메뉴 건너뛰기




Volumn 85, Issue 2, 2007, Pages 175-184

A novel cone visual cycle in the cone-dominated retina

Author keywords

cone photoreceptors; cone visual cycle; M ller cell; retina; retinal pigment epithelium

Indexed keywords

RHODOPSIN;

EID: 34447625400     PISSN: 00144835     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.exer.2007.05.003     Document Type: Review
Times cited : (53)

References (101)
  • 1
    • 0020063497 scopus 로고
    • Proteins and glycoproteins of the bovine interphotoreceptor matrix: composition and fractionation
    • Adler A.J., and Klucznik K.M. Proteins and glycoproteins of the bovine interphotoreceptor matrix: composition and fractionation. Exp. Eye Res. 34 3 (1982) 423-434
    • (1982) Exp. Eye Res. , vol.34 , Issue.3 , pp. 423-434
    • Adler, A.J.1    Klucznik, K.M.2
  • 2
    • 0023088725 scopus 로고
    • Hydrolysis of 11-cis- and all-trans-retinyl palmitate by homogenates of human retinal epithelial cells
    • Blaner W.S., Das S.R., et al. Hydrolysis of 11-cis- and all-trans-retinyl palmitate by homogenates of human retinal epithelial cells. J. Biol. Chem. 262 1 (1987) 53-58
    • (1987) J. Biol. Chem. , vol.262 , Issue.1 , pp. 53-58
    • Blaner, W.S.1    Das, S.R.2
  • 3
    • 0022344155 scopus 로고
    • Retinal photoreceptor-pigment epithelium interactions. Friedenwald lecture
    • Bok D. Retinal photoreceptor-pigment epithelium interactions. Friedenwald lecture. Invest. Ophthalmol. Vis. Sci. 26 12 (1985) 1659-1694
    • (1985) Invest. Ophthalmol. Vis. Sci. , vol.26 , Issue.12 , pp. 1659-1694
    • Bok, D.1
  • 4
    • 0021232986 scopus 로고
    • Immunocytochemical localization of cellular retinol binding protein in the rat retina
    • Bok D., Ong D.E., et al. Immunocytochemical localization of cellular retinol binding protein in the rat retina. Invest. Ophthalmol. Vis. Sci. 25 8 (1984) 877-883
    • (1984) Invest. Ophthalmol. Vis. Sci. , vol.25 , Issue.8 , pp. 877-883
    • Bok, D.1    Ong, D.E.2
  • 5
    • 0023113890 scopus 로고
    • Rhodopsin, vitamin A, and interstitial retinol-binding protein in the rd chicken
    • Bridges C.D., Alvarez R.A., et al. Rhodopsin, vitamin A, and interstitial retinol-binding protein in the rd chicken. Invest. Ophthalmol. Vis. Sci. 28 4 (1987) 613-617
    • (1987) Invest. Ophthalmol. Vis. Sci. , vol.28 , Issue.4 , pp. 613-617
    • Bridges, C.D.1    Alvarez, R.A.2
  • 6
    • 0020551985 scopus 로고
    • Immunocytochemical localization of two retinoid-binding proteins in vertebrate retina
    • Bunt-Milam A.H., and Saari J.C. Immunocytochemical localization of two retinoid-binding proteins in vertebrate retina. J. Cell Biol. 97 3 (1983) 703-712
    • (1983) J. Cell Biol. , vol.97 , Issue.3 , pp. 703-712
    • Bunt-Milam, A.H.1    Saari, J.C.2
  • 7
    • 0029587602 scopus 로고
    • Retinyl ester hydrolase and the visual cycle in the chicken eye
    • Bustamante J.J., Ziari S., et al. Retinyl ester hydrolase and the visual cycle in the chicken eye. Am. J. Physiol. 269 6 Pt 2 (1995) R1346-R1350
    • (1995) Am. J. Physiol. , vol.269 , Issue.6 PART 2
    • Bustamante, J.J.1    Ziari, S.2
  • 8
    • 0029920657 scopus 로고    scopus 로고
    • Localization of the human RGR opsin gene to chromosome 10q23
    • Chen X.N., Korenberg J.R., et al. Localization of the human RGR opsin gene to chromosome 10q23. Hum. Genet. 97 6 (1996) 720-722
    • (1996) Hum. Genet. , vol.97 , Issue.6 , pp. 720-722
    • Chen, X.N.1    Korenberg, J.R.2
  • 9
    • 0035877644 scopus 로고    scopus 로고
    • Interaction of 11-cis-retinol dehydrogenase with the chromophore of retinal g protein-coupled receptor opsin
    • Chen P., Lee T.D., et al. Interaction of 11-cis-retinol dehydrogenase with the chromophore of retinal g protein-coupled receptor opsin. J. Biol. Chem. 276 24 (2001) 21098-21104
    • (2001) J. Biol. Chem. , vol.276 , Issue.24 , pp. 21098-21104
    • Chen, P.1    Lee, T.D.2
  • 10
    • 0034502813 scopus 로고    scopus 로고
    • Rod and cone visual cycle consequences of a null mutation in the 11-cis-retinol dehydrogenase gene in man
    • Cideciyan A.V., Haeseleer F., et al. Rod and cone visual cycle consequences of a null mutation in the 11-cis-retinol dehydrogenase gene in man. Vis. Neurosci. 17 5 (2000) 667-678
    • (2000) Vis. Neurosci. , vol.17 , Issue.5 , pp. 667-678
    • Cideciyan, A.V.1    Haeseleer, F.2
  • 11
    • 0030266978 scopus 로고    scopus 로고
    • Retinoids and the visual process
    • Crouch R.K., Chader G.J., et al. Retinoids and the visual process. Photochem. Photobiol. 64 4 (1996) 613-621
    • (1996) Photochem. Photobiol. , vol.64 , Issue.4 , pp. 613-621
    • Crouch, R.K.1    Chader, G.J.2
  • 12
    • 0026901040 scopus 로고
    • Interphotoreceptor retinoid-binding protein and alpha-tocopherol preserve the isomeric and oxidation state of retinol
