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Volumn 8, Issue , 2002, Pages 171-184

Expressed sequence tag analysis of adult human lens for the NEIBank Project: Over 2000 non-redundant transcripts, novel genes and splice variants

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA ENOLASE; APOPTOSIS INHIBITOR; CARBONYL REDUCTASE; COMPLEMENTARY DNA; CRYSTALLIN; CYTOSKELETON PROTEIN; ENOLASE; GLUTAMATE AMMONIA LIGASE; GLUTATHIONE SYNTHASE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; GROWTH FACTOR; MEMBRANE PROTEIN; MESSENGER RNA; NUCLEIC ACID BINDING PROTEIN; PROSTAGLANDIN D SYNTHASE; PROTEINASE; SUPEROXIDE DISMUTASE; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 0347579854     PISSN: 10900535     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (89)

References (114)
  • 2
    • 0035281572 scopus 로고    scopus 로고
    • A large-scale in situ screen provides molecular evidence for the induction of eye anterior segment structures by the developing lens
    • Thut CJ, Rountree RB, Hwa M, Kingsley DM. A large-scale in situ screen provides molecular evidence for the induction of eye anterior segment structures by the developing lens. Dev Biol 2001; 231:63-76.
    • (2001) Dev. Biol. , vol.231 , pp. 63-76
    • Thut, C.J.1    Rountree, R.B.2    Hwa, M.3    Kingsley, D.M.4
  • 3
    • 0034656096 scopus 로고    scopus 로고
    • The lens organizes the anterior segment: Specification of neural crest cell differentiation in the avian eye
    • Beebe DC, Coats JM. The lens organizes the anterior segment: specification of neural crest cell differentiation in the avian eye. Dev Biol 2000; 220:424-31.
    • (2000) Dev. Biol. , vol.220 , pp. 424-431
    • Beebe, D.C.1    Coats, J.M.2
  • 4
    • 0026800666 scopus 로고
    • Embryonic lens induction: Shedding light on vertebrate tissue determination
    • Grainger RM. Embryonic lens induction: shedding light on vertebrate tissue determination. Trends Genet 1992; 8:349-55.
    • (1992) Trends Genet. , vol.8 , pp. 349-355
    • Grainger, R.M.1
  • 5
    • 0019786296 scopus 로고
    • Lens differentiation in vertebrates. A review of cellular and molecular features
    • Piatigorsky J. Lens differentiation in vertebrates. A review of cellular and molecular features. Differentiation 1981; 19:134-53.
    • (1981) Differentiation , vol.19 , pp. 134-153
    • Piatigorsky, J.1
  • 6
    • 0029799473 scopus 로고    scopus 로고
    • LP2, a differentiation-associated lipid-binding protein expressed in bovine lens
    • Jaworski C, Wistow G. LP2, a differentiation-associated lipid-binding protein expressed in bovine lens. Biochem J 1996; 320:49-54.
    • (1996) Biochem. J. , vol.320 , pp. 49-54
    • Jaworski, C.1    Wistow, G.2
  • 7
    • 23444441161 scopus 로고
    • Pax-6 is first expressed in a region of ectoderm anterior to the early neural plate: Implications for stepwise determination of the lens
    • Li HS, Yang JM, Jacobson RD, Pasko D, Sundin O. Pax-6 is first expressed in a region of ectoderm anterior to the early neural plate: implications for stepwise determination of the lens. Dev Biol 1994; 162:181-94.
    • (1994) Dev. Biol. , vol.162 , pp. 181-194
    • Li, H.S.1    Yang, J.M.2    Jacobson, R.D.3    Pasko, D.4    Sundin, O.5
  • 8
    • 0029317340 scopus 로고
    • From lens regeneration in the newt to in-vitro transdifferentiation of vertebrate pigmented epithelial cells
    • Kodama R, Eguchi G. From lens regeneration in the newt to in-vitro transdifferentiation of vertebrate pigmented epithelial cells. Semin Cell Biol 1995; 6:143-9.
    • (1995) Semin. Cell Biol. , vol.6 , pp. 143-149
    • Kodama, R.1    Eguchi, G.2
  • 9
    • 0000145042 scopus 로고
    • The lens: Development, proteins, metabolism and cataract
    • Davson H, editor. 3rd ed. Orlando (FL): Academic Press
    • Harding JJ, Crabbe MJC. The lens: Development, proteins, metabolism and cataract. In: Davson H, editor. The Eye, vol 1B. 3rd ed. Orlando (FL): Academic Press; 1984. p. 207-492.
    • (1984) The Eye , vol.1 B , pp. 207-492
    • Harding, J.J.1    Crabbe, M.J.C.2
  • 11
    • 0033851649 scopus 로고    scopus 로고
    • Minireview: Apoptosis as seen through a lens
    • Wride MA. Minireview: apoptosis as seen through a lens. Apoptosis 2000; 5:203-9.
