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Volumn 41, Issue 2, 2000, Pages 337-348

Biochemistry of visual pigment regeneration: The Friedenwald lecture

Author keywords

[No Author keywords available]

Indexed keywords

HYDROLASE; RHODOPSIN; TRANSDUCIN; VISUAL PIGMENT;

EID: 0033960296     PISSN: 01460404     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Conference Paper
Times cited : (219)

References (118)
  • 1
    • 0008899575 scopus 로고
    • Chemische vorgänge in der netzhaut
    • Hermann L, ed. Leipzig: Vogel
    • Kühne W. Chemische vorgänge in der netzhaut. In: Hermann L, ed. Handbuch der Physiologie, Leipzig: Vogel; 1879:235-342. English translation taken from Vision Res, 1977;17:1269-1316.
    • (1879) Handbuch der Physiologie , pp. 235-342
    • Kühne, W.1
  • 2
    • 0017606448 scopus 로고
    • Kühne W. Chemische vorgänge in der netzhaut. In: Hermann L, ed. Handbuch der Physiologie, Leipzig: Vogel; 1879:235-342. English translation taken from Vision Res, 1977;17:1269-1316.
    • (1977) Vision Res , vol.17 , pp. 1269-1316
  • 3
    • 0032555517 scopus 로고    scopus 로고
    • Molecular characterization of a novel short-chain dehydrogenase/reductase that reduces all-trans-retinal
    • Haeseleer F, Huang J, Lebioda L, Saari JC, Palczewski K. Molecular characterization of a novel short-chain dehydrogenase/reductase that reduces all-trans-retinal. J Biol Chem. 1998;273:21790-21799.
    • (1998) J Biol Chem. , vol.273 , pp. 21790-21799
    • Haeseleer, F.1    Huang, J.2    Lebioda, L.3    Saari, J.C.4    Palczewski, K.5
  • 4
    • 0033525214 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of lecithin retinol acyltransferase
    • Ruiz A, Winston A, Lim Y-H, Gilbert BA, Rando RR, Bok D. Molecular and biochemical characterization of lecithin retinol acyltransferase. J Biol Chem. 1999;274:3834-3841.
    • (1999) J Biol Chem. , vol.274 , pp. 3834-3841
    • Ruiz, A.1    Winston, A.2    Lim, Y.-H.3    Gilbert, B.A.4    Rando, R.R.5    Bok, D.6
  • 5
    • 0028816843 scopus 로고
    • The retinal pigment epithelial-specific 11-cis-retinol dehydrogenase belongs to the family of short chain alcohol dehydrogenases
    • Simon A, Hellman U, Wernstedt C, Eriksson U. The retinal pigment epithelial-specific 11-cis-retinol dehydrogenase belongs to the family of short chain alcohol dehydrogenases. J Biol Chem. 1995;270:1107-1112.
    • (1995) J Biol Chem. , vol.270 , pp. 1107-1112
    • Simon, A.1    Hellman, U.2    Wernstedt, C.3    Eriksson, U.4
  • 6
    • 0015122009 scopus 로고
    • Rhodopsin kinetics in the human eye
    • Alpern M. Rhodopsin kinetics in the human eye. J Physiol. 1971; 217:447-471.
    • (1971) J Physiol. , vol.217 , pp. 447-471
    • Alpern, M.1
  • 7
    • 1642355856 scopus 로고
    • Dark-adaptation and the regeneration of rhodopsin
    • Rushton WAH. Dark-adaptation and the regeneration of rhodopsin. J Physiol. 1961;156:166-178.
    • (1961) J Physiol. , vol.156 , pp. 166-178
    • Rushton, W.A.H.1
  • 8
    • 76549224008 scopus 로고
    • The ferrier lecture, 1962. Visual adaptation
    • Rushton WAH. The Ferrier Lecture, 1962. Visual adaptation. Proc R Soc Lond B Biol Sci. 1965;162:20-46.
    • (1965) Proc R Soc Lond B Biol Sci. , vol.162 , pp. 20-46
    • Rushton, W.A.H.1
  • 9
    • 0026091595 scopus 로고
    • The first step in vision: Femtosecond isomerization of rhodopsin
    • Schoenlein RW, Peteanu LA, Mathies RA, Shank CV. The first step in vision: femtosecond isomerization of rhodopsin. Science. 1991; 254:412-415.
    • (1991) Science , vol.254 , pp. 412-415
    • Schoenlein, R.W.1    Peteanu, L.A.2    Mathies, R.A.3    Shank, C.V.4
  • 10
    • 0015075198 scopus 로고
    • The kinetics of cone visual pigments in man
    • Alpern M, Masseidvaag F, Ohba N. The kinetics of cone visual pigments in man. Vision Res. 1971;11:539-549.
    • (1971) Vision Res. , vol.11 , pp. 539-549
    • Alpern, M.1    Masseidvaag, F.2    Ohba, N.3
  • 11
    • 0003016602 scopus 로고
    • Dark adaptation: A re-examination
    • Hess RF, Sharpe LT, Nordby K, eds. Cambridge, UK: Cambridge University Press
    • Lamb TD. Dark adaptation: a re-examination. In: Hess RF, Sharpe LT, Nordby K, eds. Night Vision. Basic, Clinical and Applied Aspects. Cambridge, UK: Cambridge University Press; 1990:177-222.
    • (1990) Night Vision. Basic, Clinical and Applied Aspects , pp. 177-222
    • Lamb, T.D.1
  • 12
    • 2642675217 scopus 로고    scopus 로고
    • Molecular basis of dark adaptation in rod photoreceptors
    • Leibrock CS, Reuter R, Lamb TD. Molecular basis of dark adaptation in rod photoreceptors. Eye. 1998;12:511-520.
    • (1998) Eye , vol.12 , pp. 511-520
    • Leibrock, C.S.1    Reuter, R.2    Lamb, T.D.3
  • 14
    • 0027444823 scopus 로고
    • Photoreceptor degeneration in vitamin A deprivation and retinitis pigmentosa: The equivalent light hypothesis
    • Fain GL, Lisman JE. Photoreceptor degeneration in vitamin A deprivation and retinitis pigmentosa: the equivalent light hypothesis. Exp Eye Res. 1993;57:335-340.
