메뉴 건너뛰기




Volumn 25, Issue , 1996, Pages 287-314

Activating mutations of rhodopsin and other G protein-coupled receptors

Author keywords

constitutive activity; Schiff base; seven helix receptor; visual pigments

Indexed keywords

11 CIS RETINAL; GUANINE NUCLEOTIDE BINDING PROTEIN; OPSIN; RHODOPSIN; SCHIFF BASE;

EID: 0029993990     PISSN: 10568700     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.bb.25.060196.001443     Document Type: Review
Times cited : (135)

References (125)
  • 1
    • 0023759613 scopus 로고
    • Low retinal noise in animals with low body temperature allows high visual sensitivity
    • Aho AC, Donner K, Hyden C, Larsen LO, Reuter T. 1988. Low retinal noise in animals with low body temperature allows high visual sensitivity. Nature 334:348-50
    • (1988) Nature , vol.334 , pp. 348-350
    • Aho, A.C.1    Donner, K.2    Hyden, C.3    Larsen, L.O.4    Reuter, T.5
  • 2
    • 8944261079 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof.
  • 3
    • 0026318020 scopus 로고
    • G-protein-coupled receptor genes as protooncogenes: Constitutively activating mutation of the α- adrenergic receptor enhances mitogenesis and tumorigenicity
    • Allen LF, Lefkowitz RJ, Caron MG, Cotecchia S. 1991. G-protein-coupled receptor genes as protooncogenes: constitutively activating mutation of the α- adrenergic receptor enhances mitogenesis and tumorigenicity. Proc. Natl. Acad. Sci. USA 88: 11354-58
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 11354-11358
    • Allen, L.F.1    Lefkowitz, R.J.2    Caron, M.G.3    Cotecchia, S.4
  • 4
    • 0025234587 scopus 로고
    • pH-Induced denaturation of protein: A single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme
    • Anderson DE, Becktel WJ, Dahlquist FW. 1990. pH-Induced denaturation of protein: a single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme. Biochemistry 29:2403-8
    • (1990) Biochemistry , vol.29 , pp. 2403-2408
    • Anderson, D.E.1    Becktel, W.J.2    Dahlquist, F.W.3
  • 5
    • 0028061193 scopus 로고
    • A conserved carboxylic acid group mediates light-dependent proton uptake and signalling by rhodopsin
    • Arnis S, Fahmy K, Hoffman KP, Sakmar TP. 1994. A conserved carboxylic acid group mediates light-dependent proton uptake and signalling by rhodopsin. J. Biol. Chem. 269: 23879-81
    • (1994) J. Biol. Chem. , vol.269 , pp. 23879-23881
    • Arnis, S.1    Fahmy, K.2    Hoffman, K.P.3    Sakmar, T.P.4
  • 6
    • 0022405801 scopus 로고
    • Fourier-transform infrared difference spectroscopy of rhodopsin and its photoproducts at low temperature
    • Bagley KA, Balogh-Nair V, Croteau AA, Dollinger G, Ebrey TG, et al. 1985. Fourier-transform infrared difference spectroscopy of rhodopsin and its photoproducts at low temperature. Biochemistry 24:6055-71
    • (1985) Biochemistry , vol.24 , pp. 6055-6071
    • Bagley, K.A.1    Balogh-Nair, V.2    Croteau, A.A.3    Dollinger, G.4    Ebrey, T.G.5
  • 7
    • 0027506471 scopus 로고
    • The probable arrangement of the helices in G protein-coupled receptors
    • Baldwin JM. 1993. The probable arrangement of the helices in G protein-coupled receptors. EMBO J. 12: 1693-703
    • (1993) EMBO J. , vol.12 , pp. 1693-1703
    • Baldwin, J.M.1
  • 8
    • 0001098005 scopus 로고
    • Retinal noise and absolute threshold
    • Barlow HB. 1956. Retinal noise and absolute threshold. J. Opt. Soc. Am. 46:634-39
    • (1956) J. Opt. Soc. Am. , vol.46 , pp. 634-639
    • Barlow, H.B.1
  • 9
    • 0024298870 scopus 로고
    • The thermal limit to seeing
    • Barlow HB. 1988. The thermal limit to seeing. Nature 334: 296-97
    • (1988) Nature , vol.334 , pp. 296-297
    • Barlow, H.B.1
  • 11
    • 0018333003 scopus 로고
    • Responses of retinal rods to single photons
    • Baylor DA, Lamb RD, Yau K-W. 1979. Responses of retinal rods to single photons. J. Physiol. 288: 613-34
    • (1979) J. Physiol. , vol.288 , pp. 613-634
    • Baylor, D.A.1    Lamb, R.D.2    Yau, K.-W.3
  • 12
    • 0019225828 scopus 로고
    • Two components of electrical dark noise in toad retinal rod outer segments
    • Baylor DA, Matthews G, Yau K-W. 1980. Two components of electrical dark noise in toad retinal rod outer segments. J. Physiol. 309:591-621
    • (1980) J. Physiol. , vol.309 , pp. 591-621
    • Baylor, D.A.1    Matthews, G.2    Yau, K.-W.3
  • 13
    • 0021646399 scopus 로고
    • The photocurrent noise and spectral sensitivity of rods of the monkey Macaca fascicularis
    • Baylor DA, Nunn BJ, Schnapf JL. 1984. The photocurrent noise and spectral sensitivity of rods of the monkey Macaca fascicularis. J. Physiol. 357:575-607
    • (1984) J. Physiol. , vol.357 , pp. 575-607
    • Baylor, D.A.1    Nunn, B.J.2    Schnapf, J.L.3
  • 14
    • 0027537949 scopus 로고
    • Retinitis pigmentosa: The Friedenwald lecture
    • Berson EL. 1993. Retinitis pigmentosa: the Friedenwald lecture. Invest. Ophthalmol. Vis. Sci. 34: 1659-76
    • (1993) Invest. Ophthalmol. Vis. Sci. , vol.34 , pp. 1659-1676
    • Berson, E.L.1
  • 15
    • 0005853391 scopus 로고
    • Two-photon spectroscopy of locked-11-cis-rhodopsin: Evidence for a protonated Schiff base in a neutral protein binding site
    • Birge RR, Murray LP, Pierce BM, Akita H, Balogh-Nair V, et al. 1985. Two-photon spectroscopy of locked-11-cis-rhodopsin: evidence for a protonated Schiff base in a neutral protein binding site. Proc. Natl. Acad. Sci. USA 82:4117-21
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 4117-4121
    • Birge, R.R.1    Murray, L.P.2    Pierce, B.M.3    Akita, H.4    Balogh-Nair, V.5
  • 16
    • 12044260162 scopus 로고
    • Mutations that alter the third cytoplasmic loop of the a-factor receptor lead to a constitutive and hypersensitive phenotype
    • Boone C, Davis NG, Sprague GF Jr. 1993. Mutations that alter the third cytoplasmic loop of the a-factor receptor lead to a constitutive and hypersensitive phenotype. Proc. Natl. Acad. Sci. USA 90:9921-25
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9921-9925
    • Boone, C.1    Davis, N.G.2    Sprague Jr., G.F.3
  • 17
    • 0014215238 scopus 로고
    • Site of attachment of retinal in rhodopsin
    • Bownds D. 1967. Site of attachment of retinal in rhodopsin. Nature 216: 1178-81
    • (1967) Nature , vol.216 , pp. 1178-1181
    • Bownds, D.1
  • 18
    • 8944236748 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof.
  • 19
    • 0027050784 scopus 로고
    • Mechanism of activation and inactivation of opsin: Role of Glu113 and Lys296
    • Cohen GB, Oprian DD, Robinson PR. 1992. Mechanism of activation and inactivation of opsin: role of Glu113 and Lys296. Biochemistry 31:12592-601
    • (1992) Biochemistry , vol.31 , pp. 12592-12601
    • Cohen, G.B.1    Oprian, D.D.2    Robinson, P.R.3
  • 20
    • 0027298812 scopus 로고
    • Constitutive activation of opsin: Influence of charge at position 134 and size at position 296
    • Cohen GB, Yang T, Robinson PR, Oprian DD. 1993. Constitutive activation of opsin: influence of charge at position 134 and size at position 296. Biochemistry 32:6111-15
    • (1993) Biochemistry , vol.32 , pp. 6111-6115
    • Cohen, G.B.1    Yang, T.2    Robinson, P.R.3    Oprian, D.D.4
  • 21
    • 0028914025 scopus 로고
    • Defective intracellular transport is the molecular basis of rhodopsin-dependent retinal degeneration
    • Colley NJ, Cassil JA, Baker EK, Zuker CS. 1995. Defective intracellular transport is the molecular basis of rhodopsin-dependent retinal degeneration. Proc. Natl. Acad. Sci. USA 92:3070-74
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3070-3074
    • Colley, N.J.1    Cassil, J.A.2    Baker, E.K.3    Zuker, C.S.4
  • 23
    • 0025212680 scopus 로고
    • Regions of the α-adrenergic receptor involved in coupling to phosphatidylinositol hydrolysis and enhanced sensitivity of biological function
    • Cotecchia S, Exum S, Caron MG, Lefkowitz RJ. 1990. Regions of the α-adrenergic receptor involved in coupling to phosphatidylinositol hydrolysis and enhanced sensitivity of biological function. Proc. Natl. Acad. Sci. USA 87:2896-900
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2896-2900
    • Cotecchia, S.1    Exum, S.2    Caron, M.G.3    Lefkowitz, R.J.4
  • 24
    • 0020571486 scopus 로고
    • Rhodopsin chromophore exchanges among opsin molecules in the dark
    • Defoe DM, Bok D. 1983. Rhodopsin chromophore exchanges among opsin molecules in the dark. Invest. Ophthalmol. Vis. Sci. 24:1211-26
    • (1983) Invest. Ophthalmol. Vis. Sci. , vol.24 , pp. 1211-1226
    • Defoe, D.M.1    Bok, D.2
  • 27
    • 0017818529 scopus 로고
    • Resonance raman studies of bovine metarhodopsin I and metarhodopsin II
    • Doukas AG, Aton B, Callender RH, Ebrey TG. 1978. Resonance raman studies of bovine metarhodopsin I and metarhodopsin II. Biochemistry 17:2430-35
    • (1978) Biochemistry , vol.17 , pp. 2430-2435
    • Doukas, A.G.1    Aton, B.2    Callender, R.H.3    Ebrey, T.G.4
  • 28
    • 0000476834 scopus 로고
    • The structure of rhodopsin and the rod outer segment disk membrane
    • Dratz EA, Hargrave PA. 1983. The structure of rhodopsin and the rod outer segment disk membrane. Trends Biochem. Sci. 8:128-31
    • (1983) Trends Biochem. Sci. , vol.8 , pp. 128-131
    • Dratz, E.A.1    Hargrave, P.A.2
  • 29
    • 0027248024 scopus 로고
    • Heterozygous missense mutation in the rhodopsin gene as a cause of congenital stationary night blindness
    • Dryja TP, Berson EL, Rao VR, Oprian DD. 1993. Heterozygous missense mutation in the rhodopsin gene as a cause of congenital stationary night blindness. Nature Genet. 4: 280-83
    • (1993) Nature Genet. , vol.4 , pp. 280-283
    • Dryja, T.P.1    Berson, E.L.2    Rao, V.R.3    Oprian, D.D.4
  • 30
    • 0028240982 scopus 로고
    • Germline mutations in the thyrotropin receptor gene cause non-autoimmune autosomal dominant hyperthyroidism
    • Duprez L, Parma J, Van Sande J, Allgeier A, Leclere J, et al. 1994. Germline mutations in the thyrotropin receptor gene cause non-autoimmune autosomal dominant hyperthyroidism. Nature Genet. 7:396-401
    • (1994) Nature Genet. , vol.7 , pp. 396-401
    • Duprez, L.1    Parma, J.2    Van Sande, J.3    Allgeier, A.4    Leclere, J.5
  • 31
    • 8944261933 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof.
  • 32
    • 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, Kuhn H, Reichert J, Hoffman KP. 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    Kuhn, H.2    Reichert, J.3    Hoffman, K.P.4
  • 33
    • 0026567907 scopus 로고
    • Response of protein structure to cavity-creating mutations and its relation to the hydrophobic effect
    • Erikkson AE, Baase WA, Zheng X-J, Heinz DW, Blaker M, et al. 1992. Response of protein structure to cavity-creating mutations and its relation to the hydrophobic effect. Science 255:178-83
    • (1992) Science , vol.255 , pp. 178-183
    • Erikkson, A.E.1    Baase, W.A.2    Zheng, X.-J.3    Heinz, D.W.4    Blaker, M.5
  • 34
    • 0027374544 scopus 로고
    • Protonation states of membrane-embedded carboxylic acid groups in rhodopsin and metarhodopsin II: A Fourier-transform infrared spectroscopy study of site-directed mutants
    • Fahmy K, Jager F, Beck M, Zvyaga TA, Sakmar TP, Siebert F. 1993. Protonation states of membrane-embedded carboxylic acid groups in rhodopsin and metarhodopsin II: a Fourier-transform infrared spectroscopy study of site-directed mutants. Proc. Natl. Acad. Sci. USA 90: 10206-10
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10206-10210
    • Fahmy, K.1    Jager, F.2    Beck, M.3    Zvyaga, T.A.4    Sakmar, T.P.5    Siebert, F.6
  • 35
    • 0027270898 scopus 로고
    • Regulation of the rhodopsin-transducin interaction by a highly conserved carboxylic acid group
    • Fahmy K, Sakmar TP. 1993. Regulation of the rhodopsin-transducin interaction by a highly conserved carboxylic acid group. Biochemistry 32: 7229-36
    • (1993) Biochemistry , vol.32 , pp. 7229-7236
    • Fahmy, K.1    Sakmar, T.P.2
  • 36
    • 0028102745 scopus 로고
    • A mutant rhodopsin photoproduct with a protonated Schiff base displays an active-state conformation: A Fourier-transform infrared spectroscopy study
    • Fahmy K, Siebert F, Sakmar TP. 1994. A mutant rhodopsin photoproduct with a protonated Schiff base displays an active-state conformation: a Fourier-transform infrared spectroscopy study. Biochemistry 33: 13700-5
    • (1994) Biochemistry , vol.33 , pp. 13700-13705
    • Fahmy, K.1    Siebert, F.2    Sakmar, T.P.3
  • 37
    • 0027716597 scopus 로고
    • Photoactivated conformational changes in rhodopsin: A time-resolved spin label study
    • Farahbakhsh ZT, Hideg K, Hubbell WL. 1993. Photoactivated conformational changes in rhodopsin: a time-resolved spin label study. Science 262:1416-19
    • (1993) Science , vol.262 , pp. 1416-1419
    • Farahbakhsh, Z.T.1    Hideg, K.2    Hubbell, W.L.3
  • 38
    • 0029035661 scopus 로고
    • Mapping light-dependent structural changes in the cytoplasmic loop connecting helices C and D in rhodopsin: A site-directed spin labelling study
    • Farahbakhsh ZT, Ridge KD, Khorana HG, Hubbell WL. 1995. Mapping light-dependent structural changes in the cytoplasmic loop connecting helices C and D in rhodopsin: a site-directed spin labelling study. Biochemistry 34:8812-19
    • (1995) Biochemistry , vol.34 , pp. 8812-8819
    • Farahbakhsh, Z.T.1    Ridge, K.D.2    Khorana, H.G.3    Hubbell, W.L.4
  • 40
    • 0026780339 scopus 로고
    • Structure and function in rhodopsin: Studies of the interaction between the rhodopsin cytoplasmic domain and transducin
    • Franke RR, Sakmar TP, Graham RM, Khorana HG. 1992. Structure and function in rhodopsin: studies of the interaction between the rhodopsin cytoplasmic domain and transducin. J. Biol. Chem. 267:14767-74
    • (1992) J. Biol. Chem. , vol.267 , pp. 14767-14774
    • Franke, R.R.1    Sakmar, T.P.2    Graham, R.M.3    Khorana, H.G.4
  • 41
    • 0028489055 scopus 로고
    • Heterozygous missense mutation in the rod cGMP phosphodiesterase β-subunit gene in autosomal dominant stationary night blindness
    • Gal A, Orth U, Baehr W, Schwinger E, Rosenberg T. 1994. Heterozygous missense mutation in the rod cGMP phosphodiesterase β-subunit gene in autosomal dominant stationary night blindness. Nature Genet. 7:64-68
    • (1994) Nature Genet. , vol.7 , pp. 64-68
    • Gal, A.1    Orth, U.2    Baehr, W.3    Schwinger, E.4    Rosenberg, T.5
  • 42
    • 0026099851 scopus 로고
    • Fourier transform infrared studies of active-site-methylated rhodopsin: Implications for chromophore-protein interaction, transducin activation, and the reaction pathway
    • Ganter UM, Longstaff C, Pajares MA, Rando RR, Siebert F. 1991. Fourier transform infrared studies of active-site-methylated rhodopsin: implications for chromophore-protein interaction, transducin activation, and the reaction pathway. Biophys. J. 59:640-44
    • (1991) Biophys. J. , vol.59 , pp. 640-644
    • Ganter, U.M.1    Longstaff, C.2    Pajares, M.A.3    Rando, R.R.4    Siebert, F.5
  • 43
    • 0000559536 scopus 로고
    • A mechanism for controlling the pKa of the retinal protonated Schiff base in retinal proteins. A study with model compounds
    • Gat Y, Sheves M. 1993.A mechanism for controlling the pKa of the retinal protonated Schiff base in retinal proteins. A study with model compounds. J. Am. Chem Soc. 115: 3772-73
    • (1993) J. Am. Chem Soc. , vol.115 , pp. 3772-3773
    • Gat, Y.1    Sheves, M.2
  • 44
    • 8944222308 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof.
  • 45
    • 0023062991 scopus 로고
    • G-proteins: Transducers of receptor generated signals
    • Gilman AG. 1987. G-proteins: transducers of receptor generated signals. Annu. Rev. Biochem. 56:615-49
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 615-649
    • Gilman, A.G.1
  • 46
    • 0028300554 scopus 로고
    • Active site-directed inactivation of constitutively active mutants of rhodopsin
    • Govardhan CP, Oprian DD. 1994. Active site-directed inactivation of constitutively active mutants of rhodopsin. J. Biol. Chem. 269:6524-27
    • (1994) J. Biol. Chem. , vol.269 , pp. 6524-6527
    • Govardhan, C.P.1    Oprian, D.D.2
  • 47
    • 0028916739 scopus 로고
    • NMR constraints on the location of the retinal chromophore in rhodopsin and bathorhodopsin
    • Han M, Smith SO. 1995. NMR constraints on the location of the retinal chromophore in rhodopsin and bathorhodopsin. Biochemistry 34: 1425-32
    • (1995) Biochemistry , vol.34 , pp. 1425-1432
    • Han, M.1    Smith, S.O.2
  • 48
    • 0027352613 scopus 로고
    • Interaction of rhodopsin with the G-protein, transducin
    • Hargrave PA, Hamm HE, Hofmann KP. 1993. Interaction of rhodopsin with the G-protein, transducin. BioEssays 15:43-50
    • (1993) BioEssays , vol.15 , pp. 43-50
    • Hargrave, P.A.1    Hamm, H.E.2    Hofmann, K.P.3
  • 49
    • 0027368165 scopus 로고
    • Strucure and mechanism of the G protein coupled receptor kinases
    • Inglese J, Freedman NJ, Koch WJ, Lefkowitz RJ. 1993. Strucure and mechanism of the G protein coupled receptor kinases. J. Biol. Chem. 268: 23735-38
    • (1993) J. Biol. Chem. , vol.268 , pp. 23735-23738
    • Inglese, J.1    Freedman, N.J.2    Koch, W.J.3    Lefkowitz, R.J.4
  • 50
    • 0028017506 scopus 로고
    • Identification of glutamic acid 113 as the schiff base proton acceptor in the metarhodopsin II photointermediate of rhodopsin
    • Jager F, Fahmy K, Sakmar TP, Sieben F. 1994. Identification of glutamic acid 113 as the schiff base proton acceptor in the metarhodopsin II photointermediate of rhodopsin. Biochemistry 33:10878-82
    • (1994) Biochemistry , vol.33 , pp. 10878-10882
    • Jager, F.1    Fahmy, K.2    Sakmar, T.P.3    Sieben, F.4
  • 51
    • 0027525290 scopus 로고
    • Non-covalent occupancy of the retinal-binding pocket of opsin diminishes bleaching adaptation of retinal cones
    • Jin J, Crouch RK, Corson DW, Katz BM, MacNichol EF, Cornwall MC. 1993. Non-covalent occupancy of the retinal-binding pocket of opsin diminishes bleaching adaptation of retinal cones. Neuron 11:513-22
    • (1993) Neuron , vol.11 , pp. 513-522
    • Jin, J.1    Crouch, R.K.2    Corson, D.W.3    Katz, B.M.4    MacNichol, E.F.5    Cornwall, M.C.6
  • 52
    • 0024385411 scopus 로고
    • Ectopic expression of the serotonin 1c receptor and the triggering of malignant transformation
    • Julius D, Livelli TJ, Jessell TM, Axel R. 1989. Ectopic expression of the serotonin 1c receptor and the triggering of malignant transformation. Science 244:1057-62
    • (1989) Science , vol.244 , pp. 1057-1062
    • Julius, D.1    Livelli, T.J.2    Jessell, T.M.3    Axel, R.4
  • 53
    • 0028287273 scopus 로고
    • Structure and function in rhodopsin. 7. Point mutations associated with autosomal dominant retinitis pigmentosa
    • Kaushal S, Khorana HG. 1994. Structure and function in rhodopsin. 7. Point mutations associated with autosomal dominant retinitis pigmentosa. Biochemistry 33:6121-28
    • (1994) Biochemistry , vol.33 , pp. 6121-6128
    • Kaushal, S.1    Khorana, H.G.2
  • 54
    • 0025944670 scopus 로고
    • Autosomal dominant retinitis pigmentosa: Four new mutations in rhodopsin, one of them in the retinal binding site
    • Keen TJ, Inglehearn CF, Lester DH, Bashir R, Jay M, et al. 1991. Autosomal dominant retinitis pigmentosa: four new mutations in rhodopsin, one of them in the retinal binding site. Genomics 11:199-205
    • (1991) Genomics , vol.11 , pp. 199-205
    • Keen, T.J.1    Inglehearn, C.F.2    Lester, D.H.3    Bashir, R.4    Jay, M.5
  • 55
    • 0025823575 scopus 로고
    • Functional equivalence of metarhodopsin II and the G activating form of photolyzed bovine rhodopsin
    • Kibelbek J, Mitchell DC, Beach JM, Litmann BJ. 1991. Functional equivalence of metarhodopsin II and the G activating form of photolyzed bovine rhodopsin. Biochemistry 30:6761-68
    • (1991) Biochemistry , vol.30 , pp. 6761-6768
    • Kibelbek, J.1    Mitchell, D.C.2    Beach, J.M.3    Litmann, B.J.4
  • 56
    • 0026592357 scopus 로고
    • Constitutive activation of the α-adrenergic receptor by all amino acid substitutions at a single site
    • Kjelsberg MA, Cotecchia S, Ostrowski J, Caron MG, Lefkowitz RJ. 1992, Constitutive activation of the α-adrenergic receptor by all amino acid substitutions at a single site. J. Biol. Chem. 267:1430-33
    • (1992) J. Biol. Chem. , vol.267 , pp. 1430-1433
    • Kjelsberg, M.A.1    Cotecchia, S.2    Ostrowski, J.3    Caron, M.G.4    Lefkowitz, R.J.5
  • 58
    • 0028113398 scopus 로고
    • Constitutive activation of cyclic AMP but not phosphatidylinositol signalling caused by four mutations in the sixth transmembrane helix of the human thyrotropin receptor
    • Kosugi S, Shenker A, Mori T. 1994. Constitutive activation of cyclic AMP but not phosphatidylinositol signalling caused by four mutations in the sixth transmembrane helix of the human thyrotropin receptor. FEBS Lett. 356:291-94
    • (1994) FEBS Lett. , vol.356 , pp. 291-294
    • Kosugi, S.1    Shenker, A.2    Mori, T.3
  • 59
    • 0024592440 scopus 로고
    • Regeneration of bovine and octopus opsins in situ with retinal and artificial retinals
    • Koutalos Y, Ebrey TG, Tsuda M, Odashima K, Lien T, et al. 1989. Regeneration of bovine and octopus opsins in situ with retinal and artificial retinals. Biochemistry 28:2732-39
    • (1989) Biochemistry , vol.28 , pp. 2732-2739
    • Koutalos, Y.1    Ebrey, T.G.2    Tsuda, M.3    Odashima, K.4    Lien, T.5
  • 60
    • 0028944310 scopus 로고
    • Genetic heterogeneity of constitutively activating mutations of the human luteinizing hormone receptor in familial male-limited precocious puberty
    • Laue L, Chan W-Y, Hseuh AJ, Kudo M, Hsu SY, et al. 1995. Genetic heterogeneity of constitutively activating mutations of the human luteinizing hormone receptor in familial male-limited precocious puberty. Proc. Natl. Acad Sci. USA 92: 1906-10
    • (1995) Proc. Natl. Acad Sci. USA , vol.92 , pp. 1906-1910
    • Laue, L.1    Chan, W.-Y.2    Hseuh, A.J.3    Kudo, M.4    Hsu, S.Y.5
  • 61
    • 0027494368 scopus 로고
    • Turned on to ill effect
    • Lefkowitz RJ. 1993. Turned on to ill effect. Nature 365:603-4
    • (1993) Nature , vol.365 , pp. 603-604
    • Lefkowitz, R.J.1
  • 62
    • 0028947938 scopus 로고
    • Constitutive activation of phototransduction by K296E opsin is not the cause of photoreceptor degeneration
    • Li T, Franson WK, Gordon JW, Berson EL, Dryja TP. 1995. Constitutive activation of phototransduction by K296E opsin is not the cause of photoreceptor degeneration. Proc. Natl. Acad. Sci. USA 92:3551-55
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3551-3555
    • Li, T.1    Franson, W.K.2    Gordon, J.W.3    Berson, E.L.4    Dryja, T.P.5
  • 63
    • 0026750971 scopus 로고
    • Resonance Raman microprobe spectroscopy of rhodopsin mutants: Effect of substitutions in the third transmembrane helix
    • Lin SW, Sakmar TP, Franke RR, Khorana HG, Matthies RA. 1992. Resonance Raman microprobe spectroscopy of rhodopsin mutants: effect of substitutions in the third transmembrane helix. Biochemistry 31: 5105-11
    • (1992) Biochemistry , vol.31 , pp. 5105-5111
    • Lin, S.W.1    Sakmar, T.P.2    Franke, R.R.3    Khorana, H.G.4    Matthies, R.A.5
  • 64
    • 0027956207 scopus 로고
    • Rapid GDP release from G in patients with gain and loss of endocrine function
    • Liri T, Herzmark P, Nakamoto J, van Dop C, Bourne HR. 1994. Rapid GDP release from G in patients with gain and loss of endocrine function. Nature 371:164-68
    • (1994) Nature , vol.371 , pp. 164-168
    • Liri, T.1    Herzmark, P.2    Nakamoto, J.3    Van Dop, C.4    Bourne, H.R.5
  • 65
    • 0011480156 scopus 로고
    • Deprotonation of the Schiff base of rhodopsin is obligate in the activation of the G protein
    • Longstaff C, Calhoon RD, Rando RR. 1986. Deprotonation of the Schiff base of rhodopsin is obligate in the activation of the G protein. Proc. Natl. Acad. Sci. USA 83: 4209-13
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 4209-4213
    • Longstaff, C.1    Calhoon, R.D.2    Rando, R.R.3
  • 67
    • 0028838954 scopus 로고
    • Truncation of the thyrotropin-releasing hormone receptor carboxy tail causes constitutive activity and leads to impaired responsiveness in Xenopus oocytes and AtT20 cells
    • Matus-Leibovitch N, Nussenzveig DR, Gershengorn MC, Oron Y. 1995. Truncation of the thyrotropin-releasing hormone receptor carboxy tail causes constitutive activity and leads to impaired responsiveness in Xenopus oocytes and AtT20 cells. J. Biol. Chem. 270:1041-47
    • (1995) J. Biol. Chem. , vol.270 , pp. 1041-1047
    • Matus-Leibovitch, N.1    Nussenzveig, D.R.2    Gershengorn, M.C.3    Oron, Y.4
  • 68
    • 0027273840 scopus 로고
    • Characterization of mutant rhodopsin responsible for autosomal dominant retinitis pigmentosa: Mutations on the cytoplasmic surface affect transducin activation
    • Min KC, Zvyaga TA, Cypess AM, Sakmar TP. 1993. Characterization of mutant rhodopsin responsible for autosomal dominant retinitis pigmentosa: mutations on the cytoplasmic surface affect transducin activation. J. Biol. Chem. 268:9400-4
    • (1993) J. Biol. Chem. , vol.268 , pp. 9400-9404
    • Min, K.C.1    Zvyaga, T.A.2    Cypess, A.M.3    Sakmar, T.P.4
  • 69
    • 0025761854 scopus 로고
    • Mapping of the amino acids in membrane-embedded helices that interact with the retinal chromophore in bovine rhodopsin
    • Nakayama TA, Khorana HG. 1991. Mapping of the amino acids in membrane-embedded helices that interact with the retinal chromophore in bovine rhodopsin. J. Biol Chem. 266: 4269-75
    • (1991) J. Biol Chem. , vol.266 , pp. 4269-4275
    • Nakayama, T.A.1    Khorana, H.G.2
  • 70
    • 0025162902 scopus 로고
    • Determinants of visual pigment absorbance: Identification of the retinylidenes Schiff's base counterion in bovine rhodopsin
    • Nathans J. 1990. Determinants of visual pigment absorbance: identification of the retinylidenes Schiff's base counterion in bovine rhodopsin. Biochemistry 29:9746-52
    • (1990) Biochemistry , vol.29 , pp. 9746-9752
    • Nathans, J.1
  • 72
    • 8944231834 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof.
  • 73
    • 0026772266 scopus 로고
    • The ligand-binding domain of rhodopsin and other G protein-linked receptors
    • Oprian DD. 1992. The ligand-binding domain of rhodopsin and other G protein-linked receptors. J. Bioenerg. Biomembr. 24:211-17
    • (1992) J. Bioenerg. Biomembr. , vol.24 , pp. 211-217
    • Oprian, D.D.1
  • 76
    • 0026505367 scopus 로고
    • The influence of arrestin (48K protein) and rhodopsin kinase on visual transduction
    • Palczewski K, Rispoli G, Detwiler PB. 1992. The influence of arrestin (48K protein) and rhodopsin kinase on visual transduction. Neuron 8: 117-26
    • (1992) Neuron , vol.8 , pp. 117-126
    • Palczewski, K.1    Rispoli, G.2    Detwiler, P.B.3
  • 77
    • 0023215761 scopus 로고
    • Assignment of fingerprint vibrations in the resonance raman spectra of rhodopsin, isorhodopsin, and bathorhodopsin: Implications for the chromophore structure and environment
    • Palings I, Pardoen A, Van den Berg E, Winkel C, Lugtenberg J, Mathies RA. 1987. Assignment of fingerprint vibrations in the resonance raman spectra of rhodopsin, isorhodopsin, and bathorhodopsin: implications for the chromophore structure and environment. Biochemistry 24:2544-56
    • (1987) Biochemistry , vol.24 , pp. 2544-2556
    • Palings, I.1    Pardoen, A.2    Van Den Berg, E.3    Winkel, C.4    Lugtenberg, J.5    Mathies, R.A.6
  • 78
    • 0025836218 scopus 로고
    • Truncation of the extended carboxyl-terminal domain increases the expression and regulatory activity of the avian β-adrenergic receptor
    • Parker EM, Ross EM. 1991. Truncation of the extended carboxyl-terminal domain increases the expression and regulatory activity of the avian β-adrenergic receptor. J. Biol. Chem. 266: 9987-96
    • (1991) J. Biol. Chem. , vol.266 , pp. 9987-9996
    • Parker, E.M.1    Ross, E.M.2
  • 79
    • 0027369421 scopus 로고
    • Somatic mutations in the thyrotropin receptor gene cause hyperfunctioning thyroid adenomas
    • Parma J, Duprez L, Van Sande J, Cochaux P, Gervy C, et al. 1993. Somatic mutations in the thyrotropin receptor gene cause hyperfunctioning thyroid adenomas. Nature 365: 649-51
    • (1993) Nature , vol.365 , pp. 649-651
    • Parma, J.1    Duprez, L.2    Van Sande, J.3    Cochaux, P.4    Gervy, C.5
  • 80
    • 0028588698 scopus 로고
    • Identification and functional characterization of two new somatic mutations causing constitutive activation of the thyrotropin receptor in hyperfunctioning autonomous adenomas of the thyroid
    • Paschke R, Tonacchera M, Van Sande J, Parma J, Vassart G. 1994. Identification and functional characterization of two new somatic mutations causing constitutive activation of the thyrotropin receptor in hyperfunctioning autonomous adenomas of the thyroid. J. Clin. Endocrinol. Metab. 79:1785-89
    • (1994) J. Clin. Endocrinol. Metab. , vol.79 , pp. 1785-1789
    • Paschke, R.1    Tonacchera, M.2    Van Sande, J.3    Parma, J.4    Vassart, G.5
  • 81
    • 0028331771 scopus 로고
    • A constitutively active mutant β-adrenergic receptor is constitutively desensitized and phosphorylated
    • Pei G, Samama, Lohse M, Wang M, Codina J, Lefkowitz RJ. 1994. A constitutively active mutant β-adrenergic receptor is constitutively desensitized and phosphorylated. Proc. Natl. Acad. Sci. USA 91:2699-702
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 2699-2702
    • Pei, G.1    Samama2    Lohse, M.3    Wang, M.4    Codina, J.5    Lefkowitz, R.J.6
  • 82
    • 0028040908 scopus 로고
    • Novel mutations of thyrotropin receptor gene in thyroid hyperfunctioning adenomas. Rapid identification by fine needle aspiration biopsy
    • Porcellini A, Ciullo I, Laviola L, Amabile G, Fenzi G, Avvedimento VE. 1994. Novel mutations of thyrotropin receptor gene in thyroid hyperfunctioning adenomas. Rapid identification by fine needle aspiration biopsy. J. Clin. Endocrinol. Metab. 79:657-61
    • (1994) J. Clin. Endocrinol. Metab. , vol.79 , pp. 657-661
    • Porcellini, A.1    Ciullo, I.2    Laviola, L.3    Amabile, G.4    Fenzi, G.5    Avvedimento, V.E.6
  • 84
    • 0028125886 scopus 로고
    • Rhodopsin mutation G90D and a molecular mechanism for congenital night blindness
    • Rao VR, Cohen GB, Oprian DD. 1994. Rhodopsin mutation G90D and a molecular mechanism for congenital night blindness. Nature 367: 639-42
    • (1994) Nature , vol.367 , pp. 639-642
    • Rao, V.R.1    Cohen, G.B.2    Oprian, D.D.3
  • 85
    • 0027296623 scopus 로고
    • Constitutively active mutants of the α-adrenergic receptor
    • Ren Q, Kurose H, Lefkowitz RJ, Cotecchia S. 1993. Constitutively active mutants of the α-adrenergic receptor. J. Biol. Chem. 268:16483-87
    • (1993) J. Biol. Chem. , vol.268 , pp. 16483-16487
    • Ren, Q.1    Kurose, H.2    Lefkowitz, R.J.3    Cotecchia, S.4
  • 86
    • 0027443076 scopus 로고
    • Formation or the meta II photointermediate is accompanied by conformational changes in the cytoplasmic surface of rhodopsin
    • Resek JF, Farahbakhsh ZT, Hubbell WL, Khorana HG. 1993. Formation or the meta II photointermediate is accompanied by conformational changes in the cytoplasmic surface of rhodopsin. Biochemistry 32:12025-32
    • (1993) Biochemistry , vol.32 , pp. 12025-12032
    • Resek, J.F.1    Farahbakhsh, Z.T.2    Hubbell, W.L.3    Khorana, H.G.4
  • 87
    • 0028111634 scopus 로고
    • Structure and function in rhodopsin: Covalent crosslinking of the rhodopsin (metarhodopsin II)-transducin complex-the rhodopsin cytoplasmic face links to the transducin a subunit
    • Resek JF, Farrens D, Khorana HG. 1994. Structure and function in rhodopsin: Covalent crosslinking of the rhodopsin (metarhodopsin II)-transducin complex-the rhodopsin cytoplasmic face links to the transducin a subunit. Proc. Natl. Acad. Sci. USA 91:7643-47
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7643-7647
    • Resek, J.F.1    Farrens, D.2    Khorana, H.G.3
  • 88
    • 0029117895 scopus 로고
    • Constitutive activation of opsin: Interaction of mutants with rhodopsin kinase and arrestin
    • Rim J, Oprian DD. 1995. Constitutive activation of opsin: interaction of mutants with rhodopsin kinase and arrestin. Biochemistry 34:11938-45
    • (1995) Biochemistry , vol.34 , pp. 11938-11945
    • Rim, J.1    Oprian, D.D.2
  • 89
    • 0027413475 scopus 로고
    • Pigmentation phenotypes of variant extension locus alleles result from point mutations that alter MSH receptor function
    • Robbins LS, Nadeau JH, Johnson KR, Kelly MA, Roselli-Rehfuss L, et al. 1993. Pigmentation phenotypes of variant extension locus alleles result from point mutations that alter MSH receptor function. Cell 72:827-34
    • (1993) Cell , vol.72 , pp. 827-834
    • Robbins, L.S.1    Nadeau, J.H.2    Johnson, K.R.3    Kelly, M.A.4    Roselli-Rehfuss, L.5
  • 90
    • 0028241969 scopus 로고
    • Opsins with mutations at the site of chromophore attachment constitutively activate transducin but are not phosphorylated by rhodopsin kinase
    • Robinson PR, Buczylko J, Ohguro H, Palczewski K. 1994. Opsins with mutations at the site of chromophore attachment constitutively activate transducin but are not phosphorylated by rhodopsin kinase. Proc. Natl. Acad. Sci. USA 91:5411-15
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 5411-5415
    • Robinson, P.R.1    Buczylko, J.2    Ohguro, H.3    Palczewski, K.4
  • 93
    • 0343177634 scopus 로고
    • Glutamic acid-113 serves as the retinylidene Schiff base counterion in bovine rhodopsin
    • Sakmar TP, Franke RR, Khorana HG. 1989. Glutamic acid-113 serves as the retinylidene Schiff base counterion in bovine rhodopsin. Proc. Natl. Acad. Sci. USA 86:309-13
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 309-313
    • Sakmar, T.P.1    Franke, R.R.2    Khorana, H.G.3
  • 94
    • 0026341233 scopus 로고
    • The role of the retinylidene Schiff base counterion in determining wavelength absorbance and Schiff base pK
    • Sakmar TP, Franke RR, Khorana HG. 1991. The role of the retinylidene Schiff base counterion in determining wavelength absorbance and Schiff base pK . Proc. Natl. Acad. Sci. USA 88:3079-83
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3079-3083
    • Sakmar, T.P.1    Franke, R.R.2    Khorana, H.G.3
  • 95
    • 0027513982 scopus 로고
    • A mutation-induced activated state of the β-adrenergic receptor
    • Samama P, Cotecchia S, Costa T, Lefkowitz RJ. 1993. A mutation-induced activated state of the β-adrenergic receptor. J. Biol. Chem. 268: 4625-36
    • (1993) J. Biol. Chem. , vol.268 , pp. 4625-4636
    • Samama, P.1    Cotecchia, S.2    Costa, T.3    Lefkowitz, R.J.4
  • 97
    • 0028943780 scopus 로고
    • A constitutively active mutant PTH-PTHrP receptor in Jansen-type metaphyseal chondrodysplasia
    • Schipani E, Kurse K, Juppner H. 1995. A constitutively active mutant PTH-PTHrP receptor in Jansen-type metaphyseal chondrodysplasia. Science 268:98-100
    • (1995) Science , vol.268 , pp. 98-100
    • Schipani, E.1    Kurse, K.2    Juppner, H.3
  • 98
    • 0024582884 scopus 로고
    • Kinetics, binding constant, and activation energy of the 48 kDa protein-rhodopsin complex by extrametarhodopsin II
    • Schleicher A, Kuhn H, Hofmann KP. 1989. Kinetics, binding constant, and activation energy of the 48 kDa protein-rhodopsin complex by extrametarhodopsin II. Biochemistry 28: 1770-75
    • (1989) Biochemistry , vol.28 , pp. 1770-1775
    • Schleicher, A.1    Kuhn, H.2    Hofmann, K.P.3
  • 99
    • 0026091595 scopus 로고
    • The first step in vision: Femtosecond isomerization of rhodopsin
    • Schoenlein RW, Peteanu LA, Mathies Ra, Shank CV. 1991. The first step in vision: femtosecond isomerization of rhodopsin. Science 254: 412-15
    • (1991) Science , vol.254 , pp. 412-415
    • Schoenlein, R.W.1    Peteanu, L.A.2    Mathies, Ra.3    Shank, C.V.4
  • 100
    • 0029011757 scopus 로고
    • Related contribution of specific helix 2 and 7 residues to conformational activation of the serotonin 5-HT receptor
    • Sealfon SC, Chi L, Ebersole BJ, Radic V, Zhang D, et al. 1995. Related contribution of specific helix 2 and 7 residues to conformational activation of the serotonin 5-HT receptor. J. Biol. Chem. 270:16683-88
    • (1995) J. Biol. Chem. , vol.270 , pp. 16683-16688
    • Sealfon, S.C.1    Chi, L.2    Ebersole, B.J.3    Radic, V.4    Zhang, D.5
  • 101
    • 0024786297 scopus 로고
    • Schiffbase deprotonation is mandatory for light-dependent rhodopsin phosphorylation
    • Seckler B, Rando RR. 1989. Schiffbase deprotonation is mandatory for light-dependent rhodopsin phosphorylation. Biochem. J. 264:489-93
    • (1989) Biochem. J. , vol.264 , pp. 489-493
    • Seckler, B.1    Rando, R.R.2
  • 102
    • 0027372340 scopus 로고
    • A constitutively activating mutation of the luteinizing hormone receptor in familial male precocious puberty
    • Shenker A, Laue L, Kosugi S, Merendino J Jr, Minegishi T, Cutler GB Jr. 1993. A constitutively activating mutation of the luteinizing hormone receptor in familial male precocious puberty. Nature 365:652-54
    • (1993) Nature , vol.365 , pp. 652-654
    • Shenker, A.1    Laue, L.2    Kosugi, S.3    Merendino Jr., J.4    Minegishi, T.5    Cutler Jr., G.B.6
  • 103
    • 0028900858 scopus 로고
    • Rhodopsin mutants discriminate sites important for the activation of rhodospin kinase and transducin
    • Shi W, Osawa S, Dickerson CD, Weiss ER. 1995. Rhodopsin mutants discriminate sites important for the activation of rhodospin kinase and transducin. J. Biol. Chem. 270: 2112-19
    • (1995) J. Biol. Chem. , vol.270 , pp. 2112-2119
    • Shi, W.1    Osawa, S.2    Dickerson, C.D.3    Weiss, E.R.4
  • 105
    • 0025034240 scopus 로고
    • Solid-state NMR studies of the mechanism of the opsin shift in the visual pigment rhodopsin
    • Smith SO, Palings I, Miley M, Courtin J, de Groot H, et al. 1990. Solid-state NMR studies of the mechanism of the opsin shift in the visual pigment rhodopsin. Biochemistry 29: 8158-64
    • (1990) Biochemistry , vol.29 , pp. 8158-8164
    • Smith, S.O.1    Palings, I.2    Miley, M.3    Courtin, J.4    De Groot, H.5
  • 106
    • 0027335795 scopus 로고
    • pK of the protonated Schiff base of bovine rhodopsin: A study with artificial pigments
    • Steinberg G, Ottolenghi M, Sheves M. 1993. pK of the protonated Schiff base of bovine rhodopsin: a study with artificial pigments. Biophys. J. 64:1499-502
    • (1993) Biophys. J. , vol.64 , pp. 1499-1502
    • Steinberg, G.1    Ottolenghi, M.2    Sheves, M.3
  • 107
    • 8944240080 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof.
  • 111
    • 0027452148 scopus 로고
    • Rhodopsin mutations responsible for autosomal dominant retinitis pigmentosa
    • Sung C-H, Davenport CM, Nathans J, 1993. Rhodopsin mutations responsible for autosomal dominant retinitis pigmentosa. J. Biol. Chem. 268:26645-49
    • (1993) J. Biol. Chem. , vol.268 , pp. 26645-26649
    • Sung, C.-H.1    Davenport, C.M.2    Nathans, J.3
  • 112
    • 0027935666 scopus 로고
    • A rhodopsin gene mutation responsible for autosomal dominant retinitis pigmentosa results in a protein that is defective in localization to the photorecepror outer segment
    • Sung C-H, Makino C, Baylor D, Nathans J. 1994. A rhodopsin gene mutation responsible for autosomal dominant retinitis pigmentosa results in a protein that is defective in localization to the photorecepror outer segment. J. Neurosci. 14:5818-33
    • (1994) J. Neurosci. , vol.14 , pp. 5818-5833
    • Sung, C.-H.1    Makino, C.2    Baylor, D.3    Nathans, J.4
  • 114
    • 0028910993 scopus 로고
    • Transducin activation by the bovine opsin apoprotein
    • Surya A, Foster KW, Knox BE. 1995. Transducin activation by the bovine opsin apoprotein. J. Biol. Chem. 270:5024-31
    • (1995) J. Biol. Chem. , vol.270 , pp. 5024-5031
    • Surya, A.1    Foster, K.W.2    Knox, B.E.3
  • 115
    • 0014411230 scopus 로고
    • Molecular basis of visual excitation
    • Wald G. 1968. Molecular basis of visual excitation. Science 162: 230-39
    • (1968) Science , vol.162 , pp. 230-239
    • Wald, G.1
  • 116
    • 8944249968 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof.
  • 117
    • 0027723278 scopus 로고
    • Rhodopsin activation: Effects of the metarhodopsin I-metarhodopsin II equilibrium of neutralization or introduction of charged amino acids within putative transmembrane segments
    • Weitz CJ, Nathans J. 1993. Rhodopsin activation: effects of the metarhodopsin I-metarhodopsin II equilibrium of neutralization or introduction of charged amino acids within putative transmembrane segments. Biochemistry 32:14176-82
    • (1993) Biochemistry , vol.32 , pp. 14176-14182
    • Weitz, C.J.1    Nathans, J.2
  • 118
    • 0000025689 scopus 로고
    • Phosphodiesterase activation by photoexcited rhodopsin is quenched when rhodopsin is phosphorylated and binds the intrinsic 48-kDa protein of rod outer segments
    • Wilden U, Hall SW, Kuhn H. 1986. Phosphodiesterase activation by photoexcited rhodopsin is quenched when rhodopsin is phosphorylated and binds the intrinsic 48-kDa protein of rod outer segments. Proc. Natl. Acad. Sci USA 83:1174-78
    • (1986) Proc. Natl. Acad. Sci USA , vol.83 , pp. 1174-1178
    • Wilden, U.1    Hall, S.W.2    Kuhn, H.3
  • 119
    • 8944257060 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof.
  • 120
    • 0028031727 scopus 로고
    • A reciprocal mutation supports helix 2 and helix 7 proximity in the gonadotropin-releasing hormone receptor
    • Zhou W, Flanagan C, Ballesteros JA, Konvicka K, Davidson JS, et al. 1994. A reciprocal mutation supports helix 2 and helix 7 proximity in the gonadotropin-releasing hormone receptor. Mol. Pharmacol. 45:165-70
    • (1994) Mol. Pharmacol. , vol.45 , pp. 165-170
    • Zhou, W.1    Flanagan, C.2    Ballesteros, J.A.3    Konvicka, K.4    Davidson, J.S.5
  • 121
    • 0024362631 scopus 로고
    • Effect of carboxylic acid side chains on the absorption maximum of visual pigments
    • Zhukovsky EA, Oprian DD. 1989. Effect of carboxylic acid side chains on the absorption maximum of visual pigments. Science 246:928-30
    • (1989) Science , vol.246 , pp. 928-930
    • Zhukovsky, E.A.1    Oprian, D.D.2
  • 122
    • 0025757195 scopus 로고
    • Transducin activation by rhodopsin without a covalent bond to the 11-cis-retinal chromophore
    • Zhukovsky EA, Robinson PR, Oprian DD. 1991. Transducin activation by rhodopsin without a covalent bond to the 11-cis-retinal chromophore. Science 251:558-60
    • (1991) Science , vol.251 , pp. 558-560
    • Zhukovsky, E.A.1    Robinson, P.R.2    Oprian, D.D.3
  • 123
    • 0026475571 scopus 로고
    • Changing the location of the Schiff base counterion in rhodopsin
    • Zhukovsky EA, Robinson PR, Oprian DD. 1992. Changing the location of the Schiff base counterion in rhodopsin. Biochemistry 31:10400-5
    • (1992) Biochemistry , vol.31 , pp. 10400-10405
    • Zhukovsky, E.A.1    Robinson, P.R.2    Oprian, D.D.3
  • 124
    • 0028128646 scopus 로고
    • Characterization of rhodopsin-transducin interaction: A mutant rhodopsin photoproduct with a protonated Schiff base activates transducin
    • Zvyaga TA, Fahmy K, Sakmar TP. 1994. Characterization of rhodopsin-transducin interaction: a mutant rhodopsin photoproduct with a protonated Schiff base activates transducin. Biochemistry 33:9753-61
    • (1994) Biochemistry , vol.33 , pp. 9753-9761
    • Zvyaga, T.A.1    Fahmy, K.2    Sakmar, T.P.3
  • 125
    • 0027462158 scopus 로고
    • Movement of the retinylidene Schiff base counterion in rhodopsin by one helix turn reverses the pH dependence of the metarhodopsin I to metarhodopsin II transition
    • Corr: J. Biol. Chem. 1994, 269: 13056
    • Zvyaga TA, Min KC, Beck M, Sakmar TP. 1993. Movement of the retinylidene Schiff base counterion in rhodopsin by one helix turn reverses the pH dependence of the metarhodopsin I to metarhodopsin II transition. J. Biol. Chem. 268:4661-67 (Corr: J. Biol. Chem. 1994, 269: 13056)
    • (1993) J. Biol. Chem. , vol.268 , pp. 4661-4667
    • Zvyaga, T.A.1    Min, K.C.2    Beck, M.3    Sakmar, T.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.