메뉴 건너뛰기




Volumn 175, Issue 1, 2002, Pages 75-88

Evolution of the visual cycle: The role of retinoid-binding proteins

Author keywords

[No Author keywords available]

Indexed keywords

HORMONE BINDING PROTEIN; RETINOID; RETINOID BINDING PROTEIN; VISUAL PIGMENT;

EID: 0036802166     PISSN: 00220795     EISSN: None     Source Type: Journal    
DOI: 10.1677/joe.0.1750075     Document Type: Article
Times cited : (35)

References (103)
  • 2
    • 0033843425 scopus 로고    scopus 로고
    • Human interphotoreceptor matrix contains serum albumin and retinol-binding protein
    • Adler AJ & Edwards RB 2000 Human interphotoreceptor matrix contains serum albumin and retinol-binding protein. Experimental Eye Research 70 227-234.
    • (2000) Experimental Eye Research , vol.70 , pp. 227-234
    • Adler, A.J.1    Edwards, R.B.2
  • 3
    • 0023726059 scopus 로고
    • Comparison of proteins in the interphotoreceptor matrix of vertebrates
    • Adler AJ, Spencer SA, Heth CA & Schmidt SY 1988 Comparison of proteins in the interphotoreceptor matrix of vertebrates. Ophthalmic Research 20 275-285.
    • (1988) Ophthalmic Research , vol.20 , pp. 275-285
    • Adler, A.J.1    Spencer, S.A.2    Heth, C.A.3    Schmidt, S.Y.4
  • 4
    • 0031913261 scopus 로고    scopus 로고
    • Soluble expression in E. coli of a functional interphotoreceptor retinoid-binding protein module fused to thioredoxin: Correlation of vitamin A binding regions with conserved domains of C-terminal processing proteases
    • Baer CA, Retief JD, Van Niel E, Braiman MS & Gonzalez-Fernandez F 1998 Soluble expression in E. coli of a functional interphotoreceptor retinoid-binding protein module fused to thioredoxin: correlation of vitamin A binding regions with conserved domains of C-terminal processing proteases. Experimental Eye Research 66 249-262.
    • (1998) Experimental Eye Research , vol.66 , pp. 249-262
    • Baer, C.A.1    Retief, J.D.2    Van Niel, E.3    Braiman, M.S.4    Gonzalez-Fernandez, F.5
  • 5
    • 0034696581 scopus 로고    scopus 로고
    • Substrate recognition through a PDZ domain in tail-specific protease
    • Beebe KD, Shin J, Peng C, Chaudhury J, Khera J & Pei D 2000 Substrate recognition through a PDZ domain in tail-specific protease. Biochemistry 39 3149-3155.
    • (2000) Biochemistry , vol.39 , pp. 3149-3155
    • Beebe, K.D.1    Shin, J.2    Peng, C.3    Chaudhury, J.4    Khera, J.5    Pei, D.6
  • 6
    • 0030037645 scopus 로고    scopus 로고
    • Structure of 4-chlorobenzoyl coenzyme A dehalogenase determined to 1.8 Å resolution: An enzyme catalyst generated via adaptive mutation
    • Benning MM, Taylor KL, Liu R-Q, Yang G, Xiang H, Wesenberg G, Dunaway-Mariano D & Holden HM 1996 Structure of 4-chlorobenzoyl coenzyme A dehalogenase determined to 1.8 Å resolution: an enzyme catalyst generated via adaptive mutation. Biochemistry 35 8103-8109.
    • (1996) Biochemistry , vol.35 , pp. 8103-8109
    • Benning, M.M.1    Taylor, K.L.2    Liu, R.-Q.3    Yang, G.4    Xiang, H.5    Wesenberg, G.6    Dunaway-Mariano, D.7    Holden, H.M.8
  • 7
    • 0000284971 scopus 로고
    • Isomerization of all-trans retinoids to 11-cis retinoids in vitro
    • Bernstein PS, Law WC & Rando RR 1987 Isomerization of all-trans retinoids to 11-cis retinoids in vitro. PNAS 84 1849-1853.
    • (1987) PNAS , vol.84 , pp. 1849-1853
    • Bernstein, P.S.1    Law, W.C.2    Rando, R.R.3
  • 10
    • 0027741818 scopus 로고
    • The retinal pigment epithelium: A versatile partner in vision
    • Bok D 1993 The retinal pigment epithelium: a versatile partner in vision. Journal of Cell Science 17 189-195.
    • (1993) Journal of Cell Science , vol.17 , pp. 189-195
    • Bok, D.1
  • 11
    • 0021232986 scopus 로고
    • Immunocytochemical localization of cellular retinol binding protein in the rat retina
    • Bok D, Ong DE & Chytil F 1984 Immunocytochemical localization of cellular retinol binding protein in the rat retina. Investigative Ophthalmology and Visual Science 25 877-883.