    • Crouch R.K., Hazard E.S., et al. Interphotoreceptor retinoid-binding protein and alpha-tocopherol preserve the isomeric and oxidation state of retinol. Photochem. Photobiol. 56 2 (1992) 251-255
    • (1992) Photochem. Photobiol. , vol.56 , Issue.2 , pp. 251-255
    • Crouch, R.K.1    Hazard, E.S.2
  • 13
    • 0026775432 scopus 로고
    • Muller cells of chicken retina synthesize 11-cis-retinol
    • Das S.R., Bhardwaj N., et al. Muller cells of chicken retina synthesize 11-cis-retinol. Biochem. J. 285 Pt 3 (1992) 907-913
    • (1992) Biochem. J. , vol.285 , Issue.PART 3 , pp. 907-913
    • Das, S.R.1    Bhardwaj, N.2
  • 14
    • 0001433667 scopus 로고
    • Chemistry of visual adaptation in the rat
    • Dowling J.E. Chemistry of visual adaptation in the rat. Nature (London) 188 (1960) 114-118
    • (1960) Nature (London) , vol.188 , pp. 114-118
    • Dowling, J.E.1
  • 15
    • 0029094231 scopus 로고
    • Cloning and expression of a cDNA encoding bovine retinal pigment epithelial 11-cis retinol dehydrogenase
    • Driessen C.A., Janssen B.P., et al. Cloning and expression of a cDNA encoding bovine retinal pigment epithelial 11-cis retinol dehydrogenase. Invest. Ophthalmol. Vis. Sci. 36 10 (1995) 1988-1996
    • (1995) Invest. Ophthalmol. Vis. Sci. , vol.36 , Issue.10 , pp. 1988-1996
    • Driessen, C.A.1    Janssen, B.P.2
  • 16
    • 0030703172 scopus 로고    scopus 로고
    • Cloning and structural analysis of the murine GCN5L1 gene
    • Driessen C.A., Winkens H.J., et al. Cloning and structural analysis of the murine GCN5L1 gene. Gene 203 1 (1997) 27-31
    • (1997) Gene , vol.203 , Issue.1 , pp. 27-31
    • Driessen, C.A.1    Winkens, H.J.2
  • 17
    • 0022394395 scopus 로고
    • Localization of retinoid-binding proteins in developing rat retina
    • Eisenfeld A.J., Bunt-Milam A.H., et al. Localization of retinoid-binding proteins in developing rat retina. Exp. Eye Res. 41 3 (1985) 299-304
    • (1985) Exp. Eye Res. , vol.41 , Issue.3 , pp. 299-304
    • Eisenfeld, A.J.1    Bunt-Milam, A.H.2
  • 18
    • 0344392142 scopus 로고    scopus 로고
    • Isorhodopsin rather than rhodopsin mediates rod function in RPE65 knock-out mice
    • Fan J., Rohrer B., et al. Isorhodopsin rather than rhodopsin mediates rod function in RPE65 knock-out mice. Proc. Natl. Acad. Sci. U.S.A. 100 23 (2003) 13662-13667
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , Issue.23 , pp. 13662-13667
    • Fan, J.1    Rohrer, B.2
  • 19
    • 0025635793 scopus 로고
    • Interstitial retinol-binding protein: purification, characterization, molecular cloning, and sequence
    • Fong S.L., and Bridges C.D. Interstitial retinol-binding protein: purification, characterization, molecular cloning, and sequence. Methods Enzymol. 189 (1990) 207-213
    • (1990) Methods Enzymol. , vol.189 , pp. 207-213
    • Fong, S.L.1    Bridges, C.D.2
  • 20
    • 0017638288 scopus 로고
    • Occurrence of 11-cis-retinal-binding protein restricted to the retina
    • Futterman S., and Saari J.C. Occurrence of 11-cis-retinal-binding protein restricted to the retina. Invest. Ophthalmol. Vis. Sci. 16 8 (1977) 768-771
    • (1977) Invest. Ophthalmol. Vis. Sci. , vol.16 , Issue.8 , pp. 768-771
    • Futterman, S.1    Saari, J.C.2
  • 21
    • 0017398399 scopus 로고
    • Occurrence of a binding protein for 11-cis-retinal in retina
    • Futterman S., Saari J.C., et al. Occurrence of a binding protein for 11-cis-retinal in retina. J. Biol. Chem. 252 10 (1977) 3267-3271
    • (1977) J. Biol. Chem. , vol.252 , Issue.10 , pp. 3267-3271
    • Futterman, S.1    Saari, J.C.2
  • 22
    • 0033988472 scopus 로고    scopus 로고
    • Substrate specificities and 13-cis-retinoic acid inhibition of human, mouse and bovine cis-retinol dehydrogenases
    • Gamble M.V., Mata N.L., et al. Substrate specificities and 13-cis-retinoic acid inhibition of human, mouse and bovine cis-retinol dehydrogenases. Biochim. Biophys. Acta 1476 1 (2000) 3-8
    • (2000) Biochim. Biophys. Acta , vol.1476 , Issue.1 , pp. 3-8
    • Gamble, M.V.1    Mata, N.L.2
  • 23
    • 0014151041 scopus 로고
    • Early receptor potential of the isolated frog (Rana pipiens) retina
    • Goldstein E.B. Early receptor potential of the isolated frog (Rana pipiens) retina. Vis. Res. 7 11 (1967) 837-845
    • (1967) Vis. Res. , vol.7 , Issue.11 , pp. 837-845
    • Goldstein, E.B.1
  • 24
    • 0014318098 scopus 로고
    • Visual pigments and the early receptor potential of the isolated frog retina
    • Goldstein E.B. Visual pigments and the early receptor potential of the isolated frog retina. Vis. Res. 8 8 (1968) 953-963
    • (1968) Vis. Res. , vol.8 , Issue.8 , pp. 953-963
    • Goldstein, E.B.1
  • 25
    • 0015597662 scopus 로고
    • Regeneration of the green-rod pigment in the isolated frog retina
    • Goldstein E.B., and Wolf B.M. Regeneration of the green-rod pigment in the isolated frog retina. Vis. Res. 13 3 (1973) 527-534
    • (1973) Vis. Res. , vol.13 , Issue.3 , pp. 527-534
    • Goldstein, E.B.1    Wolf, B.M.2
  • 26
    • 0038629063 scopus 로고    scopus 로고
    • All-trans-retinyl esters are the substrates for isomerization in the vertebrate visual cycle
    • Gollapalli D.R., and Rando R.R. All-trans-retinyl esters are the substrates for isomerization in the vertebrate visual cycle. Biochemistry 42 19 (2003) 5809-5818
    • (2003) Biochemistry , vol.42 , Issue.19 , pp. 5809-5818
    • Gollapalli, D.R.1    Rando, R.R.2
  • 27
    • 0346995020 scopus 로고    scopus 로고
    • Molecular logic of 11-cis-retinoid biosynthesis in a cone-dominated species
    • Gollapalli D.R., and Rando R.R. Molecular logic of 11-cis-retinoid biosynthesis in a cone-dominated species. Biochemistry 42 50 (2003) 14921-14929
    • (2003) Biochemistry , vol.42 , Issue.50 , pp. 14921-14929
    • Gollapalli, D.R.1    Rando, R.R.2
  • 28
    • 0019222685 scopus 로고
    • Quantitative determination of retinals with complete retention of their geometric configuration
    • Groenendijk G.W., De Grip W.J., et al. Quantitative determination of retinals with complete retention of their geometric configuration. Biochim. Biophys. Acta 617 3 (1980) 430-438
    • (1980) Biochim. Biophys. Acta , vol.617 , Issue.3 , pp. 430-438
    • Groenendijk, G.W.1    De Grip, W.J.2
  • 29
    • 0032555517 scopus 로고    scopus 로고
    • Molecular characterization of a novel short-chain dehydrogenase/reductase that reduces all-trans-retinal
    • Haeseleer F., Huang J., et al. Molecular characterization of a novel short-chain dehydrogenase/reductase that reduces all-trans-retinal. J. Biol. Chem. 273 34 (1998) 21790-21799
    • (1998) J. Biol. Chem. , vol.273 , Issue.34 , pp. 21790-21799
    • Haeseleer, F.1    Huang, J.2
  • 30
    • 0034055306 scopus 로고    scopus 로고
    • Analysis of chromophore of RGR: retinal G-protein-coupled receptor from pigment epithelium
    • Hao W., Chen P., et al. Analysis of chromophore of RGR: retinal G-protein-coupled receptor from pigment epithelium. Methods Enzymol. 316 (2000) 413-422
    • (2000) Methods Enzymol. , vol.316 , pp. 413-422
    • Hao, W.1    Chen, P.2
  • 31
    • 0024494201 scopus 로고
    • Mechanism of vitamin A movement between rod outer segments, interphotoreceptor retinoid-binding protein, and liposomes
    • Ho M.T., Massey J.B., et al. Mechanism of vitamin A movement between rod outer segments, interphotoreceptor retinoid-binding protein, and liposomes. J. Biol. Chem. 264 2 (1989) 928-935
    • (1989) J. Biol. Chem. , vol.264 , Issue.2 , pp. 928-935
    • Ho, M.T.1    Massey, J.B.2
  • 32
    • 0015793631 scopus 로고
    • Recovery of cone receptor activity in the frog's isolated retina
    • Hood D.C., and Hock P.A. Recovery of cone receptor activity in the frog's isolated retina. Vis. Res. 13 10 (1973) 1943-1951
    • (1973) Vis. Res. , vol.13 , Issue.10 , pp. 1943-1951
    • Hood, D.C.1    Hock, P.A.2
  • 33
    • 0034623239 scopus 로고    scopus 로고
    • Stereoisomeric specificity of the retinoid cycle in the vertebrate retina
    • Jang G.F., McBee J.K., et al. Stereoisomeric specificity of the retinoid cycle in the vertebrate retina. J. Biol. Chem. 275 36 (2000) 28128-28138
    • (2000) J. Biol. Chem. , vol.275 , Issue.36 , pp. 28128-28138
    • Jang, G.F.1    McBee, J.K.2
  • 34
    • 0027756089 scopus 로고
    • An opsin homologue in the retina and pigment epithelium
    • Jiang M., Pandey S., et al. An opsin homologue in the retina and pigment epithelium. Invest. Ophthalmol. Vis. Sci. 34 13 (1993) 3669-3678
    • (1993) Invest. Ophthalmol. Vis. Sci. , vol.34 , Issue.13 , pp. 3669-3678
    • Jiang, M.1    Pandey, S.2
  • 35
    • 0028387340 scopus 로고
    • Movement of retinal along cone and rod photoreceptors
    • Jin J., Jones G.J., et al. Movement of retinal along cone and rod photoreceptors. Vis. Neurosci. 11 2 (1994) 389-399
    • (1994) Vis. Neurosci. , vol.11 , Issue.2 , pp. 389-399
    • Jin, J.1    Jones, G.J.2
  • 36
    • 23744447355 scopus 로고    scopus 로고
    • Rpe65 is the retinoid isomerase in bovine retinal pigment epithelium
    • Jin M., Li S., et al. Rpe65 is the retinoid isomerase in bovine retinal pigment epithelium. Cell 122 3 (2005) 449-459
    • (2005) Cell , vol.122 , Issue.3 , pp. 449-459
    • Jin, M.1    Li, S.2
  • 37
    • 0024357993 scopus 로고
    • Retinoid requirements for recovery of sensitivity after visual-pigment bleaching in isolated photoreceptors
    • Jones G.J., Crouch R.K., et al. Retinoid requirements for recovery of sensitivity after visual-pigment bleaching in isolated photoreceptors. Proc. Natl. Acad. Sci. U.S.A. 86 23 (1989) 9606-9610
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , Issue.23 , pp. 9606-9610
    • Jones, G.J.1    Crouch, R.K.2
  • 38
    • 15744363978 scopus 로고    scopus 로고
    • Delayed dark adaptation in 11-cis-retinol dehydrogenase-deficient mice: a role of RDH11 in visual processes in vivo
    • Kim T.S., Maeda A., et al. Delayed dark adaptation in 11-cis-retinol dehydrogenase-deficient mice: a role of RDH11 in visual processes in vivo. J. Biol. Chem. 280 10 (2005) 8694-8704
    • (2005) J. Biol. Chem. , vol.280 , Issue.10 , pp. 8694-8704
    • Kim, T.S.1    Maeda, A.2
  • 39
    • 33846202529 scopus 로고    scopus 로고
    • Visual cycle and its metabolic support in gecko photoreceptors
    • Kolesnikov A.V., Ala-Laurila P., et al. Visual cycle and its metabolic support in gecko photoreceptors. Vis. Res. 47 3 (2007) 363-374
    • (2007) Vis. Res. , vol.47 , Issue.3 , pp. 363-374
    • Kolesnikov, A.V.1    Ala-Laurila, P.2
  • 40
    • 0019952202 scopus 로고
    • Interphotoreceptor retinol-binding proteins: possible transport vehicles between compartments of the retina
    • Lai Y.L., Wiggert B., et al. Interphotoreceptor retinol-binding proteins: possible transport vehicles between compartments of the retina. Nature 298 5877 (1982) 848-849
    • (1982) Nature , vol.298 , Issue.5877 , pp. 848-849
    • Lai, Y.L.1    Wiggert, B.2
  • 41
    • 2942617209 scopus 로고    scopus 로고
    • Dark adaptation and the retinoid cycle of vision
    • Lamb T.D., and Pugh Jr. E.N. Dark adaptation and the retinoid cycle of vision. Prog. Retin. Eye Res. 23 3 (2004) 307-380
    • (2004) Prog. Retin. Eye Res. , vol.23 , Issue.3 , pp. 307-380
    • Lamb, T.D.1    Pugh Jr., E.N.2
  • 42
    • 0016755760 scopus 로고
    • Biochemical aspects of the visual process. XXVII. Stereospecificity of ocular retinol dehydrogenases and the visual cycle
    • Lion F., Rotmans J.P., et al. Biochemical aspects of the visual process. XXVII. Stereospecificity of ocular retinol dehydrogenases and the visual cycle. Biochim. Biophys. Acta 384 2 (1975) 283-292
    • (1975) Biochim. Biophys. Acta , vol.384 , Issue.2 , pp. 283-292
    • Lion, F.1    Rotmans, J.P.2
  • 43
    • 0024334087 scopus 로고
    • Human interstitial retinoid-binding protein. Gene structure and primary structure
    • Liou G.I., Ma D.P., et al. Human interstitial retinoid-binding protein. Gene structure and primary structure. J. Biol. Chem. 264 14 (1989) 8200-8206
    • (1989) J. Biol. Chem. , vol.264 , Issue.14 , pp. 8200-8206
    • Liou, G.I.1    Ma, D.P.2
  • 44
    • 0031976032 scopus 로고    scopus 로고
    • Visual sensitivity and interphotoreceptor retinoid binding protein in the mouse: regulation by vitamin A
    • Liou G.I., Matragoon S., et al. Visual sensitivity and interphotoreceptor retinoid binding protein in the mouse: regulation by vitamin A. Faseb J. 12 1 (1998) 129-138
    • (1998) Faseb J. , vol.12 , Issue.1 , pp. 129-138
    • Liou, G.I.1    Matragoon, S.2
  • 45
    • 33645552900 scopus 로고    scopus 로고
    • Aberrant metabolites in mouse models of congenital blinding diseases: formation and storage of retinyl esters
    • Maeda A., Maeda T., et al. Aberrant metabolites in mouse models of congenital blinding diseases: formation and storage of retinyl esters. Biochemistry 45 13 (2006) 4210-4219
    • (2006) Biochemistry , vol.45 , Issue.13 , pp. 4210-4219
    • Maeda, A.1    Maeda, T.2
  • 46
    • 0037911521 scopus 로고    scopus 로고
    • Evaluation of the role of the retinal G protein-coupled receptor (RGR) in the vertebrate retina in vivo
    • Maeda T., Van Hooser J.P., et al. Evaluation of the role of the retinal G protein-coupled receptor (RGR) in the vertebrate retina in vivo. J. Neurochem. 85 4 (2003) 944-956
    • (2003) J. Neurochem. , vol.85 , Issue.4 , pp. 944-956
    • Maeda, T.1    Van Hooser, J.P.2
  • 47
    • 0029796051 scopus 로고    scopus 로고
    • Comparison of retinyl ester hydrolase activities in bovine liver and retinal pigment epithelium
    • Mata N.L., Mata J.R., et al. Comparison of retinyl ester hydrolase activities in bovine liver and retinal pigment epithelium. J. Lipid Res. 37 9 (1996) 1947-1952
    • (1996) J. Lipid Res. , vol.37 , Issue.9 , pp. 1947-1952
    • Mata, N.L.1    Mata, J.R.2
  • 48
    • 0031897043 scopus 로고    scopus 로고
    • Substrate specificity of retinyl ester hydrolase activity in retinal pigment epithelium
    • Mata J.R., Mata N.L., et al. Substrate specificity of retinyl ester hydrolase activity in retinal pigment epithelium. J. Lipid Res. 39 3 (1998) 604-612
    • (1998) J. Lipid Res. , vol.39 , Issue.3 , pp. 604-612
    • Mata, J.R.1    Mata, N.L.2
  • 49
    • 0037179792 scopus 로고    scopus 로고
    • Isomerization and oxidation of vitamin A in cone-dominant retinas: a novel pathway for visual-pigment regeneration in daylight
    • Mata N.L., Radu R.A., et al. Isomerization and oxidation of vitamin A in cone-dominant retinas: a novel pathway for visual-pigment regeneration in daylight. Neuron 36 1 (2002) 69-80
    • (2002) Neuron , vol.36 , Issue.1 , pp. 69-80
    • Mata, N.L.1    Radu, R.A.2
  • 50
    • 24344470086 scopus 로고    scopus 로고
    • Chicken retinas contain a retinoid isomerase activity that catalyzes the direct conversion of all-trans-retinol to 11-cis-retinol
    • Mata N.L., Ruiz A., et al. Chicken retinas contain a retinoid isomerase activity that catalyzes the direct conversion of all-trans-retinol to 11-cis-retinol. Biochemistry 44 35 (2005) 11715-11721
    • (2005) Biochemistry , vol.44 , Issue.35 , pp. 11715-11721
    • Mata, N.L.1    Ruiz, A.2
  • 51
    • 0026702571 scopus 로고
    • Hydrolysis of 11-cis- and all-trans-retinyl palmitate by retinal pigment epithelium microsomes
    • Mata N.L., Tsin A.T., et al. Hydrolysis of 11-cis- and all-trans-retinyl palmitate by retinal pigment epithelium microsomes. J. Biol. Chem. 267 14 (1992) 9794-9799
    • (1992) J. Biol. Chem. , vol.267 , Issue.14 , pp. 9794-9799
    • Mata, N.L.1    Tsin, A.T.2
  • 52
    • 0031689828 scopus 로고    scopus 로고
    • Distribution of 11-cis LRAT, 11-cis RD and 11-cis REH in bovine retinal pigment epithelium membranes
    • Mata N.L., and Tsin A.T. Distribution of 11-cis LRAT, 11-cis RD and 11-cis REH in bovine retinal pigment epithelium membranes. Biochim. Biophys. Acta 1394 1 (1998) 16-22
    • (1998) Biochim. Biophys. Acta , vol.1394 , Issue.1 , pp. 16-22
    • Mata, N.L.1    Tsin, A.T.2
  • 53
    • 0031748911 scopus 로고    scopus 로고
    • Colocalization of 11-cis retinyl esters and retinyl ester hydrolase activity in retinal pigment epithelium plasma membrane
    • Mata N.L., Villazana E.T., et al. Colocalization of 11-cis retinyl esters and retinyl ester hydrolase activity in retinal pigment epithelium plasma membrane. Invest. Ophthalmol. Vis. Sci. 39 8 (1998) 1312-1319
    • (1998) Invest. Ophthalmol. Vis. Sci. , vol.39 , Issue.8 , pp. 1312-1319
    • Mata, N.L.1    Villazana, E.T.2
  • 54
    • 84984763750 scopus 로고    scopus 로고
    • Mutation of the gene encoding cellular retinaldehyde-binding protein in autosomal recessive retinitis pigmentosa
    • Maw M.A., Kennedy B., et al. Mutation of the gene encoding cellular retinaldehyde-binding protein in autosomal recessive retinitis pigmentosa. Nat. Genet. 17 2 (1997) 198-200
    • (1997) Nat. Genet. , vol.17 , Issue.2 , pp. 198-200
    • Maw, M.A.1    Kennedy, B.2
  • 55
    • 0034982559 scopus 로고    scopus 로고
    • Confronting complexity: the interlink of phototransduction and retinoid metabolism in the vertebrate retina
    • McBee J.K., Palczewski K., et al. Confronting complexity: the interlink of phototransduction and retinoid metabolism in the vertebrate retina. Prog. Retin. Eye Res. 20 4 (2001) 469-529
    • (2001) Prog. Retin. Eye Res. , vol.20 , Issue.4 , pp. 469-529
    • McBee, J.K.1    Palczewski, K.2
  • 56
    • 0035930520 scopus 로고    scopus 로고
    • Isomerization of 11-cis-retinoids to all-trans-retinoids in vitro and in vivo
    • McBee J.K., Van Hooser J.P., et al. Isomerization of 11-cis-retinoids to all-trans-retinoids in vitro and in vivo. J. Biol. Chem. 276 51 (2001) 48483-48493
    • (2001) J. Biol. Chem. , vol.276 , Issue.51 , pp. 48483-48493
    • McBee, J.K.1    Van Hooser, J.P.2
  • 57
    • 24644507141 scopus 로고    scopus 로고
    • RPE65 is the isomerohydrolase in the retinoid visual cycle
    • Moiseyev G., Chen Y., et al. RPE65 is the isomerohydrolase in the retinoid visual cycle. Proc. Natl. Acad. Sci. U.S.A. 102 35 (2005) 12413-12418
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , Issue.35 , pp. 12413-12418
    • Moiseyev, G.1    Chen, Y.2
  • 58
    • 0034595283 scopus 로고    scopus 로고
    • Lecithin retinol acyltransferase contains cysteine residues essential for catalysis
    • Mondal M.S., Ruiz A., et al. Lecithin retinol acyltransferase contains cysteine residues essential for catalysis. Biochemistry 39 17 (2000) 5215-5220
    • (2000) Biochemistry , vol.39 , Issue.17 , pp. 5215-5220
    • Mondal, M.S.1    Ruiz, A.2
  • 59
    • 33749507044 scopus 로고    scopus 로고
    • 11-cis-Acyl-CoA:retinol O-acyltransferase activity in the primary culture of chicken Muller cells
    • Muniz A., Villazana-Espinoza E.T., et al. 11-cis-Acyl-CoA:retinol O-acyltransferase activity in the primary culture of chicken Muller cells. Biochemistry 45 40 (2006) 12265-12273
    • (2006) Biochemistry , vol.45 , Issue.40 , pp. 12265-12273
    • Muniz, A.1    Villazana-Espinoza, E.T.2
  • 60
    • 0033869452 scopus 로고    scopus 로고
    • A gene knockout corroborates the integral function of cellular retinol-binding protein in retinoid metabolism
    • Napoli J.L. A gene knockout corroborates the integral function of cellular retinol-binding protein in retinoid metabolism. Nutr. Rev. 58 8 (2000) 230-236
    • (2000) Nutr. Rev. , vol.58 , Issue.8 , pp. 230-236
    • Napoli, J.L.1
  • 61
    • 0034660094 scopus 로고    scopus 로고
    • Retinoid-binding proteins: mediators of retinoid action
    • Noy N. Retinoid-binding proteins: mediators of retinoid action. Biochem. J. 348 Pt 3 (2000) 481-495
    • (2000) Biochem. J. , vol.348 , Issue.PART 3 , pp. 481-495
    • Noy, N.1
  • 62
    • 0024401427 scopus 로고
    • Interphotoreceptor retinoid-binding protein: role in delivery of retinol to the pigment epithelium
    • Okajima T.I., Pepperberg D.R., et al. Interphotoreceptor retinoid-binding protein: role in delivery of retinol to the pigment epithelium. Exp. Eye Res. 49 4 (1989) 629-644
    • (1989) Exp. Eye Res. , vol.49 , Issue.4 , pp. 629-644
    • Okajima, T.I.1    Pepperberg, D.R.2
  • 63
    • 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 J.P., et al. 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 38 37 (1999) 12012-12019
    • (1999) Biochemistry , vol.38 , Issue.37 , pp. 12012-12019
    • Palczewski, K.1    Van Hooser, J.P.2
  • 64
    • 0021738687 scopus 로고
    • Rhodopsin photoproducts and the visual response of vertebrate rods
    • Pepperberg D.R., and Clack J.W. Rhodopsin photoproducts and the visual response of vertebrate rods. Vis. Res. 24 11 (1984) 1481-1486
    • (1984) Vis. Res. , vol.24 , Issue.11 , pp. 1481-1486
    • Pepperberg, D.R.1    Clack, J.W.2
  • 65
    • 0026279305 scopus 로고
    • Functional properties of interphotoreceptor retinoid-binding protein
    • Pepperberg D.R., Okajima T.L., et al. Functional properties of interphotoreceptor retinoid-binding protein. Photochem. Photobiol. 54 6 (1991) 1057-1060
    • (1991) Photochem. Photobiol. , vol.54 , Issue.6 , pp. 1057-1060
    • Pepperberg, D.R.1    Okajima, T.L.2
  • 66
    • 0020416622 scopus 로고
    • Utilization of retinoids in the bullfrog retina
    • Perlman J.I., Nodes B.R., et al. Utilization of retinoids in the bullfrog retina. J. Gen. Physiol. 80 6 (1982) 885-913
    • (1982) J. Gen. Physiol. , vol.80 , Issue.6 , pp. 885-913
    • Perlman, J.I.1    Nodes, B.R.2
  • 67
    • 0035385140 scopus 로고    scopus 로고
    • The biochemistry of the visual cycle
    • Rando R.R. The biochemistry of the visual cycle. Chem. Rev. 101 7 (2001) 1881-1896
    • (2001) Chem. Rev. , vol.101 , Issue.7 , pp. 1881-1896
    • Rando, R.R.1
  • 68
    • 0034646715 scopus 로고    scopus 로고
    • Identification and characterization of all-trans-retinol dehydrogenase from photoreceptor outer segments, the visual cycle enzyme that reduces all-trans-retinal to all-trans-retinol
    • Rattner A., Smallwood P.M., et al. Identification and characterization of all-trans-retinol dehydrogenase from photoreceptor outer segments, the visual cycle enzyme that reduces all-trans-retinal to all-trans-retinol. J. Biol. Chem. 275 15 (2000) 11034-11043
    • (2000) J. Biol. Chem. , vol.275 , Issue.15 , pp. 11034-11043
    • Rattner, A.1    Smallwood, P.M.2
  • 69
    • 26444596185 scopus 로고    scopus 로고
    • Mutation of key residues of RPE65 abolishes its enzymatic role as isomerohydrolase in the visual cycle
    • Redmond T.M., Poliakov E., et al. Mutation of key residues of RPE65 abolishes its enzymatic role as isomerohydrolase in the visual cycle. Proc. Natl. Acad. Sci. U.S.A. 102 38 (2005) 13658-13663
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , Issue.38 , pp. 13658-13663
    • Redmond, T.M.1    Poliakov, E.2
  • 70
    • 17344366357 scopus 로고    scopus 로고
    • Rpe65 is necessary for production of 11-cis-vitamin A in the retinal visual cycle
    • Redmond T.M., Yu S., et al. Rpe65 is necessary for production of 11-cis-vitamin A in the retinal visual cycle. Nat. Genet. 20 4 (1998) 344-351
    • (1998) Nat. Genet. , vol.20 , Issue.4 , pp. 344-351
    • Redmond, T.M.1    Yu, S.2
  • 71
    • 0034121428 scopus 로고    scopus 로고
    • The rhodopsin cycle is preserved in IRBP "knockout" mice despite abnormalities in retinal structure and function
    • Ripps H., Peachey N.S., et al. The rhodopsin cycle is preserved in IRBP "knockout" mice despite abnormalities in retinal structure and function. Vis. Neurosci. 17 1 (2000) 97-105
    • (2000) Vis. Neurosci. , vol.17 , Issue.1 , pp. 97-105
    • Ripps, H.1    Peachey, N.S.2
  • 72
    • 0024497916 scopus 로고
    • Retinyl esters in the vertebrate neuroretina
    • Rodriguez K.A., and Tsin A.T. Retinyl esters in the vertebrate neuroretina. Am. J. Physiol. 256 1 Pt 2 (1989) R255-R258
    • (1989) Am. J. Physiol. , vol.256 , Issue.1 PART 2
    • Rodriguez, K.A.1    Tsin, A.T.2
  • 73
    • 34447650022 scopus 로고    scopus 로고
    • Ruiz, A., Winston, A., et al. (1999). Molecular and Biochemical Characterization of Lecithin Retinol Acyltransferase.
  • 74
    • 0020008446 scopus 로고
    • Isolation of cellular retinoid-binding proteins from bovine retina with bound endogenous ligands
    • Saari J.C. Isolation of cellular retinoid-binding proteins from bovine retina with bound endogenous ligands. Methods Enzymol. 81 (1982) 819-826
    • (1982) Methods Enzymol. , vol.81 , pp. 819-826
    • Saari, J.C.1
  • 75
    • 0033960296 scopus 로고    scopus 로고
    • Biochemistry of visual pigment regeneration: the Friedenwald lecture
    • Saari J.C. Biochemistry of visual pigment regeneration: the Friedenwald lecture. Invest. Ophthalmol. Vis. Sci. 41 2 (2000) 337-348
    • (2000) Invest. Ophthalmol. Vis. Sci. , vol.41 , Issue.2 , pp. 337-348
    • Saari, J.C.1
  • 76
    • 0023898382 scopus 로고
    • CoA- and non-CoA-dependent retinol esterification in retinal pigment epithelium
    • Saari J.C., and Bredberg D.L. CoA- and non-CoA-dependent retinol esterification in retinal pigment epithelium. J. Biol. Chem. 263 17 (1988) 8084-8090
    • (1988) J. Biol. Chem. , vol.263 , Issue.17 , pp. 8084-8090
    • Saari, J.C.1    Bredberg, D.L.2
  • 77
    • 0024314805 scopus 로고
    • Lecithin:retinol acyltransferase in retinal pigment epithelial microsomes
    • Saari J.C., and Bredberg D.L. Lecithin:retinol acyltransferase in retinal pigment epithelial microsomes. J. Biol. Chem. 264 15 (1989) 8636-8640
    • (1989) J. Biol. Chem. , vol.264 , Issue.15 , pp. 8636-8640
    • Saari, J.C.1    Bredberg, D.L.2
  • 78
    • 0020416139 scopus 로고
    • Identification of the endogenous retinoids associated with three cellular retinoid-binding proteins from bovine retina and retinal pigment epithelium
    • Saari J.C., Bredberg L., et al. Identification of the endogenous retinoids associated with three cellular retinoid-binding proteins from bovine retina and retinal pigment epithelium. J. Biol. Chem. 257 22 (1982) 13329-13333
    • (1982) J. Biol. Chem. , vol.257 , Issue.22 , pp. 13329-13333
    • Saari, J.C.1    Bredberg, L.2
  • 79
    • 0027269908 scopus 로고
    • Retinol esterification in bovine retinal pigment epithelium: reversibility of lecithin:retinol acyltransferase
    • Saari J.C., Bredberg D.L., et al. Retinol esterification in bovine retinal pigment epithelium: reversibility of lecithin:retinol acyltransferase. Biochem. J. 291 Pt 3 (1993) 697-700
    • (1993) Biochem. J. , vol.291 , Issue.PART 3 , pp. 697-700
    • Saari, J.C.1    Bredberg, D.L.2
  • 80
    • 0028211275 scopus 로고
    • Control of substrate flow at a branch in the visual cycle
    • Saari J.C., Bredberg D.L., et al. Control of substrate flow at a branch in the visual cycle. Biochemistry 33 10 (1994) 3106-3112
    • (1994) Biochemistry , vol.33 , Issue.10 , pp. 3106-3112
    • Saari, J.C.1    Bredberg, D.L.2
  • 81
    • 0018170082 scopus 로고
    • Cellular retinol- and retinoic acid-binding proteins of bovine retina. Purification and properties
    • Saari J.C., Futterman S., et al. Cellular retinol- and retinoic acid-binding proteins of bovine retina. Purification and properties. J. Biol. Chem. 253 18 (1978) 6432-6436
    • (1978) J. Biol. Chem. , vol.253 , Issue.18 , pp. 6432-6436
    • Saari, J.C.1    Futterman, S.2
  • 82
    • 17944379443 scopus 로고    scopus 로고
    • New views on RPE65 deficiency: the rod system is the source of vision in a mouse model of Leber congenital amaurosis
    • Seeliger M.W., Grimm C., et al. New views on RPE65 deficiency: the rod system is the source of vision in a mouse model of Leber congenital amaurosis. Nat. Genet. 29 1 (2001) 70-74
    • (2001) Nat. Genet. , vol.29 , Issue.1 , pp. 70-74
    • Seeliger, M.W.1    Grimm, C.2
  • 83
    • 0027944675 scopus 로고
    • A human opsin-related gene that encodes a retinaldehyde-binding protein
    • Shen D., Jiang M., et al. A human opsin-related gene that encodes a retinaldehyde-binding protein. Biochemistry 33 44 (1994) 13117-13125
    • (1994) Biochemistry , vol.33 , Issue.44 , pp. 13117-13125
    • Shen, D.1    Jiang, M.2
  • 84
    • 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., et al. The retinal pigment epithelial-specific 11-cis retinol dehydrogenase belongs to the family of short chain alcohol dehydrogenases. J. Biol. Chem. 270 3 (1995) 1107-1112
    • (1995) J. Biol. Chem. , vol.270 , Issue.3 , pp. 1107-1112
    • Simon, A.1    Hellman, U.2
  • 85
    • 0033004738 scopus 로고    scopus 로고
    • Intracellular localization and membrane topology of 11-cis retinol dehydrogenase in the retinal pigment epithelium suggest a compartmentalized synthesis of 11-cis retinaldehyde
    • Simon A., Romert A., et al. Intracellular localization and membrane topology of 11-cis retinol dehydrogenase in the retinal pigment epithelium suggest a compartmentalized synthesis of 11-cis retinaldehyde. J. Cell Sci. 112 Pt 4 (1999) 549-558
    • (1999) J. Cell Sci. , vol.112 , Issue.PART 4 , pp. 549-558
    • Simon, A.1    Romert, A.2
  • 86
    • 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 M.H., et al. Preferential release of 11-cis-retinol from retinal pigment epithelial cells in the presence of cellular retinaldehyde-binding protein. J. Biol. Chem. 274 13 (1999) 8577-8585
    • (1999) J. Biol. Chem. , vol.274 , Issue.13 , pp. 8577-8585
    • Stecher, H.1    Gelb, M.H.2
  • 87
    • 0018711506 scopus 로고
    • 11-cis-Retinal-binding protein from bovine retina. Isolation and partial characterization
    • Stubbs G.W., Saari J.C., et al. 11-cis-Retinal-binding protein from bovine retina. Isolation and partial characterization. J. Biol. Chem. 254 17 (1979) 8529-8533
    • (1979) J. Biol. Chem. , vol.254 , Issue.17 , pp. 8529-8533
    • Stubbs, G.W.1    Saari, J.C.2
  • 88
    • 0027168449 scopus 로고
    • Identification and immunohistochemistry of retinol dehydrogenase from bovine retinal pigment epithelium
    • Suzuki Y., Ishiguro S., et al. Identification and immunohistochemistry of retinol dehydrogenase from bovine retinal pigment epithelium. Biochim. Biophys. Acta 1163 2 (1993) 201-208
    • (1993) Biochim. Biophys. Acta , vol.1163 , Issue.2 , pp. 201-208
    • Suzuki, Y.1    Ishiguro, S.2
  • 89
    • 33847021802 scopus 로고    scopus 로고
    • Diseases caused by defects in the visual cycle: retinoids as potential therapeutic agents
    • Travis G.H., Golczak M., et al. Diseases caused by defects in the visual cycle: retinoids as potential therapeutic agents. Annu. Rev. Pharmacol. Toxicol. 47 (2007) 469-512
    • (2007) Annu. Rev. Pharmacol. Toxicol. , vol.47 , pp. 469-512
    • Travis, G.H.1    Golczak, M.2
  • 90
    • 28444461079 scopus 로고    scopus 로고
    • Retinoid cycles in the cone-dominated chicken retina
    • Trevino S.G., Villazana-Espinoza E.T., et al. Retinoid cycles in the cone-dominated chicken retina. J. Exp. Biol. 208 Pt 21 (2005) 4151-4157
    • (2005) J. Exp. Biol. , vol.208 , Issue.PART 21 , pp. 4151-4157
    • Trevino, S.G.1    Villazana-Espinoza, E.T.2
  • 91
    • 0034016094 scopus 로고    scopus 로고
    • Substrate specificities of retinyl ester hydrolases in retinal pigment epithelium
    • Tsin A.T., Mata N.L., et al. Substrate specificities of retinyl ester hydrolases in retinal pigment epithelium. Methods Enzymol. 316 (2000) 384-400
    • (2000) Methods Enzymol. , vol.316 , pp. 384-400
    • Tsin, A.T.1    Mata, N.L.2
  • 92
    • 33747876563 scopus 로고    scopus 로고
    • In-vitro conversion of all-trans retinol to 11-cis retinol in chicken eye
    • ARVO E abstract #2036
    • Villazana-Espinoza E., Hatch A., et al. In-vitro conversion of all-trans retinol to 11-cis retinol in chicken eye. Invest. Ophthalmol. Vis. Sci. (2006) ARVO E abstract #2036
    • (2006) Invest. Ophthalmol. Vis. Sci.