    • (1993) Exp Eye Res. , vol.57 , pp. 335-340
    • Fain, G.L.1    Lisman, J.E.2
  • 16
    • 0027525290 scopus 로고
    • Noncovalent 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. Noncovalent occupancy of the retinal-binding pocket of opsin diminishes bleaching adaptation of retinal cones. Neuron. 1993;11:513-522.
    • (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
  • 17
    • 0028125886 scopus 로고
    • Rhodopsin mutation G90D and a molecular mechanism for congenital night blindness
    • Rao VR, Cohen GB, Oprian DD. Rhodopsin mutation G90D and a molecular mechanism for congenital night blindness. Nature. 1994;367:639-642.
    • (1994) Nature , vol.367 , pp. 639-642
    • Rao, V.R.1    Cohen, G.B.2    Oprian, D.D.3
  • 18
    • 0000904977 scopus 로고
    • Zur anatomie und physiologie der retina
    • Boll F. Zur anatomie und physiologie der retina. Monatsber Akad Wissensch, Berlin. 1876;23:783-787.
    • (1876) Monatsber Akad Wissensch, Berlin , vol.23 , pp. 783-787
    • Boll, F.1
  • 19
    • 0002451702 scopus 로고
    • Zur anatomie und physiologic der retina
    • Boll F. Zur anatomie und physiologic der retina. Arch Anat Physiol Abstr. 1877:4-35. English translation taken from Vision Res. 1977;17:1253-1264.
    • (1877) Arch Anat Physiol Abstr. , pp. 4-35
    • Boll, F.1
  • 20
    • 0008946643 scopus 로고
    • Boll F. Zur anatomie und physiologic der retina. Arch Anat Physiol Abstr. 1877:4-35. English translation taken from Vision Res. 1977;17:1253-1264.
    • (1977) Vision Res. , vol.17 , pp. 1253-1264
  • 23
    • 0002386911 scopus 로고
    • Carotenoids and the vitamin A cycle in vision
    • Wald G. Carotenoids and the vitamin A cycle in vision. Nature. 1934;134:65.
    • (1934) Nature , vol.134 , pp. 65
    • Wald, G.1
  • 24
    • 0001433667 scopus 로고
    • Chemistry of visual adaptation in the rat
    • Dowling JE. Chemistry of visual adaptation in the rat. Nature. 1960;168:114-118.
    • (1960) Nature , vol.168 , pp. 114-118
    • Dowling, J.E.1
  • 25
    • 0017143552 scopus 로고
    • Vitamin A and the role of the pigment epithelium during bleaching and regeneration of rhodopsin in the frog eye
    • Bridges CDB. Vitamin A and the role of the pigment epithelium during bleaching and regeneration of rhodopsin in the frog eye. Exp Eye Res. 1976;22:435-455.
    • (1976) Exp Eye Res. , vol.22 , pp. 435-455
    • Bridges, C.D.B.1
  • 26
    • 0016174313 scopus 로고
    • The distribution and proportions of vitamin A compounds during the visual cycle in the rat
    • Zimmerman WF. The distribution and proportions of vitamin A compounds during the visual cycle in the rat. Vision Res. 1974; 14:795-802.
    • (1974) Vision Res. , vol.14 , pp. 795-802
    • Zimmerman, W.F.1
  • 27
    • 0000284971 scopus 로고
    • Isomerization of all-trans-retinoids to 11-cis-retinoids in vitro
    • Bernstein PS, Law WC, Rando RR. Isomerization of all-trans-retinoids to 11-cis-retinoids in vitro. Proc Natl Acad Sci USA., 1987;84:1849-1853.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 1849-1853
    • Bernstein, P.S.1    Law, W.C.2    Rando, R.R.3
  • 28
    • 0030112776 scopus 로고    scopus 로고
    • Polyenes and vision
    • Rando RR. Polyenes and vision. Chem Biol. 1996;3:255-262.
    • (1996) Chem Biol. , vol.3 , pp. 255-262
    • Rando, R.R.1
  • 29
    • 0031689828 scopus 로고    scopus 로고
    • Distribution of 11-cis-LRAT, 11-cis-RD and 11-cis-REH in bovine retinal pigment epithelium membranes
    • Mata NL, Tsin ATC. Distribution of 11-cis-LRAT, 11-cis-RD and 11-cis-REH in bovine retinal pigment epithelium membranes. Biochim Biophys Acta. 1998;1394:16-22.
    • (1998) Biochim Biophys Acta , vol.1394 , pp. 16-22
    • Mata, N.L.1    Tsin, A.T.C.2
  • 30
    • 0000761427 scopus 로고    scopus 로고
    • Retinal stimulates ATP hydrolysis by purified and reconstituted ABCR, the photoreceptor-specinc ATP-binding cassette transporter responsible for stargardt disease
    • Sun H, Molday RS, Nathans J. Retinal stimulates ATP hydrolysis by purified and reconstituted ABCR, the photoreceptor-specinc ATP-binding cassette transporter responsible for Stargardt disease. J Biol Chem. 1999;274:8269-8281.
    • (1999) J Biol Chem. , vol.274 , pp. 8269-8281
    • Sun, H.1    Molday, R.S.2    Nathans, J.3
  • 31
    • 0033538438 scopus 로고    scopus 로고
    • Insights into the function of rim protein in photoreceptors and etiology of Stargardt's disease from the phenotype in aber knock-out mice
    • Weng J, Mata NL, Azarian SM, Tzekov RT, Birch DG, Travis GH. Insights into the function of rim protein in photoreceptors and etiology of Stargardt's disease from the phenotype in aber knock-out mice. Cell. 1999;98:13-23.
    • (1999) Cell , vol.98 , pp. 13-23
    • Weng, J.1    Mata, N.L.2    Azarian, S.M.3    Tzekov, R.T.4    Birch, D.G.5    Travis, G.H.6
  • 32
    • 0025030229 scopus 로고
    • Processing and transport of retinoids by the retinal pigment epithelium
    • Bok D. Processing and transport of retinoids by the retinal pigment epithelium. Eye. 1990;4:326-332.
    • (1990) Eye , vol.4 , pp. 326-332
    • Bok, D.1
  • 34
    • 0027563554 scopus 로고
    • Interphotoreceptor retinoid-binding protein (IRBP): Molecular biology and physiological role in the visual cycle of rhodopsin
    • Pepperberg DR, Okajima T-IL, Wiggert B, Ripps H, Crouch K, Chader GJ. Interphotoreceptor retinoid-binding protein (IRBP): molecular biology and physiological role in the visual cycle of rhodopsin. Mol Neurobiol. 1993;1993:7:61-84.