    • (1984) Investigative Ophthalmology and Visual Science , vol.25 , pp. 877-883
    • Bok, D.1    Ong, D.E.2    Chytil, F.3
  • 13
    • 0003671264 scopus 로고
    • The Interphotoreceptor Matrix in Health and Disease
    • New York: Alan R Liss, Inc
    • Bridges CD & Adler AJ 1985 The Interphotoreceptor Matrix in Health and Disease. New York: Alan R Liss, Inc.
    • (1985)
    • Bridges, C.D.1    Adler, A.J.2
  • 14
    • 0020551985 scopus 로고
    • Immunocytochemical localization of two retinoid-binding proteins in vertebrate retina
    • Bunt-Milam AH & Saari JC 1983 Immunocytochemical localization of two retinoid-binding proteins in vertebrate retina. Journal of Cell Biology 97 703-712.
    • (1983) Journal of Cell Biology , vol.97 , pp. 703-712
    • Bunt-Milam, A.H.1    Saari, J.C.2
  • 17
    • 0026732864 scopus 로고
    • Promotion of the release of 11-cis-retinal from cultured retinal pigment epithelium by interphotoreceptor retinoid-binding protein
    • Carlson A & Bok D 1992 Promotion of the release of 11-cis-retinal from cultured retinal pigment epithelium by interphotoreceptor retinoid-binding protein. Biochemistry 31 9056-9062.
    • (1992) Biochemistry , vol.31 , pp. 9056-9062
    • Carlson, A.1    Bok, D.2
  • 18
    • 0032920347 scopus 로고    scopus 로고
    • Polarity of 11-cis retinal release from cultured retinal pigment epithelium
    • Carlson A & Bok D 1999 Polarity of 11-cis retinal release from cultured retinal pigment epithelium. Investigative Ophthalmology and Visual Science 40 533-537.
    • (1999) Investigative Ophthalmology and Visual Science , vol.40 , pp. 533-537
    • Carlson, A.1    Bok, D.2
  • 19
    • 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 1992 Interphotoreceptor retinoid-binding protein and alpha-tocopherol preserve the isomeric and oxidation state of retinol. Photochemistry and Photobiology 56 251-255.
    • (1992) Photochemistry and Photobiology , vol.56 , pp. 251-255
    • Crouch, R.K.1    Hazard, E.S.2    Lind, T.3    Wiggert, B.4    Chader, G.5    Corson, D.W.6
  • 20
    • 0033770905 scopus 로고    scopus 로고
    • Coordination between production and turnover of interphotoreceptor retinoid-binding protein in zebrafish
    • Cunningham LL & Gonzalez-Fernandez F 2000 Coordination between production and turnover of interphotoreceptor retinoid-binding protein in zebrafish. Investigative Ophthalmology and Visual Science 41 3590-3599.
    • (2000) Investigative Ophthalmology and Visual Science , vol.41 , pp. 3590-3599
    • Cunningham, L.L.1    Gonzalez-Fernandez, F.2
  • 21
    • 0033120920 scopus 로고    scopus 로고
    • Interphotoreceptor retinoid-binding protein (IRBP) is rapidly cleared from the Xenopus interphotoreceptor matrix
    • Cunningham LL, Yang L & Gonzalez-Fernandez F 1999 Interphotoreceptor retinoid-binding protein (IRBP) is rapidly cleared from the Xenopus interphotoreceptor matrix. Experimental Eye Research 68 399-410.
    • (1999) Experimental Eye Research , vol.68 , pp. 399-410
    • Cunningham, L.L.1    Yang, L.2    Gonzalez-Fernandez, F.3
  • 22
    • 0023856162 scopus 로고
    • Retinoid metabolism in cultured human retinal pigment epithelium
    • Das SR & Gouras P 1988 Retinoid metabolism in cultured human retinal pigment epithelium. Biochemical Journal 250 459-465.
    • (1988) Biochemical Journal , vol.250 , pp. 459-465
    • Das, S.R.1    Gouras, P.2
  • 24
    • 0001433667 scopus 로고
    • Chemistry of visual adaptation in the rat
    • Dowling JE 1960 Chemistry of visual adaptation in the rat. Nature 168 114-118.
    • (1960) Nature , vol.168 , pp. 114-118
    • Dowling, J.E.1
  • 27
    • 0029791410 scopus 로고    scopus 로고
    • Crystal structure of enoyl-coenzyme A (CoA) hydratase at 2.5 Å resolution: A spiral fold defines the CoA-binding pocket
    • Engel CK, Mathieu M, Zeelen JP, Hiltunen JK & Wierenga RK 1996 Crystal structure of enoyl-coenzyme A (CoA) hydratase at 2.5 Å resolution: a spiral fold defines the CoA-binding pocket. EMBO Journal 15 5135-5145.