    • (2000) Apoptosis , vol.5 , pp. 203-209
    • Wride, M.A.1
  • 13
    • 0031894491 scopus 로고    scopus 로고
    • A role for caspases in lens fiber differentiation
    • Ishizaki Y, Jacobson MD, Raff MC. A role for caspases in lens fiber differentiation. J Cell Biol 1998; 140:153-8.
    • (1998) J. Cell Biol. , vol.140 , pp. 153-158
    • Ishizaki, Y.1    Jacobson, M.D.2    Raff, M.C.3
  • 14
    • 0032946425 scopus 로고    scopus 로고
    • Lens fibre cell differentiation - A link with apoptosis?
    • Dahm R. Lens fibre cell differentiation - A link with apoptosis? Ophthalmic Res 1999; 31:163-83.
    • (1999) Ophthalmic Res. , vol.31 , pp. 163-183
    • Dahm, R.1
  • 15
    • 0026444633 scopus 로고
    • Embryology of the eye and its adnexae
    • Barishak YR. Embryology of the eye and its adnexae. Dev Ophthalmol 1992; 24:1-142.
    • (1992) Dev. Ophthalmol. , vol.24 , pp. 1-142
    • Barishak, Y.R.1
  • 16
    • 0036979798 scopus 로고    scopus 로고
    • A project for ocular bioinformatics: NEIBank
    • Wistow G. A project for ocular bioinformatics: NEIBank. Mol Vis 2002; 8:161-3 .
    • (2002) Mol. Vis. , vol.8 , pp. 161-163
    • Wistow, G.1
  • 17
    • 0346949024 scopus 로고
    • mRNA isolation for high quality cDNA
    • Simms D. mRNA isolation for high quality cDNA. Focus 1995; 17:39-42.
    • (1995) Focus , vol.17 , pp. 39-42
    • Simms, D.1
  • 18
    • 0026038362 scopus 로고
    • Plasmid transformation of Escherichia coli and other bacteria
    • Hanahan D, Jessee J, Bloom FR. Plasmid transformation of Escherichia coli and other bacteria. Methods Enzymol 1991; 204:63-113.
    • (1991) Methods Enzymol. , vol.204 , pp. 63-113
    • Hanahan, D.1    Jessee, J.2    Bloom, F.R.3
  • 20
    • 0028348481 scopus 로고
    • The isolation of differentially expressed genes in fibroblast growth factor stimulated BC3H1 cells by subtractive hybridization
    • Li WB, Gruber CE, Lin JJ, Lim R, D'Alessio JM, Jessee JA. The isolation of differentially expressed genes in fibroblast growth factor stimulated BC3H1 cells by subtractive hybridization. Biotechniques 1994; 16:722-9.
    • (1994) Biotechniques , vol.16 , pp. 722-729
    • Li, W.B.1    Gruber, C.E.2    Lin, J.J.3    Lim, R.4    D'Alessio, J.M.5    Jessee, J.A.6
  • 21
    • 0025782224 scopus 로고
    • A simple and efficient cDNA library subtraction procedure: Isolation of human retina-specific cDNA clones
    • Swaroop A, Xu JZ, Agarwal N, Weissman SM. A simple and efficient cDNA library subtraction procedure: isolation of human retina-specific cDNA clones. Nucleic Acids R es 1991; 19:1954.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 1954
    • Swaroop, A.1    Xu, J.Z.2    Agarwal, N.3    Weissman, S.M.4
  • 22
    • 0031978181 scopus 로고    scopus 로고
    • Base-calling of automated sequencer traces using phred. II. Error probabilities
    • Ewing B, Green P. Base-calling of automated sequencer traces using phred. II. Error probabilities. Genome Res 1998; 8:186-94.
    • (1998) Genome Res. , vol.8 , pp. 186-194
    • Ewing, B.1    Green, P.2
  • 27
    • 0345051044 scopus 로고    scopus 로고
    • Normalization and subtraction: Two approaches to facilitate gene discovery
    • Bonaldo MF, Lennon G, Soares MB. Normalization and subtraction: two approaches to facilitate gene discovery. Genome Res 1996; 6:791-806.
    • (1996) Genome Res. , vol.6 , pp. 791-806
    • Bonaldo, M.F.1    Lennon, G.2    Soares, M.B.3
  • 28
    • 0027296295 scopus 로고
    • The IRE (iron regulatory element) family: Structures which regulate mRNA translation or stability
    • Theil EC. The IRE (iron regulatory element) family: structures which regulate mRNA translation or stability. Biofactors 1993; 4:87-93.
