메뉴 건너뛰기




Volumn 88, Issue 2, 2009, Pages 165-172

Lens intermediate filaments

Author keywords

beaded filaments; CP49; filensin; Intermediate filaments; lens; Phakinin; Phakosin; vimentin

Indexed keywords

CASPASE; FILENSIN; GLIAL FIBRILLARY ACIDIC PROTEIN; VIMENTIN;

EID: 61849139080     PISSN: 00144835     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.exer.2008.11.007     Document Type: Review
Times cited : (44)

References (128)
  • 1
    • 0022966765 scopus 로고
    • Expression of glial filament protein (GFP) in nerve sheaths and non-neural cells re-examined using monoclonal antibodies, with special emphasis on the co-expression of GFP and cytokeratins in epithelial cells of human salivary gland and pleomorphic adenomas
    • Achstatter T., Moll R., et al. Expression of glial filament protein (GFP) in nerve sheaths and non-neural cells re-examined using monoclonal antibodies, with special emphasis on the co-expression of GFP and cytokeratins in epithelial cells of human salivary gland and pleomorphic adenomas. Differentiation 31 3 (1986) 206-227
    • (1986) Differentiation , vol.31 , Issue.3 , pp. 206-227
    • Achstatter, T.1    Moll, R.2
  • 2
    • 0000834504 scopus 로고    scopus 로고
    • Analysis of skeletal and cardiac muscle from desmin knock-out and normal mice by high resolution separation of myosin heavy-chain isoforms
    • Agbulut O., Li Z., et al. Analysis of skeletal and cardiac muscle from desmin knock-out and normal mice by high resolution separation of myosin heavy-chain isoforms. Biol. Cell 88 3 (1996) 131-135
    • (1996) Biol. Cell , vol.88 , Issue.3 , pp. 131-135
    • Agbulut, O.1    Li, Z.2
  • 3
    • 0026693017 scopus 로고
    • The molecular biology of intermediate filament proteins
    • Albers K., and Fuchs E. The molecular biology of intermediate filament proteins. Int. Rev. Cytol. 134 (1992) 243-279
    • (1992) Int. Rev. Cytol. , vol.134 , pp. 243-279
    • Albers, K.1    Fuchs, E.2
  • 4
    • 0036902453 scopus 로고    scopus 로고
    • Targeted genomic deletion of the lens-specific intermediate filament protein CP49
    • Alizadeh A., Clark J.I., et al. Targeted genomic deletion of the lens-specific intermediate filament protein CP49. Invest. Ophthalmol. Vis. Sci. 43 12 (2002) 3722-3727
    • (2002) Invest. Ophthalmol. Vis. Sci. , vol.43 , Issue.12 , pp. 3722-3727
    • Alizadeh, A.1    Clark, J.I.2
  • 5
    • 0344851543 scopus 로고    scopus 로고
    • Targeted deletion of the lens fiber cell-specific intermediate filament protein filensin
    • Alizadeh A., Clark J., et al. Targeted deletion of the lens fiber cell-specific intermediate filament protein filensin. Invest. Ophthalmol. Vis. Sci. 44 12 (2003) 5252-5258
    • (2003) Invest. Ophthalmol. Vis. Sci. , vol.44 , Issue.12 , pp. 5252-5258
    • Alizadeh, A.1    Clark, J.2
  • 6
    • 1542427222 scopus 로고    scopus 로고
    • Characterization of a mutation in the lens-specific CP49 in the 129 strain of mouse
    • Alizadeh A., Clark J., et al. Characterization of a mutation in the lens-specific CP49 in the 129 strain of mouse. Invest. Ophthalmol. Vis. Sci. 45 3 (2004) 884-891
    • (2004) Invest. Ophthalmol. Vis. Sci. , vol.45 , Issue.3 , pp. 884-891
    • Alizadeh, A.1    Clark, J.2
  • 7
    • 0029871418 scopus 로고    scopus 로고
    • Calpains in the human lens: relations to membranes and possible role in cataract formation
    • Andersson M., Sjostrand J., et al. Calpains in the human lens: relations to membranes and possible role in cataract formation. Ophthalmic Res. 28 Suppl. 1 (1996) 51-54
    • (1996) Ophthalmic Res. , vol.28 , Issue.SUPPL. 1 , pp. 51-54
    • Andersson, M.1    Sjostrand, J.2
  • 8
    • 0024512061 scopus 로고
