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Volumn 46, Issue 27, 2006, Pages 4519-4531

Comparison of the retinitis pigmentosa mutations in rhodopsin with a functional map of the C5a receptor

Author keywords

C5a Receptor; Congenital disease; G protein coupled receptor; Retinitis pigmentosa; Rhodopsin; Vision loss

Indexed keywords

COMPLEMENT COMPONENT C5A RECEPTOR; RHODOPSIN;

EID: 33750606225     PISSN: 00426989     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.visres.2006.07.010     Document Type: Article
Times cited : (5)

References (87)
  • 2
    • 0029818551 scopus 로고    scopus 로고
    • Structural features and light-dependent changes in the cytoplasmic interhelical E-F loop region of rhodopsin: a site-directed spin-labeling study
    • Altenbach C., Yang K., Farrens D.L., Farahbakhsh Z.T., Khorana H.G., and Hubbell W.L. Structural features and light-dependent changes in the cytoplasmic interhelical E-F loop region of rhodopsin: a site-directed spin-labeling study. Biochemistry 35 38 (1996) 12470-12478
    • (1996) Biochemistry , vol.35 , Issue.38 , pp. 12470-12478
    • Altenbach, C.1    Yang, K.2    Farrens, D.L.3    Farahbakhsh, Z.T.4    Khorana, H.G.5    Hubbell, W.L.6
  • 3
    • 2442529839 scopus 로고    scopus 로고
    • Hetero-oligomerization between GABA-A and GABA-B receptors regulates GABAB receptor trafficking
    • Balasubramanian S., Teissere J.A., Raju D.V., and Hall R.A. Hetero-oligomerization between GABA-A and GABA-B receptors regulates GABAB receptor trafficking. The Journal of Biological Chemistry 279 18 (2004) 18840-18850
    • (2004) The Journal of Biological Chemistry , vol.279 , Issue.18 , pp. 18840-18850
    • Balasubramanian, S.1    Teissere, J.A.2    Raju, D.V.3    Hall, R.A.4
  • 4
    • 0031565726 scopus 로고    scopus 로고
    • An alpha-carbon template for the transmembrane helices in the rhodopsin family of G-protein-coupled receptors
    • Baldwin J.M., Schertler G.F., and Unger V.M. An alpha-carbon template for the transmembrane helices in the rhodopsin family of G-protein-coupled receptors. Journal of Molecular Biology 272 1 (1997) 144-164
    • (1997) Journal of Molecular Biology , vol.272 , Issue.1 , pp. 144-164
    • Baldwin, J.M.1    Schertler, G.F.2    Unger, V.M.3
  • 6
    • 0031472117 scopus 로고    scopus 로고
    • Cell membrane lipid composition and distribution: implications for cell function and lessons learned from photoreceptors and platelets
    • Boesze-Battaglia K., and Schimmel R. Cell membrane lipid composition and distribution: implications for cell function and lessons learned from photoreceptors and platelets. The Journal of Experimental Biology 200 Pt 23 (1997) 2927-2936
    • (1997) The Journal of Experimental Biology , vol.200 , Issue.PART 23 , pp. 2927-2936
    • Boesze-Battaglia, K.1    Schimmel, R.2
  • 7
    • 0038482177 scopus 로고    scopus 로고
    • Structural and functional role of helices I and II in rhodopsin. A novel interplay evidenced by mutations at Gly-51 and Gly-89 in the transmembrane domain
    • Bosch L., Ramon E., Del Valle L.J., and Garriga P. Structural and functional role of helices I and II in rhodopsin. A novel interplay evidenced by mutations at Gly-51 and Gly-89 in the transmembrane domain. The Journal of Biological Chemistry 278 22 (2003) 20203-20209
    • (2003) The Journal of Biological Chemistry , vol.278 , Issue.22 , pp. 20203-20209
    • Bosch, L.1    Ramon, E.2    Del Valle, L.J.3    Garriga, P.4
  • 9
    • 0027050784 scopus 로고
    • Mechanism of activation and inactivation of opsin: role of Glu113 and Lys296
    • Cohen G.B., Oprian D.D., and Robinson P.R. Mechanism of activation and inactivation of opsin: role of Glu113 and Lys296. Biochemistry 31 50 (1992) 12592-12601
    • (1992) Biochemistry , vol.31 , Issue.50 , pp. 12592-12601
    • Cohen, G.B.1    Oprian, D.D.2    Robinson, P.R.3
  • 10
    • 0027787795 scopus 로고
    • Effects of Asn87 and Asp318 mutations on ligand binding and signal transduction in the rat GnRH receptor