    • (1993) Biofactors , vol.4 , pp. 87-93
    • Theil, E.C.1
  • 29
    • 0032580087 scopus 로고    scopus 로고
    • Cloning and mapping the mouse Crygs gene and non-lens expression of [gamma]S-crystallin
    • Sinha D, Esumi N, Jaworski C, Kozak CA, Pierce E, Wistow G. Cloning and mapping the mouse Crygs gene and non-lens expression of [gamma]S-crystallin. Mol Vis 1998; 4:8 .
    • (1998) Mol. Vis. , vol.4 , pp. 8
    • Sinha, D.1    Esumi, N.2    Jaworski, C.3    Kozak, C.A.4    Pierce, E.5    Wistow, G.6
  • 30
    • 0034678945 scopus 로고    scopus 로고
    • The human gene for gammaS-crystallin: Alternative transcripts and expressed sequences from the first intron
    • Wistow G, Sardarian L, Gan W, Wyatt MK. The human gene for gammaS-crystallin: alternative transcripts and expressed sequences from the first intron. Mol Vis 2000; 6:79-84 .
    • (2000) Mol. Vis. , vol.6 , pp. 79-84
    • Wistow, G.1    Sardarian, L.2    Gan, W.3    Wyatt, M.K.4
  • 31
    • 0024218965 scopus 로고
    • The evolution of lenticular proteins: The beta- and gamma-crystallin super gene family
    • Lubsen NH, Aarts HJ, Schoenmakers JG. The evolution of lenticular proteins: the beta- and gamma-crystallin super gene family. Prog Biophys Mol Biol 1988; 51:47-76.
    • (1988) Prog. Biophys. Mol. Biol. , vol.51 , pp. 47-76
    • Lubsen, N.H.1    Aarts, H.J.2    Schoenmakers, J.G.3
  • 33
    • 0023942003 scopus 로고
    • Rat lens gamma-crystallins. Characterization of the six gene products and their spatial and temporal distribution resulting from differential synthesis
    • Siezen RJ, Wu E, Kaplan ED, Thomson JA, Benedek GB. Rat lens gamma-crystallins. Characterization of the six gene products and their spatial and temporal distribution resulting from differential synthesis. J Mol Biol 1988; 199:475-90.
    • (1988) J. Mol. Biol. , vol.199 , pp. 475-490
    • Siezen, R.J.1    Wu, E.2    Kaplan, E.D.3    Thomson, J.A.4    Benedek, G.B.5
  • 34
    • 0028446532 scopus 로고
    • The beaded intermediate filaments and their potential functions in eye lens
    • Georgatos SD, Gounari F, Remington S. The beaded intermediate filaments and their potential functions in eye lens. Bioessays 1994; 16:413-8.
    • (1994) Bioessays , vol.16 , pp. 413-418
    • Georgatos, S.D.1    Gounari, F.2    Remington, S.3
  • 36
    • 0033343738 scopus 로고    scopus 로고
    • Cytoplasmic dynein and microtubule transport in the axon: The action connection
    • Pfister KK. Cytoplasmic dynein and microtubule transport in the axon: the action connection. Mol Neurobiol 1999; 20:81-91.
    • (1999) Mol. Neurobiol. , vol.20 , pp. 81-91
    • Pfister, K.K.1
  • 37
    • 0032820553 scopus 로고    scopus 로고
    • Molecular architecture of the lens fiber cell basal membrane complex
    • Bassnett S, Missey H, Vucemilo I. Molecular architecture of the lens fiber cell basal membrane complex. J Cell Sci 1999; 112:2155-65.
    • (1999) J. Cell Sci. , vol.112 , pp. 2155-2165
    • Bassnett, S.1    Missey, H.2    Vucemilo, I.3
  • 38
    • 0035140977 scopus 로고    scopus 로고
    • Actin dynamics and cell-cell adhesion in epithelia
    • Vasioukhin V, Fuchs E. Actin dynamics and cell-cell adhesion in epithelia. Curr Opin Cell Biol 2001; 13:76-84.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 76-84
    • Vasioukhin, V.1    Fuchs, E.2
  • 40
    • 0033788835 scopus 로고    scopus 로고
    • Plakoglobin and beta-catenin: Protein interactions, regulation and biological roles
    • Zhurinsky J, Shtutman M, Ben-Ze'ev A. Plakoglobin and beta-catenin: protein interactions, regulation and biological roles. J Cell Sci 2000; 113:3127-39.
    • (2000) J. Cell Sci. , vol.113 , pp. 3127-3139
    • Zhurinsky, J.1    Shtutman, M.2    Ben-Ze'ev, A.3
  • 42
    • 0031080640 scopus 로고    scopus 로고
    • Expression of aquaporins in the rat ocular tissue
    • Patil RV, Saito I, Yang X, Wax MB. Expression of aquaporins in the rat ocular tissue. Exp Eye Res 1997; 64:203-9.