    • (1996) EMBO Journal , vol.15 , pp. 5135-5145
    • Engel, C.K.1    Mathieu, M.2    Zeelen, J.P.3    Hiltunen, J.K.4    Wierenga, R.K.5
  • 28
    • 0034441289 scopus 로고    scopus 로고
    • Photosensitized light-induced damage of IRBP (interphotoreceptor retinoid-binding protein): Effects on binding properties
    • Fedorovich IB, Semenova EM, Grant K, Converse CA & Ostrovsky MA 2000 Photosensitized light-induced damage of IRBP (interphotoreceptor retinoid-binding protein): effects on binding properties. Current Eye Research 21 975-980.
    • (2000) Current Eye Research , vol.21 , pp. 975-980
    • Fedorovich, I.B.1    Semenova, E.M.2    Grant, K.3    Converse, C.A.4    Ostrovsky, M.A.5
  • 30
    • 0023886083 scopus 로고
    • IRBP-like proteins in the eyes of six cephalopod species - Immunochemical relationship to vertebrate interstitial retinol-binding protein (IRBP) and cephalopod retinal-binding protein
    • Fong SL, Lee PG, Ozaki K, Hara R, Hara T & Bridges CD 1988 IRBP-like proteins in the eyes of six cephalopod species - immunochemical relationship to vertebrate interstitial retinol-binding protein (IRBP) and cephalopod retinal-binding protein. Vision Research 28 563-573.
    • (1988) Vision Research , vol.28 , pp. 563-573
    • Fong, S.L.1    Lee, P.G.2    Ozaki, K.3    Hara, R.4    Hara, T.5    Bridges, C.D.6
  • 32
    • 0014151041 scopus 로고
    • Early receptor potential of the isolated frog (Rana pipiens) retina
    • Goldstein EB 1967 Early receptor potential of the isolated frog (Rana pipiens) retina. Vision Research 7 837-845.
    • (1967) Vision Research , vol.7 , pp. 837-845
    • Goldstein, E.B.1
  • 33
    • 0014860056 scopus 로고
    • Cone pigment regeneration in the isolated frog retina
    • Goldstein EB 1970 Cone pigment regeneration in the isolated frog retina. Vision Research 10 1065-1068.
    • (1970) Vision Research , vol.10 , pp. 1065-1068
    • Goldstein, E.B.1
  • 34
    • 0015597662 scopus 로고
    • Regeneration of the green-rod pigment in the isolated frog retina
    • Goldstein EB & Wolf BM 1973 Regeneration of the green-rod pigment in the isolated frog retina. Vision Research 13 527-534.
    • (1973) Vision Research , vol.13 , pp. 527-534
    • Goldstein, E.B.1    Wolf, B.M.2
  • 36
    • 0035001384 scopus 로고    scopus 로고
    • Studies of vitamin A metabolism in mouse model systems
    • Gottesman ME, Quadro L & Blaner WS 2001 Studies of vitamin A metabolism in mouse model systems. Bioessays 23 409-419.
    • (2001) Bioessays , vol.23 , pp. 409-419
    • Gottesman, M.E.1    Quadro, L.2    Blaner, W.S.3
  • 38
    • 0026012251 scopus 로고
    • Sequestration of basic fibroblast growth factor in the primate retinal interphotoreceptor matrix
    • Hageman GS, Kirchoff-Rempe MA, Lewis GP, Fisher SK & Anderson DH 1991 Sequestration of basic fibroblast growth factor in the primate retinal interphotoreceptor matrix. PNAS 88 6706-6710.
    • (1991) PNAS , vol.88 , pp. 6706-6710
    • Hageman, G.S.1    Kirchoff-Rempe, M.A.2    Lewis, G.P.3    Fisher, S.K.4    Anderson, D.H.5
  • 40
    • 0342907036 scopus 로고
    • Isomerization of retinal catalysed by retinochrome in the light
    • Hara T & Hara R 1973 Isomerization of retinal catalysed by retinochrome in the light. Nature New Biology 242 39-43.
    • (1973) Nature New Biology , vol.242 , pp. 39-43
    • Hara, T.1    Hara, R.2
  • 41
    • 0017196401 scopus 로고
    • Distribution of rhodopsin and retinochrome in the squid retina
    • Hara T & Hara R 1976 Distribution of rhodopsin and retinochrome in the squid retina. Journal of General Physiology 67 791-805.
    • (1976) Journal of General Physiology , vol.67 , pp. 791-805
    • Hara, T.1    Hara, R.2
  • 42
    • 0025011565 scopus 로고
    • Cloning and nucleotide sequence of cDNA for retinochrome, retinal photoisomerase from the squid retina
    • Hara-Nishimura I, Matsumoto T, Mori H, Nishimura M, Hara R & Hara T 1990 Cloning and nucleotide sequence of cDNA for retinochrome, retinal photoisomerase from the squid retina. FEBS Letters 271 106-110.