    • (1993) Mol Neurobiol. 1993 , vol.7 , pp. 61-84
    • Pepperberg, D.R.1    Okajima, T.-I.L.2    Wiggert, B.3    Ripps, H.4    Crouch, K.5    Chader, G.J.6
  • 35
    • 0002463912 scopus 로고
    • Retinoids in photosensitive systems
    • Sporn MB, Roberts AH, Goodman DS, eds. New York: Raven Press
    • Saari JC. Retinoids in photosensitive systems In: Sporn MB, Roberts AH, Goodman DS, eds. The Retinoids: Biology, Chemistry, and Medicine. 2nd ed. New York: Raven Press; 1994:351-385.
    • (1994) The Retinoids: Biology, Chemistry, and Medicine. 2nd Ed. , pp. 351-385
    • Saari, J.C.1
  • 36
    • 0014411230 scopus 로고
    • Molecular basis of visual excitation
    • Wald G. Molecular basis of visual excitation. Science. 1968;162: 230-239.
    • (1968) Science , vol.162 , pp. 230-239
    • Wald, G.1
  • 37
    • 0021232986 scopus 로고
    • Immunocytochemical localization of cellular retinol binding protein in the rat retina
    • Bok D, Ong DE, Chytil F. Immunocytochemical localization of cellular retinol binding protein in the rat retina. Invest Ophthalmol Vis Sci. 1984;25:877-883.
    • (1984) Invest Ophthalmol Vis Sci. , vol.25 , pp. 877-883
    • Bok, D.1    Ong, D.E.2    Chytil, F.3
  • 38
    • 0020551985 scopus 로고
    • Immunocytochemical localization of two retinoid-binding proteins in vertebrate retina
    • Bunt-Milam AH, Saari JC. Immunocytochemical localization of two retinoid-binding proteins in vertebrate retina. J Cell Biol. 1983;97:703-712.
    • (1983) J Cell Biol. , vol.97 , pp. 703-712
    • Bunt-Milam, A.H.1    Saari, J.C.2
  • 39
    • 0021733920 scopus 로고
    • Properties and immunocytochemical localization of three retinoid-binding proteins from bovine retina
    • Saari JC, Bunt-Milam AH, Bredberg DL, Garwin GG. Properties and immunocytochemical localization of three retinoid-binding proteins from bovine retina. Vision Res. 1984;24:1595-1603.
    • (1984) Vision Res. , vol.24 , pp. 1595-1603
    • Saari, J.C.1    Bunt-Milam, A.H.2    Bredberg, D.L.3    Garwin, G.G.4
  • 40
    • 0017903027 scopus 로고
    • Kinetics of bleaching and regeneration of rhodopsin in abnormal (RCS) and normal albino rats in vivo
    • Perlman I. Kinetics of bleaching and regeneration of rhodopsin in abnormal (RCS) and normal albino rats in vivo. J Physiol. 1978; 278:141-159.
    • (1978) J Physiol. , vol.278 , pp. 141-159
    • Perlman, I.1
  • 41
    • 0018096339 scopus 로고
    • Isolated retinas synthesize visual pigments from retinol congeners delivered by liposomes
    • Yoshikami S, Noll GN. Isolated retinas synthesize visual pigments from retinol congeners delivered by liposomes. Science. 1978; 200:1393-1395.
    • (1978) Science , vol.200 , pp. 1393-1395
    • Yoshikami, S.1    Noll, G.N.2
  • 42
    • 0032078364 scopus 로고    scopus 로고
    • Reduction of all-trans-retinal limits regeneration of visual pigment in mice
    • Saari JC, Garwin GG, Van Hooser JP, Palczewski K. Reduction of all-trans-retinal limits regeneration of visual pigment in mice. Vision Res. 1998;38:1325-1333.
    • (1998) Vision Res. , vol.38 , pp. 1325-1333
    • Saari, J.C.1    Garwin, G.G.2    Van Hooser, J.P.3    Palczewski, K.4
  • 46
    • 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 interphotoreceptor retinoid-binding protein or arrestin
    • Palczewski K, Van Hooser JP, Garwin GG, Saari JC. Kinetics of visual pigment regeneration in excised mouse eyes and in mice with a targeted disruption of the gene encoding interphotoreceptor retinoid-binding protein or arrestin. Biochemistry. 1999;39: 12012-12019.
    • (1999) Biochemistry , vol.39 , pp. 12012-12019
    • Palczewski, K.1    Van Hooser, J.P.2    Garwin, G.G.3    Saari, J.C.4
  • 47
    • 0000581885 scopus 로고
    • Retinene isomerase
    • Hubbard R. Retinene isomerase. J Gen Physiol. 1956;39:935-962.
    • (1956) J Gen Physiol. , vol.39 , pp. 935-962
    • Hubbard, R.1
  • 48
    • 0020579801 scopus 로고
    • Studies on the catalyzed interconversions of vitamin A derivatives
    • Rando RR, Chang A. Studies on the catalyzed interconversions of vitamin A derivatives. J Am Chem Soc. 1983;105:2879-2882.
    • (1983) J Am Chem Soc. , vol.105 , pp. 2879-2882
    • Rando, R.R.1    Chang, A.2
  • 49
    • 0024403617 scopus 로고
    • Membranes as the energy source in the endergonic transformation of vitamin A to 11-cis-retinol
    • Deigner PS, Law WC, Canada FJ, Rando RR. Membranes as the energy source in the endergonic transformation of vitamin A to 11-cis-retinol. Science. 1989;244:968-971.
    • (1989) Science , vol.244 , pp. 968-971
    • Deigner, P.S.1    Law, W.C.2    Canada, F.J.3    Rando, R.R.4
  • 50
    • 0001116929 scopus 로고
    • Effects of glucose and oxygen deprivation on function of isolated mammalian retina
    • Ames A III, Gurian BS. Effects of glucose and oxygen deprivation on function of isolated mammalian retina. J Neurophysiol. 1963; 26:617-634.
    • (1963) J Neurophysiol. , vol.26 , pp. 617-634
    • Ames A. III1    Gurian, B.S.2
  • 51
    • 0000760596 scopus 로고
    • The role of reduced triphosphopyridine nucleotide in the visual cycle
    • Futterman S. The role of reduced triphosphopyridine nucleotide in the visual cycle. J Biol Chem. 1963;238:1145-1150.