    • (1997) Exp. Eye Res. , vol.64 , pp. 203-209
    • Patil, R.V.1    Saito, I.2    Yang, X.3    Wax, M.B.4
  • 45
    • 0025043970 scopus 로고
    • Molecular cloning and complete nucleotide sequence of the cDNA encoding a bovine lens intrinsic membrane protein (MP19)
    • Gutekunst KA, Rao GN, Church RL. Molecular cloning and complete nucleotide sequence of the cDNA encoding a bovine lens intrinsic membrane protein (MP19). Curr Eye Res 1990; 9:955-61.
    • (1990) Curr. Eye Res. , vol.9 , pp. 955-961
    • Gutekunst, K.A.1    Rao, G.N.2    Church, R.L.3
  • 46
    • 0024364998 scopus 로고
    • Bovine lens 23, 21 and 19 kDa intrinsic membrane proteins have an identical amino-terminal amino acid sequence
    • Rao GN, Gutekunst KA, Church RL. Bovine lens 23, 21 and 19 kDa intrinsic membrane proteins have an identical amino-terminal amino acid sequence. FEBS Lett 1989; 250:483-6.
    • (1989) FEBS Lett. , vol.250 , pp. 483-486
    • Rao, G.N.1    Gutekunst, K.A.2    Church, R.L.3
  • 47
    • 0025941909 scopus 로고
    • Age-dependent covalent changes in MP18 from bovine lens membrane
    • Subramanian G, Takemoto L. Age-dependent covalent changes in MP18 from bovine lens membrane. Invest Ophthalmol Vis Sci 1991; 32:2588-92.
    • (1991) Invest. Ophthalmol. Vis. Sci. , vol.32 , pp. 2588-2592
    • Subramanian, G.1    Takemoto, L.2
  • 48
    • 0027452876 scopus 로고
    • Cloning and expression of a major rat lens membrane protein, MP20
    • Kumar NM, Jarvis LJ, Tenbroek E, Louis CF. Cloning and expression of a major rat lens membrane protein, MP20. Exp Eye Res 1993: 56:35-43.
    • (1993) Exp. Eye Res. , vol.56 , pp. 35-43
    • Kumar, N.M.1    Jarvis, L.J.2    Tenbroek, E.3    Louis, C.F.4
  • 49
    • 0030947554 scopus 로고    scopus 로고
    • The tetraspanin superfamily: Molecular facilitators
    • Maecker HT, Todd SC, Levy S. The tetraspanin superfamily: molecular facilitators. FASEB J 1997; 11:428-42.
    • (1997) FASEB J. , vol.11 , pp. 428-442
    • Maecker, H.T.1    Todd, S.C.2    Levy, S.3
  • 51
    • 0034595482 scopus 로고    scopus 로고
    • Lim2(To3) transgenic mice establish a causative relationship between the mutation identified in the lim2 gene and cataractogeneis in the To3 muse mutant
    • Steele EC Jr, Wang JH, Saperstein DA, Li X, Church RL. Lim2(To3) transgenic mice establish a causative relationship between the mutation identified in the lim2 gene and cataractogeneis in the To3 muse mutant. Mol Vis 2000; 6:85-94 .
    • (2000) Mol. Vis. , vol.6 , pp. 85-94
    • Steele E.C., Jr.1    Wang, J.H.2    Saperstein, D.A.3    Li, X.4    Church, R.L.5
  • 53
    • 0027730885 scopus 로고
    • The human lens fiber-cell intrinsic membrane protein MP19 gene: Isolation and sequence analysis
    • Church RL, Wang JH. The human lens fiber-cell intrinsic membrane protein MP19 gene: isolation and sequence analysis. Curr Eye Res 1993; 12:1057-65.
    • (1993) Curr. Eye Res. , vol.12 , pp. 1057-1065
    • Church, R.L.1    Wang, J.H.2
  • 54
    • 0023648790 scopus 로고
    • The enzyme lactate dehydrogenase as a structural protein in avian and crocodilian lenses
    • Wistow GJ, Mulders JW, de Jong WW. The enzyme lactate dehydrogenase as a structural protein in avian and crocodilian lenses. Nature 1987; 326:622-4.
    • (1987) Nature , vol.326 , pp. 622-624
    • Wistow, G.J.1    Mulders, J.W.2    de Jong, W.W.3
  • 55
    • 0023225865 scopus 로고
    • Recruitment of enzymes as lens structural proteins
    • Wistow G, Piatigorsky J. Recruitment of enzymes as lens structural proteins. Science 1987; 236:1554-6.
    • (1987) Science , vol.236 , pp. 1554-1556
    • Wistow, G.1    Piatigorsky, J.2
  • 56
    • 0027225772 scopus 로고
    • Lens crystallins: Gene recruitment and evolutionary dynamism
    • Wistow G. Lens crystallins: gene recruitment and evolutionary dynamism. Trends Biochem Sci 1993; 18:301-6.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 301-306
    • Wistow, G.1
  • 57
    • 0003637527 scopus 로고
    • Molecular biology and evolution of crystallins: Gene recruitment and multifunctional proteins in the eye lens
    • Austin (TX): R.G. Landes
    • Wistow GJ. Molecular biology and evolution of crystallins: gene recruitment and multifunctional proteins in the eye lens. Austin (TX): R.G. Landes; 1995.
    • (1995)
    • Wistow, G.J.1
  • 58
    • 0029151027 scopus 로고
    • Oxidative stress-induced cataract: Mechanism of action
    • Spector A. Oxidative stress-induced cataract: mechanism of action. FASEB J 1995; 9:1173-82.
    • (1995) FASEB J. , vol.9 , pp. 1173-1182
    • Spector, A.1
  • 61
    • 0346949039 scopus 로고    scopus 로고
    • Expressed sequence tag analysis of adult human iris for the NEIBank Project: Steroid-response factors and similarities with retinal pigment epithelium
    • Wistow G, Bernstein SL, Ray S, Wyatt MK, Behal A, Touchman JW, Bouffard G, Smith D, Peterson K. Expressed sequence tag analysis of adult human iris for the NEIBank Project: Steroid-response factors and similarities with retinal pigment epithelium. Mol Vis 2002; 8:185-95 .
    • (2002) Mol. Vis. , vol.8 , pp. 185-195
    • Wistow, G.1    Bernstein, S.L.2    Ray, S.3    Wyatt, M.K.4    Behal, A.5    Touchman, J.W.6    Bouffard, G.7    Smith, D.8    Peterson, K.9
  • 65
    • 0033979041 scopus 로고    scopus 로고
    • The glutamine synthetases of rhizobia: Phylogenetics and evolutionary implications
    • Turner SL, Young JP. The glutamine synthetases of rhizobia: phylogenetics and evolutionary implications. Mol Biol Evol 2000; 17:309-19.
    • (2000) Mol. Biol. Evol. , vol.17 , pp. 309-319
    • Turner, S.L.1    Young, J.P.2
  • 68
    • 0034012636 scopus 로고    scopus 로고
    • Glutathione: A vital lens antioxidant
    • Giblin FJ. Glutathione: a vital lens antioxidant. J Ocul Pharmacol Ther 2000; 16:121-35.
    • (2000) J. Ocul. Pharmacol. Ther. , vol.16 , pp. 121-135
    • Giblin, F.J.1
  • 69
    • 0029266564 scopus 로고
    • Potential contribution of the glutathione S-transferase supergene family to resistance to oxidative stress
    • Hayes JD, Strange RC. Potential contribution of the glutathione S-transferase supergene family to resistance to oxidative stress. Free Radic Res 1995; 22:193-207.
    • (1995) Free Radic. Res. , vol.22 , pp. 193-207
    • Hayes, J.D.1    Strange, R.C.2
  • 70
    • 0032563204 scopus 로고    scopus 로고
    • Purification, molecular cloning, and characterization of TRP32, a novel thioredoxin-related mammalian protein of 32 kDa
    • Lee KK, Murakawa M, Takahashi S, Tsubuki S, Kawashima S, Sakamaki K, Yonehara S. Purification, molecular cloning, and characterization of TRP32, a novel thioredoxin-related mammalian protein of 32 kDa. J Biol Chem 1998; 273:19160-6.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19160-19166
    • Lee, K.K.1    Murakawa, M.2    Takahashi, S.3    Tsubuki, S.4    Kawashima, S.5    Sakamaki, K.6    Yonehara, S.7
  • 71
    • 0033775891 scopus 로고    scopus 로고
    • Physiological functions of thioredoxin and thioredoxin reductase
    • Arner ES, Holmgren A. Physiological functions of thioredoxin and thioredoxin reductase. Eur J Biochem 2000; 267:6102-9.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6102-6109
    • Arner, E.S.1    Holmgren, A.2
  • 72
    • 0033301995 scopus 로고    scopus 로고
    • From cytoprotection to tumor suppression: The multifactorial role of peroxiredoxins
    • Butterfield LH, Merino A, Golub SH, Shau H. From cytoprotection to tumor suppression: the multifactorial role of peroxiredoxins. Antioxid Redox Signal 1999; 1:385-402.
    • (1999) Antioxid Redox Signal , vol.1 , pp. 385-402
    • Butterfield, L.H.1    Merino, A.2    Golub, S.H.3    Shau, H.4
  • 73
    • 0034666150 scopus 로고    scopus 로고
    • Identification and functional characterization of human soluble epoxide hydrolase genetic polymorphisms
    • Sandberg M, Hassett C, Adman ET, Meijer J, Omiecinski CJ. Identification and functional characterization of human soluble epoxide hydrolase genetic polymorphisms. J Biol Chem 2000; 275:28873-81.
