메뉴 건너뛰기




Volumn 134, Issue , 2015, Pages 433-448

A History of the Classical Visual Cycle

Author keywords

RPE65; Visual cycle; Vitamin A

Indexed keywords

ISOMERASE; PROTEIN; PROTEIN RPE65; RETINOID; RETINOL; RHODOPSIN; UNCLASSIFIED DRUG; CIS TRANS ISOMERASE; RETINOID ISOMEROHYDROLASE;

EID: 84957872547     PISSN: 18771173     EISSN: 18780814     Source Type: Book Series    
DOI: 10.1016/bs.pmbts.2015.06.009     Document Type: Conference Paper
Times cited : (37)

References (73)
  • 1
    • 0017610094 scopus 로고
    • Boll's phenomenon
    • C. Baumann Boll's phenomenon Vision Res 17 11-12 1977 1325 1327
    • (1977) Vision Res , vol.17 , Issue.11-12 , pp. 1325-1327
    • Baumann, C.1
  • 2
    • 0017879023 scopus 로고
    • 100 years of the visual cycle
    • M.F. Marmor, and L.J. Martin 100 years of the visual cycle Surv Ophthalmol 22 4 1978 279 285
    • (1978) Surv Ophthalmol , vol.22 , Issue.4 , pp. 279-285
    • Marmor, M.F.1    Martin, L.J.2
  • 3
    • 84944817605 scopus 로고
    • On the stable colours of the retina
    • 105
    • W. Kühne On the stable colours of the retina J Physiol 1 2-3 1878 109 212 105
    • (1878) J Physiol , vol.1 , Issue.2-3 , pp. 109-212
    • Kühne, W.1
  • 4
    • 77955769684 scopus 로고
    • On the physiology of the retinal epithelium
    • W. Kühne, and H. Sewall On the physiology of the retinal epithelium J Physiol 3 1 1880 88 92
    • (1880) J Physiol , vol.3 , Issue.1 , pp. 88-92
    • Kühne, W.1    Sewall, H.2
  • 5
    • 84967771032 scopus 로고
    • Carotenoids and the visual cycle
    • G. Wald Carotenoids and the visual cycle J Gen Physiol 19 2 1935 351 371
    • (1935) J Gen Physiol , vol.19 , Issue.2 , pp. 351-371
    • Wald, G.1
  • 6
    • 79955860094 scopus 로고
    • Visual adaptation and chemistry of the rods
    • G. Wald, and A.B. Clark Visual adaptation and chemistry of the rods J Gen Physiol 21 1 1937 93 105
    • (1937) J Gen Physiol , vol.21 , Issue.1 , pp. 93-105
    • Wald, G.1    Clark, A.B.2
  • 7
    • 0000073823 scopus 로고
    • The molar extinction of rhodopsin
    • G. Wald, and P.K. Brown The molar extinction of rhodopsin J Gen Physiol 37 2 1953 189 200
    • (1953) J Gen Physiol , vol.37 , Issue.2 , pp. 189-200
    • Wald, G.1    Brown, P.K.2
  • 9
    • 0014428724 scopus 로고
    • The molecular basis of visual excitation
    • G. Wald The molecular basis of visual excitation Nature 219 5156 1968 800 807
    • (1968) Nature , vol.219 , Issue.5156 , pp. 800-807
    • Wald, G.1
  • 10
    • 78649454765 scopus 로고    scopus 로고
    • Retinol dehydrogenases (RDHs) in the visual cycle
    • R.O. Parker, and R.K. Crouch Retinol dehydrogenases (RDHs) in the visual cycle Exp Eye Res 91 6 2010 788 792
    • (2010) Exp Eye Res , vol.91 , Issue.6 , pp. 788-792
    • Parker, R.O.1    Crouch, R.K.2
  • 11
    • 21444437579 scopus 로고    scopus 로고
    • Role of photoreceptor-specific retinol dehydrogenase in the retinoid cycle in vivo
    • A. Maeda, T. Maeda, Y. Imanishi, and et al. Role of photoreceptor-specific retinol dehydrogenase in the retinoid cycle in vivo J Biol Chem 280 19 2005 18822 18832
    • (2005) J Biol Chem , vol.280 , Issue.19 , pp. 18822-18832
    • Maeda, A.1    Maeda, T.2    Imanishi, Y.3
  • 12
    • 3542999277 scopus 로고    scopus 로고
    • Mutations in RDH12 encoding a photoreceptor cell retinol dehydrogenase cause childhood-onset severe retinal dystrophy
    • A.R. Janecke, D.A. Thompson, G. Utermann, and et al. Mutations in RDH12 encoding a photoreceptor cell retinol dehydrogenase cause childhood-onset severe retinal dystrophy Nat Genet 36 8 2004 850 854
    • (2004) Nat Genet , vol.36 , Issue.8 , pp. 850-854
    • Janecke, A.R.1    Thompson, D.A.2    Utermann, G.3
  • 13
    • 0004846410 scopus 로고
    • Metabolism of the retina. V. the role of microsomes in Vitamin A esterification in the visual cycle
    • J.S. Andrews, and S. Futterman Metabolism of the retina. V. The role of microsomes in vitamin A esterification in the visual cycle J Biol Chem 239 1964 4073 4076
    • (1964) J Biol Chem , vol.239 , pp. 4073-4076
    • Andrews, J.S.1    Futterman, S.2
  • 14
    • 0016174313 scopus 로고
    • The distribution and proportions of Vitamin A compounds during the visual cycle in the rat
    • W.F. Zimmerman The distribution and proportions of vitamin A compounds during the visual cycle in the rat Vision Res 14 9 1974 795 802
    • (1974) Vision Res , vol.14 , Issue.9 , pp. 795-802
    • Zimmerman, W.F.1
  • 15
    • 0000284971 scopus 로고
    • Isomerization of all-trans-retinoids to 11-cis-retinoids in vitro
    • P.S. Bernstein, W.C. Law, and R.R. Rando Isomerization of all-trans-retinoids to 11-cis-retinoids in vitro Proc Natl Acad Sci USA 84 7 1987 1849 1853
    • (1987) Proc Natl Acad Sci USA , vol.84 , Issue.7 , pp. 1849-1853
    • Bernstein, P.S.1    Law, W.C.2    Rando, R.R.3
  • 16
    • 0020416622 scopus 로고
    • Utilization of retinoids in the bullfrog retina
    • J.I. Perlman, B.R. Nodes, and D.R. Pepperberg 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    Pepperberg, D.R.3
  • 17
    • 0025092392 scopus 로고
    • Substrate specificities and mechanism in the enzymatic processing of Vitamin A into 11-cis-retinol
    • F.J. Canada, W.C. Law, R.R. Rando, T. Yamamoto, F. Derguini, and K. Nakanishi Substrate specificities and mechanism in the enzymatic processing of vitamin A into 11-cis-retinol Biochemistry 29 41 1990 9690 9697
    • (1990) Biochemistry , vol.29 , Issue.41 , pp. 9690-9697
    • Canada, F.J.1    Law, W.C.2    Rando, R.R.3    Yamamoto, T.4    Derguini, F.5    Nakanishi, K.6
  • 18
    • 0025159338 scopus 로고
    • Inhibitors of retinyl ester formation also prevent the biosynthesis of 11-cis-retinol
    • A. Trehan, F.J. Canada, and R.R. Rando Inhibitors of retinyl ester formation also prevent the biosynthesis of 11-cis-retinol Biochemistry 29 2 1990 309 312
    • (1990) Biochemistry , vol.29 , Issue.2 , pp. 309-312
    • Trehan, A.1    Canada, F.J.2    Rando, R.R.3
  • 19
    • 0033033364 scopus 로고    scopus 로고
    • Mutations in the gene encoding 11-cis retinol dehydrogenase cause delayed dark adaptation and fundus albipunctatus
    • H. Yamamoto, A. Simon, U. Eriksson, E. Harris, E.L. Berson, and T.P. Dryja 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    Eriksson, U.3    Harris, E.4    Berson, E.L.5    Dryja, T.P.6
  • 20
    • 0017684624 scopus 로고
    • Vitamin A receptors. I. Comparison of retinol binding to serum retinol-binding protein and to tissue receptors in chick retina and pigment epithelium
    • T. Abe, B. Wiggert, D.R. Bergsma, and G.J. Chader Vitamin A receptors. I. Comparison of retinol binding to serum retinol-binding protein and to tissue receptors in chick retina and pigment epithelium Biochim Biophys Acta 498 1 1977 355 365
    • (1977) Biochim Biophys Acta , vol.498 , Issue.1 , pp. 355-365
    • Abe, T.1    Wiggert, B.2    Bergsma, D.R.3    Chader, G.J.4
  • 21
    • 0021015311 scopus 로고
    • Rapid isolation of bovine interphotoreceptor retinol-binding protein
    • A.J. Adler, and C.D. Evans Rapid isolation of bovine interphotoreceptor retinol-binding protein Biochim Biophys Acta 761 3 1983 217 222
    • (1983) Biochim Biophys Acta , vol.761 , Issue.3 , pp. 217-222
    • Adler, A.J.1    Evans, C.D.2
  • 22
    • 0021749655 scopus 로고
    • Visual cycle in the mammalian eye. Retinoid-binding proteins and the distribution of 11-cis retinoids
    • C.D. Bridges, R.A. Alvarez, S.L. Fong, F. Gonzalez-Fernandez, D.M. Lam, and G.I. Liou Visual cycle in the mammalian eye. Retinoid-binding proteins and the distribution of 11-cis retinoids Vision Res 24 11 1984 1581 1594
    • (1984) Vision Res , vol.24 , Issue.11 , pp. 1581-1594
    • Bridges, C.D.1    Alvarez, R.A.2    Fong, S.L.3    Gonzalez-Fernandez, F.4    Lam, D.M.5    Liou, G.I.6
  • 23
    • 0023657241 scopus 로고
    • Biochemical characterization of the retinoid isomerase system of the eye
    • P.S. Bernstein, W.C. Law, and R.R. Rando Biochemical characterization of the retinoid isomerase system of the eye J Biol Chem 262 35 1987 16848 16857
    • (1987) J Biol Chem , vol.262 , Issue.35 , pp. 16848-16857
    • Bernstein, P.S.1    Law, W.C.2    Rando, R.R.3
  • 24
    • 0026316417 scopus 로고
    • Monoclonal antibodies which recognize endoplasmic reticulum in the retinal pigment epithelium
    • H. Sagara, and K. Hirosawa Monoclonal antibodies which recognize endoplasmic reticulum in the retinal pigment epithelium Exp Eye Res 53 6 1991 765 771
    • (1991) Exp Eye Res , vol.53 , Issue.6 , pp. 765-771
    • Sagara, H.1    Hirosawa, K.2
  • 25
    • 0027535377 scopus 로고
    • A developmentally regulated microsomal protein specific for the pigment epithelium of the vertebrate retina
    • C.P. Hamel, E. Tsilou, E. Harris, and et al. A developmentally regulated microsomal protein specific for the pigment epithelium of the vertebrate retina J Neurosci Res 34 4 1993 414 425
    • (1993) J Neurosci Res , vol.34 , Issue.4 , pp. 414-425
    • Hamel, C.P.1    Tsilou, E.2    Harris, E.3
  • 26
    • 0027242119 scopus 로고
    • Molecular cloning and expression of RPE65, a novel retinal pigment epithelium-specific microsomal protein that is post-transcriptionally regulated in vitro
    • C.P. Hamel, E. Tsilou, B.A. Pfeffer, J.J. Hooks, B. Detrick, and T.M. Redmond Molecular cloning and expression of RPE65, a novel retinal pigment epithelium-specific microsomal protein that is post-transcriptionally regulated in vitro J Biol Chem 268 21 1993 15751 15757
    • (1993) J Biol Chem , vol.268 , Issue.21 , pp. 15751-15757
    • Hamel, C.P.1    Tsilou, E.2    Pfeffer, B.A.3    Hooks, J.J.4    Detrick, B.5    Redmond, T.M.6
  • 27
    • 17344366357 scopus 로고    scopus 로고
    • Rpe65 is necessary for production of 11-cis-Vitamin A in the retinal visual cycle
    • T.M. Redmond, S. Yu, E. Lee, and 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    Lee, E.3
  • 28
  • 29
    • 23744447355 scopus 로고    scopus 로고
    • Rpe65 is the retinoid isomerase in bovine retinal pigment epithelium
    • M. Jin, S. Li, W.N. Moghrabi, H. Sun, and G.H. Travis 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    Moghrabi, W.N.3    Sun, H.4    Travis, G.H.5
  • 30
    • 26444596185 scopus 로고    scopus 로고
    • Mutation of key residues of RPE65 abolishes its enzymatic role as isomerohydrolase in the visual cycle
    • T.M. Redmond, E. Poliakov, S. Yu, J.-Y. Tsai, Z. Lu, and S. Gentleman Mutation of key residues of RPE65 abolishes its enzymatic role as isomerohydrolase in the visual cycle Proc Natl Acad Sci USA 102 38 2005 13658 13663
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.38 , pp. 13658-13663
    • Redmond, T.M.1    Poliakov, E.2    Yu, S.3    Tsai, J.-Y.4    Lu, Z.5    Gentleman, S.6
  • 31
    • 77954620409 scopus 로고    scopus 로고
    • Membrane-binding and enzymatic properties of RPE65
    • P.D. Kiser, and K. Palczewski Membrane-binding and enzymatic properties of RPE65 Prog Retin Eye Res 29 5 2010 428 442
    • (2010) Prog Retin Eye Res , vol.29 , Issue.5 , pp. 428-442
    • Kiser, P.D.1    Palczewski, K.2
  • 32
    • 0032167754 scopus 로고    scopus 로고
    • Role of the 3′-untranslated region of RPE65 mRNA in the translational regulation of the RPE65 gene: Identification of a specific translation inhibitory element