    • (1963) J Biol Chem. , vol.238 , pp. 1145-1150
    • Futterman, S.1
  • 52
    • 0016755760 scopus 로고
    • Biochemical aspects of the visual process, XXVII: Stereospecificity of ocular retinol dehydrogenases and the visual cycle
    • Lion F, Rotmans JP, Daemen FJM, Bonting SL. Biochemical aspects of the visual process, XXVII: Stereospecificity of ocular retinol dehydrogenases and the visual cycle. Biochim Biophys Acta. 1975;384:283-292.
    • (1975) Biochim Biophys Acta , vol.384 , pp. 283-292
    • Lion, F.1    Rotmans, J.P.2    Daemen, F.J.M.3    Bonting, S.L.4
  • 53
    • 0028834278 scopus 로고
    • Targeted disruption of the housekeeping gene encoding glucose 6-phosphate dehydrogenase (G6PD): G6PD is dispensable for pentose synthesis but essential for defense against oxidative stress
    • Pandolfi PP, Sonati F, Rivi R, Mason P, Grosveld F, Luzatto L. Targeted disruption of the housekeeping gene encoding glucose 6-phosphate dehydrogenase (G6PD): G6PD is dispensable for pentose synthesis but essential for defense against oxidative stress. EMBO J. 1995;14:5209-5215.
    • (1995) EMBO J. , vol.14 , pp. 5209-5215
    • Pandolfi, P.P.1    Sonati, F.2    Rivi, R.3    Mason, P.4    Grosveld, F.5    Luzatto, L.6
  • 55
    • 0032562785 scopus 로고    scopus 로고
    • Importance of glucose-6-phosphate dehydrogenase activity for cell growth
    • Tian W-N, Braunstaein LD, Pang J, et al. Importance of glucose-6-phosphate dehydrogenase activity for cell growth. J Biol Chem. 1998;273:10609-10617.
    • (1998) J Biol Chem. , vol.273 , pp. 10609-10617
    • Tian, W.-N.1    Braunstaein, L.D.2    Pang, J.3
  • 56
    • 0028234370 scopus 로고
    • Glucose metabolism in photoreceptor outer segments: Its role in phototransduction and in NADPH-requiring reactions
    • Hsu S-C, Molday RS. Glucose metabolism in photoreceptor outer segments: its role in phototransduction and in NADPH-requiring reactions. J Biol Chem. 1994;269:17954-17959.
    • (1994) J Biol Chem. , vol.269 , pp. 17954-17959
    • Hsu, S.-C.1    Molday, R.S.2
  • 57
    • 0014310043 scopus 로고
    • Quantitative histochemistry of nicotinamide adenine nucleotides in retina of monkey and rabbit
    • Matchinsky FM. Quantitative histochemistry of nicotinamide adenine nucleotides in retina of monkey and rabbit. J Neurochem. 1968;15:643-657.
    • (1968) J Neurochem. , vol.15 , pp. 643-657
    • Matchinsky, F.M.1
  • 58
    • 0023630905 scopus 로고
    • Real-time hexose monophosphate shunt activity in light- and dark-adapted rabbit retinas
    • Aguiar E, Cheng H-M, Lam DM-K. Real-time hexose monophosphate shunt activity in light- and dark-adapted rabbit retinas. Ophthalmic Res. 1987;19:290-302.
    • (1987) Ophthalmic Res. , vol.19 , pp. 290-302
    • Aguiar, E.1    Cheng, H.-M.2    Dm-K, L.3
  • 59
    • 0018187914 scopus 로고
    • Immunocytochemical localization of a large intrinsic membrane protein to the incisures and margins of frog rod outer segment disks
    • Papermaster DS, Schneider BG, Zorn MA, Kraehenbuhl JP. Immunocytochemical localization of a large intrinsic membrane protein to the incisures and margins of frog rod outer segment disks. J Cell Biol. 1978;78:415-425.
    • (1978) J Cell Biol. , vol.78 , pp. 415-425
    • Papermaster, D.S.1    Schneider, B.G.2    Zorn, M.A.3    Kraehenbuhl, J.P.4
  • 60
    • 0030969303 scopus 로고    scopus 로고
    • The 220-kDa rim protein of retinal rod outer segments is a member of the AHC transporter super-family
    • Illing M, Molday LL, Molday RS. The 220-kDa rim protein of retinal rod outer segments is a member of the AHC transporter super-family. J Biol Chem. 1997;272:10303-10310.
    • (1997) J Biol Chem. , vol.272 , pp. 10303-10310
    • Illing, M.1    Molday, L.L.2    Molday, R.S.3
  • 61
    • 0030861514 scopus 로고    scopus 로고
    • Photoreceptor rim protein: Partial sequences of cDNA show a high degree of similarity to ABC transporters
    • Thomson JL, Brzeski H, Dunbar B, et al. Photoreceptor rim protein: partial sequences of cDNA show a high degree of similarity to ABC transporters. Curr Eye Res. 1997;16:741-745.
    • (1997) Curr Eye Res. , vol.16 , pp. 741-745
    • Thomson, J.L.1    Brzeski, H.2    Dunbar, B.3
  • 62
    • 0024314805 scopus 로고
    • Lecithin:Retinol acyltransferase in retinal pigment epithelial microsomes
    • Saari JC, Bredberg DL. Lecithin:retinol acyltransferase in retinal pigment epithelial microsomes. J Biol Chem. 1989;264:8636-8640.
    • (1989) J Biol Chem. , vol.264 , pp. 8636-8640
    • Saari, J.C.1    Bredberg, D.L.2
  • 63
    • 0024311947 scopus 로고
    • Solubilization and partial purification of retinyl ester synthetase and retinoid isomerase from bovine ocular pigment epithelium
    • Barry RJ, Canada FJ, Rando RR. Solubilization and partial purification of retinyl ester synthetase and retinoid isomerase from bovine ocular pigment epithelium. J Biol Chem. 1989;264:9231-9238.
    • (1989) J Biol Chem. , vol.264 , pp. 9231-9238
    • Barry, R.J.1    Canada, F.J.2    Rando, R.R.3
  • 64
    • 0030955316 scopus 로고    scopus 로고
    • GTP-binding-coupled receptor kinases: Two mechanistic models
    • Palczewski K. GTP-binding-coupled receptor kinases: two mechanistic models. Eur J Biochem. 1997;248:261-269.