    • Villazana-Espinoza, E.1    Hatch, A.2
  • 93
    • 33747880110 scopus 로고    scopus 로고
    • Effect of light exposure on the accumulation and depletion of retinyl ester in the chicken retina
    • Villazana-Espinoza E.T., Hatch A.L., et al. Effect of light exposure on the accumulation and depletion of retinyl ester in the chicken retina. Exp. Eye Res. 83 4 (2006) 871-876
    • (2006) Exp. Eye Res. , vol.83 , Issue.4 , pp. 871-876
    • Villazana-Espinoza, E.T.1    Hatch, A.L.2
  • 94
    • 0014411230 scopus 로고
    • Molecular basis of visual excitation
    • Wald G. Molecular basis of visual excitation. Science 162 850 (1968) 230-239
    • (1968) Science , vol.162 , Issue.850 , pp. 230-239
    • Wald, G.1
  • 95
    • 23844496400 scopus 로고    scopus 로고
    • The retinal G protein-coupled receptor (RGR) enhances isomerohydrolase activity independent of light
    • Wenzel A., Oberhauser V., et al. The retinal G protein-coupled receptor (RGR) enhances isomerohydrolase activity independent of light. J. Biol. Chem. 280 33 (2005) 29874-29884
    • (2005) J. Biol. Chem. , vol.280 , Issue.33 , pp. 29874-29884
    • Wenzel, A.1    Oberhauser, V.2
  • 96
    • 33847727462 scopus 로고    scopus 로고
    • RPE65 is essential for the function of cone photoreceptors in NRL-deficient mice
    • Wenzel A., von Lintig J., et al. RPE65 is essential for the function of cone photoreceptors in NRL-deficient mice. Invest. Ophthalmol. Vis. Sci. 48 2 (2007) 534-542
    • (2007) Invest. Ophthalmol. Vis. Sci. , vol.48 , Issue.2 , pp. 534-542
    • Wenzel, A.1    von Lintig, J.2
  • 97
    • 0033033364 scopus 로고    scopus 로고
    • Mutations in the gene encoding 11-cis retinol dehydrogenase cause delayed dark adaptation and fundus albipunctatus
    • Yamamoto H., Simon A., et al. Mutations in the gene encoding 11-cis retinol dehydrogenase cause delayed dark adaptation and fundus albipunctatus. Nat. Genet. 22 2 (1999) 188-191
    • (1999) Nat. Genet. , vol.22 , Issue.2 , pp. 188-191
    • Yamamoto, H.1    Simon, A.2
  • 98
    • 0036479135 scopus 로고    scopus 로고
    • Synthesis of the all-trans-retinal chromophore of retinal G protein-coupled receptor opsin in cultured pigment epithelial cells
    • Yang M., and Fong H.K. Synthesis of the all-trans-retinal chromophore of retinal G protein-coupled receptor opsin in cultured pigment epithelial cells. J. Biol. Chem. 277 5 (2002) 3318-3324
    • (2002) J. Biol. Chem. , vol.277 , Issue.5 , pp. 3318-3324
    • Yang, M.1    Fong, H.K.2
  • 99
    • 0016174313 scopus 로고
    • The distribution and proportions of Vitamin A compounds during the visual cycle in the rat
    • Zimmerman W.F. The distribution and proportions of Vitamin A compounds during the visual cycle in the rat. Vis. Res. 14 9 (1974) 795-802
    • (1974) Vis. Res. , vol.14 , Issue.9 , pp. 795-802
    • Zimmerman, W.F.1
  • 100
    • 0016752092 scopus 로고
    • Biochemical aspects of the visual process. XXX. Distribution of stereospecific retinol dehydrogenase activities in subcellular fractions of bovine retina and pigment epithelium
    • Zimmerman W.F., Lion F., et al. Biochemical aspects of the visual process. XXX. Distribution of stereospecific retinol dehydrogenase activities in subcellular fractions of bovine retina and pigment epithelium. Exp. Eye Res. 21 4 (1975) 325-332
    • (1975) Exp. Eye Res. , vol.21 , Issue.4 , pp. 325-332
    • Zimmerman, W.F.1    Lion, F.2
  • 101
    • 0016338624 scopus 로고
    • Dynamics and function of vitamin A compounds in rat retina after a small bleach of rhodopsin
    • Zimmerman W.F., Yost M.T., et al. Dynamics and function of vitamin A compounds in rat retina after a small bleach of rhodopsin. Nature 250 461 (1974) 66-67
    • (1974) Nature , vol.250 , Issue.461 , pp. 66-67
    • Zimmerman, W.F.1    Yost, M.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.