    • S.Y. Liu, and T.M. Redmond Role of the 3′-untranslated region of RPE65 mRNA in the translational regulation of the RPE65 gene: identification of a specific translation inhibitory element Arch Biochem Biophys 357 1 1998 37 44
    • (1998) Arch Biochem Biophys , vol.357 , Issue.1 , pp. 37-44
    • Liu, S.Y.1    Redmond, T.M.2
  • 33
    • 0028942746 scopus 로고
    • Molecular characterization of the human gene encoding an abundant 61 kDa protein specific to the retinal pigment epithelium
    • A. Nicoletti, D.J. Wong, K. Kawase, and et al. Molecular characterization of the human gene encoding an abundant 61 kDa protein specific to the retinal pigment epithelium Hum Mol Genet 4 4 1995 641 649
    • (1995) Hum Mol Genet , vol.4 , Issue.4 , pp. 641-649
    • Nicoletti, A.1    Wong, D.J.2    Kawase, K.3
  • 34
    • 0032966359 scopus 로고    scopus 로고
    • Identification of RPE65 in transformed kidney cells
    • J.X. Ma, D. Zhang, M. Laser, and et al. Identification of RPE65 in transformed kidney cells FEBS Lett 452 3 1999 199 204
    • (1999) FEBS Lett , vol.452 , Issue.3 , pp. 199-204
    • Ma, J.X.1    Zhang, D.2    Laser, M.3
  • 35
    • 0242578614 scopus 로고    scopus 로고
    • Visual cycle retinoid processing proteins are present in HEK293S cells
    • Y. Chen, G. Moiseyev, B.X. Wu, J.X. Ma, and R.K. Crouch Visual cycle retinoid processing proteins are present in HEK293S cells Vision Res 43 28 2003 3037 3044
    • (2003) Vision Res , vol.43 , Issue.28 , pp. 3037-3044
    • Chen, Y.1    Moiseyev, G.2    Wu, B.X.3    Ma, J.X.4    Crouch, R.K.5
  • 36
    • 0032569985 scopus 로고    scopus 로고
    • Cloning and localization of RPE65 mRNA in salamander cone photoreceptor cells
    • J. Ma, L. Xu, D.K. Othersen, T.M. Redmond, and R.K. Crouch Cloning and localization of RPE65 mRNA in salamander cone photoreceptor cells Biochim Biophys Acta 1443 1-2 1998 255 261
    • (1998) Biochim Biophys Acta , vol.1443 , Issue.1-2 , pp. 255-261
    • Ma, J.1    Xu, L.2    Othersen, D.K.3    Redmond, T.M.4    Crouch, R.K.5
  • 37
    • 0036236801 scopus 로고    scopus 로고
    • Identification of the RPE65 protein in mammalian cone photoreceptors
    • S.L. Znoiko, R.K. Crouch, G. Moiseyev, and J.-X. Ma Identification of the RPE65 protein in mammalian cone photoreceptors Invest Ophthalmol Vis Sci 43 5 2002 1604 1609
    • (2002) Invest Ophthalmol Vis Sci , vol.43 , Issue.5 , pp. 1604-1609
    • Znoiko, S.L.1    Crouch, R.K.2    Moiseyev, G.3    Ma, J.-X.4
  • 38
    • 83455247258 scopus 로고    scopus 로고
    • RPE65 is present in human green/red cones and promotes photopigment regeneration in an in vitro cone cell model
    • P.H. Tang, M.C. Buhusi, J.-X. Ma, and R.K. Crouch RPE65 is present in human green/red cones and promotes photopigment regeneration in an in vitro cone cell model J Neurosci 31 50 2011 18618 18626
    • (2011) J Neurosci , vol.31 , Issue.50 , pp. 18618-18626
    • Tang, P.H.1    Buhusi, M.C.2    Ma, J.-X.3    Crouch, R.K.4
  • 39
    • 0035794153 scopus 로고    scopus 로고
    • Identification, expression, and substrate specificity of a mammalian beta-carotene 15,15′-dioxygenase
    • T.M. Redmond, S. Gentleman, T. Duncan, and et al. Identification, expression, and substrate specificity of a mammalian beta-carotene 15,15′-dioxygenase J Biol Chem 276 9 2001 6560 6565
    • (2001) J Biol Chem , vol.276 , Issue.9 , pp. 6560-6565
    • Redmond, T.M.1    Gentleman, S.2    Duncan, T.3
  • 40
  • 41
    • 77951229802 scopus 로고    scopus 로고
    • Importance of membrane structural integrity for RPE65 retinoid isomerization activity
    • M. Golczak, P.D. Kiser, D.T. Lodowski, A. Maeda, and K. Palczewski Importance of membrane structural integrity for RPE65 retinoid isomerization activity J Biol Chem 285 13 2010 9667 9682
    • (2010) J Biol Chem , vol.285 , Issue.13 , pp. 9667-9682
    • Golczak, M.1    Kiser, P.D.2    Lodowski, D.T.3    Maeda, A.4    Palczewski, K.5
  • 42
    • 84867345070 scopus 로고    scopus 로고
    • Structure of RPE65 isomerase in a lipidic matrix reveals roles for phospholipids and iron in catalysis
    • P.D. Kiser, E.R. Farquhar, W. Shi, X. Sui, M.R. Chance, and K. Palczewski Structure of RPE65 isomerase in a lipidic matrix reveals roles for phospholipids and iron in catalysis Proc Natl Acad Sci USA 109 41 2012 E2747 E2756
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.41 , pp. E2747-E2756
    • Kiser, P.D.1    Farquhar, E.R.2    Shi, W.3    Sui, X.4    Chance, M.R.5    Palczewski, K.6
  • 43
    • 0035005157 scopus 로고    scopus 로고
    • Expression, purification, and MALDI analysis of RPE65
    • J. Ma, J. Zhang, K.L. Othersen, and et al. Expression, purification, and MALDI analysis of RPE65 Invest Ophthalmol Vis Sci 42 7 2001 1429 1435
    • (2001) Invest Ophthalmol Vis Sci , vol.42 , Issue.7 , pp. 1429-1435
    • Ma, J.1    Zhang, J.2    Othersen, K.L.3
  • 44
    • 34248191755 scopus 로고    scopus 로고
    • The roles of three palmitoylation sites of RPE65 in its membrane association and isomerohydrolase activity
    • Y. Takahashi, G. Moiseyev, Y. Chen, and J.X. Ma The roles of three palmitoylation sites of RPE65 in its membrane association and isomerohydrolase activity Invest Ophthalmol Vis Sci 47 12 2006 5191 5196
    • (2006) Invest Ophthalmol Vis Sci , vol.47 , Issue.12 , pp. 5191-5196
    • Takahashi, Y.1    Moiseyev, G.2    Chen, Y.3    Ma, J.X.4
  • 45
    • 79957740398 scopus 로고    scopus 로고
    • Binding to lipid membrane induces conformational changes in RPE65: Implications for its isomerohydrolase activity
    • O. Nikolaeva, G. Moiseyev, K. Rodgers, and J.-X. Ma Binding to lipid membrane induces conformational changes in RPE65: implications for its isomerohydrolase activity Biochem J 436 3 2011 591 597
    • (2011) Biochem J , vol.436 , Issue.3 , pp. 591-597
    • Nikolaeva, O.1    Moiseyev, G.2    Rodgers, K.3    Ma, J.-X.4
  • 46
    • 33644851684 scopus 로고    scopus 로고
    • Binding of RPE65 fragments to lipid monolayers and identification of its partners by glutathione S-transferase pull-down assays
    • E. Trudel, S. Beaufils, A. Renault, R. Breton, and C. Salesse Binding of RPE65 fragments to lipid monolayers and identification of its partners by glutathione S-transferase pull-down assays Biochemistry 45 10 2006 3337 3347
    • (2006) Biochemistry , vol.45 , Issue.10 , pp. 3337-3347
    • Trudel, E.1    Beaufils, S.2    Renault, A.3    Breton, R.4    Salesse, C.5
  • 47
    • 34547092674 scopus 로고    scopus 로고
    • Role of LRAT on the retinoid isomerase activity and membrane association of Rpe65
    • M. Jin, Q. Yuan, S. Li, and G.H. Travis Role of LRAT on the retinoid isomerase activity and membrane association of Rpe65 J Biol Chem 282 29 2007 20915 20924
    • (2007) J Biol Chem , vol.282 , Issue.29 , pp. 20915-20924
    • Jin, M.1    Yuan, Q.2    Li, S.3    Travis, G.H.4
  • 48
    • 59149105603 scopus 로고    scopus 로고
    • Identification of a novel palmitoylation site essential for membrane association and isomerohydrolase activity of RPE65
    • Y. Takahashi, G. Moiseyev, Z. Ablonczy, Y. Chen, R.K. Crouch, and J.X. Ma Identification of a novel palmitoylation site essential for membrane association and isomerohydrolase activity of RPE65 J Biol Chem 284 5 2009 3211 3218
    • (2009) J Biol Chem , vol.284 , Issue.5 , pp. 3211-3218
    • Takahashi, Y.1    Moiseyev, G.2    Ablonczy, Z.3    Chen, Y.4    Crouch, R.K.5    Ma, J.X.6
  • 49
    • 33646353950 scopus 로고    scopus 로고
    • RPE65 is an iron(II)-dependent isomerohydrolase in the retinoid visual cycle
    • G. Moiseyev, Y. Takahashi, Y. Chen, and et al. RPE65 is an iron(II)-dependent isomerohydrolase in the retinoid visual cycle J Biol Chem 281 5 2006 2835 2840
    • (2006) J Biol Chem , vol.281 , Issue.5 , pp. 2835-2840
    • Moiseyev, G.1    Takahashi, Y.2    Chen, Y.3
  • 50
    • 25844464185 scopus 로고    scopus 로고
    • Identification of conserved histidines and glutamic acid as key residues for isomerohydrolase activity of RPE65, an enzyme of the visual cycle in the retinal pigment epithelium
    • Y. Takahashi, G. Moiseyev, Y. Chen, and J.X. Ma Identification of conserved histidines and glutamic acid as key residues for isomerohydrolase activity of RPE65, an enzyme of the visual cycle in the retinal pigment epithelium FEBS Lett 579 24 2005 5414 5418
    • (2005) FEBS Lett , vol.579 , Issue.24 , pp. 5414-5418
    • Takahashi, Y.1    Moiseyev, G.2    Chen, Y.3    Ma, J.X.4
  • 51
    • 0024403617 scopus 로고
    • Membranes as the energy source in the endergonic transformation of Vitamin A to 11-cis-retinol
    • P.S. Deigner, W.C. Law, F.J. Canada, and R.R. Rando Membranes as the energy source in the endergonic transformation of vitamin A to 11-cis-retinol Science 244 4907 1989 968 971
    • (1989) Science , vol.244 , Issue.4907 , pp. 968-971
    • Deigner, P.S.1    Law, W.C.2    Canada, F.J.3    Rando, R.R.4
  • 52
    • 0034687090 scopus 로고    scopus 로고
    • Isomerization of all-trans-retinol to cis-retinols in bovine retinal pigment epithelial cells: Dependence on the specificity of retinoid-binding proteins
    • J.K. McBee, V. Kuksa, R. Alvarez, and et al. Isomerization of all-trans-retinol to cis-retinols in bovine retinal pigment epithelial cells: dependence on the specificity of retinoid-binding proteins Biochemistry 39 37 2000 11370 11380
    • (2000) Biochemistry , vol.39 , Issue.37 , pp. 11370-11380
    • McBee, J.K.1    Kuksa, V.2    Alvarez, R.3
  • 53
    • 76249086955 scopus 로고    scopus 로고
    • RPE65, visual cycle retinol isomerase, is not inherently 11-cis-specific: Support for a carbocation mechanism of retinol isomerization
    • T.M. Redmond, E. Poliakov, S. Kuo, P. Chander, and S. Gentleman RPE65, visual cycle retinol isomerase, is not inherently 11-cis-specific: support for a carbocation mechanism of retinol isomerization J Biol Chem 285 3 2010 1919 1927
    • (2010) J Biol Chem , vol.285 , Issue.3 , pp. 1919-1927
    • Redmond, T.M.1    Poliakov, E.2    Kuo, S.3    Chander, P.4    Gentleman, S.5
  • 54
    • 84865764391 scopus 로고    scopus 로고
    • Aromatic residues in the substrate cleft of RPE65 protein govern retinol isomerization and modulate its progression
    • P. Chander, S. Gentleman, E. Poliakov, and T.M. Redmond Aromatic residues in the substrate cleft of RPE65 protein govern retinol isomerization and modulate its progression J Biol Chem 287 36 2012 30552 30559
    • (2012) J Biol Chem , vol.287 , Issue.36 , pp. 30552-30559
    • Chander, P.1    Gentleman, S.2    Poliakov, E.3    Redmond, T.M.4
  • 55
    • 80051521870 scopus 로고    scopus 로고
    • Aromatic lipophilic spin traps effectively inhibit RPE65 isomerohydrolase activity
    • E. Poliakov, T. Parikh, M. Ayele, and et al. Aromatic lipophilic spin traps effectively inhibit RPE65 isomerohydrolase activity Biochemistry 50 32 2011 6739 6741
    • (2011) Biochemistry , vol.50 , Issue.32 , pp. 6739-6741
    • Poliakov, E.1    Parikh, T.2    Ayele, M.3
  • 56
    • 79551632873 scopus 로고    scopus 로고
    • The cone-specific visual cycle
    • J.-S. Wang, and V.J. Kefalov The cone-specific visual cycle Prog Retin Eye Res 30 2 2011 115 128
    • (2011) Prog Retin Eye Res , vol.30 , Issue.2 , pp. 115-128
    • Wang, J.-S.1    Kefalov, V.J.2
  • 57
    • 0031255068 scopus 로고    scopus 로고
    • Mutations in RPE65 cause autosomal recessive childhood-onset severe retinal dystrophy
    • S.M. Gu, D.A. Thompson, C.R. Srikumari, and et al. Mutations in RPE65 cause autosomal recessive childhood-onset severe retinal dystrophy Nat Genet 17 2 1997 194 197
    • (1997) Nat Genet , vol.17 , Issue.2 , pp. 194-197
    • Gu, S.M.1    Thompson, D.A.2    Srikumari, C.R.3
  • 58
    • 0031252434 scopus 로고    scopus 로고
    • Mutations in RPE65 cause Leber's congenital amaurosis
    • F. Marlhens, C. Bareil, J.M. Griffoin, and et al. Mutations in RPE65 cause Leber's congenital amaurosis Nat Genet 17 2 1997 139 141
    • (1997) Nat Genet , vol.17 , Issue.2 , pp. 139-141
    • Marlhens, F.1    Bareil, C.2    Griffoin, J.M.3
  • 59
    • 0034735147 scopus 로고    scopus 로고
    • A homozygous deletion in RPE65 in a small Sardinian family with autosomal recessive retinal dystrophy
    • W.J. Poehner, M. Fossarello, A.L. Rapoport, and et al. A homozygous deletion in RPE65 in a small Sardinian family with autosomal recessive retinal dystrophy Mol Vis 6 2000 192 198
    • (2000) Mol Vis , vol.6 , pp. 192-198
    • Poehner, W.J.1    Fossarello, M.2    Rapoport, A.L.3
  • 60
    • 79955574258 scopus 로고    scopus 로고
    • Fundus albipunctatus associated with compound heterozygous mutations in RPE65
    • P. Schatz, M. Preising, B. Lorenz, B. Sander, M. Larsen, and T. Rosenberg Fundus albipunctatus associated with compound heterozygous mutations in RPE65 Ophthalmology 118 5 2011 888 894
    • (2011) Ophthalmology , vol.118 , Issue.5 , pp. 888-894
    • Schatz, P.1    Preising, M.2    Lorenz, B.3    Sander, B.4    Larsen, M.5    Rosenberg, T.6
  • 62
    • 77954620055 scopus 로고    scopus 로고
    • Leber congenital amaurosis due to RPE65 mutations and its treatment with gene therapy
    • A.V. Cideciyan Leber congenital amaurosis due to RPE65 mutations and its treatment with gene therapy Prog Retin Eye Res 29 5 2010 398 427
    • (2010) Prog Retin Eye Res , vol.29 , Issue.5 , pp. 398-427
    • Cideciyan, A.V.1
  • 63
    • 38549098447 scopus 로고    scopus 로고
    • Leber congenital amaurosis: Disease, genetics and therapy
    • E. Ahmed, and J. Loewenstein Leber congenital amaurosis: disease, genetics and therapy Semin Ophthalmol 23 1 2008 39 43
    • (2008) Semin Ophthalmol , vol.23 , Issue.1 , pp. 39-43
    • Ahmed, E.1    Loewenstein, J.2
  • 64
    • 0033118884 scopus 로고    scopus 로고
    • Retinal dystrophy of Swedish briard/briard-beagle dogs is due to a 4-bp deletion in RPE65
    • A. Veske, S.E. Nilsson, K. Narfstrom, and A. Gal Retinal dystrophy of Swedish briard/briard-beagle dogs is due to a 4-bp deletion in RPE65 Genomics 57 1 1999 57 61
    • (1999) Genomics , vol.57 , Issue.1 , pp. 57-61
    • Veske, A.1    Nilsson, S.E.2    Narfstrom, K.3    Gal, A.4
  • 65
    • 0032582425 scopus 로고    scopus 로고
    • Congenital stationary night blindness in the dog: Common mutation in the RPE65 gene indicates founder effect
    • G.D. Aguirre, V. Baldwin, S. Pearce-Kelling, K. Narfstrom, K. Ray, and G.M. Acland Congenital stationary night blindness in the dog: common mutation in the RPE65 gene indicates founder effect Mol Vis 4 1998 23
    • (1998) Mol Vis , vol.4 , pp. 23
    • Aguirre, G.D.1    Baldwin, V.2    Pearce-Kelling, S.3    Narfstrom, K.4    Ray, K.5    Acland, G.M.6
  • 66
    • 33745865867 scopus 로고    scopus 로고
    • Impacts of two point mutations of RPE65 from Leber's congenital amaurosis on the stability, subcellular localization and isomerohydrolase activity of RPE65
    • Y. Chen, G. Moiseyev, Y. Takahashi, and J.X. Ma Impacts of two point mutations of RPE65 from Leber's congenital amaurosis on the stability, subcellular localization and isomerohydrolase activity of RPE65 FEBS Lett 580 17 2006 4200 4204
    • (2006) FEBS Lett , vol.580 , Issue.17 , pp. 4200-4204
    • Chen, Y.1    Moiseyev, G.2    Takahashi, Y.3    Ma, J.X.4
  • 67
    • 11144356431 scopus 로고    scopus 로고
    • Leber congenital amaurosis: Comprehensive survey of the genetic heterogeneity, refinement of the clinical definition, and genotype-phenotype correlations as a strategy for molecular diagnosis
    • S. Hanein, I. Perrault, S. Gerber, and et al. Leber congenital amaurosis: comprehensive survey of the genetic heterogeneity, refinement of the clinical definition, and genotype-phenotype correlations as a strategy for molecular diagnosis Hum Mutat 23 4 2004 306 317
    • (2004) Hum Mutat , vol.23 , Issue.4 , pp. 306-317
    • Hanein, S.1    Perrault, I.2    Gerber, S.3
  • 68
    • 0032539851 scopus 로고    scopus 로고
    • Mutations in the RPE65 gene in patients with autosomal recessive retinitis pigmentosa or Leber congenital amaurosis
    • H. Morimura, G.A. Fishman, S.A. Grover, A.B. Fulton, E.L. Berson, and T.P. Dryja Mutations in the RPE65 gene in patients with autosomal recessive retinitis pigmentosa or Leber congenital amaurosis Proc Natl Acad Sci USA 95 6 1998 3088 3093
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.6 , pp. 3088-3093
    • Morimura, H.1    Fishman, G.A.2    Grover, S.A.3    Fulton, A.B.4    Berson, E.L.5    Dryja, T.P.6
  • 69
    • 67749097721 scopus 로고    scopus 로고
    • Predicting the pathogenicity of RPE65 mutations
    • A.R. Philp, M. Jin, S. Li, and et al. Predicting the pathogenicity of RPE65 mutations Hum Mutat 30 8 2009 1183 1188
    • (2009) Hum Mutat , vol.30 , Issue.8 , pp. 1183-1188
    • Philp, A.R.1    Jin, M.2    Li, S.3
  • 70
    • 36248964755 scopus 로고    scopus 로고
    • Leber congenital amaurosis - A model for efficient genetic testing of heterogeneous disorders: LXIV Edward Jackson Memorial Lecture
    • E.M. Stone Leber congenital amaurosis - a model for efficient genetic testing of heterogeneous disorders: LXIV Edward Jackson Memorial Lecture Am J Ophthalmol 144 6 2007 791 811
    • (2007) Am J Ophthalmol , vol.144 , Issue.6 , pp. 791-811
    • Stone, E.M.1
  • 71
    • 70149121705 scopus 로고    scopus 로고
    • Mutations that are a common cause of Leber congenital amaurosis in northern America are rare in southern India
    • P. Sundaresan, P. Vijayalakshmi, S. Thompson, A.C. Ko, J.H. Fingert, and E.M. Stone Mutations that are a common cause of Leber congenital amaurosis in northern America are rare in southern India Mol Vis 15 2009 1781 1787
    • (2009) Mol Vis , vol.15 , pp. 1781-1787
    • Sundaresan, P.1    Vijayalakshmi, P.2    Thompson, S.3    Ko, A.C.4    Fingert, J.H.5    Stone, E.M.6
  • 72
    • 84859476187 scopus 로고    scopus 로고
    • Novel RPE65 mutations associated with Leber congenital amaurosis in Chinese patients
    • F. Xu, Q. Dong, L. Liu, and et al. Novel RPE65 mutations associated with Leber congenital amaurosis in Chinese patients Mol Vis 18 2012 744 750
    • (2012) Mol Vis , vol.18 , pp. 744-750
    • Xu, F.1    Dong, Q.2    Liu, L.3
  • 73
    • 80053050730 scopus 로고    scopus 로고
    • A dominant mutation in RPE65 identified by whole-exome sequencing causes retinitis pigmentosa with choroidal involvement
    • S.J. Bowne, M.M. Humphries, L.S. Sullivan, and et al. A dominant mutation in RPE65 identified by whole-exome sequencing causes retinitis pigmentosa with choroidal involvement Eur J Hum Genet 19 10 2011 1074 1081
    • (2011) Eur J Hum Genet , vol.19 , Issue.10 , pp. 1074-1081
    • Bowne, S.J.1    Humphries, M.M.2    Sullivan, L.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.