    • Cook J.V., Faccenda E., Anderson L., Couper G.G., Eidne K.A., and Taylor P.L. Effects of Asn87 and Asp318 mutations on ligand binding and signal transduction in the rat GnRH receptor. Journal of Endocrinology 139 3 (1993) R1-R4
    • (1993) Journal of Endocrinology , vol.139 , Issue.3
    • Cook, J.V.1    Faccenda, E.2    Anderson, L.3    Couper, G.G.4    Eidne, K.A.5    Taylor, P.L.6
  • 11
    • 0033118960 scopus 로고    scopus 로고
    • Conserved polar residues in the transmembrane domain of the human tachykinin NK2 receptor: functional roles and structural implications
    • Donnelly D., Maudsley S., Gent J.P., Moser R.N., Hurrell C.R., and Findlay J.B. Conserved polar residues in the transmembrane domain of the human tachykinin NK2 receptor: functional roles and structural implications. The Biochemical Journal 339 Pt 1 (1999) 55-61
    • (1999) The Biochemical Journal , vol.339 , Issue.PART 1 , pp. 55-61
    • Donnelly, D.1    Maudsley, S.2    Gent, J.P.3    Moser, R.N.4    Hurrell, C.R.5    Findlay, J.B.6
  • 12
    • 0027248024 scopus 로고
    • Heterozygous missense mutation in the rhodopsin gene as a cause of congenital stationary night blindness
    • Dryja T.P., Berson E.L., Rao V.R., and Oprian D.D. Heterozygous missense mutation in the rhodopsin gene as a cause of congenital stationary night blindness. Nature Genetics 4 3 (1993) 280-283
    • (1993) Nature Genetics , vol.4 , Issue.3 , pp. 280-283
    • Dryja, T.P.1    Berson, E.L.2    Rao, V.R.3    Oprian, D.D.4
  • 15
    • 0025105161 scopus 로고
    • A point mutation of the rhodopsin gene in one form of retinitis pigmentosa
    • Dryja T.P., McGee T.L., Reichel E., Hahn L.B., Cowley G.S., Yandell D.W., et al. A point mutation of the rhodopsin gene in one form of retinitis pigmentosa. Nature 343 6256 (1990) 364-366
    • (1990) Nature , vol.343 , Issue.6256 , pp. 364-366
    • Dryja, T.P.1    McGee, T.L.2    Reichel, E.3    Hahn, L.B.4    Cowley, G.S.5    Yandell, D.W.6
  • 16
    • 0000948942 scopus 로고
    • Energy parameters in polypeptides. 8. Empirical potential energy algorithm for the conformational analysis of large molecules
    • Dunfield L., Burgess A., and Scheraga H. Energy parameters in polypeptides. 8. Empirical potential energy algorithm for the conformational analysis of large molecules. Journal of Physical Chemistry 82 (1978) 2609-2616
    • (1978) Journal of Physical Chemistry , vol.82 , pp. 2609-2616
    • Dunfield, L.1    Burgess, A.2    Scheraga, H.3
  • 17
    • 0033555936 scopus 로고    scopus 로고
    • Conformational changes in rhodopsin. Movement of helix f detected by site-specific chemical labeling and fluorescence spectroscopy
    • Dunham T.D., and Farrens D.L. Conformational changes in rhodopsin. Movement of helix f detected by site-specific chemical labeling and fluorescence spectroscopy. The Journal of Biological Chemistry 274 3 (1999) 1683-1690
    • (1999) The Journal of Biological Chemistry , vol.274 , Issue.3 , pp. 1683-1690
    • Dunham, T.D.1    Farrens, D.L.2
  • 18
    • 0036500230 scopus 로고    scopus 로고
    • On the genetics of retinitis pigmentosa and on mutation-independent approaches to therapeutic intervention
    • Farrar G.J., Kenna P.F., and Humphries P. On the genetics of retinitis pigmentosa and on mutation-independent approaches to therapeutic intervention. EMBO Journal 21 5 (2002) 857-864
    • (2002) EMBO Journal , vol.21 , Issue.5 , pp. 857-864
    • Farrar, G.J.1    Kenna, P.F.2    Humphries, P.3
  • 19
    • 0029907599 scopus 로고    scopus 로고
    • Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin
    • Farrens D.L., Altenbach C., Yang K., Hubbell W.L., and Khorana H.G. Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin. Science 274 5288 (1996) 768-770
    • (1996) Science , vol.274 , Issue.5288 , pp. 768-770
    • Farrens, D.L.1    Altenbach, C.2    Yang, K.3    Hubbell, W.L.4    Khorana, H.G.5
  • 21
    • 0032879688 scopus 로고    scopus 로고
    • The functional microdomain in transmembrane helices 2 and 7 regulates expression, activation, and coupling pathways of the gonadotropin-releasing hormone receptor
    • Flanagan C.A., Zhou W., Chi L., Yuen T., Rodic V., Robertson D., et al. The functional microdomain in transmembrane helices 2 and 7 regulates expression, activation, and coupling pathways of the gonadotropin-releasing hormone receptor. The Journal of Biological Chemistry 274 41 (1999) 28880-28886
    • (1999) The Journal of Biological Chemistry , vol.274 , Issue.41 , pp. 28880-28886
    • Flanagan, C.A.1    Zhou, W.2    Chi, L.3    Yuen, T.4    Rodic, V.5    Robertson, D.6
  • 22
    • 0041315583 scopus 로고    scopus 로고
    • C5a receptor oligomerization. II. Fluorescence resonance energy transfer studies of a human G protein-coupled receptor expressed in yeast
    • Floyd D.H., Geva A., Bruinsma S.P., Overton M.C., Blumer K.J., and Baranski T.J. C5a receptor oligomerization. II. Fluorescence resonance energy transfer studies of a human G protein-coupled receptor expressed in yeast. The Journal of Biological Chemistry 278 37 (2003) 35354-35361
    • (2003) The Journal of Biological Chemistry , vol.278 , Issue.37 , pp. 35354-35361
    • Floyd, D.H.1    Geva, A.2    Bruinsma, S.P.3    Overton, M.C.4    Blumer, K.J.5    Baranski, T.J.6
  • 24
  • 26
    • 0026078539 scopus 로고
    • The chemotactic receptor for human C5a anaphylatoxin
    • Gerard N.P., and Gerard C. The chemotactic receptor for human C5a anaphylatoxin. Nature 349 6310 (1991) 614-617
    • (1991) Nature , vol.349 , Issue.6310 , pp. 614-617
    • Gerard, N.P.1    Gerard, C.2
  • 28
    • 0034634690 scopus 로고    scopus 로고
    • Genetic mapping of the human C5a receptor. Identification of transmembrane amino acids critical for receptor function
    • Geva A., Lassere T.B., Lichtarge O., Pollitt S.K., and Baranski T.J. Genetic mapping of the human C5a receptor. Identification of transmembrane amino acids critical for receptor function. The Journal of Biological Chemistry 275 45 (2000) 35393-35401
    • (2000) The Journal of Biological Chemistry , vol.275 , Issue.45 , pp. 35393-35401
    • Geva, A.1    Lassere, T.B.2    Lichtarge, O.3    Pollitt, S.K.4    Baranski, T.J.5
  • 29
    • 0028300554 scopus 로고
    • Active site-directed inactivation of constitutively active mutants of rhodopsin
    • Govardhan C.P., and Oprian D.D. Active site-directed inactivation of constitutively active mutants of rhodopsin. The Journal of Biological Chemistry 269 9 (1994) 6524-6527
    • (1994) The Journal of Biological Chemistry , vol.269 , Issue.9 , pp. 6524-6527
    • Govardhan, C.P.1    Oprian, D.D.2
  • 31
    • 0037465429 scopus 로고    scopus 로고
    • Characterization of rhodopsin congenital night blindness mutant T94I
    • Gross A.K., Rao V.R., and Oprian D.D. Characterization of rhodopsin congenital night blindness mutant T94I. Biochemistry 42 7 (2003) 2009-2015
    • (2003) Biochemistry , vol.42 , Issue.7 , pp. 2009-2015
    • Gross, A.K.1    Rao, V.R.2    Oprian, D.D.3
  • 32
    • 0037465424 scopus 로고    scopus 로고
    • Slow binding of retinal to rhodopsin mutants G90D and T94D
    • Gross A.K., Xie G., and Oprian D.D. Slow binding of retinal to rhodopsin mutants G90D and T94D. Biochemistry 42 7 (2003) 2002-2008
    • (2003) Biochemistry , vol.42 , Issue.7 , pp. 2002-2008
    • Gross, A.K.1    Xie, G.2    Oprian, D.D.3
  • 34
    • 2642572661 scopus 로고    scopus 로고
    • Oligomerization of wild type and nonfunctional mutant angiotensin II type I receptors inhibits Gαq protein signaling but not ERK activation
    • Hansen J.L., Theilade J., Haunso S., and Sheikh S.P. Oligomerization of wild type and nonfunctional mutant angiotensin II type I receptors inhibits Gαq protein signaling but not ERK activation. The Journal of Biological Chemistry 279 23 (2004) 24108-24115
    • (2004) The Journal of Biological Chemistry , vol.279 , Issue.23 , pp. 24108-24115
    • Hansen, J.L.1    Theilade, J.2    Haunso, S.3    Sheikh, S.P.4
  • 35
    • 33750623825 scopus 로고    scopus 로고
    • Hofmann, K.P. (2006). 10th Annual Vision Research Conference: Rhodopsin-Advances and Perspecitves. Fort Lauderdale, Florida.
  • 36
    • 0028789921 scopus 로고
    • Autosomal recessive retinitis pigmentosa caused by mutations in the α subunit of rod cGMP phosphodiesterase
    • Huang S.H., Pittler S.J., Huang X., Oliveira L., Berson E.L., and Dryja T.P. Autosomal recessive retinitis pigmentosa caused by mutations in the α subunit of rod cGMP phosphodiesterase. Nature Genetics 11 4 (1995) 468-471
    • (1995) Nature Genetics , vol.11 , Issue.4 , pp. 468-471
    • Huang, S.H.1    Pittler, S.J.2    Huang, X.3    Oliveira, L.4    Berson, E.L.5    Dryja, T.P.6
  • 37
    • 0037285444 scopus 로고    scopus 로고
    • Rhodopsin structure, dynamics, and activation: a perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking
    • Hubbell W.L., Altenbach C., Hubbell C.M., and Khorana H.G. Rhodopsin structure, dynamics, and activation: a perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking. Advances in Protein Chemistry 63 (2003) 243-290
    • (2003) Advances in Protein Chemistry , vol.63 , pp. 243-290
    • Hubbell, W.L.1    Altenbach, C.2    Hubbell, C.M.3    Khorana, H.G.4
  • 39
    • 0037743559 scopus 로고    scopus 로고
    • Opsin activation as a cause of congenital night blindness
    • Jin S., Cornwall M.C., and Oprian D.D. Opsin activation as a cause of congenital night blindness. Nature Neuroscience 6 7 (2003) 731-735
    • (2003) Nature Neuroscience , vol.6 , Issue.7 , pp. 731-735
    • Jin, S.1    Cornwall, M.C.2    Oprian, D.D.3
  • 40
    • 0028287273 scopus 로고
    • Structure and function in rhodopsin. 7. Point mutations associated with autosomal dominant retinitis pigmentosa
    • Kaushal S., and Khorana H.G. Structure and function in rhodopsin. 7. Point mutations associated with autosomal dominant retinitis pigmentosa. Biochemistry 33 20 (1994) 6121-6128
    • (1994) Biochemistry , vol.33 , Issue.20 , pp. 6121-6128
    • Kaushal, S.1    Khorana, H.G.2
  • 41
    • 0025944670 scopus 로고
    • Autosomal dominant retinitis pigmentosa: four new mutations in rhodopsin, one of them in the retinal attachment site
    • Keen T.J., Inglehearn C.F., Lester D.H., Bashir R., Jay M., Bird A.C., et al. Autosomal dominant retinitis pigmentosa: four new mutations in rhodopsin, one of them in the retinal attachment site. Genomics 11 1 (1991) 199-205
    • (1991) Genomics , vol.11 , Issue.1 , pp. 199-205
    • Keen, T.J.1    Inglehearn, C.F.2    Lester, D.H.3    Bashir, R.4    Jay, M.5    Bird, A.C.6
  • 42
    • 33744959047 scopus 로고    scopus 로고
    • Genetic analysis of the first and third extracellular loops of the C5a receptor reveals an essential WXFG motif in the first loop
    • Klco J.M., Nikiforovich G.V., and Baranski T.J. Genetic analysis of the first and third extracellular loops of the C5a receptor reveals an essential WXFG motif in the first loop. The Journal of Biological Chemistry 281 17 (2006) 12010-12019
    • (2006) The Journal of Biological Chemistry , vol.281 , Issue.17 , pp. 12010-12019
    • Klco, J.M.1    Nikiforovich, G.V.2    Baranski, T.J.3
  • 44
    • 0034861323 scopus 로고    scopus 로고
    • Anaphylatoxins and infectious and non-infectious inflammatory diseases
    • Kohl J. Anaphylatoxins and infectious and non-infectious inflammatory diseases. Molecular Immunology 38 2-3 (2001) 175-187
    • (2001) Molecular Immunology , vol.38 , Issue.2-3 , pp. 175-187
    • Kohl, J.1
  • 45
    • 1642603437 scopus 로고    scopus 로고
    • Constitutive opsin signaling: night blindness or retinal degeneration?
    • Lem J., and Fain G.L. Constitutive opsin signaling: night blindness or retinal degeneration?. Trends in Molecular Medicine 10 4 (2004) 150-157
    • (2004) Trends in Molecular Medicine , vol.10 , Issue.4 , pp. 150-157
    • Lem, J.1    Fain, G.L.2
  • 46
    • 0028892944 scopus 로고
    • Support for the equivalent light hypothesis for RP
    • Lisman J., and Fain G. Support for the equivalent light hypothesis for RP. Nature Medicine 1 12 (1995) 1254-1255
    • (1995) Nature Medicine , vol.1 , Issue.12 , pp. 1254-1255
    • Lisman, J.1    Fain, G.2
  • 48
    • 0036473397 scopus 로고    scopus 로고
    • The role of beta-arrestins in the termination and transduction of G-protein-coupled receptor signals
    • Luttrell L.M., and Lefkowitz R.J. The role of beta-arrestins in the termination and transduction of G-protein-coupled receptor signals. Journal of Cell Science 115 Pt 3 (2002) 455-465
    • (2002) Journal of Cell Science , vol.115 , Issue.PART 3 , pp. 455-465
    • Luttrell, L.M.1    Lefkowitz, R.J.2
  • 49
    • 0027270053 scopus 로고
    • Recessive mutations in the gene encoding the beta-subunit of rod phosphodiesterase in patients with retinitis pigmentosa
    • McLaughlin M.E., Sandberg M.A., Berson E.L., and Dryja T.P. Recessive mutations in the gene encoding the beta-subunit of rod phosphodiesterase in patients with retinitis pigmentosa. Nature Genetics 4 2 (1993) 130-134
    • (1993) Nature Genetics , vol.4 , Issue.2 , pp. 130-134
    • McLaughlin, M.E.1    Sandberg, M.A.2    Berson, E.L.3    Dryja, T.P.4
  • 50
    • 0343580431 scopus 로고    scopus 로고
    • A comparison of the efficiency of G protein activation by ligand-free and light-activated forms of rhodopsin
    • Melia T.J.J., Cowan C.W., Angleson J.K., and Wensel T.G. A comparison of the efficiency of G protein activation by ligand-free and light-activated forms of rhodopsin. Biophysical Journal 73 6 (1997) 3182-3191
    • (1997) Biophysical Journal , vol.73 , Issue.6 , pp. 3182-3191
    • Melia, T.J.J.1    Cowan, C.W.2    Angleson, J.K.3    Wensel, T.G.4
  • 51
    • 17044363529 scopus 로고    scopus 로고
    • Mechanisms of cell death in rhodopsin retinitis pigmentosa: implications for therapy
    • Mendes H.F., van der Spuy J., Chapple J.P., and Cheetham M.E. Mechanisms of cell death in rhodopsin retinitis pigmentosa: implications for therapy. Trends in Molecular Medicine 11 4 (2005) 177-185
    • (2005) Trends in Molecular Medicine , vol.11 , Issue.4 , pp. 177-185
    • Mendes, H.F.1    van der Spuy, J.2    Chapple, J.P.3    Cheetham, M.E.4
  • 52
    • 0035498937 scopus 로고    scopus 로고
    • Receptor activation: what does the rhodopsin structure tell us?
    • Meng E.C., and Bourne H.R. Receptor activation: what does the rhodopsin structure tell us?. Trends in Pharmacological Sciences 22 11 (2001) 587-593
    • (2001) Trends in Pharmacological Sciences , vol.22 , Issue.11 , pp. 587-593
    • Meng, E.C.1    Bourne, H.R.2
  • 53
    • 0037452868 scopus 로고    scopus 로고
    • Sequence analyses of G-protein-coupled receptors: similarities to rhodopsin
    • Mirzadegan T., Benko G., Filipek S., and Palczewski K. Sequence analyses of G-protein-coupled receptors: similarities to rhodopsin. Biochemistry 42 10 (2003) 2759-2767
    • (2003) Biochemistry , vol.42 , Issue.10 , pp. 2759-2767
    • Mirzadegan, T.1    Benko, G.2    Filipek, S.3    Palczewski, K.4
  • 54
    • 0032006965 scopus 로고    scopus 로고
    • Oguchi disease with sectoral retinitis pigmentosa harboring adenine deletion at position 1147 in the arrestin gene
    • Nakamachi Y., Nakamura M., Fujii S., Yamamoto M., and Okubo K. Oguchi disease with sectoral retinitis pigmentosa harboring adenine deletion at position 1147 in the arrestin gene. American Journal of Ophthalmology 125 2 (1998) 249-251
    • (1998) American Journal of Ophthalmology , vol.125 , Issue.2 , pp. 249-251
    • Nakamachi, Y.1    Nakamura, M.2    Fujii, S.3    Yamamoto, M.4    Okubo, K.5
  • 55
    • 0031894886 scopus 로고    scopus 로고
    • Arrestin gene mutations in autosomal recessive retinitis pigmentosa
    • Nakazawa M., Wada Y., and Tamai M. Arrestin gene mutations in autosomal recessive retinitis pigmentosa. Archives of Ophthalmology 116 4 (1998) 498-501
    • (1998) Archives of Ophthalmology , vol.116 , Issue.4 , pp. 498-501
    • Nakazawa, M.1    Wada, Y.2    Tamai, M.3
  • 56
    • 33845550595 scopus 로고
    • Energy parameters in polypeptides. 9. Updating of geometrical parameters, nonbonded interactions, and hydrogen bond interactions for the naturally occurring amino acids
    • Nemethy G., Pottle M., and Scheraga H. Energy parameters in polypeptides. 9. Updating of geometrical parameters, nonbonded interactions, and hydrogen bond interactions for the naturally occurring amino acids. Journal of Physical Chemistry 87 (1983) 1883-1887
    • (1983) Journal of Physical Chemistry , vol.87 , pp. 1883-1887
    • Nemethy, G.1    Pottle, M.2    Scheraga, H.3
  • 57
    • 0037205055 scopus 로고    scopus 로고
    • G protein pathways
    • Neves S.R., Ram P.T., and Iyengar R. G protein pathways. Science 296 5573 (2002) 1636-1639
    • (2002) Science , vol.296 , Issue.5573 , pp. 1636-1639
    • Neves, S.R.1    Ram, P.T.2    Iyengar, R.3
  • 58
    • 0035237770 scopus 로고    scopus 로고
    • Novel approach to computer modeling of seven-helical transmembrane proteins: current progress in the test case of bacteriorhodopsin
    • Nikiforovich G.V., Galaktionov S., Balodis J., and Marshall G.R. Novel approach to computer modeling of seven-helical transmembrane proteins: current progress in the test case of bacteriorhodopsin. Acta Biochimica Polonica 48 1 (2001) 53-64
    • (2001) Acta Biochimica Polonica , vol.48 , Issue.1 , pp. 53-64
    • Nikiforovich, G.V.1    Galaktionov, S.2    Balodis, J.3    Marshall, G.R.4
  • 59
    • 0026191334 scopus 로고
    • Topographical requirements for delta-selective opioid peptides
    • Nikiforovich G.V., Hruby V.J., Prakash O., and Gehrig C.A. Topographical requirements for delta-selective opioid peptides. Biopolymers 31 8 (1991) 941-955
    • (1991) Biopolymers , vol.31 , Issue.8 , pp. 941-955
    • Nikiforovich, G.V.1    Hruby, V.J.2    Prakash, O.3    Gehrig, C.A.4
  • 60
    • 0042165824 scopus 로고    scopus 로고
    • Three-dimensional model for meta-II rhodopsin, an activated G-protein-coupled receptor
    • Nikiforovich G.V., and Marshall G.R. Three-dimensional model for meta-II rhodopsin, an activated G-protein-coupled receptor. Biochemistry 42 30 (2003) 9110-9120
    • (2003) Biochemistry , vol.42 , Issue.30 , pp. 9110-9120
    • Nikiforovich, G.V.1    Marshall, G.R.2
  • 62
    • 33750621804 scopus 로고    scopus 로고
    • Nikiforovich, G.V., Sen, S., & Baranski, T.J. (2006) Rational design of constitutively active mutants of the human C5a receptor. 29th European Peptide Symposium, Gdansk, Poland.
  • 64
    • 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., Sugihara M., Bondar A.N., Elstner M., Entel P., and Buss V. The retinal conformation and its environment in rhodopsin in light of a new 2.2 Å crystal structure. Journal of Molecular Biology 342 2 (2004) 571-583
    • (2004) Journal of Molecular Biology , vol.342 , Issue.2 , pp. 571-583
    • Okada, T.1    Sugihara, M.2    Bondar, A.N.3    Elstner, M.4    Entel, P.5    Buss, V.6
  • 66
    • 0030922145 scopus 로고    scopus 로고
    • Interactions between conserved residues in transmembrane helices 1, 2, and 7 of the thyrotropin-releasing hormone receptor
    • Perlman J.H., Colson A.O., Wang W., Bence K., Osman R., and Gershengorn M.C. Interactions between conserved residues in transmembrane helices 1, 2, and 7 of the thyrotropin-releasing hormone receptor. The Journal of Biological Chemistry 272 18 (1997) 11937-11942
    • (1997) The Journal of Biological Chemistry , vol.272 , Issue.18 , pp. 11937-11942
    • Perlman, J.H.1    Colson, A.O.2    Wang, W.3    Bence, K.4    Osman, R.5    Gershengorn, M.C.6
  • 67
    • 0034622122 scopus 로고    scopus 로고
    • A brief review of retinitis pigmentosa and the identified retinitis pigmentosa genes
    • Phelan J.K., and Bok D. A brief review of retinitis pigmentosa and the identified retinitis pigmentosa genes. Molecular Vision 6 (2000) 116-124
    • (2000) Molecular Vision , vol.6 , pp. 116-124
    • Phelan, J.K.1    Bok, D.2
  • 68
    • 12544250742 scopus 로고    scopus 로고
    • Suppression of wild-type rhodopsin maturation by mutants linked to autosomal dominant retinitis pigmentosa
    • Rajan R.S., and Kopito R.R. Suppression of wild-type rhodopsin maturation by mutants linked to autosomal dominant retinitis pigmentosa. The Journal of Biological Chemistry 280 2 (2005) 1284-1291
    • (2005) The Journal of Biological Chemistry , vol.280 , Issue.2 , pp. 1284-1291
    • Rajan, R.S.1    Kopito, R.R.2
  • 69
    • 0037458628 scopus 로고    scopus 로고
    • Unusual thermal and conformational properties of the rhodopsin congenital night blindness mutant Thr-94 → Ile
    • Ramon E., del Valle L.J., and Garriga P. Unusual thermal and conformational properties of the rhodopsin congenital night blindness mutant Thr-94 → Ile. The Journal of Biological Chemistry 278 8 (2003) 6427-6432
    • (2003) The Journal of Biological Chemistry , vol.278 , Issue.8 , pp. 6427-6432
    • Ramon, E.1    del Valle, L.J.2    Garriga, P.3
  • 70
    • 0028125886 scopus 로고
    • Rhodopsin mutation G90D and a molecular mechanism for congenital night blindness
    • Rao V.R., Cohen G.B., and Oprian D.D. Rhodopsin mutation G90D and a molecular mechanism for congenital night blindness. Nature 367 6464 (1994) 639-642
    • (1994) Nature , vol.367 , Issue.6464 , pp. 639-642
    • Rao, V.R.1    Cohen, G.B.2    Oprian, D.D.3
  • 72
    • 14844343093 scopus 로고    scopus 로고
    • A transmembrane intracellular estrogen receptor mediates rapid cell signaling
    • Revankar C.M., Cimino D.F., Sklar L.A., Arterburn J.B., and Prossnitz E.R. A transmembrane intracellular estrogen receptor mediates rapid cell signaling. Science 307 5715 (2005) 1625-1630
    • (2005) Science , vol.307 , Issue.5715 , pp. 1625-1630
    • Revankar, C.M.1    Cimino, D.F.2    Sklar, L.A.3    Arterburn, J.B.4    Prossnitz, E.R.5
  • 74
    • 0029011757 scopus 로고
    • Related contribution of specific helix 2 and 7 residues to conformational activation of the serotonin 5-HT2A receptor
    • Sealfon S.C., Chi L., Ebersole B.J., Rodic V., Zhang D., Ballesteros J.A., et al. Related contribution of specific helix 2 and 7 residues to conformational activation of the serotonin 5-HT2A receptor. The Journal of Biological Chemistry 270 28 (1995) 16683-16688
    • (1995) The Journal of Biological Chemistry , vol.270 , Issue.28 , pp. 16683-16688
    • Sealfon, S.C.1    Chi, L.2    Ebersole, B.J.3    Rodic, V.4    Zhang, D.5    Ballesteros, J.A.6
  • 75
    • 0029778268 scopus 로고    scopus 로고
    • Rhodopsin activation blocked by metal-ion-binding sites linking transmembrane helices C and F
    • Sheikh S.P., Zvyaga T.A., Lichtarge O., Sakmar T.P., and Bourne H.R. Rhodopsin activation blocked by metal-ion-binding sites linking transmembrane helices C and F. Nature 383 6598 (1996) 347-350
    • (1996) Nature , vol.383 , Issue.6598 , pp. 347-350
    • Sheikh, S.P.1    Zvyaga, T.A.2    Lichtarge, O.3    Sakmar, T.P.4    Bourne, H.R.5
  • 76
    • 0141755153 scopus 로고    scopus 로고
    • Retinitis pigmentosa rhodopsin mutations L125R and A164V perturb critical interhelical interactions: new insights through compensatory mutations and crystal structure analysis
    • Stojanovic A., Hwang I., Khorana H.G., and Hwa J. Retinitis pigmentosa rhodopsin mutations L125R and A164V perturb critical interhelical interactions: new insights through compensatory mutations and crystal structure analysis. The Journal of Biological Chemistry 278 40 (2003) 39020-39028
    • (2003) The Journal of Biological Chemistry , vol.278 , Issue.40 , pp. 39020-39028
    • Stojanovic, A.1    Hwang, I.2    Khorana, H.G.3    Hwa, J.4
  • 77
    • 0027452148 scopus 로고
    • Rhodopsin mutations responsible for autosomal dominant retinitis pigmentosa. Clustering of functional classes along the polypeptide chain
    • Sung C.H., Davenport C.M., and Nathans J. Rhodopsin mutations responsible for autosomal dominant retinitis pigmentosa. Clustering of functional classes along the polypeptide chain. The Journal of Biological Chemistry 268 35 (1993) 26645-26649
    • (1993) The Journal of Biological Chemistry , vol.268 , Issue.35 , pp. 26645-26649
    • Sung, C.H.1    Davenport, C.M.2    Nathans, J.3
  • 80
    • 0037024360 scopus 로고    scopus 로고
    • Identification of G protein-coupled receptor genes from the human genome sequence
    • Takeda S., Kadowaki S., Haga T., Takaesu H., and Mitaku S. Identification of G protein-coupled receptor genes from the human genome sequence. FEBS Letters 520 1-3 (2002) 97-101
    • (2002) FEBS Letters , vol.520 , Issue.1-3 , pp. 97-101
    • Takeda, S.1    Kadowaki, S.2    Haga, T.3    Takaesu, H.4    Mitaku, S.5
  • 81
    • 0035800032 scopus 로고    scopus 로고
    • Advances in determination of a high-resolution three-dimensional structure of rhodopsin, a model of G-protein-coupled receptors (GPCRs)
    • Teller D.C., Okada T., Behnke C.A., Palczewski K., and Stenkamp R.E. Advances in determination of a high-resolution three-dimensional structure of rhodopsin, a model of G-protein-coupled receptors (GPCRs). Biochemistry 40 26 (2001) 7761-7772
    • (2001) Biochemistry , vol.40 , Issue.26 , pp. 7761-7772
    • Teller, D.C.1    Okada, T.2    Behnke, C.A.3    Palczewski, K.4    Stenkamp, R.E.5
  • 82
    • 0035252096 scopus 로고    scopus 로고
    • Role of endocytosis in mediating downregulation of G-protein-coupled receptors
    • Tsao P., Cao T., and von Zastrow M. Role of endocytosis in mediating downregulation of G-protein-coupled receptors. Trends in Pharmacological Sciences 22 2 (2001) 91-96
    • (2001) Trends in Pharmacological Sciences , vol.22 , Issue.2 , pp. 91-96
    • Tsao, P.1    Cao, T.2    von Zastrow, M.3
  • 84
    • 0036898466 scopus 로고    scopus 로고
    • Constitutive activation and endocytosis of the complement factor 5a receptor: evidence for multiple activated conformations of a G protein-coupled receptor
    • Whistler J.L., Gerber B.O., Meng E.C., Baranski T.J., von Zastrow M., and Bourne H.R. Constitutive activation and endocytosis of the complement factor 5a receptor: evidence for multiple activated conformations of a G protein-coupled receptor. Traffic 3 12 (2002) 866-877
    • (2002) Traffic , vol.3 , Issue.12 , pp. 866-877
    • Whistler, J.L.1    Gerber, B.O.2    Meng, E.C.3    Baranski, T.J.4    von Zastrow, M.5    Bourne, H.R.6
  • 85
    • 0141707934 scopus 로고    scopus 로고
    • Spontaneous activity of opsin apoprotein is a cause of Leber congenital amaurosis
    • Woodruff M.L., Wang Z., Chung H.Y., Redmond T.M., Fain G.L., and Lem J. Spontaneous activity of opsin apoprotein is a cause of Leber congenital amaurosis. Nature Genetics 35 2 (2003) 158-164
    • (2003) Nature Genetics , vol.35 , Issue.2 , pp. 158-164
    • Woodruff, M.L.1    Wang, Z.2    Chung, H.Y.3    Redmond, T.M.4    Fain, G.L.5    Lem, J.6
  • 86
    • 0028031727 scopus 로고
    • A reciprocal mutation supports helix 2 and helix 7 proximity in the gonadotropin-releasing hormone receptor
    • Zhou W., Flanagan C., Ballesteros J.A., Konvicka K., Davidson J.S., Weinstein H., et al. A reciprocal mutation supports helix 2 and helix 7 proximity in the gonadotropin-releasing hormone receptor. Molecular Pharmacology 45 2 (1994) 165-170
    • (1994) Molecular Pharmacology , vol.45 , Issue.2 , pp. 165-170
    • Zhou, W.1    Flanagan, C.2    Ballesteros, J.A.3    Konvicka, K.4    Davidson, J.S.5    Weinstein, H.6


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