    • Domain- and sequence-specific phosphorylation of vimentin induces disassembly of the filament structure
    • Ando S., Tanabe K., et al. Domain- and sequence-specific phosphorylation of vimentin induces disassembly of the filament structure. Biochemistry 28 7 (1989) 2974-2979
    • (1989) Biochemistry , vol.28 , Issue.7 , pp. 2974-2979
    • Ando, S.1    Tanabe, K.2
  • 9
    • 0022297854 scopus 로고
    • Vimentin synthesis by ocular lens cells
    • Bagchi M., Caporale M.J., et al. Vimentin synthesis by ocular lens cells. Exp. Eye Res. 40 3 (1985) 385-392
    • (1985) Exp. Eye Res. , vol.40 , Issue.3 , pp. 385-392
    • Bagchi, M.1    Caporale, M.J.2
  • 10
    • 0030987138 scopus 로고    scopus 로고
    • Nonchromatin nuclear proteins of mammalian lens epithelial cells
    • Bagchi M., Ansari S.A., et al. Nonchromatin nuclear proteins of mammalian lens epithelial cells. J. Cell. Biochem. 64 4 (1997) 644-650
    • (1997) J. Cell. Biochem. , vol.64 , Issue.4 , pp. 644-650
    • Bagchi, M.1    Ansari, S.A.2
  • 11
    • 0036022133 scopus 로고    scopus 로고
    • Associated proteins of lens adherens junction
    • Bagchi M., Katar M., et al. Associated proteins of lens adherens junction. J. Cell. Biochem. 86 4 (2002) 700-703
    • (2002) J. Cell. Biochem. , vol.86 , Issue.4 , pp. 700-703
    • Bagchi, M.1    Katar, M.2
  • 12
    • 11144260046 scopus 로고    scopus 로고
    • ERM proteins of the lens
    • Bagchi M., Katar M., et al. ERM proteins of the lens. J. Cell. Biochem. 92 3 (2004) 626-630
    • (2004) J. Cell. Biochem. , vol.92 , Issue.3 , pp. 626-630
    • Bagchi, M.1    Katar, M.2
  • 13
    • 21244506693 scopus 로고    scopus 로고
    • Desmin filaments influence myofilament spacing and lateral compliance of slow skeletal muscle fibres
    • Balogh J., Li Z., et al. Desmin filaments influence myofilament spacing and lateral compliance of slow skeletal muscle fibres. Biophys. J. 88 (2004) 1156-1165
    • (2004) Biophys. J. , vol.88 , pp. 1156-1165
    • Balogh, J.1    Li, Z.2
  • 14
    • 0035094146 scopus 로고    scopus 로고
    • Changes in adhesion complexes define stages in the differentiation of lens fiber cells
    • Beebe D.C., Vasiliev O., et al. Changes in adhesion complexes define stages in the differentiation of lens fiber cells. Invest. Ophthalmol. Vis. Sci. 42 3 (2001) 727-734
    • (2001) Invest. Ophthalmol. Vis. Sci. , vol.42 , Issue.3 , pp. 727-734
    • Beebe, D.C.1    Vasiliev, O.2
  • 15
    • 0028837059 scopus 로고
    • Calcium cataract: a model for optical anisotropy fluctuations
    • Bettelheim F.A., Qin C., et al. Calcium cataract: a model for optical anisotropy fluctuations. Exp. Eye Res. 60 2 (1995) 153-157
    • (1995) Exp. Eye Res. , vol.60 , Issue.2 , pp. 153-157
    • Bettelheim, F.A.1    Qin, C.2
  • 16
    • 0036139632 scopus 로고    scopus 로고
    • Unexpected variation in unique features of the lens-specific type I cytokeratin CP49
    • Binkley P.A., Hess J., et al. Unexpected variation in unique features of the lens-specific type I cytokeratin CP49. Invest. Ophthalmol. Vis. Sci. 43 1 (2002) 225-235
    • (2002) Invest. Ophthalmol. Vis. Sci. , vol.43 , Issue.1 , pp. 225-235
    • Binkley, P.A.1    Hess, J.2
  • 17
    • 34548086031 scopus 로고    scopus 로고
    • Structural specializations emerging late in mouse lens fiber cell differentiation
    • Blankenship T., Bradshaw L., et al. Structural specializations emerging late in mouse lens fiber cell differentiation. Invest. Ophthalmol. Vis. Sci. 48 7 (2007) 3269-3276
    • (2007) Invest. Ophthalmol. Vis. Sci. , vol.48 , Issue.7 , pp. 3269-3276
    • Blankenship, T.1    Bradshaw, L.2
  • 18
    • 0035097221 scopus 로고    scopus 로고
    • Development- and differentiation-dependent reorganization of intermediate filaments in fiber cells