    • (1990) FEBS Letters , vol.271 , pp. 106-110
    • Hara-Nishimura, I.1    Matsumoto, T.2    Mori, H.3    Nishimura, M.4    Hara, R.5    Hara, T.6
  • 43
    • 0027425382 scopus 로고
    • Amino acid sequence surrounding the retinal-binding site in retinochrome of the squid, Todarodes pacificus
    • Hara-Nishimura I, Kondo M, Nishimura M, Hara R & Hara T 1993a Amino acid sequence surrounding the retinal-binding site in retinochrome of the squid, Todarodes pacificus. FEBS Letters 335 94-98.
    • (1993) FEBS Letters , vol.335 , pp. 94-98
    • Hara-Nishimura, I.1    Kondo, M.2    Nishimura, M.3    Hara, R.4    Hara, T.5
  • 44
    • 0027406791 scopus 로고
    • Cloning and nucleotide sequence of cDNA for rhodopsin of the squid Todarodes pacificus
    • Hara-Nishimura I, Kondo M, Nishimura M, Hara R & Hara T 1993b Cloning and nucleotide sequence of cDNA for rhodopsin of the squid Todarodes pacificus. FEBS Letters 317 5-11.
    • (1993) FEBS Letters , vol.317 , pp. 5-11
    • Hara-Nishimura, I.1    Kondo, M.2    Nishimura, M.3    Hara, R.4    Hara, T.5
  • 45
    • 0023002413 scopus 로고
    • Photoreceptor array of the dipteran retina
    • Hardie RC 1986 Photoreceptor array of the dipteran retina. Trends in Neurosciences 9 419-423.
    • (1986) Trends in Neurosciences , vol.9 , pp. 419-423
    • Hardie, R.C.1
  • 47
    • 0025017465 scopus 로고
    • Photoreceptor survival-promoting activity in interphotoreceptor matrix preparations: Characterization and partial purification
    • Hewitt AT, Lindsey JD, Carbott D & Adler R 1990 Photoreceptor survival-promoting activity in interphotoreceptor matrix preparations: characterization and partial purification. Experimental Eye Research 50 79-88.
    • (1990) Experimental Eye Research , vol.50 , pp. 79-88
    • Hewitt, A.T.1    Lindsey, J.D.2    Carbott, D.3    Adler, R.4
  • 48
    • 0024494201 scopus 로고
    • Mechanism of vitamin A movement between rod outer segments, interphotoreceptor retinoid-binding protein, and liposomes
    • Ho MT, Massey JB, Pownall HJ, Anderson RE & Hollyfield JG 1989 Mechanism of vitamin A movement between rod outer segments, interphotoreceptor retinoid-binding protein, and liposomes. Journal of Biological Chemistry 264 928-935.
    • (1989) Journal of Biological Chemistry , 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
  • 49
    • 0024583935 scopus 로고
    • Retinal attachment to the pigment epithelium. Linkage through an extracellular sheath surrounding cone photoreceptors
    • Hollyfield JG, Varner HH, Rayborn ME & Osterfeld AM 1989 Retinal attachment to the pigment epithelium. Linkage through an extracellular sheath surrounding cone photoreceptors. Retina 9 59-68.
    • (1989) Retina , vol.9 , pp. 59-68
    • Hollyfield, J.G.1    Varner, H.H.2    Rayborn, M.E.3    Osterfeld, A.M.4
  • 50
    • 0031937262 scopus 로고    scopus 로고
    • Hyaluronan in the Interphotoreceptor matrix of the eye - Species differences in content distribution, ligand binding and degradation
    • Hollyfield JG, Rayborn ME, Tammi M & Tammi R 1998 Hyaluronan in the Interphotoreceptor matrix of the eye - species differences in content distribution, ligand binding and degradation. Experimental Eye Research 66 241-248.
    • (1998) Experimental Eye Research , vol.66 , pp. 241-248
    • Hollyfield, J.G.1    Rayborn, M.E.2    Tammi, M.3    Tammi, R.4
  • 51
    • 0032731741 scopus 로고    scopus 로고
    • Hyaluronan and the functional organization of the interphotoreceptor matrix
    • Hollyfield JG 1999 Hyaluronan and the functional organization of the interphotoreceptor matrix. Investigative Ophthalmology and Visual Science 40 2767-2769.
    • (1999) Investigative Ophthalmology and Visual Science , vol.40 , pp. 2767-2769
    • Hollyfield, J.G.1
  • 52
    • 0028387340 scopus 로고
    • Movement of retinal along cone and rod photoreceptors
    • Jin J, Jones GJ & Cornwall MC 1994 Movement of retinal along cone and rod photoreceptors. Visual Neuroscience 11 389-399.
    • (1994) Visual Neuroscience , vol.11 , pp. 389-399
    • Jin, J.1    Jones, G.J.2    Cornwall, M.C.3
  • 53
    • 0027441825 scopus 로고
    • Visual pigment bleaching in isolated salamander retinal cones: Microspectrophotometry and light adaptation
    • Jones GJ, Fein A, MacNichol EF & Cornwall MC 1993 Visual pigment bleaching in isolated salamander retinal cones: microspectrophotometry and light adaptation. Journal of General Physiology 102 483-502.
    • (1993) Journal of General Physiology , vol.102 , pp. 483-502
    • Jones, G.J.1    Fein, A.2    MacNichol, E.F.3    Cornwall, M.C.4
  • 54
    • 0032702201 scopus 로고    scopus 로고
    • Expression and characterization of the IPM 150 gene (IMPG1) product, a novel human photoreceptor cell-associated chondroitin-sulfate proteoglycan
    • Kuehn MH & Hageman GS 1999 Expression and characterization of the IPM 150 gene (IMPG1) product, a novel human photoreceptor cell-associated chondroitin-sulfate proteoglycan. Matrix Biology 18 509-518.
    • (1999) Matrix Biology , vol.18 , pp. 509-518
    • Kuehn, M.H.1    Hageman, G.S.2
  • 55
    • 0028912640 scopus 로고
    • Mice deficient in cellular retinoic acid binding protein II (CRABPII) or in both CRABPI and CRABPII are essentially normal
    • Lampron C, Rochette-Egly C, Gorry P, Dolle P, Mark M, Lufkin T, LeMeur M & Chambon P 1995 Mice deficient in cellular retinoic acid binding protein II (CRABPII) or in both CRABPI and CRABPII are essentially normal. Development 121 539-548.
    • (1995) Development , vol.121 , pp. 539-548
    • Lampron, C.1    Rochette-Egly, C.2    Gorry, P.3    Dolle, P.4    Mark, M.5    Lufkin, T.6    LeMeur, M.7    Chambon, P.8
  • 58
    • 0013773201 scopus 로고
    • Sensitive low-light-level microspectrophotometer: Detection of photosensitive pigments of retinal cones
    • Liebman PA & Entine G 1964 Sensitive low-light-level microspectrophotometer: detection of photosensitive pigments of retinal cones. Journal of the Optical Society of America 54 1451-1459.
    • (1964) Journal of the Optical Society of America , vol.54 , pp. 1451-1459
    • Liebman, P.A.1    Entine, G.2
  • 59
    • 0036156095 scopus 로고    scopus 로고
    • Crystal structure of the functional unit of interphotoreceptor retinoid binding protein
    • Loew A & Gonzalez-Fernandez F 2002 Crystal structure of the functional unit of interphotoreceptor retinoid binding protein. Structure 10 43-49.
    • (2002) Structure , vol.10 , pp. 43-49
    • Loew, A.1    Gonzalez-Fernandez, F.2
  • 60
    • 0034775371 scopus 로고    scopus 로고
    • The functional unit of interphotorecptor retinoid-binding protein (IRBP) - Purification, characterization and preliminary crystallographic analysis
    • Loew A, Baer CA & Gonzalez-Fernandez F 2001 The functional unit of interphotorecptor retinoid-binding protein (IRBP) - purification, characterization and preliminary crystallographic analysis. Experimental Eye Research 73 257-264.
    • (2001) Experimental Eye Research , vol.73 , pp. 257-264
    • Loew, A.1    Baer, C.A.2    Gonzalez-Fernandez, F.3
  • 63
    • 0034982559 scopus 로고    scopus 로고
    • Confronting complexity: The interlink of phototransduction and retinoid metabolism in the vertebrate retina
    • McBee JK, Palczewski K, Baehr W & Pepperberg DR 2001a Confronting complexity: the interlink of phototransduction and retinoid metabolism in the vertebrate retina. Progress in Retinal and Eye Research 20 469-529.
    • (2001) Progress in Retinal and Eye Research , vol.20 , pp. 469-529
    • McBee, J.K.1    Palczewski, K.2    Baehr, W.3    Pepperberg, D.R.4
  • 66
    • 0030471289 scopus 로고    scopus 로고
    • The interphotoreceptor matrix, a space in sight
    • Mieziewska K 1996 The interphotoreceptor matrix, a space in sight. Microscopy Research and Technique 35 463-471.
    • (1996) Microscopy Research and Technique , vol.35 , pp. 463-471
    • Mieziewska, K.1
  • 67
    • 0032528950 scopus 로고    scopus 로고
    • The crystal structure of dienoyl-CoA isomerase at 1.5 Å resolution reveals the importance of aspartate and glutamate sidechains for catalysis
    • Modis Y, Filppula S, Novikov DK, Norledge B, Hiltunen JK & Wierenga RK 1998 The crystal structure of dienoyl-CoA isomerase at 1.5 Å resolution reveals the importance of aspartate and glutamate sidechains for catalysis. Structure 6 957-970.
    • (1998) Structure , vol.6 , pp. 957-970
    • Modis, Y.1    Filppula, S.2    Novikov, D.K.3    Norledge, B.4    Hiltunen, J.K.5    Wierenga, R.K.6
  • 68
    • 0026565591 scopus 로고
    • Immunocytochemical localization of retinal binding protein in the octopus retina: A shuttle protein for 11-cis retinal
    • Molina TM, Torres SC, Flores A, Hara T, Hara R & Robles LJ 1992 Immunocytochemical localization of retinal binding protein in the octopus retina: a shuttle protein for 11-cis retinal. Experimental Eye Research 54 83-90.
    • (1992) Experimental Eye Research , vol.54 , pp. 83-90
    • Molina, T.M.1    Torres, S.C.2    Flores, A.3    Hara, T.4    Hara, R.5    Robles, L.J.6
  • 69
    • 0033028464 scopus 로고    scopus 로고
    • How vertebrate and invertebrate visual pigments differ in their mechanism of photoactivation
    • Nakagawa M, Iwasa T, Kikkawa S, Tsuda M & Ebrey TG 1999 How vertebrate and invertebrate visual pigments differ in their mechanism of photoactivation. PNAS 96 6189-6192.
    • (1999) PNAS , vol.96 , pp. 6189-6192
    • Nakagawa, M.1    Iwasa, T.2    Kikkawa, S.3    Tsuda, M.4    Ebrey, T.G.5
  • 70
    • 0011121877 scopus 로고    scopus 로고
    • Predicted structure, function and evolution of the repeated domain present in interphotoreceptor binding protein (IRBP) and its homologs
    • (Abstract)
    • Nickerson JM, Goodman M, Lin ZY, Czelusniak J & Mian IS 1997 Predicted structure, function and evolution of the repeated domain present in interphotoreceptor binding protein (IRBP) and its homologs. Investigative Ophthalmology and Visual Science 38 S3 (Abstract).
    • (1997) Investigative Ophthalmology and Visual Science , vol.38
    • Nickerson, J.M.1    Goodman, M.2    Lin, Z.Y.3    Czelusniak, J.4    Mian, I.S.5
  • 71
    • 0029682036 scopus 로고    scopus 로고
    • Eye ancestry: Old genes for new eyes
    • Nilsson DE 1996 Eye ancestry: old genes for new eyes. Current Biology 6 39-42.
    • (1996) Current Biology , vol.6 , pp. 39-42
    • Nilsson, D.E.1
  • 72
  • 73
    • 0025175698 scopus 로고
    • Interphotoreceptor retinoid-binding protein promotes rhodopsin regeneration in toad photoreceptors
    • Okajima TI, Pepperberg DR, Ripps H, Wiggert B & Chader GJ 1990 Interphotoreceptor retinoid-binding protein promotes rhodopsin regeneration in toad photoreceptors. PNAS 87 6907-6911.
    • (1990) PNAS , vol.87 , pp. 6907-6911
    • Okajima, T.I.1    Pepperberg, D.R.2    Ripps, H.3    Wiggert, B.4    Chader, G.J.5
  • 74
    • 0023192062 scopus 로고
    • Isolation and characterization of a retinal-binding protein from the squid retina
    • Ozaki K, Terakita A, Hara R & Hara T 1987 Isolation and characterization of a retinal-binding protein from the squid retina. Vision Research 27 1057-1070.
    • (1987) Vision Research , vol.27 , pp. 1057-1070
    • Ozaki, K.1    Terakita, A.2    Hara, R.3    Hara, T.4
  • 75
    • 0028107101 scopus 로고
    • Molecular characterization and functional expression of squid retinal-binding protein. A novel species of hydrophobic ligand-binding protein
    • Ozaki K, Terakita A, Ozaki M, Hara R, Hara T, Hara-Nishimura I, Mori H & Nishimura M 1994 Molecular characterization and functional expression of squid retinal-binding protein. A novel species of hydrophobic ligand-binding protein. Journal of Biological Chemistry 269 3838-3845.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 3838-3845
    • Ozaki, K.1    Terakita, A.2    Ozaki, M.3    Hara, R.4    Hara, T.5    Hara-Nishimura, I.6    Mori, H.7    Nishimura, M.8
  • 76
    • 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, Chen J, Liou GI & Saari JC 1999 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 12012-12019.
    • (1999) Biochemistry , vol.38 , pp. 12012-12019
    • Palczewski, K.1    Van Hooser, J.P.2    Garwin, G.G.3    Chen, J.4    Liou, G.I.5    Saari, J.C.6
  • 77
    • 0027563554 scopus 로고
    • Interphotoreceptor retinoid-binding protein (IRBP). Molecular biology and physiological role in the visual cycle of rhodopsin
    • Pepperberg DR, Okajima TL, Wiggert B, Ripps H, Crouch RK & Chader GJ 1993 Interphotoreceptor retinoid-binding protein (IRBP). Molecular biology and physiological role in the visual cycle of rhodopsin. Molecular Neurobiology 7 61-85.
    • (1993) Molecular Neurobiology , vol.7 , pp. 61-85
    • Pepperberg, D.R.1    Okajima, T.L.2    Wiggert, B.3    Ripps, H.4    Crouch, R.K.5    Chader, G.J.6
  • 78
    • 0026502842 scopus 로고
    • The presence of neutral metalloproteolytic activity and metalloproteinase inhibitors in the interphotoreceptor matrix
    • Plantner JJ 1992 The presence of neutral metalloproteolytic activity and metalloproteinase inhibitors in the interphotoreceptor matrix. Current Eye Research 11 91-101.
    • (1992) Current Eye Research , vol.11 , pp. 91-101
    • Plantner, J.J.1
  • 79
    • 0031055372 scopus 로고    scopus 로고
    • Evidence for PDZ domains in bacteria, yeast, and plants
    • Ponting CP 2001 Evidence for PDZ domains in bacteria, yeast, and plants. Protein Science 6 464-468.
    • (2001) Protein Science , vol.6 , pp. 464-468
    • Ponting, C.P.1
  • 83
    • 0025828834 scopus 로고
    • New insights into the visual cycle
    • Eds. NN Osborne & GJ Chader. Oxford: Pergamon Press
    • Rando RR, Bernstein PS & Barry RJ 1991 New insights into the visual cycle. In Progress in Retinal Research, pp 161-178. Eds NN Osborne & GJ Chader. Oxford: Pergamon Press.
    • (1991) Progress in Retinal Research , pp. 161-178
    • Rando, R.R.1    Bernstein, P.S.2    Barry, R.J.3
  • 85
    • 0035783719 scopus 로고    scopus 로고
    • The visual cycle - A twist in the tale
    • Rjpps H 2001 The visual cycle - a twist in the tale. Progress in Brain Research 131 335-350.
    • (2001) Progress in Brain Research , vol.131 , pp. 335-350
    • Rjpps, H.1
  • 86
    • 0034121428 scopus 로고    scopus 로고
    • The rhodopsin cycle is preserved in IRBP 'knockout' mice despite abnormalities in retinal structure and function
    • Ripps H, Peachey NS, Xu X, Nozell SE, Smith SB & Liou GI 2000 The rhodopsin cycle is preserved in IRBP 'knockout' mice despite abnormalities in retinal structure and function. Visual Neuroscience 17 97-105.
    • (2000) Visual Neuroscience , vol.17 , pp. 97-105
    • Ripps, H.1    Peachey, N.S.2    Xu, X.3    Nozell, S.E.4    Smith, S.B.5    Liou, G.I.6
  • 88
    • 0026440992 scopus 로고
    • Inactivation of MyoD in mice leads to up-regulation of the myogenic HLH gene Myf-5 and results in apparently normal muscle development
    • Rudnicki MA, Braun T, Hinuma S & Jaenisch R 1992 Inactivation of MyoD in mice leads to up-regulation of the myogenic HLH gene Myf-5 and results in apparently normal muscle development. Cell 71 383-390.
    • (1992) Cell , vol.71 , pp. 383-390
    • Rudnicki, M.A.1    Braun, T.2    Hinuma, S.3    Jaenisch, R.4
  • 89
    • 0002463912 scopus 로고
    • Retinoids in photosensitive systems
    • Eds MB Sporn, AB Roberts & DS Goodman. New York: Raven Press
    • Saari JC 1994 Retinoids in photosensitive systems. In The Retinoids: Biology, Chemistry and Medicine, pp 351-385. Eds MB Sporn, AB Roberts & DS Goodman. New York: Raven Press.
    • (1994) The Retinoids: Biology, Chemistry and Medicine , pp. 351-385
    • Saari, J.C.1
  • 90
    • 0033960296 scopus 로고    scopus 로고
    • Biochemistry of visual pigment regeneration: The Friedenwald lecture
    • Saari JC 2000 Biochemistry of visual pigment regeneration: the Friedenwald lecture. Investigative Ophthalmology and Visual Science 41 337-348.
    • (2000) Investigative Ophthalmology and Visual Science , vol.41 , pp. 337-348
    • Saari, J.C.1
  • 91
    • 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 1982 Identification of the endogenous retinoids associated with three cellular retinoid-binding proteins from bovine retina and retinal pigment epithelium. Journal of Biological Chemistry 257 13329-13333.