    • (1997) Eur J Biochem. , vol.248 , pp. 261-269
    • Palczewski, K.1
  • 65
    • 0027993328 scopus 로고
    • Structure and functions of arrestins
    • Palczewski K. Structure and functions of arrestins. Protein Sci. 1994;3:1355-1361.
    • (1994) Protein Sci. , vol.3 , pp. 1355-1361
    • Palczewski, K.1
  • 67
    • 0028138288 scopus 로고
    • Rod outer segment retinol dehydrogenase: Substrate specificity and role in phototransduction
    • Palczewski K, Jager S, Buczylko J, et al. Rod outer segment retinol dehydrogenase: substrate specificity and role in phototransduction. Biochemistry. 1994;33:13741-13750.
    • (1994) Biochemistry , vol.33 , pp. 13741-13750
    • Palczewski, K.1    Jager, S.2    Buczylko, J.3
  • 68
    • 0023665122 scopus 로고
    • Size and shape of bovine interphotoreceptor retinoid-binding protein by electron microscopy and hydrodynamic analysis
    • Adler AJ, Stafford III WF, Slayter HS. Size and shape of bovine interphotoreceptor retinoid-binding protein by electron microscopy and hydrodynamic analysis. J Biol Chem. 1987;262:13198-13203.
    • (1987) J Biol Chem. , vol.262 , pp. 13198-13203
    • Adler, A.J.1    Stafford W.F. III2    Slayter, H.S.3
  • 69
    • 0027371156 scopus 로고
    • Interactions of all-trans-retinol and long-chain fatty acids with interphotoreceptor retinoid-binding protein
    • Chen Y, Saari JC, Noy N. Interactions of all-trans-retinol and long-chain fatty acids with interphotoreceptor retinoid-binding protein. Biochemistry. 1993;32:11311-11318.
    • (1993) Biochemistry , vol.32 , pp. 11311-11318
    • Chen, Y.1    Saari, J.C.2    Noy, N.3
  • 70
    • 0019952202 scopus 로고
    • Interphotoreceptor retinol-binding proteins: Possible transport vehicles between compartments of the retina
    • Lai YL, Wiggert B, Liu YP, Chader GJ. Interphotoreceptor retinol-binding proteins: possible transport vehicles between compartments of the retina. Science. 1982;298:848-849.
    • (1982) Science , vol.298 , pp. 848-849
    • Lai, Y.L.1    Wiggert, B.2    Liu, Y.P.3    Chader, G.J.4
  • 71
    • 0021993673 scopus 로고
    • Properties of an interphotoreceptor retinoid-binding protein from bovine retina
    • Saari JC, Teller DC, Crabb JW, Bredberg D. Properties of an interphotoreceptor retinoid-binding protein from bovine retina. J Biol Chem. 1985;265:195-201.
    • (1985) J Biol Chem. , vol.265 , pp. 195-201
    • Saari, J.C.1    Teller, D.C.2    Crabb, J.W.3    Bredberg, D.4
  • 72
    • 0021230110 scopus 로고
    • Purification and characterization of a retinol-binding glycoprotein synthesized and secreted by bovine neural retina
    • Fong S-L, Liou GI, Landers RA, Alvarez RA, Bridges CD. Purification and characterization of a retinol-binding glycoprotein synthesized and secreted by bovine neural retina. J Biol Chem. 1984;259:6534-6542.
    • (1984) J Biol Chem. , vol.259 , pp. 6534-6542
    • Fong, S.-L.1    Liou, G.I.2    Landers, R.A.3    Alvarez, R.A.4    Bridges, C.D.5
  • 73
    • 0025861272 scopus 로고
    • Effect of light on endogenous ligands carried by interphotoreceptor retinoid-binding protein
    • Adler AJ, Spencer SA. Effect of light on endogenous ligands carried by interphotoreceptor retinoid-binding protein. Exp Eye Res. 1991;53:337-346.
    • (1991) Exp Eye Res. , vol.53 , pp. 337-346
    • Adler, A.J.1    Spencer, S.A.2
  • 74
    • 0021932157 scopus 로고
    • Zonulae adherentes pore size in the external limiting membrane of the rabbit retina
    • Bunt-Milam AH, Saari JC, Klock IH, Garwin GG. Zonulae adherentes pore size in the external limiting membrane of the rabbit retina. Invest Ophthalmol Vis Sci. 1985;26:1377-1380.
    • (1985) Invest Ophthalmol Vis Sci. , vol.26 , pp. 1377-1380
    • Bunt-Milam, A.H.1    Saari, J.C.2    Klock, I.H.3    Garwin, G.G.4
  • 75
    • 0021024604 scopus 로고
    • The presence of a soluble interphotoreceptor retinol-hinding protein (IRBP) in the retinal interphotoreceptor space
    • Pfeffer B, Wiggert B, Lee L, Zonnenberg B, Newsome D, Chader G. The presence of a soluble interphotoreceptor retinol-hinding protein (IRBP) in the retinal interphotoreceptor space. J Cell Physiol. 1983;117:333-341.
    • (1983) J Cell Physiol. , vol.117 , pp. 333-341
    • Pfeffer, B.1    Wiggert, B.2    Lee, L.3    Zonnenberg, B.4    Newsome, D.5    Chader, G.6
  • 76
    • 0032526453 scopus 로고    scopus 로고
    • Early onset photoreceptor abnormalities induced by targeted disruption of the interphotoreceptor retinoid-binding protein gene
    • Lion GI, Fei Y, Peachey NS, et al. Early onset photoreceptor abnormalities induced by targeted disruption of the interphotoreceptor retinoid-binding protein gene. J Neurosci. 1998;18: 4511-4520.
    • (1998) J Neurosci. , vol.18 , pp. 4511-4520
    • Lion, G.I.1    Fei, Y.2    Peachey, N.S.3
  • 77
    • 0026732864 scopus 로고
    • Promotion of release of 11-cis-retinal from cultured retinal pigment epithelium by interphotoreceptor retinoid-hinding protein
    • Carlson A, Bok D. Promotion of release of 11-cis-retinal from cultured retinal pigment epithelium by interphotoreceptor retinoid-hinding protein. Biochemistry. 1992;31:9056-9062.
    • (1992) Biochemistry , vol.31 , pp. 9056-9062
    • Carlson, A.1    Bok, D.2
  • 78
    • 0032920347 scopus 로고    scopus 로고
    • Polarity of 11-cis retinal release from cultured retinal pigment epithelium
    • Carlson A, Bok D. Polarity of 11-cis retinal release from cultured retinal pigment epithelium. Invest Ophthalmol Vis Sci. 1999;40: 533-537.