    • Blankenship T.N., Hess J.F., et al. Development- and differentiation-dependent reorganization of intermediate filaments in fiber cells. Invest. Ophthalmol. Vis. Sci. 42 3 (2001) 735-742
    • (2001) Invest. Ophthalmol. Vis. Sci. , vol.42 , Issue.3 , pp. 735-742
    • Blankenship, T.N.1    Hess, J.F.2
  • 19
    • 0019886319 scopus 로고
    • The lens cytoskeleton. Intermediate-sized filaments, their biosynthesis and association with plasma membranes
    • Bloemendal H., Benedetti E.L., et al. The lens cytoskeleton. Intermediate-sized filaments, their biosynthesis and association with plasma membranes. Mol. Biol. Rep. 7 1-3 (1981) 167-168
    • (1981) Mol. Biol. Rep. , vol.7 , Issue.1-3 , pp. 167-168
    • Bloemendal, H.1    Benedetti, E.L.2
  • 20
    • 0021701648 scopus 로고
    • Interaction of crystallins with the cytoskeletal-plasma membrane complex of the bovine lens
    • Bloemendal H., Berbers G.A., et al. Interaction of crystallins with the cytoskeletal-plasma membrane complex of the bovine lens. Ciba Found. Symp. 106 (1984) 177-190
    • (1984) Ciba Found. Symp. , vol.106 , pp. 177-190
    • Bloemendal, H.1    Berbers, G.A.2
  • 21
    • 0021969018 scopus 로고
    • Isolation of the intermediate filament protein vimentin by chromatofocusing
    • Bloemendal H., Willemsen M., et al. Isolation of the intermediate filament protein vimentin by chromatofocusing. FEBS Lett. 180 2 (1985) 181-184
    • (1985) FEBS Lett. , vol.180 , Issue.2 , pp. 181-184
    • Bloemendal, H.1    Willemsen, M.2
  • 22
    • 0030766135 scopus 로고    scopus 로고
    • Transgenic mice carrying chimeric or mutated type III intermediate filament (IF) genes
    • Bloemendal H., Raats J.M., et al. Transgenic mice carrying chimeric or mutated type III intermediate filament (IF) genes. Cell Mol. Life Sci. 53 1 (1997) 1-12
    • (1997) Cell Mol. Life Sci. , vol.53 , Issue.1 , pp. 1-12
    • Bloemendal, H.1    Raats, J.M.2
  • 23
    • 34548601698 scopus 로고    scopus 로고
    • Cytolinker cross-talk: periplakin N-terminus interacts with plectin to regulate keratin organisation and epithelial migration
    • Boczonadi V., McInroy L., et al. Cytolinker cross-talk: periplakin N-terminus interacts with plectin to regulate keratin organisation and epithelial migration. Exp. Cell Res. 313 16 (2007) 3579-3591
    • (2007) Exp. Cell Res. , vol.313 , Issue.16 , pp. 3579-3591
    • Boczonadi, V.1    McInroy, L.2
  • 24
    • 0029847068 scopus 로고    scopus 로고
    • Breaking the connection: displacement of the desmosomal plaque protein desmoplakin from cell-cell interfaces disrupts anchorage of intermediate filament bundles and alters intercellular junction assembly
    • Bornslaeger E.A., Corcoran C.M., et al. Breaking the connection: displacement of the desmosomal plaque protein desmoplakin from cell-cell interfaces disrupts anchorage of intermediate filament bundles and alters intercellular junction assembly. J. Cell Biol. 134 4 (1996) 985-1001
    • (1996) J. Cell Biol. , vol.134 , Issue.4 , pp. 985-1001
    • Bornslaeger, E.A.1    Corcoran, C.M.2
  • 25
    • 0025108669 scopus 로고
    • Expression of glial fibrillary acidic protein and vimentin in mouse lens epithelial cells during development in vivo and during proliferation and differentiation in vitro: comparison with the developmental appearance of GFAP in the mouse central nervous system
    • Boyer S., Maunoury R., et al. Expression of glial fibrillary acidic protein and vimentin in mouse lens epithelial cells during development in vivo and during proliferation and differentiation in vitro: comparison with the developmental appearance of GFAP in the mouse central nervous system. J. Neurosci. Res. 27 1 (1990) 55-64
    • (1990) J. Neurosci. