996) Biochemistry , vol.35 , pp. 15857-15864
    • Kikkawa, S.1    Tominaga, K.2    Nakagawa, M.3    Iwasa, T.4    Tsuda, M.5
  • 29
    • 0033573379 scopus 로고    scopus 로고
    • Blue- and green-absorbing visual pigments of Drosophila: Ectopic expression and physiological characterization of the R8 photoreceptor cell-specific Rh5 and Rh6 rhodopsins
    • E. Salcedo A. Huber S. Henrich L. V. Chadwell W. H. Chou R. Paulsen S. G. Britt Blue- and green-absorbing visual pigments of Drosophila: ectopic expression and physiological characterization of the R8 photoreceptor cell-specific Rh5 and Rh6 rhodopsins J. Neurosci. 1999 19 10716 10726
    • (1999) J. Neurosci. , vol.19 , pp. 10716-10726
    • Salcedo, E.1    Huber, A.2    Henrich, S.3    Chadwell, L.V.4    Chou, W.H.5    Paulsen, R.6    Britt, S.G.7
  • 30
    • 0032053409 scopus 로고    scopus 로고
    • Honeybee blue- and ultraviolet-sensitive opsins: Cloning, heterologous expression in Drosophila, and physiological characterization
    • S. M. Townson B. S. Chang E. Salcedo L. V. Chadwell N. E. Pierce S. G. Britt Honeybee blue- and ultraviolet-sensitive opsins: cloning, heterologous expression in Drosophila, and physiological characterization J. Neurosci. 1998 18 2412 2422
    • (1998) J. Neurosci. , vol.18 , pp. 2412-2422
    • Townson, S.M.1    Chang, B.S.2    Salcedo, E.3    Chadwell, L.V.4    Pierce, N.E.5    Britt, S.G.6
  • 32
    • 42449108772 scopus 로고    scopus 로고
    • Expression and comparative characterization of Gq-coupled invertebrate visual pigments and melanopsin
    • A. Terakita H. Tsukamoto M. Koyanagi M. Sugahara T. Yamashita Y. Shichida Expression and comparative characterization of Gq-coupled invertebrate visual pigments and melanopsin J. Neurochem. 2008 105 883 890
    • (2008) J. Neurochem. , vol.105 , pp. 883-890
    • Terakita, A.1    Tsukamoto, H.2    Koyanagi, M.3    Sugahara, M.4    Yamashita, T.5    Shichida, Y.6
  • 35
    • 0034661790 scopus 로고    scopus 로고
    • Light transduction in invertebrate hyperpolarizing photoreceptors: Possible involvement of a Go-regulated guanylate cyclase
    • M. P. Gomez E. Nasi Light transduction in invertebrate hyperpolarizing photoreceptors: possible involvement of a Go-regulated guanylate cyclase J. Neurosci. 2000 20 5254 5263
    • (2000) J. Neurosci. , vol.20 , pp. 5254-5263
    • Gomez, M.P.1    Nasi, E.2
  • 36
    • 0037145820 scopus 로고    scopus 로고
    • Amphioxus homologs of Go-coupled rhodopsin and peropsin having 11-cis- and all-trans-retinals as their chromophores
    • M. Koyanagi A. Terakita K. Kubokawa Y. Shichida Amphioxus homologs of Go-coupled rhodopsin and peropsin having 11-cis- and all-trans-retinals as their chromophores FEBS Lett. 2002 531 525 528
    • (2002) FEBS Lett. , vol.531 , pp. 525-528
    • Koyanagi, M.1    Terakita, A.2    Kubokawa, K.3    Shichida, Y.4
  • 39
    • 31444456318 scopus 로고    scopus 로고
    • Melanopsin: Another way of signaling light
    • S. Peirson R. G. Foster Melanopsin: another way of signaling light Neuron 2006 49 331 339
    • (2006) Neuron , vol.49 , pp. 331-339
    • Peirson, S.1    Foster, R.G.2
  • 41
    • 0030886657 scopus 로고    scopus 로고
    • Peropsin, a novel visual pigment-like protein located in the apical microvilli of the retinal pigment epithelium
    • H. Sun D. J. Gilbert N. G. Copeland N. A. Jenkins J. Nathans Peropsin, a novel visual pigment-like protein located in the apical microvilli of the retinal pigment epithelium Proc. Natl. Acad. Sci. U. S. A. 1997 94 9893 9898
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 9893-9898
    • Sun, H.1    Gilbert, D.J.2    Copeland, N.G.3    Jenkins, N.A.4    Nathans, J.5
  • 42
    • 0006304290 scopus 로고
    • Slow photic responses of the isolated pineal organ of lamprey
    • Y. Morita E. Dodt Slow photic responses of the isolated pineal organ of lamprey Nova Acta Leopoldina 1973 38
    • (1973) Nova Acta Leopoldina , pp. 38
    • Morita, Y.1    Dodt, E.2
  • 43
    • 0006307493 scopus 로고
    • Evidence of UV receptors in pineal organ ? electophysiological and high performance liquid chromatography analysis
    • Y. Morita K. Uchida S. Tamotsu M. Samejima Evidence of UV receptors in pineal organ ? electophysiological and high performance liquid chromatography analysis Adv. Pineal Res. 1991 5 97 99
    • (1991) Adv. Pineal Res. , vol.5 , pp. 97-99
    • Morita, Y.1    Uchida, K.2    Tamotsu, S.3    Samejima, M.4
  • 44
    • 0000328982 scopus 로고
    • The photosensory function of the pineal organ of the pike (Esox lucius L.) correlation between structure and function
    • J. Falcon H. Meissl The photosensory function of the pineal organ of the pike (Esox lucius L.) correlation between structure and function J. Comp. Physiol. 1981 144 127 137
    • (1981) J. Comp. Physiol. , vol.144 , pp. 127-137
    • Falcon, J.1    Meissl, H.2
  • 45
    • 0000459384 scopus 로고
    • Mode of action of pineal nerve fibers in frogs
    • E. Dodt E. Heerd Mode of action of pineal nerve fibers in frogs J. Neurophysiol. 1962 25 405 429
    • (1962) J. Neurophysiol. , vol.25 , pp. 405-429
    • Dodt, E.1    Heerd, E.2
  • 46
    • 0020364217 scopus 로고
    • The pineal and parietal organs of lower vertebrates
    • E. Dodt H. Meissl The pineal and parietal organs of lower vertebrates Experientia 1982 38 996 1000
    • (1982) Experientia , vol.38 , pp. 996-1000
    • Dodt, E.1    Meissl, H.2
  • 47
    • 0019799122 scopus 로고
    • Pineal complex of the clawed toad, Xenopus laevis Daud.: Structure and function
    • H. W. Korf R. Liesner H. Meissl A. Kirk Pineal complex of the clawed toad, Xenopus laevis Daud.: structure and function Cell Tissue Res. 1981 216 113 130
    • (1981) Cell Tissue Res. , vol.216 , pp. 113-130
    • Korf, H.W.1    Liesner, R.2    Meissl, H.3    Kirk, A.4
  • 48
    • 0025324926 scopus 로고
    • Blue sensitive visual pigment and photoregeneration in pineal photoreceptors measured by high performance liquid chromatography
    • S. Tamotsu Y. Morita Blue sensitive visual pigment and photoregeneration in pineal photoreceptors measured by high performance liquid chromatography Comp. Biochem. Physiol., Part B: Biochem. Mol. Biol. 1990 96 487 490
    • (1990) Comp. Biochem. Physiol., Part B: Biochem. Mol. Biol. , vol.96 , pp. 487-490
    • Tamotsu, S.1    Morita, Y.2
  • 49
    • 0001287274 scopus 로고
    • Studies on rhodopsin. VIII. Retinylidenemethylamine, an indicator yellow analogue
    • G. A. Pitt F. D. Collins R. A. Morton P. Stok Studies on rhodopsin. VIII. Retinylidenemethylamine, an indicator yellow analogue Biochem. J. 1955 59 122 128
    • (1955) Biochem. J. , vol.59 , pp. 122-128
    • Pitt, G.A.1    Collins, F.D.2    Morton, R.A.3    Stok, P.4
  • 51
    • 0023050369 scopus 로고
    • The opsin family of proteins
    • J. B. Findlay D. J. Pappin The opsin family of proteins Biochem. J. 1986 238 625 642
    • (1986) Biochem. J. , vol.238 , pp. 625-642
    • Findlay, J.B.1    Pappin, D.J.2
  • 52
    • 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
    • A. Terakita T. Yamashita 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. 2000 97 14263 14267
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 14263-14267
    • Terakita, A.1    Yamashita, T.2    Shichida, Y.3
  • 53
    • 0024362631 scopus 로고
    • Effect of carboxylic acid side chains on the absorption maximum of visual pigments
    • E. A. Zhukovsky D. D. Oprian Effect of carboxylic acid side chains on the absorption maximum of visual pigments Science 1989 246 928 930
    • (1989) Science , vol.246 , pp. 928-930
    • Zhukovsky, E.A.1    Oprian, D.D.2
  • 54
    • 0025162902 scopus 로고
    • Determinants of visual pigment absorbance: Identification of the retinylidene Schiff's base counterion in bovine rhodopsin
    • J. Nathans Determinants of visual pigment absorbance: identification of the retinylidene Schiff's base counterion in bovine rhodopsin Biochemistry 1990 29 9746 9752
    • (1990) Biochemistry , vol.29 , pp. 9746-9752
    • Nathans, J.1
  • 55
    • 0343177634 scopus 로고
    • Glutamic acid-113 serves as the retinylidene Schiff base counterion in bovine rhodopsin
    • T. P. Sakmar R. R. Franke H. G. Khorana Glutamic acid-113 serves as the retinylidene Schiff base counterion in bovine rhodopsin Proc. Natl. Acad. Sci. U. S. A. 1989 86 8309 8313
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , pp. 8309-8313
    • Sakmar, T.P.1    Franke, R.R.2    Khorana, H.G.3
  • 58
    • 0034602145 scopus 로고    scopus 로고
    • Distinct roles of the second and third cytoplasmic loops of bovine rhodopsin in G protein activation
    • T. Yamashita A. Terakita Y. Shichida Distinct roles of the second and third cytoplasmic loops of bovine rhodopsin in G protein activation J. Biol. Chem. 2000 275 34272 34279
    • (2000) J. Biol. Chem. , vol.275 , pp. 34272-34279
    • Yamashita, T.1    Terakita, A.2    Shichida, Y.3
  • 59
    • 33947356279 scopus 로고    scopus 로고
    • G protein coupled receptor structure and activation
    • B. K. Kobilka G protein coupled receptor structure and activation Biochim. Biophys. Acta, Biomembr. 2007 1768 794 807
    • (2007) Biochim. Biophys. Acta, Biomembr. , vol.1768 , pp. 794-807
    • Kobilka, B.K.1
  • 60
    • 68949143130 scopus 로고    scopus 로고
    • The magnitude of the light-induced conformational change in different rhodopsins correlates with their ability to activate G proteins
    • H. Tsukamoto D. L. Farrens M. Koyanagi A. Terakita The magnitude of the light-induced conformational change in different rhodopsins correlates with their ability to activate G proteins J. Biol. Chem. 2009 284 20676 20683
    • (2009) J. Biol. Chem. , vol.284 , pp. 20676-20683
    • Tsukamoto, H.1    Farrens, D.L.2    Koyanagi, M.3    Terakita, A.4
  • 61
    • 0029907599 scopus 로고    scopus 로고
    • Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin
    • D. L. Farrens C. Altenbach K. Yang W. L. Hubbell H. G. Khorana Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin Science 1996 274 768 770
    • (1996) Science , vol.274 , pp. 768-770
    • Farrens, D.L.1    Altenbach, C.2    Yang, K.3    Hubbell, W.L.4    Khorana, H.G.5
  • 64
    • 47049130668 scopus 로고    scopus 로고
    • Crystal structure of the ligand-free G-protein-coupled receptor opsin
    • J. H. Park P. Scheerer K. P. Hofmann H. W. Choe O. P. Ernst Crystal structure of the ligand-free G-protein-coupled receptor opsin Nature 2008 454 183 187
    • (2008) Nature , vol.454 , pp. 183-187
    • Park, J.H.1    Scheerer, P.2    Hofmann, K.P.3    Choe, H.W.4    Ernst, O.P.5
  • 65
    • 56649102191 scopus 로고    scopus 로고
    • Conformational changes involved in G-protein-coupled-receptor activation
    • J. Wess S. J. Han S. K. Kim K. A. Jacobson J. H. Li Conformational changes involved in G-protein-coupled-receptor activation Trends Pharmacol. Sci. 2008 29 616 625
    • (2008) Trends Pharmacol. Sci. , vol.29 , pp. 616-625
    • Wess, J.1    Han, S.J.2    Kim, S.K.3    Jacobson, K.A.4    Li, J.H.5
  • 66
    • 0034464742 scopus 로고    scopus 로고
    • Uncovering molecular mechanisms involved in activation of G protein-coupled receptors
    • U. Gether Uncovering molecular mechanisms involved in activation of G protein-coupled receptors Endocr. Rev. 2000 21 90 113
    • (2000) Endocr. Rev. , vol.21 , pp. 90-113
    • Gether, U.1
  • 67
    • 0033534145 scopus 로고    scopus 로고
    • Determination of protein secondary structure and solvent accessibility using site-directed fluorescence labeling. Studies of T4 lysozyme using the fluorescent probe monobromobimane
    • S. E. Mansoor H. S. McHaourab D. L. Farrens Determination of protein secondary structure and solvent accessibility using site-directed fluorescence labeling. Studies of T4 lysozyme using the fluorescent probe monobromobimane Biochemistry 1999 38 16383 16393
    • (1999) Biochemistry , vol.38 , pp. 16383-16393
    • Mansoor, S.E.1    McHaourab, H.S.2    Farrens, D.L.3
  • 68
    • 0037176909 scopus 로고    scopus 로고
    • Mapping proximity within proteins using fluorescence spectroscopy. A study of T4 lysozyme showing that tryptophan residues quench bimane fluorescence
    • S. E. Mansoor H. S. McHaourab D. L. Farrens Mapping proximity within proteins using fluorescence spectroscopy. A study of T4 lysozyme showing that tryptophan residues quench bimane fluorescence Biochemistry 2002 41 2475 2784
    • (2002) Biochemistry , vol.41 , pp. 2475-2784
    • Mansoor, S.E.1    McHaourab, H.S.2    Farrens, D.L.3
  • 69
    • 0033555936 scopus 로고    scopus 로고
    • Conformational changes in rhodopsin. Movement of helix f detected by site-specific chemical labeling and fluorescence spectroscopy
    • T. D. Dunham D. L. Farrens Conformational changes in rhodopsin. Movement of helix f detected by site-specific chemical labeling and fluorescence spectroscopy J. Biol. Chem. 1999 274 1683 1690
    • (1999) J. Biol. Chem. , vol.274 , pp. 1683-1690
    • Dunham, T.D.1    Farrens, D.L.2
  • 70
    • 3242726738 scopus 로고    scopus 로고
    • High-throughput protein structural analysis using site-directed fluorescence labeling and the bimane derivative (2-pyridyl)dithiobimane
    • S. E. Mansoor D. L. Farrens High-throughput protein structural analysis using site-directed fluorescence labeling and the bimane derivative (2-pyridyl)dithiobimane Biochemistry 2004 43 9426 9438
    • (2004) Biochemistry , vol.43 , pp. 9426-9438
    • Mansoor, S.E.1    Farrens, D.L.2
  • 72
    • 4344581120 scopus 로고    scopus 로고
    • The retinal conformation and its environment in rhodopsin in light of a new 2.2 A crystal structure
    • T. Okada M. Sugihara A. N. Bondar M. Elstner P. Entel V. Buss The retinal conformation and its environment in rhodopsin in light of a new 2.2 A crystal structure J. Mol. Biol. 2004 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
  • 73
    • 0028017506 scopus 로고
    • Identification of glutamic acid 113 as the Schiff base proton acceptor in the metarhodopsin II photointermediate of rhodopsin
    • F. Jager K. Fahmy T. P. Sakmar F. Siebert Identification of glutamic acid 113 as the Schiff base proton acceptor in the metarhodopsin II photointermediate of rhodopsin Biochemistry 1994 33 10878 10882
    • (1994) Biochemistry , vol.33 , pp. 10878-10882
    • Jager, F.1    Fahmy, K.2    Sakmar, T.P.3    Siebert, F.4
  • 76
    • 77952906089 scopus 로고    scopus 로고
    • Structure and activation of the visual pigment rhodopsin
    • S. O. Smith Structure and activation of the visual pigment rhodopsin Annu. Rev. Biophys. 2010 39 309 328
    • (2010) Annu. Rev. Biophys. , vol.39 , pp. 309-328
    • Smith, S.O.1
  • 77
    • 77951238241 scopus 로고    scopus 로고
    • A pivot between helices v and VI near the retinal-binding site is necessary for activation in rhodopsins
    • H. Tsukamoto A. Terakita Y. Shichida A pivot between helices V and VI near the retinal-binding site is necessary for activation in rhodopsins J. Biol. Chem. 2010 285 7351 7357
    • (2010) J. Biol. Chem. , vol.285 , pp. 7351-7357
    • Tsukamoto, H.1    Terakita, A.2    Shichida, Y.3
  • 78
    • 38749131545 scopus 로고    scopus 로고
    • New G-protein-coupled receptor crystal structures: Insights and limitations
    • B. Kobilka G. F. Schertler New G-protein-coupled receptor crystal structures: insights and limitations Trends Pharmacol. Sci. 2008 29 79 83
    • (2008) Trends Pharmacol. Sci. , vol.29 , pp. 79-83
    • Kobilka, B.1    Schertler, G.F.2
  • 79
    • 58149203324 scopus 로고    scopus 로고
    • Discovery of new GPCR biology: One receptor structure at a time
    • M. A. Hanson R. C. Stevens Discovery of new GPCR biology: one receptor structure at a time Structure 2009 17 8 14
    • (2009) Structure , vol.17 , pp. 8-14
    • Hanson, M.A.1    Stevens, R.C.2
  • 80
    • 66249144426 scopus 로고    scopus 로고
    • The structure and function of G-protein-coupled receptors
    • D. M. Rosenbaum S. G. Rasmussen B. K. Kobilka The structure and function of G-protein-coupled receptors Nature 2009 459 356 63
    • (2009) Nature , vol.459 , pp. 356-363
    • Rosenbaum, D.M.1    Rasmussen, S.G.2    Kobilka, B.K.3
  • 82
    • 38949192595 scopus 로고    scopus 로고
    • A crystal clear view of the beta2-adrenergic receptor
    • R. J. Lefkowitz J. P. Sun A. K. Shukla A crystal clear view of the beta2-adrenergic receptor Nat. Biotechnol. 2008 26 189 191
    • (2008) Nat. Biotechnol. , vol.26 , pp. 189-191
    • Lefkowitz, R.J.1    Sun, J.P.2    Shukla, A.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.