    • (2000) J. Biol. Chem. , vol.275 , pp. 28873-28881
    • Sandberg, M.1    Hassett, C.2    Adman, E.T.3    Meijer, J.4    Omiecinski, C.J.5
  • 74
    • 0035919479 scopus 로고    scopus 로고
    • Regulation of clock and NPAS2 DNA binding by the redox state of NAD cofactors
    • Rutter J, Reick M, Wu LC, McKnight SL. Regulation of clock and NPAS2 DNA binding by the redox state of NAD cofactors. Science 2001; 293:510-4.
    • (2001) Science , vol.293 , pp. 510-514
    • Rutter, J.1    Reick, M.2    Wu, L.C.3    McKnight, S.L.4
  • 75
    • 0035919618 scopus 로고    scopus 로고
    • NPAS2: An analog of clock operative in the mammalian forebrain
    • Reick M, Garcia JA, Dudley C, McKnight SL. NPAS2: an analog of clock operative in the mammalian forebrain. Science 2001; 293:506-9.
    • (2001) Science , vol.293 , pp. 506-509
    • Reick, M.1    Garcia, J.A.2    Dudley, C.3    McKnight, S.L.4
  • 77
    • 0031126337 scopus 로고    scopus 로고
    • Activation of calpain in lens: A review and proposed mechanism
    • Azuma M, Fukiage C, David LL, Shearer TR. Activation of calpain in lens: a review and proposed mechanism. Exp Eye Res 1997; 64:529-38.
    • (1997) Exp. Eye Res. , vol.64 , pp. 529-538
    • Azuma, M.1    Fukiage, C.2    David, L.L.3    Shearer, T.R.4
  • 78
    • 0030918546 scopus 로고    scopus 로고
    • Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors
    • Turk B, Turk V, Turk D. Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors. Biol Chem 1997; 378:141-50.
    • (1997) Biol. Chem. , vol.378 , pp. 141-150
    • Turk, B.1    Turk, V.2    Turk, D.3
  • 79
    • 0034769477 scopus 로고    scopus 로고
    • Removal of oxidatively damaged proteins from lens cells by the ubiquitin-proteasome pathway
    • Shang F, Nowell TR Jr, Taylor A. Removal of oxidatively damaged proteins from lens cells by the ubiquitin-proteasome pathway. Exp Eye Res 2001; 73:229-38.
    • (2001) Exp. Eye Res. , vol.73 , pp. 229-238
    • Shang, F.1    Nowell T.R., Jr.2    Taylor, A.3
  • 80
    • 0030772933 scopus 로고    scopus 로고
    • Targeting of substrates to the 26S proteasome
    • Pickart CM. Targeting of substrates to the 26S proteasome. FASEB J 1997; 11:1055-66.
    • (1997) FASEB J. , vol.11 , pp. 1055-1066
    • Pickart, C.M.1
  • 81
    • 0025333047 scopus 로고
    • Cold shock and DNA binding
    • Wistow G. Cold shock and DNA binding. Nature 1990; 344:823-4.
    • (1990) Nature , vol.344 , pp. 823-824
    • Wistow, G.1
  • 82
    • 0026769818 scopus 로고
    • RNP-1, an RNA-binding motif is conserved in the DNA-binding cold shock domain
    • Landsman D. RNP-1, an RNA-binding motif is conserved in the DNA-binding cold shock domain. Nucleic Acids Res 1992; 20:2861-4.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 2861-2864
    • Landsman, D.1
  • 83
    • 0032575666 scopus 로고    scopus 로고
    • Purification and characterization of a novel physiological substrate for calcineurin in mammalian cells
    • Groblewski GE, Yoshida M, Bragado MJ, Ernst SA, Leykam J, Williams JA. Purification and characterization of a novel physiological substrate for calcineurin in mammalian cells. J Biol Chem 1998; 273:22738-44.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22738-22744
    • Groblewski, G.E.1    Yoshida, M.2    Bragado, M.J.3    Ernst, S.A.4    Leykam, J.5    Williams, J.A.6
  • 84
    • 0000117979 scopus 로고
    • Transcriptional regulation of crystallin genes: Cis elements, trans-factors and signal transduction systems in the lens
    • Wassarman P, editor. Greenwich (CT): JAI Press
    • Piatigorsky J, Zelenka PS. Transcriptional regulation of crystallin genes: cis elements, trans-factors and signal transduction systems in the lens. In: Wassarman P, editor. Advances in developmental biochemistry, vol 1. Greenwich (CT): JAI Press; 1992. p. 211-56.
