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Volumn 289, Issue 13, 2014, Pages 9288-9303

Inherent instability of the retinitis pigmentosa P23H mutant opsin

Author keywords

[No Author keywords available]

Indexed keywords

COVALENT BONDS; OPHTHALMOLOGY;

EID: 84897414068     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.551713     Document Type: Article
Times cited : (47)

References (86)
  • 1
    • 33750947173 scopus 로고    scopus 로고
    • Retinitis pigmentosa
    • DOI 10.1016/S0140-6736(06)69740-7, PII S0140673606697407
    • Hartong, D. T., Berson, E. L., and Dryja, T. P. (2006) Retinitis pigmentosa. Lancet 368, 1795-1809 (Pubitemid 44739028)
    • (2006) Lancet , vol.368 , Issue.9549 , pp. 1795-1809
    • Hartong, D.T.1    Berson, E.L.2    Dryja, T.P.3
  • 2
    • 0033399668 scopus 로고    scopus 로고
    • Molecular genetics of human retinal disease
    • DOI 10.1146/annurev.genet.33.1.89
    • Rattner, A., Sun, H., and Nathans, J. (1999) Molecular genetics of human retinal disease. Annu. Rev. Genet. 33, 89-131 (Pubitemid 30083120)
    • (1999) Annual Review of Genetics , vol.33 , pp. 89-131
    • Rattner, A.1    Sun, H.2    Nathans, J.3
  • 3
    • 0029906304 scopus 로고    scopus 로고
    • Retinitis pigmentosa: Unfolding its mystery
    • Berson, E. L. (1996) Retinitis pigmentosa: unfolding its mystery. Proc. Natl. Acad. Sci. U.S.A. 93, 4526-4528
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 4526-4528
    • Berson, E.L.1
  • 5
    • 33846957381 scopus 로고    scopus 로고
    • Perspective on genes and mutations causing retinitis pigmentosa
    • Daiger, S. P., Bowne, S. J., and Sullivan, L. S. (2007) Perspective on genes and mutations causing retinitis pigmentosa. Arch. Ophthalmol. 125, 151-158
    • (2007) Arch. Ophthalmol. , vol.125 , pp. 151-158
    • Daiger, S.P.1    Bowne, S.J.2    Sullivan, L.S.3
  • 6
    • 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. (2005) Mechanisms of cell death in rhodopsin retinitis pigmentosa: implications for therapy. Trends Mol. Med. 11, 177-185
    • (2005) Trends Mol. Med. , vol.11 , pp. 177-185
    • Mendes, H.F.1    Van Der Spuy, J.2    Chapple, J.P.3    Cheetham, M.E.4
  • 7
    • 0028287273 scopus 로고
    • Structure and function in rhodopsin. 7. Point mutations associated with autosomal dominant retinitis pigmentosa
    • DOI 10.1021/bi00186a011
    • Kaushal, S., and Khorana, H. G. (1994) Structure and function in rhodopsin. 7. Point mutations associated with autosomal dominant retinitis pigmentosa. Biochemistry 33, 6121-6128 (Pubitemid 24190763)
    • (1994) Biochemistry , vol.33 , Issue.20 , pp. 6121-6128
    • Kaushal, S.1    Khorana, H.G.2
  • 8
    • 0038529723 scopus 로고    scopus 로고
    • Pharmacological chaperone-mediated in vivo folding and stabilization of the P23H-opsin mutant associated with autosomal dominant retinitis pigmentosa
    • DOI 10.1074/jbc.M300087200
    • Noorwez, S. M., Kuksa, V., Imanishi, Y., Zhu, L., Filipek, S., Palczewski, K., and Kaushal, S. (2003) Pharmacological chaperone-mediated in vivo folding and stabilization of the P23H-opsin mutant associated with autosomal dominant retinitis pigmentosa. J. Biol. Chem. 278, 14442-14450 (Pubitemid 36799997)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.16 , pp. 14442-14450
    • Noorwez, S.M.1    Kuksa, V.2    Imanishi, Y.3    Zhu, L.4    Filipek, S.5    Palczewski, K.6    Kaushal, S.7
  • 9
    • 1942469395 scopus 로고    scopus 로고
    • Retinoids Assist the Cellular Folding of the Autosomal Dominant Retinitis Pigmentosa Opsin Mutant P23H
    • DOI 10.1074/jbc.M312101200
    • Noorwez, S. M., Malhotra, R., McDowell, J. H., Smith, K. A., Krebs, M. P., and Kaushal, S. (2004) Retinoids assist the cellular folding of the autosomal dominant retinitis pigmentosa opsin mutant P23H. J. Biol. Chem. 279, 16278-16284 (Pubitemid 38509322)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.16 , pp. 16278-16284
    • Noorwez, S.M.1    Malhotra, R.2    McDowell, J.H.3    Smith, K.A.4    Krebs, M.P.5    Kaushal, S.6
  • 10
    • 33748100274 scopus 로고    scopus 로고
    • Characterization of rhodopsin P23H-induced retinal degeneration in a Xenopus laevis model of retinitis pigmentosa
    • DOI 10.1167/iovs.06-0213
    • Tam, B. M., and Moritz, O. L. (2006) Characterization of rhodopsin P23H-induced retinal degeneration in a Xenopus laevis model of retinitis pigmentosa. Invest. Ophthalmol. Vis. Sci. 47, 3234-3241 (Pubitemid 351639681)
    • (2006) Investigative Ophthalmology and Visual Science , vol.47 , Issue.8 , pp. 3234-3241
    • Tam, B.M.1    Moritz, O.L.2
  • 12
    • 0031880563 scopus 로고    scopus 로고
    • Ribozyme rescue of photoreceptor cells in a transgenic rat model of autosomal dominant retinitis pigmentosa
    • DOI 10.1038/nm0898-967
    • Lewin, A. S., Drenser, K. A., Hauswirth, W. W., Nishikawa, S., Yasumura, D., Flannery, J. G., and LaVail, M. M. (1998) Ribozyme rescue of photoreceptor cells in a transgenic rat model of autosomal dominant retinitis pigmentosa. Nat. Med. 4, 967-971 (Pubitemid 28364040)
    • (1998) Nature Medicine , vol.4 , Issue.8 , pp. 967-971
    • Lewin, A.S.1    Drenser, K.A.2    Hauswirth, W.W.3    Nishikawa, S.4    Yasumura, D.5    Flannery, J.G.6    Lavail, M.M.7
  • 14
    • 77957352000 scopus 로고    scopus 로고
    • Inactivation of VCP/ter94 suppresses retinal pathology caused by misfolded rhodopsin in Drosophila
    • Griciuc, A., Aron, L., Roux, M. J., Klein, R., Giangrande, A., and Ueffing, M. (2010) Inactivation of VCP/ter94 suppresses retinal pathology caused by misfolded rhodopsin in Drosophila. PLoS Genet. 6, e1001075
    • (2010) PLoS Genet. , vol.6
    • Griciuc, A.1    Aron, L.2    Roux, M.J.3    Klein, R.4    Giangrande, A.5    Ueffing, M.6
  • 17
    • 0037099080 scopus 로고    scopus 로고
    • The cellular fate of mutant rhodopsin: Quality control, degradation and aggresome formation
    • Saliba, R. S., Munro, P. M., Luthert, P. J., and Cheetham, M. E. (2002) The cellular fate of mutant rhodopsin: quality control, degradation and aggresome formation. J. Cell Sci. 115, 2907-2918
    • (2002) J. Cell Sci. , vol.115 , pp. 2907-2918
    • Saliba, R.S.1    Munro, P.M.2    Luthert, P.J.3    Cheetham, M.E.4
  • 18
    • 33645535034 scopus 로고    scopus 로고
    • G protein-coupled receptor rhodopsin
    • Palczewski, K. (2006) G protein-coupled receptor rhodopsin. Annu. Rev. Biochem. 75, 743-767
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 743-767
    • Palczewski, K.1
  • 19
    • 77953683083 scopus 로고    scopus 로고
    • Retinoids for treatment of retinal diseases
    • Palczewski, K. (2010) Retinoids for treatment of retinal diseases. Trends Pharmacol. Sci. 31, 284-295
    • (2010) Trends Pharmacol. Sci. , vol.31 , pp. 284-295
    • Palczewski, K.1
  • 20
    • 36049049392 scopus 로고    scopus 로고
    • IRE1 signaling affects cell fate during the unfolded protein response
    • DOI 10.1126/science.1146361
    • Lin, J. H., Li, H., Yasumura, D., Cohen, H. R., Zhang, C., Panning, B., Shokat, K. M., Lavail, M. M., and Walter, P. (2007) IRE1 signaling affects cell fate during the unfolded protein response. Science 318, 944-949 (Pubitemid 350098984)
    • (2007) Science , vol.318 , Issue.5852 , pp. 944-949
    • Lin, J.H.1    Li, H.2    Yasumura, D.3    Cohen, H.R.4    Zhang, C.5    Panning, B.6    Shokat, K.M.7    LaVail, M.M.8    Walter, P.9
  • 24
    • 79953181251 scopus 로고    scopus 로고
    • Probing mechanisms of photoreceptor degeneration in a new mouse model of the common form of autosomal dominant retinitis pigmentosa due to P23H opsin mutations
    • Sakami, S., Maeda, T., Bereta, G., Okano, K., Golczak, M., Sumaroka, A., Roman, A. J., Cideciyan, A. V., Jacobson, S. G., and Palczewski, K. (2011) Probing mechanisms of photoreceptor degeneration in a new mouse model of the common form of autosomal dominant retinitis pigmentosa due to P23H opsin mutations. J. Biol. Chem. 286, 10551-10567
    • (2011) J. Biol. Chem. , vol.286 , pp. 10551-10567
    • Sakami, S.1    Maeda, T.2    Bereta, G.3    Okano, K.4    Golczak, M.5    Sumaroka, A.6    Roman, A.J.7    Cideciyan, A.V.8    Jacobson, S.G.9    Palczewski, K.10
  • 25
    • 84897390436 scopus 로고    scopus 로고
    • P23H opsin knock-in mice reveal a novel step in retinal rod disc morphogenesis
    • Sakami, S., Kolesnikov, A. V., Kefalov, V. J., and Palczewski, K. (2014) P23H opsin knock-in mice reveal a novel step in retinal rod disc morphogenesis. Hum. Mol. Genet. 23, 1723-1741
    • (2014) Hum. Mol. Genet. , vol.23 , pp. 1723-1741
    • Sakami, S.1    Kolesnikov, A.V.2    Kefalov, V.J.3    Palczewski, K.4
  • 26
    • 0017782026 scopus 로고
    • The nematode Caenorhabditis elegans: A new organism for intensive biological study
    • Edgar, R. S., and Wood, W. B. (1977) The nematode Caenorhabditis elegans: a new organism for intensive biological study. Science 198, 1285-1286
    • (1977) Science , vol.198 , pp. 1285-1286
    • Edgar, R.S.1    Wood, W.B.2
  • 28
    • 84856546232 scopus 로고    scopus 로고
    • Heterologous expression of functional G-protein-coupled receptors in Caenorhabditis elegans
    • Salom, D., Cao, P., Sun, W., Kramp, K., Jastrzebska, B., Jin, H., Feng, Z., and Palczewski, K. (2012) Heterologous expression of functional G-protein-coupled receptors in Caenorhabditis elegans. FASEB J. 26, 492-502
    • (2012) FASEB J. , vol.26 , pp. 492-502
    • Salom, D.1    Cao, P.2    Sun, W.3    Kramp, K.4    Jastrzebska, B.5    Jin, H.6    Feng, Z.7    Palczewski, K.8
  • 30
    • 84856516788 scopus 로고    scopus 로고
    • Light-sensitive coupling of rhodopsin and melanopsin to G(i/o) and G(q) signal transduction in Caenorhabditis elegans
    • Cao, P., Sun, W., Kramp, K., Zheng, M., Salom, D., Jastrzebska, B., Jin, H., Palczewski, K., and Feng, Z. (2012) Light-sensitive coupling of rhodopsin and melanopsin to G(i/o) and G(q) signal transduction in Caenorhabditis elegans. FASEB J. 26, 480-491
    • (2012) FASEB J. , vol.26 , pp. 480-491
    • Cao, P.1    Sun, W.2    Kramp, K.3    Zheng, M.4    Salom, D.5    Jastrzebska, B.6    Jin, H.7    Palczewski, K.8    Feng, Z.9
  • 31
    • 38449085292 scopus 로고    scopus 로고
    • Maintenance of C. elegans
    • Stiernagle, T. (2006) Maintenance of C. elegans. WormBook, 1-11
    • (2006) WormBook , pp. 1-11
    • Stiernagle, T.1
  • 32
    • 0028359705 scopus 로고
    • Codon usage in Caenorhabditis elegans: Delineation of translational selection and mutational biases
    • Stenico, M., Lloyd, A. T., and Sharp, P. M. (1994) Codon usage in Caenorhabditis elegans: Delineation of translational selection and mutational biases. Nucleic Acids Res. 22, 2437-2446 (Pubitemid 24222417)
    • (1994) Nucleic Acids Research , vol.22 , Issue.13 , pp. 2437-2446
    • Stenico, M.1    Lloyd, A.T.2    Sharp, P.M.3
  • 33
    • 23844539924 scopus 로고    scopus 로고
    • Multidrug resistance-associated protein MRP-1 regulates dauer diapause by its export activity in Caenorhabditis elegans
    • DOI 10.1242/dev.01909
    • Yabe, T., Suzuki, N., Furukawa, T., Ishihara, T., and Katsura, I. (2005) Multidrug resistance-associated protein MRP-1 regulates dauer diapause by its export activity in Caenorhabditis elegans. Development 132, 3197-3207 (Pubitemid 41167148)
    • (2005) Development , vol.132 , Issue.14 , pp. 3197-3207
    • Yabe, T.1    Suzuki, N.2    Furukawa, T.3    Ishihara, T.4    Katsura, I.5
  • 34
    • 57649118503 scopus 로고    scopus 로고
    • Heterologous expression and purification of the serotonin type 4 receptor from transgenic mouse retina
    • Salom, D., Wu, N., Sun, W., Dong, Z., Palczewski, K., Jordan, S., and Salon, J. A. (2008) Heterologous expression and purification of the serotonin type 4 receptor from transgenic mouse retina. Biochemistry 47, 13296-13307
    • (2008) Biochemistry , vol.47 , pp. 13296-13307
    • Salom, D.1    Wu, N.2    Sun, W.3    Dong, Z.4    Palczewski, K.5    Jordan, S.6    Salon, J.A.7
  • 35
    • 56749095220 scopus 로고    scopus 로고
    • Different properties of the native and reconstituted heterotrimeric G protein transducin
    • Goc, A., Angel, T. E., Jastrzebska, B., Wang, B., Wintrode, P. L., and Palczewski, K. (2008) Different properties of the native and reconstituted heterotrimeric G protein transducin. Biochemistry 47, 12409-12419
    • (2008) Biochemistry , vol.47 , pp. 12409-12419
    • Goc, A.1    Angel, T.E.2    Jastrzebska, B.3    Wang, B.4    Wintrode, P.L.5    Palczewski, K.6
  • 36
    • 0027270898 scopus 로고
    • Regulation of the rhodopsin-transducin interaction by a highly conserved carboxylic acid group
    • Fahmy, K., and Sakmar, T. P. (1993) Regulation of the rhodopsin-transducin interaction by a highly conserved carboxylic acid group. Biochemistry 32, 7229-7236 (Pubitemid 23223127)
    • (1993) Biochemistry , vol.32 , Issue.28 , pp. 7229-7236
    • Fahmy, K.1    Sakmar, T.P.2
  • 37
    • 0029907599 scopus 로고    scopus 로고
    • Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin
    • DOI 10.1126/science.274.5288.768
    • Farrens, D. L., Altenbach, C., Yang, K., Hubbell, W. L., and Khorana, H. G. (1996) Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin. Science 274, 768-770 (Pubitemid 26398253)
    • (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
  • 38
    • 0035971240 scopus 로고    scopus 로고
    • Maximal rate and nucleotide dependence of rhodopsin-catalyzed transducin activation: Initial rate analysis based on a double displacement mechanism
    • Heck, M., and Hofmann, K. P. (2001) Maximal rate and nucleotide dependence of rhodopsin-catalyzed transducin activation: initial rate analysis based on a double displacement mechanism. J. Biol. Chem. 276, 10000-10009
    • (2001) J. Biol. Chem. , vol.276 , pp. 10000-10009
    • Heck, M.1    Hofmann, K.P.2
  • 39
    • 0028957661 scopus 로고
    • Structure and function in rhodopsin. Measurement of the rate of metarhodopsin II decay by fluorescence spectroscopy
    • Farrens, D. L., and Khorana, H. G. (1995) Structure and function in rhodopsin. Measurement of the rate of metarhodopsin II decay by fluorescence spectroscopy. J. Biol. Chem. 270, 5073-5076
    • (1995) J. Biol. Chem. , vol.270 , pp. 5073-5076
    • Farrens, D.L.1    Khorana, H.G.2
  • 40
    • 0042591319 scopus 로고    scopus 로고
    • Ligand channeling within a G-protein-coupled receptor: The entry and exit of retinals in native opsin
    • DOI 10.1074/jbc.M302115200
    • Schadel, S. A., Heck, M., Maretzki, D., Filipek, S., Teller, D. C., Palczewski, K., and Hofmann, K. P. (2003) Ligand channeling within a G-protein-coupled receptor. The entry and exit of retinals in native opsin. J. Biol. Chem. 278, 24896-24903 (Pubitemid 37548649)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.27 , pp. 24896-24903
    • Schadel, S.A.1    Heck, M.2    Maretzki, D.3    Filipek, S.4    Teller, D.C.5    Palczewski, K.6    Hofmann, K.P.7
  • 41
    • 0038729667 scopus 로고    scopus 로고
    • Signaling states of rhodopsin. Formation of the storage form, metarhodopsin III, from active metarhodopsin II
    • DOI 10.1074/jbc.M209675200
    • Heck, M., Schädel, S. A., Maretzki, D., Bartl, F. J., Ritter, E., Palczewski, K., and Hofmann, K. P. (2003) Signaling states of rhodopsin. Formation of the storage form, metarhodopsin III, from active metarhodopsin II. J. Biol. Chem. 278, 3162-3169 (Pubitemid 36801226)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.5 , pp. 3162-3169
    • Heck, M.1    Schadel, S.A.2    Maretzki, D.3    Bartl, F.J.4    Ritter, E.5    Palczewski, K.6    Hofmann, K.P.7
  • 42
    • 0027820508 scopus 로고
    • Light-dependent transducin activation by an ultraviolet-absorbing rhodopsin mutant
    • DOI 10.1021/bi00086a023
    • Fahmy, K., and Sakmar, T. P. (1993) Light-dependent transducin activation by an ultraviolet-absorbing rhodopsin mutant. Biochemistry 32, 9165-9171 (Pubitemid 24186239)
    • (1993) Biochemistry , vol.32 , Issue.35 , pp. 9165-9171
    • Fahmy, K.1    Sakmar, T.P.2
  • 43
    • 80051495439 scopus 로고    scopus 로고
    • Posttranslational modifications of the photoreceptor-specific ABC transporter ABCA4
    • Tsybovsky, Y., Wang, B., Quazi, F., Molday, R. S., and Palczewski, K. (2011) Posttranslational modifications of the photoreceptor-specific ABC transporter ABCA4. Biochemistry 50, 6855-6866
    • (2011) Biochemistry , vol.50 , pp. 6855-6866
    • Tsybovsky, Y.1    Wang, B.2    Quazi, F.3    Molday, R.S.4    Palczewski, K.5
  • 44
    • 79954987167 scopus 로고    scopus 로고
    • Profiling a Caenorhabditis elegans behavioral parametric dataset with a supervised K-means clustering algorithm identifies genetic networks regulating locomotion
    • Zhang, S., Jin, W., Huang, Y., Su, W., Yang, J., and Feng, Z. (2011) Profiling a Caenorhabditis elegans behavioral parametric dataset with a supervised K-means clustering algorithm identifies genetic networks regulating locomotion. J. Neurosci. Methods 197, 315-323
    • (2011) J. Neurosci. Methods , vol.197 , pp. 315-323
    • Zhang, S.1    Jin, W.2    Huang, Y.3    Su, W.4    Yang, J.5    Feng, Z.6
  • 45
    • 0037072934 scopus 로고    scopus 로고
    • Arhodopsin mutant linked to autosomal dominant retinitis pigmentosa is prone to aggregate and interacts with the ubiquitin proteasome system
    • Illing, M. E., Rajan, R. S., Bence, N. F., and Kopito, R. R. (2002)Arhodopsin mutant linked to autosomal dominant retinitis pigmentosa is prone to aggregate and interacts with the ubiquitin proteasome system. J. Biol. Chem. 277, 34150-34160
    • (2002) J. Biol. Chem. , vol.277 , pp. 34150-34160
    • Illing, M.E.1    Rajan, R.S.2    Bence, N.F.3    Kopito, R.R.4
  • 46
    • 34248215318 scopus 로고    scopus 로고
    • Visual rhodopsin sees the light: Structure and mechanism of G protein signaling
    • DOI 10.1074/jbc.R600032200
    • Ridge, K. D., and Palczewski, K. (2007) Visual rhodopsin sees the light: structure and mechanism of G protein signaling. J. Biol. Chem. 282, 9297-9301 (Pubitemid 47104561)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.13 , pp. 9297-9301
    • Ridge, K.D.1    Palczewski, K.2
  • 47
    • 0025085912 scopus 로고
    • Assembly of functional rhodopsin requires a disulfide bond between cysteine residues 110 and 187
    • Karnik, S. S., and Khorana, H. G. (1990) Assembly of functional rhodopsin requires a disulfide bond between cysteine residues 110 and 187. J. Biol. Chem. 265, 17520-17524
    • (1990) J. Biol. Chem. , vol.265 , pp. 17520-17524
    • Karnik, S.S.1    Khorana, H.G.2
  • 48
    • 0033554369 scopus 로고    scopus 로고
    • Kinetics of visual pigment regeneration in excised mouse eyes and in mice with a targeted disruption of the gene encoding inter-photoreceptor retinoid-binding protein or arrestin
    • Palczewski, K., Van Hooser, J. P., Garwin, G. G., Chen, J., Liou, G. I., and Saari, J. C. (1999) Kinetics of visual pigment regeneration in excised mouse eyes and in mice with a targeted disruption of the gene encoding inter-photoreceptor retinoid-binding protein or arrestin. Biochemistry 38, 12012-12019
    • (1999) Biochemistry , vol.38 , pp. 12012-12019
    • Palczewski, K.1    Van Hooser, J.P.2    Garwin, G.G.3    Chen, J.4    Liou, G.I.5    Saari, J.C.6
  • 50
    • 84859091769 scopus 로고    scopus 로고
    • Characterization of the proteostasis roles of glycerol accumulation, protein degradation and protein synthesis during osmotic stress in C. elegans
    • Burkewitz, K., Choe, K. P., Lee, E. C., Deonarine, A., and Strange, K. (2012) Characterization of the proteostasis roles of glycerol accumulation, protein degradation and protein synthesis during osmotic stress in C. elegans. PLoS One 7, e34153
    • (2012) PLoS One , vol.7
    • Burkewitz, K.1    Choe, K.P.2    Lee, E.C.3    Deonarine, A.4    Strange, K.5
  • 51
    • 0029449151 scopus 로고
    • Proteins and protein assemblies
    • Epstein, H. F., and Liu, F. (1995) Proteins and protein assemblies. Methods Cell Biol. 48, 437-450
    • (1995) Methods Cell Biol , vol.48 , pp. 437-450
    • Epstein, H.F.1    Liu, F.2
  • 52
    • 79955366725 scopus 로고    scopus 로고
    • A screenable in vivo assay to study proteostasis networks in Caenorhabditis elegans
    • Segref, A., Torres, S., and Hoppe, T. (2011) A screenable in vivo assay to study proteostasis networks in Caenorhabditis elegans. Genetics 187, 1235-1240
    • (2011) Genetics , vol.187 , pp. 1235-1240
    • Segref, A.1    Torres, S.2    Hoppe, T.3
  • 53
    • 84884695800 scopus 로고    scopus 로고
    • Integration of the unfolded protein and oxidative stress responses through SKN-1/Nrf
    • Glover-Cutter, K. M., Lin, S., and Blackwell, T. K. (2013) Integration of the unfolded protein and oxidative stress responses through SKN-1/Nrf. PLoS Genet. 9, e1003701
    • (2013) PLoS Genet. , vol.9
    • Glover-Cutter, K.M.1    Lin, S.2    Blackwell, T.K.3
  • 55
    • 0025768030 scopus 로고
    • Retinal function and rhodopsin levels in autosomal dominant retinitis pigmentosa with rhodopsin mutations
    • Jacobson, S. G., Kemp, C. M., Sung, C. H., and Nathans, J. (1991) Retinal function and rhodopsin levels in autosomal dominant retinitis pigmentosa with rhodopsin mutations. Am. J. Ophthalmol. 112, 256-271
    • (1991) Am. J. Ophthalmol. , vol.112 , pp. 256-271
    • Jacobson, S.G.1    Kemp, C.M.2    Sung, C.H.3    Nathans, J.4
  • 56
    • 52949134162 scopus 로고    scopus 로고
    • Pharmacological manipulation of gain-of-function and dominant-negative mechanisms in rhodopsin retinitis pigmentosa
    • Mendes, H. F., and Cheetham, M. E. (2008) Pharmacological manipulation of gain-of-function and dominant-negative mechanisms in rhodopsin retinitis pigmentosa. Hum. Mol. Genet. 17, 3043-3054
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 3043-3054
    • Mendes, H.F.1    Cheetham, M.E.2
  • 57
    • 83255192162 scopus 로고    scopus 로고
    • Key enzymes of the retinoid (visual) cycle in vertebrate retina
    • Kiser, P. D., Golczak, M., Maeda, A., and Palczewski, K. (2012) Key enzymes of the retinoid (visual) cycle in vertebrate retina. Biochim. Biophys. Acta 1821, 137-151
    • (2012) Biochim. Biophys. Acta , vol.1821 , pp. 137-151
    • Kiser, P.D.1    Golczak, M.2    Maeda, A.3    Palczewski, K.4
  • 58
    • 84856008050 scopus 로고    scopus 로고
    • Rhodopsin mutant P23H destabilizes rod photoreceptor disk membranes
    • Haeri, M., and Knox, B. E. (2012) Rhodopsin mutant P23H destabilizes rod photoreceptor disk membranes. PLoS One 7, e30101
    • (2012) PLoS One , vol.7
    • Haeri, M.1    Knox, B.E.2
  • 61
    • 0028858741 scopus 로고
    • Functional abnormalities in transgenic mice expressing a mutant rhodopsin gene
    • Goto, Y., Peachey, N. S., Ripps, H., and Naash, M. I. (1995) Functional abnormalities in transgenic mice expressing a mutant rhodopsin gene. Invest. Ophthalmol. Vis. Sci. 36, 62-71
    • (1995) Invest. Ophthalmol. Vis. Sci. , vol.36 , pp. 62-71
    • Goto, Y.1    Peachey, N.S.2    Ripps, H.3    Naash, M.I.4
  • 62
    • 0026089384 scopus 로고
    • Ocular findings in patients with autosomal dominant retinitis pigmentosa and a rhodopsin gene defect (Pro-23-His)
    • Berson, E. L., Rosner, B., Sandberg, M. A., and Dryja, T. P. (1991) Ocular findings in patients with autosomal dominant retinitis pigmentosa and a rhodopsin gene defect (Pro-23-His). Arch. Ophthalmol. 109, 92-101
    • (1991) Arch. Ophthalmol. , vol.109 , pp. 92-101
    • Berson, E.L.1    Rosner, B.2    Sandberg, M.A.3    Dryja, T.P.4
  • 63
    • 84860145044 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and unfolded protein response pathways: Potential for treating age-related retinal degeneration
    • Haeri, M., and Knox, B. E. (2012) Endoplasmic reticulum stress and unfolded protein response pathways: potential for treating age-related retinal degeneration. J. Ophthalmic Vis. Res. 7, 45-59
    • (2012) J. Ophthalmic Vis. Res. , vol.7 , pp. 45-59
    • Haeri, M.1    Knox, B.E.2
  • 64
    • 78651295470 scopus 로고    scopus 로고
    • Misfolded proteins and retinal dystrophies
    • Lin, J. H., and Lavail, M. M. (2010) Misfolded proteins and retinal dystrophies. Adv. Exp. Med. Biol. 664, 115-121
    • (2010) Adv. Exp. Med. Biol. , vol.664 , pp. 115-121
    • Lin, J.H.1    Lavail, M.M.2
  • 65
    • 84878999228 scopus 로고    scopus 로고
    • Proteasome overload is a common stress factor in multiple forms of inherited retinal degeneration
    • Lobanova, E. S., Finkelstein, S., Skiba, N. P., and Arshavsky, V. Y. (2013) Proteasome overload is a common stress factor in multiple forms of inherited retinal degeneration. Proc. Natl. Acad. Sci. U.S.A. 110, 9986-9991
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 9986-9991
    • Lobanova, E.S.1    Finkelstein, S.2    Skiba, N.P.3    Arshavsky, V.Y.4
  • 66
    • 80054026314 scopus 로고    scopus 로고
    • A review of the mammalian unfolded protein response
    • Chakrabarti, A., Chen, A. W., and Varner, J. D. (2011) A review of the mammalian unfolded protein response. Biotechnol. Bioeng. 108, 2777-2793
    • (2011) Biotechnol. Bioeng. , vol.108 , pp. 2777-2793
    • Chakrabarti, A.1    Chen, A.W.2    Varner, J.D.3
  • 67
    • 0018787250 scopus 로고
    • Rhodopsin carbohydrate. Structure of small oligosaccharides attached at two sites near the NH2 terminus
    • Fukuda, M. N., Papermaster, D. S., and Hargrave, P. A. (1979) Rhodopsin carbohydrate. Structure of small oligosaccharides attached at two sites near the NH2 terminus. J. Biol. Chem. 254, 8201-8207
    • (1979) J. Biol. Chem. , vol.254 , pp. 8201-8207
    • Fukuda, M.N.1    Papermaster, D.S.2    Hargrave, P.A.3
  • 68
    • 0020020228 scopus 로고
    • Structural analysis of carbohydrate moiety of bovine rhodopsin
    • Fukuda, M. N., Papermaster, D. S., and Hargrave, P. A. (1982) Structural analysis of carbohydrate moiety of bovine rhodopsin. Methods Enzymol. 81, 214-223
    • (1982) Methods Enzymol. , vol.81 , pp. 214-223
    • Fukuda, M.N.1    Papermaster, D.S.2    Hargrave, P.A.3
  • 69
    • 0018288888 scopus 로고
    • Structure of the carbohydrate moieties of bovine rhodopsin
    • Liang, C. J., Yamashita, K., Muellenberg, C. G., Shichi, H., and Kobata, A. (1979) Structure of the carbohydrate moieties of bovine rhodopsin. J. Biol. Chem. 254, 6414-6418 (Pubitemid 9243606)
    • (1979) Journal of Biological Chemistry , vol.254 , Issue.14 , pp. 6414-6418
    • Liang, C.J.1    Yamashita, K.2    Muellenberg, C.G.3
  • 71
    • 70350657146 scopus 로고    scopus 로고
    • Rhodopsin: The functional significance of Asn-linked glycosylation and other post-translational modifications
    • Murray, A. R., Fliesler, S. J., and Al-Ubaidi, M. R. (2009) Rhodopsin: the functional significance of Asn-linked glycosylation and other post-translational modifications. Ophthalmic Genet. 30, 109-120
    • (2009) Ophthalmic Genet. , vol.30 , pp. 109-120
    • Murray, A.R.1    Fliesler, S.J.2    Al-Ubaidi, M.R.3
  • 72
    • 0024110575 scopus 로고
    • Cysteine residues 110 and 187 are essential for the formation of correct structure in bovine rhodopsin
    • Karnik, S. S., Sakmar, T. P., Chen, H. B., and Khorana, H. G. (1988) Cysteine residues 110 and 187 are essential for the formation of correct structure in bovine rhodopsin. Proc. Natl. Acad. Sci. U.S.A. 85, 8459-8463
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 8459-8463
    • Karnik, S.S.1    Sakmar, T.P.2    Chen, H.B.3    Khorana, H.G.4
  • 73
    • 0035942215 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: Mass spectrometric identification of the abnormal intradiscal disulfide bond in misfolded retinitis pigmentosa mutants
    • DOI 10.1073/pnas.061632798
    • Hwa, J., Klein-Seetharaman, J., and Khorana, H. G. (2001) Structure and function in rhodopsin: Mass spectrometric identification of the abnormal intradiscal disulfide bond in misfolded retinitis pigmentosa mutants. Proc. Natl. Acad. Sci. U.S.A. 98, 4872-4876 (Pubitemid 32397049)
    • (2001) Proceedings of the National Academy of Sciences of the United States of America , vol.98 , Issue.9 , pp. 4872-4876
    • Hwa, J.1    Klein-Seetharaman, J.2    Khorana, H.G.3
  • 74
    • 36248992965 scopus 로고    scopus 로고
    • Opsin Stability and Folding: The Role of Cys185 and Abnormal Disulfide Bond Formation in the Intradiscal Domain
    • DOI 10.1016/j.jmb.2007.10.013, PII S002228360701306X
    • McKibbin, C., Toye, A. M., Reeves, P. J., Khorana, H. G., Edwards, P. C., Villa, C., and Booth, P. J. (2007) Opsin stability and folding: the role of Cys-185 and abnormal disulfide bond formation in the intradiscal domain. J. Mol. Biol. 374, 1309-1318 (Pubitemid 350122542)
    • (2007) Journal of Molecular Biology , vol.374 , Issue.5 , pp. 1309-1318
    • McKibbin, C.1    Toye, A.M.2    Reeves, P.J.3    Khorana, H.G.4    Edwards, P.C.5    Villa, C.6    Booth, P.J.7
  • 75
    • 0028110523 scopus 로고
    • Rhodopsin accumulation at abnormal sites in retinas of mice with a human P23H rhodopsin transgene
    • Roof, D. J., Adamian, M., and Hayes, A. (1994) Rhodopsin accumulation at abnormal sites in retinas of mice with a human P23H rhodopsin transgene. Invest. Ophthalmol. Vis. Sci. 35, 4049-4062 (Pubitemid 24350669)
    • (1994) Investigative Ophthalmology and Visual Science , vol.35 , Issue.12 , pp. 4049-4062
    • Roof, D.J.1    Adamian, M.2    Hayes, A.3
  • 76
    • 0032483063 scopus 로고    scopus 로고
    • Opsin localization and rhodopsin photochemistry in a transgenic mouse model of retinitis pigmentosa
    • DOI 10.1016/S0306-4522(98)00173-0, PII S0306452298001730
    • Wu, T. H., Ting, T. D., Okajima, T. I., Pepperberg, D. R., Ho, Y. K., Ripps, H., and Naash, M. I. (1998) Opsin localization and rhodopsin photochemistry in a transgenic mouse model of retinitis pigmentosa. Neuroscience 87, 709-717 (Pubitemid 28396555)
    • (1998) Neuroscience , vol.87 , Issue.3 , pp. 709-717
    • Wu, T.-H.1    Ting, T.D.2    Okajima, T.-I.L.3    Pepperberg, D.R.4    Ho, Y.-K.5    Ripps, H.6    Naash, M.I.7
  • 77
    • 84867544047 scopus 로고    scopus 로고
    • Gene therapy in animal models of autosomal dominant retinitis pigmentosa
    • Rossmiller, B., Mao, H., and Lewin, A. S. (2012) Gene therapy in animal models of autosomal dominant retinitis pigmentosa. Mol. Vis. 18, 2479-2496
    • (2012) Mol. Vis. , vol.18 , pp. 2479-2496
    • Rossmiller, B.1    Mao, H.2    Lewin, A.S.3
  • 84
    • 41949114713 scopus 로고    scopus 로고
    • The status of cones in the rhodopsin mutant P23H-3 retina: Light-regulated damage and repair in parallel with rods
    • Chrysostomou, V., Stone, J., Stowe, S., Barnett, N. L., and Valter, K. (2008) The status of cones in the rhodopsin mutant P23H-3 retina: light-regulated damage and repair in parallel with rods. Invest. Ophthalmol. Vis. Sci. 49, 1116-1125
    • (2008) Invest. Ophthalmol. Vis. Sci. , vol.49 , pp. 1116-1125
    • Chrysostomou, V.1    Stone, J.2    Stowe, S.3    Barnett, N.L.4    Valter, K.5
  • 85
    • 34249736779 scopus 로고    scopus 로고
    • Caenorhabditis elegans: A versatile platform for drug discovery
    • Artal-Sanz, M., de Jong, L., and Tavernarakis, N. (2006) Caenorhabditis elegans: a versatile platform for drug discovery. Biotechnol. J. 1, 1405-1418
    • (2006) Biotechnol. J. , vol.1 , pp. 1405-1418
    • Artal-Sanz, M.1    De Jong, L.2    Tavernarakis, N.3
  • 86
    • 84876898289 scopus 로고    scopus 로고
    • An ultra high-throughput, whole-animal screen for small molecule modulators of a specific genetic pathway in Caenorhabditis elegans
    • Leung, C. K., Wang, Y., Malany, S., Deonarine, A., Nguyen, K., Vasile, S., and Choe, K. P. (2013) An ultra high-throughput, whole-animal screen for small molecule modulators of a specific genetic pathway in Caenorhabditis elegans. PLoS One 8, e62166
    • (2013) PLoS One , vol.8
    • Leung, C.K.1    Wang, Y.2    Malany, S.3    Deonarine, A.4    Nguyen, K.5    Vasile, S.6    Choe, K.P.7


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