    • (1982) Journal of Biological Chemistry , vol.257 , pp. 13329-13333
    • Saari, J.C.1    Bredberg, L.2    Garwin, G.G.3
  • 92
    • 0021733920 scopus 로고
    • Properties and immunocytochemical localization of three retinoid-binding proteins from bovine retina
    • Saari JC, Bunt-Milam AH, Bredberg DL & Garwin GG 1984 Properties and immunocytochemical localization of three retinoid-binding proteins from bovine retina. Vision Research 24 1595-1603.
    • (1984) Vision Research , vol.24 , pp. 1595-1603
    • Saari, J.C.1    Bunt-Milam, A.H.2    Bredberg, D.L.3    Garwin, G.G.4
  • 93
    • 0028211275 scopus 로고
    • Control of substrate flow at a branch in the visual cycle
    • Saari JC, Bredberg DL & Noy N 1994 Control of substrate flow at a branch in the visual cycle. Biochemistry 33 3106-3112.
    • (1994) Biochemistry , vol.33 , pp. 3106-3112
    • Saari, J.C.1    Bredberg, D.L.2    Noy, N.3
  • 94
    • 0035046365 scopus 로고    scopus 로고
    • Visual cycle impairment in cellular retinaldehyde binding protein (CRALBP) knockout mice results in delayed dark adaptation
    • Saari JC, Nawrot M, Kennedy BN, Garwin GG, Hurley JB, Huang J, Possin DE & Crabb JW 2001 Visual cycle impairment in cellular retinaldehyde binding protein (CRALBP) knockout mice results in delayed dark adaptation. Neuron 29 739-748.
    • (2001) Neuron , vol.29 , pp. 739-748
    • Saari, J.C.1    Nawrot, M.2    Kennedy, B.N.3    Garwin, G.G.4    Hurley, J.B.5    Huang, J.6    Possin, D.E.7    Crabb, J.W.8
  • 96
    • 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 1999 Preferential release of 11-cis-retinol from retinal pigment epithelial cells in the presence of cellular retinaldehyde-binding protein. Journal of Biological Chemistry 274 8577-8585.
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 8577-8585
    • Stecher, H.1    Gelb, M.H.2    Saari, J.C.3    Palczewski, K.4
  • 97
    • 0026446915 scopus 로고
    • Rhodopsin regeneration in the normal and in the detached/replaced retina of the skate
    • Sun Y & Ripps H 1992 Rhodopsin regeneration in the normal and in the detached/replaced retina of the skate. Experimental Eye Research 55 679-689.
    • (1992) Experimental Eye Research , vol.55 , pp. 679-689
    • Sun, Y.1    Ripps, H.2
  • 98
    • 0024362506 scopus 로고
    • Retinal-binding protein as a shuttle for retinal in the rhodopsin-retinochrome system of the squid visual cells
    • Terakita A, Hara R & Hara T 1989 Retinal-binding protein as a shuttle for retinal in the rhodopsin-retinochrome system of the squid visual cells. Vision Research 29 639-652.
    • (1989) Vision Research , vol.29 , pp. 639-652
    • Terakita, A.1    Hara, R.2    Hara, T.3
  • 99
    • 4243389139 scopus 로고    scopus 로고
    • Identification of a new pathway for retinol isomerization in cone-dominant ground squirrel and chicken retinas
    • (ARVO abstract)
    • Travis GH, Radu RA, Lee J & Mata NL 2002 Identification of a new pathway for retinol isomerization in cone-dominant ground squirrel and chicken retinas. Investigative Ophthalmology and Visual Science B592 (ARVO abstract).
    • (2002) Investigative Ophthalmology and Visual Science
    • Travis, G.H.1    Radu, R.A.2    Lee, J.3    Mata, N.L.4
  • 100
    • 0002386911 scopus 로고
    • Carotenoids and the vitamin A cycle in vision
    • Wald G 1934 Carotenoids and the vitamin A cycle in vision. Nature 134 65.
    • (1934) Nature , vol.134 , pp. 65
    • Wald, G.1
  • 101
    • 0027738464 scopus 로고
    • The MyoD family and myogenesis: Redundancy, networks, and thresholds
    • Weintraub H 1993 The MyoD family and myogenesis: redundancy, networks, and thresholds. Cell 75 1241-1244.
    • (1993) Cell , vol.75 , pp. 1241-1244
    • Weintraub, H.1
  • 102
    • 0032539650 scopus 로고    scopus 로고
    • Regulation of isomerohydrolase activity in the visual cycle
    • Winston A & Rando RR. 1998 Regulation of isomerohydrolase activity in the visual cycle. Biochemistry 17 2044-2055.
    • (1998) Biochemistry , vol.17 , pp. 2044-2055
    • Winston, A.1    Rando, R.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.