    • (1992) Advances in Developmental Biochemistry , vol.1 , pp. 211-256
    • Piatigorsky, J.1    Zelenka, P.S.2
  • 85
    • 0029134882 scopus 로고
    • Insulin regulates expression of c-fos and c-jun and suppresses apoptosis of lens epithelial cells
    • Rampalli AM, Zelenka PS. Insulin regulates expression of c-fos and c-jun and suppresses apoptosis of lens epithelial cells. Cell Growth Differ 1995; 6:945-53.
    • (1995) Cell Growth Differ , vol.6 , pp. 945-953
    • Rampalli, A.M.1    Zelenka, P.S.2
  • 86
    • 0034595859 scopus 로고    scopus 로고
    • Canonical heat shock element in the alpha B-crystallin gene shows tissue-specific and developmentally controlled interactions with heat shock factor
    • Somasundaram T, Bhat SP. Canonical heat shock element in the alpha B-crystallin gene shows tissue-specific and developmentally controlled interactions with heat shock factor. J Biol Chem 2000; 275:17154-9.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17154-17159
    • Somasundaram, T.1    Bhat, S.P.2
  • 87
    • 0032819331 scopus 로고    scopus 로고
    • Unlocking the mechanisms of transcription factor YY1: Are chromatin modifying enzymes the key?
    • Thomas MJ, Seto E. Unlocking the mechanisms of transcription factor YY1: are chromatin modifying enzymes the key? Gene 1999; 236:197-208.
    • (1999) Gene , vol.236 , pp. 197-208
    • Thomas, M.J.1    Seto, E.2
  • 88
    • 0030790020 scopus 로고    scopus 로고
    • Current views on eye development
    • Oliver G, Gruss P. Current views on eye development. Trends Neurosci 1997; 20:415-21.
    • (1997) Trends Neurosci. , vol.20 , pp. 415-421
    • Oliver, G.1    Gruss, P.2
  • 89
    • 0033616621 scopus 로고    scopus 로고
    • Requirement for the c-Maf transcription factor in crystallin gene regulation and lens development
    • Kim JI, Li T, Ho IC, Grusby MJ, Glimcher LH. Requirement for the c-Maf transcription factor in crystallin gene regulation and lens development. Proc Natl Acad Sci U S A 1999; 96:3781-5.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 3781-3785
    • Kim, J.I.1    Li, T.2    Ho, I.C.3    Grusby, M.J.4    Glimcher, L.H.5
  • 91
    • 0033967140 scopus 로고    scopus 로고
    • Regulation of mouse lens fiber cell development and differentiation by the Maf gene
    • Ring BZ, Cordes SP, Overbeek PA, Barsh GS. Regulation of mouse lens fiber cell development and differentiation by the Maf gene. Development 2000; 127:307-17.
    • (2000) Development , vol.127 , pp. 307-317
    • Ring, B.Z.1    Cordes, S.P.2    Overbeek, P.A.3    Barsh, G.S.4
  • 92
    • 0032478785 scopus 로고    scopus 로고
    • Induction of lens differentiation by activation of a bZIP transcription factor, L-Maf
    • Ogino H, Yasuda K. Induction of lens differentiation by activation of a bZIP transcription factor, L-Maf. Science 1998; 280:115-8.
    • (1998) Science , vol.280 , pp. 115-118
    • Ogino, H.1    Yasuda, K.2
  • 94
    • 0032496139 scopus 로고    scopus 로고
    • Multivalent DNA binding complex generated by small Maf and Bach1 as a possible biochemical basis for beta-globin locus control region complex
    • Igarashi K, Hoshino H, Muto A, Suwabe N, Nishikawa S, Nakauchi H, Yamamoto M. Multivalent DNA binding complex generated by small Maf and Bach1 as a possible biochemical basis for beta-globin locus control region complex. J Biol Chem 1998; 273:11783-90.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11783-11790
    • Igarashi, K.1    Hoshino, H.2    Muto, A.3    Suwabe, N.4    Nishikawa, S.5    Nakauchi, H.6    Yamamoto, M.7
  • 95
    • 0033198374 scopus 로고    scopus 로고
    • Pax 6: Mastering eye morphogenesis and eye evolution
    • Gehring WJ, Ikeo K. Pax 6: mastering eye morphogenesis and eye evolution. Trends Genet 1999; 15:371-7.
    • (1999) Trends Genet. , vol.15 , pp. 371-377
    • Gehring, W.J.1    Ikeo, K.2
  • 97
    • 0034650544 scopus 로고    scopus 로고
    • A forkhead gene, FoxE3, is essential for lens epithelial proliferation and closure of the lens vesicle
    • Blixt A, Mahlapuu M, Aitola M, Pelto-Huikko M, Enerback S, Carlsson P. A forkhead gene, FoxE3, is essential for lens epithelial proliferation and closure of the lens vesicle. Genes Dev 2000; 14:245-54.
    • (2000) Genes Dev. , vol.14 , pp. 245-254
    • Blixt, A.1    Mahlapuu, M.2    Aitola, M.3    Pelto-Huikko, M.4    Enerback, S.5    Carlsson, P.6
  • 98
    • 0033746121 scopus 로고    scopus 로고
    • Hmx: An evolutionary conserved homeobox gene family expressed in the developing nervous system in mice and Drosophila
    • Wang W, Lo P, Frasch M, Lufkin T. Hmx: an evolutionary conserved homeobox gene family expressed in the developing nervous system in mice and Drosophila. Mech Dev 2000; 99:123-37.
    • (2000) Mech. Dev. , vol.99 , pp. 123-137
    • Wang, W.1    Lo, P.2    Frasch, M.3    Lufkin, T.4
  • 102
    • 84995839584 scopus 로고
    • Pax-QNR/Pax-6, a paired box- and homeobox-containing gene expressed in neurons, is also expressed in pancreatic endocrine cells
    • Turque N, Plaza S, Radvanyi F, Carriere C, Saule S. Pax-QNR/Pax-6, a paired box- and homeobox-containing gene expressed in neurons, is also expressed in pancreatic endocrine cells. Mol Endocrinol 1994; 8:929-38.
    • (1994) Mol. Endocrinol. , vol.8 , pp. 929-938
    • Turque, N.1    Plaza, S.2    Radvanyi, F.3    Carriere, C.4    Saule, S.5
  • 103
    • 0017399251 scopus 로고
    • Steroid cataract--a review and a conclusion
    • Lubkin VL. Steroid cataract--a review and a conclusion. J Asthma Res 1977; 14:55-9.
    • (1977) J. Asthma Res. , vol.14 , pp. 55-59
    • Lubkin, V.L.1
  • 104
    • 0026064688 scopus 로고
    • The role of growth factors in the embryogenesis and differentiation of the eye
    • Tripathi BJ, Tripathi RC, Livingston AM, Borisuth NS. The role of growth factors in the embryogenesis and differentiation of the eye. Am J Anat 1991; 192:442-71.
    • (1991) Am. J. Anat. , vol.192 , pp. 442-471
    • Tripathi, B.J.1    Tripathi, R.C.2    Livingston, A.M.3    Borisuth, N.S.4
  • 106
    • 0032873956 scopus 로고    scopus 로고
    • Role of transforming growth factor-beta in transdifferentiation and fibrosis of lens epithelial cells
    • Lee EH, Joo CK. Role of transforming growth factor-beta in transdifferentiation and fibrosis of lens epithelial cells. Invest Ophthalmol Vis Sci 1999; 40:2025-32.
    • (1999) Invest. Ophthalmol. Vis. Sci. , vol.40 , pp. 2025-2032
    • Lee, E.H.1    Joo, C.K.2
  • 108
    • 0032430772 scopus 로고    scopus 로고
    • BMP4 is essential for lens induction in the mouse embryo
    • Furuta Y, Hogan BL. BMP4 is essential for lens induction in the mouse embryo. Genes Dev 1998; 12:3764-75.
    • (1998) Genes Dev. , vol.12 , pp. 3764-3775
    • Furuta, Y.1    Hogan, B.L.2
  • 109
    • 0032699449 scopus 로고    scopus 로고
    • Which factors stimulate lens fiber cell differentiation in vivo?
    • Lang RA. Which factors stimulate lens fiber cell differentiation in vivo? Invest Ophthalmol Vis Sci 1999; 40:3075-8.
    • (1999) Invest. Ophthalmol. Vis. Sci. , vol.40 , pp. 3075-3078
    • Lang, R.A.1
  • 111
    • 0034193557 scopus 로고    scopus 로고
    • EGF receptor signalling: The importance of presentation
    • Klambt C. EGF receptor signalling: the importance of presentation. Curr Biol 2000; 10:R388-91.
    • (2000) Curr. Biol. , vol.10
    • Klambt, C.1
  • 112
    • 0035793557 scopus 로고    scopus 로고
    • Livin, a novel inhibitor of apoptosis protein family member
    • Kasof GM, Gomes BC. Livin, a novel inhibitor of apoptosis protein family member. J Biol Chem 2001; 276:3238-46.
    • (2001) J. Biol. Chem. , vol.276 , pp. 3238-3246
    • Kasof, G.M.1    Gomes, B.C.2
  • 114
    • 0034278085 scopus 로고    scopus 로고
    • The IAP family: Endogenous caspase inhibitors with multiple biological activities
    • Yang YL, Li XM. The IAP family: endogenous caspase inhibitors with multiple biological activities. Cell Res 2000; 10:169-77.
    • (2000) Cell Res. , vol.10 , pp. 169-177
    • Yang, Y.L.1    Li, X.M.2


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