    • (1999) Invest Ophthalmol Vis Sci. , vol.40 , pp. 533-537
    • Carlson, A.1    Bok, D.2
  • 79
    • 0025175698 scopus 로고
    • Interphotoreceptor retinoid-binding protein promotes rhodopsin regeneration in toad photoreceptors
    • Okajima T-IL, Pepperberg DR, Ripps H, Wiggert B, Chader GJ. Interphotoreceptor retinoid-binding protein promotes rhodopsin regeneration in toad photoreceptors. Proc Natl Acad Sci USA. 1990;87:6907-6911.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 6907-6911
    • Okajima, T.-I.L.1    Pepperberg, D.R.2    Ripps, H.3    Wiggert, B.4    Chader, G.J.5
  • 80
    • 0021854447 scopus 로고
    • Molecular properties of bovine interphotoreceptor retinol-binding protein
    • Adler AJ, Evans CD, Stafford WF III. Molecular properties of bovine interphotoreceptor retinol-binding protein. J Biol Chem. 1985;260:4850-4855.
    • (1985) J Biol Chem. , vol.260 , pp. 4850-4855
    • Adler, A.J.1    Evans, C.D.2    Stafford W.F. III3
  • 81
    • 0021987736 scopus 로고
    • Isolation and characterization of monkey interphotoreceptor retinoid-binding protein, a unique extracellular matrix component of the retina
    • Redmond TM, Wiggert B, Robey FA, et al. Isolation and characterization of monkey interphotoreceptor retinoid-binding protein, a unique extracellular matrix component of the retina. Biochemistry. 1985;24:787-793.
    • (1985) Biochemistry , vol.24 , pp. 787-793
    • Redmond, T.M.1    Wiggert, B.2    Robey, F.A.3
  • 82
    • 0024494201 scopus 로고
    • Mechanism of vitamin a movement between rod outer segments, interphotoreceptor retinoid-binding protein, and liposomes
    • Ho M-TP, Massey JB, Pownall HJ, Anderson RE, Hollyfield JG. Mechanism of vitamin A movement between rod outer segments, interphotoreceptor retinoid-binding protein, and liposomes. J Biol Chem. 1989;264:928-935.
    • (1989) J Biol Chem. , vol.264 , pp. 928-935
    • Ho, M.-T.1    Massey, J.B.2    Pownall, H.J.3    Anderson, R.E.4    Hollyfield, J.G.5
  • 83
    • 0026901040 scopus 로고
    • Interphotoreceptor retinoid-binding protein and alpha-tocopherol preserve the isomeric and oxidation state of retinol
    • Crouch RK, Hazard ES, Lind T, Wiggert B, Chader G, Corson DW. Interphotoreceptor retinoid-binding protein and alpha-tocopherol preserve the isomeric and oxidation state of retinol. Photochem Photobiol. 1992;56:251-252.
    • (1992) Photochem Photobiol. , vol.56 , pp. 251-252
    • Crouch, R.K.1    Hazard, E.S.2    Lind, T.3    Wiggert, B.4    Chader, G.5    Corson, D.W.6
  • 84
    • 17344366357 scopus 로고    scopus 로고
    • Rpe65 is necessary for production of 11-cis-vitamin A in the retinal visual cycle
    • Redmond TM, Yu S, Lee E. et al. Rpe65 is necessary for production of 11-cis-vitamin A in the retinal visual cycle. Nat Gen. 1998;20:344-351.
    • (1998) Nat Gen. , vol.20 , pp. 344-351
    • Redmond, T.M.1    Yu, S.2    Lee, E.3
  • 85
    • 0030886657 scopus 로고    scopus 로고
    • Peropsin, a novel visual pigment-like protein located in the apical microvilli of the retinal pigment epithelium
    • Sun H, Gilbert DJ, Copeland NG, Jenkins NA, Nathans J. Peropsin, a novel visual pigment-like protein located in the apical microvilli of the retinal pigment epithelium. Proc Natl Acad Sci USA. 1997;94:9893-9898.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 9893-9898
    • Sun, H.1    Gilbert, D.J.2    Copeland, N.G.3    Jenkins, N.A.4    Nathans, J.5
  • 86
    • 0027944675 scopus 로고
    • A human opsin-related gene that encodes a retinaldehyde-binding protein
    • Shen D, Jiang M, Hao W, Tao L, Salazar M, Fong HKW. A human opsin-related gene that encodes a retinaldehyde-binding protein. Biochemistry. 1994;33:13117-13125.
    • (1994) Biochemistry , vol.33 , pp. 13117-13125
    • Shen, D.1    Jiang, M.2    Hao, W.3    Tao, L.4    Salazar, M.5    Fong, H.K.W.6
  • 87
    • 0031919154 scopus 로고    scopus 로고
    • Molecular mechanisms of prostaglandin transport
    • Schuster VL. Molecular mechanisms of prostaglandin transport. Annu Rev Physiol. 1998;60:221-242.
    • (1998) Annu Rev Physiol. , vol.60 , pp. 221-242
    • Schuster, V.L.1
  • 88
    • 0026775432 scopus 로고
    • Muller cells of chicken retina synthesize 11-cis-retinol
    • Das SR, Bhardwaj N, Kjeldbye H, Gouras P. Muller cells of chicken retina synthesize 11-cis-retinol. Biochem J. 1992;285: 907-913.
    • (1992) Biochem J. , vol.285 , pp. 907-913
    • Das, S.R.1    Bhardwaj, N.2    Kjeldbye, H.3    Gouras, P.4
  • 89
    • 0026592409 scopus 로고
    • Abnormal rod dark adaptation in autosomal dominant retinitis pigmentosa with proline-23-histidine rhodopsin mutation
    • Kemp CM, Jacobson SG, Roman AJ, Sung CH, Nathans J. Abnormal rod dark adaptation in autosomal dominant retinitis pigmentosa with proline-23-histidine rhodopsin mutation. Am J Ophthalmol. 1992;15:165-174.
    • (1992) Am J Ophthalmol. , vol.15 , pp. 165-174
    • Kemp, C.M.1    Jacobson, S.G.2    Roman, A.J.3    Sung, C.H.4    Nathans, J.5
  • 90
  • 92
    • 0029993990 scopus 로고    scopus 로고
    • Activating mutations of rhodopsin and other G protein-coupled receptors
    • Rao VR, Oprian DD. Activating mutations of rhodopsin and other G protein-coupled receptors. Annu Rev Biophys Biomol Struct. 1996;25:287-314.
    • (1996) Annu Rev Biophys Biomol Struct. , vol.25 , pp. 287-314
    • Rao, V.R.1    Oprian, D.D.2
  • 93
    • 0029902034 scopus 로고    scopus 로고
    • Missense mutation in the gene encoding the a subunit of rod transducin in the Nougaret form of congenital stationary night blindness
    • Dryja TP, Hahn LB, Reboul T, Arnaud B. Missense mutation in the gene encoding the a subunit of rod transducin in the Nougaret form of congenital stationary night blindness. Nat Gen. 1996;13: 358-360.
    • (1996) Nat Gen. , vol.13 , pp. 358-360
    • Dryja, T.P.1    Hahn, L.B.2    Reboul, T.3    Arnaud, B.4
  • 94
    • 0029067542 scopus 로고
    • A homozygous 1-base pair deletion in the arrestin gene is a frequent cause of Oguchi disease in Japanese
    • Fuchs S, Hakazawa M, Maw M, Tamai M, Oguchi Y, Gal A. A homozygous 1-base pair deletion in the arrestin gene is a frequent cause of Oguchi disease in Japanese. Nat Gen 1995; 10:360-362.
    • (1995) Nat Gen , vol.10 , pp. 360-362
    • Fuchs, S.1    Hakazawa, M.2    Maw, M.3    Tamai, M.4    Oguchi, Y.5    Gal, A.6
  • 95
    • 0031038950 scopus 로고    scopus 로고
    • Defects in the rhodopsin kinase gene in the Oguchi form of stationary night blindness
    • Yamamoto S, Sippel KC, Berson EL, Dryja TP. Defects in the rhodopsin kinase gene in the Oguchi form of stationary night blindness. Nat Gen. 1997;15:175-178.
    • (1997) Nat Gen. , vol.15 , pp. 175-178
    • Yamamoto, S.1    Sippel, K.C.2    Berson, E.L.3    Dryja, T.P.4
  • 96
    • 0031037951 scopus 로고    scopus 로고
    • A photoreceptor cell-specific ATP-binding transporter gene (ABCR) is mutated in recessive stargardt macular dystrophy
    • Allikmets R, Singh N, Sun H, et al. et al. A photoreceptor cell-specific ATP-binding transporter gene (ABCR) is mutated in recessive Stargardt macular dystrophy. Nat Genet. 1997;15:236-245.
    • (1997) Nat Genet. , vol.15 , pp. 236-245
    • Allikmets, R.1    Singh, N.2    Sun, H.3
  • 97
    • 0031255068 scopus 로고    scopus 로고
    • Mutations in RPE65 cause autosomal recessive childhood onset severe retinal dystrophy
    • Gu S-M, Thompson DA, Srisailapathy Srikumari CR, et al. Mutations in RPE65 cause autosomal recessive childhood onset severe retinal dystrophy. Nat Genet. 1997;17:194-197.
    • (1997) Nat Genet. , vol.17 , pp. 194-197
    • Gu, S.-M.1    Thompson, D.A.2    Srisailapathy Srikumari, C.R.3
  • 98
    • 0031252434 scopus 로고    scopus 로고
    • Mutations in RPE65 cause Leber's congenital amaurosis
    • Marlhens F, Bareil C, Griffoin J-M, et al. Mutations in RPE65 cause Leber's congenital amaurosis. Nat Genet. 1997;17:139-141.
    • (1997) Nat Genet. , vol.17 , pp. 139-141
    • Marlhens, F.1    Bareil, C.2    Griffoin, J.-M.3
  • 99
    • 0033033364 scopus 로고    scopus 로고
    • Mutations in the gene encoding 11-cis-retinol dehydrogenase (RDH1) in patients with fundus albipunctatus
    • Yamamoto H., Simon A, Eriksson U, Harris E, Berson EL, and Dryja TP. Mutations in the gene encoding 11-cis-retinol dehydrogenase (RDH1) in patients with fundus albipunctatus. Nature Genetics. 1999;22:188-191.
    • (1999) Nature Genetics , vol.22 , pp. 188-191
    • Yamamoto, H.1    Simon, A.2    Eriksson, U.3    Harris, E.4    Berson, E.L.5    Dryja, T.P.6
  • 100
    • 0000932112 scopus 로고
    • Abnormalities of cone and rod function
    • Ryan SJ, Ogden TE, Shachat AP, eds. St Louis: Mosby
    • Carr RE. Abnormalities of cone and rod function. In: Ryan SJ, Ogden TE, Shachat AP, eds. Retina. 2nd ed. Vol 1. St Louis: Mosby; 1994:502-514.
    • (1994) Retina. 2nd Ed. , vol.1 , pp. 502-514
    • Carr, R.E.1
  • 101
    • 0000055594 scopus 로고
    • Rhodopsin kinetics and rod adaptation in Oguchi's disease
    • Carr RE, Ripps H. Rhodopsin kinetics and rod adaptation in Oguchi's disease. Invest Ophthalmol Vis Sci. 1967;6:426-436.
    • (1967) Invest Ophthalmol Vis Sci. , vol.6 , pp. 426-436
    • Carr, R.E.1    Ripps, H.2
  • 102
    • 0020384571 scopus 로고
    • Night blindness revisited: From man to molecules
    • Ripps H. Night blindness revisited: from man to molecules. Invest Ophthalmol Vis Sci. 1982;23:588-609.
    • (1982) Invest Ophthalmol Vis Sci. , vol.23 , pp. 588-609
    • Ripps, H.1
  • 103
    • 0023644934 scopus 로고
    • Photochemistry and stereoselectivity of cellular retinaldehyde-binding protein from bovine retina
    • Saari JC, Bredberg DL. Photochemistry and stereoselectivity of cellular retinaldehyde-binding protein from bovine retina. J Biol Chem. 1987;262:7618-7622.
    • (1987) J Biol Chem. , vol.262 , pp. 7618-7622
    • Saari, J.C.1    Bredberg, D.L.2
  • 104
    • 0020416139 scopus 로고
    • Identification of the endogenous retinoids associated with three cellular retinoid-binding proteins from bovine retina and retinal pigment epithelium
    • Saari JC, Bredberg L, Garwin GG. Identification of the endogenous retinoids associated with three cellular retinoid-binding proteins from bovine retina and retinal pigment epithelium. J Biol Chem. 1982;257:13329-13333.
    • (1982) J Biol Chem. , vol.257 , pp. 13329-13333
    • Saari, J.C.1    Bredberg, L.2    Garwin, G.G.3
  • 105
    • 0028211275 scopus 로고
    • Control of substrate flow at a branch in the visual cycle
    • Saari JC, Bredberg DL, Noy N. Control of substrate flow at a branch in the visual cycle. Biochemistry. 1994;33:3106-3112.
    • (1994) Biochemistry , vol.33 , pp. 3106-3112
    • Saari, J.C.1    Bredberg, D.L.2    Noy, N.3
  • 106
    • 0033605656 scopus 로고    scopus 로고
    • Preferential release of 11-cis-retinol from retinal pigment epithelial cells in the presence of cellular retinaldehyde-binding protein
    • Stecher H, Gelb MH, Saari JC, Palczewski K. Preferential release of 11-cis-retinol from retinal pigment epithelial cells in the presence of cellular retinaldehyde-binding protein. J Biol Chem. 1999;274:8577-8585.
    • (1999) J Biol Chem. , vol.274 , pp. 8577-8585
    • Stecher, H.1    Gelb, M.H.2    Saari, J.C.3    Palczewski, K.4
  • 107
    • 0032539650 scopus 로고    scopus 로고
    • Regulation of isomerohydrolase activity in the visual cycle
    • Winston AE, Rando RR. Regulation of isomerohydrolase activity in the visual cycle. Biochemistry. 1998;37:2044-2050.
    • (1998) Biochemistry , vol.37 , pp. 2044-2050
    • Winston, A.E.1    Rando, R.R.2
  • 108
    • 17144439473 scopus 로고    scopus 로고
    • Molecular characterization of the mouse gene encoding cellular retinaldehyde-binding protein
    • Kennedy BN, Huang J, Saari JC, Crabb JW. Molecular characterization of the mouse gene encoding cellular retinaldehyde-binding protein. Mol Vis. 1998;4:14-21.
    • (1998) Mol Vis. , vol.4 , pp. 14-21
    • Kennedy, B.N.1    Huang, J.2    Saari, J.C.3    Crabb, J.W.4
  • 109
    • 84984763750 scopus 로고    scopus 로고
    • Mutation of the gene encoding cellular retinaldehyde-binding protein in autosomal recessive retinitis pigmentosa
    • Maw, MA, Kennedy B, Knight A, et al. Mutation of the gene encoding cellular retinaldehyde-binding protein in autosomal recessive retinitis pigmentosa. Nat Gen. 1997;17:198-200.
    • (1997) Nat Gen. , vol.17 , pp. 198-200
    • Maw, M.A.1    Kennedy, B.2    Knight, A.3
  • 110
    • 0033066801 scopus 로고    scopus 로고
    • Recessive mutations in the RLBP1 gene encoding cellular retinaldehyde-binding protein in a form of retinitis punctata albescens
    • Morimura H, Berson EL, Dryja TP. Recessive mutations in the RLBP1 gene encoding cellular retinaldehyde-binding protein in a form of retinitis punctata albescens. Invest Ophthalmot Vis Sci. 1999;40:1000-1004.
    • (1999) Invest Ophthalmot Vis Sci. , vol.40 , pp. 1000-1004
    • Morimura, H.1    Berson, E.L.2    Dryja, T.P.3
  • 111
    • 0033066974 scopus 로고    scopus 로고
    • Bothnia dystrophy caused by mutations in the cellular retinaldehyde-binding protein gene (RLBP1) on chromosome 15q26
    • Burstedl MSI, Sandgren O, Holmgren G, Forsman-Semb K. Bothnia dystrophy caused by mutations in the cellular retinaldehyde-binding protein gene (RLBP1) on chromosome 15q26. Invest Ophthalmol Vis Sci. 1999;40:995-1000.
    • (1999) Invest Ophthalmol Vis Sci. , vol.40 , pp. 995-1000
    • Burstedl, M.S.I.1    Sandgren, O.2    Holmgren, G.3    Forsman-Semb, K.4
  • 113
    • 0024357993 scopus 로고
    • Retinoid requirements for recovery of sensitivity after visual-pigment bleaching in isolated photoreceptors
    • Jones GJ, Crouch RK, Wiggert B, Cornwall MC, Chader GJ. Retinoid requirements for recovery of sensitivity after visual-pigment bleaching in isolated photoreceptors. Proc Natl Acad Sci USA. 1989;86:9606-9610.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 9606-9610
    • Jones, G.J.1    Crouch, R.K.2    Wiggert, B.3    Cornwall, M.C.4    Chader, G.J.5
  • 114
    • 0014151041 scopus 로고
    • Early receptor potential of the isolated frog (Rana pipiens) retina
    • Goldstein EB. Early receptor potential of the isolated frog (Rana pipiens) retina. Vision Res. 1967;7:837-845.
    • (1967) Vision Res. , vol.7 , pp. 837-845
    • Goldstein, E.B.1
  • 115
    • 0014860056 scopus 로고
    • Cone pigment regeneration in the isolated frog retina
    • Goldstein EB. Cone pigment regeneration in the isolated frog retina. Vision Res. 1970;10:1065-1068.
    • (1970) Vision Res. , vol.10 , pp. 1065-1068
    • Goldstein, E.B.1
  • 116
    • 0015597662 scopus 로고
    • Regeneration of the green-rod pigment in the isolated frog retina
    • Goldstein EB, Wolf BM. Regeneration of the green-rod pigment in the isolated frog retina. Vision Res. 1973;13:527-534.
    • (1973) Vision Res. , vol.13 , pp. 527-534
    • Goldstein, E.B.1    Wolf, B.M.2
  • 117
    • 0008933274 scopus 로고
    • Early receptor potential of the vertebrate eye
    • Cone RA. Early receptor potential of the vertebrate eye. Nature. 1964;204:736-739.
    • (1964) Nature , vol.204 , pp. 736-739
    • Cone, R.A.1
  • 118
    • 0014481894 scopus 로고
    • Rhodopsin cycle in the living eye of the rat
    • Cone RA, Cobbs WH III. Rhodopsin cycle in the living eye of the rat. Nature. 1969;221:820-822.
    • (1969) Nature , vol.221 , pp. 820-822
    • Cone, R.A.1    Cobbs W.H. III2


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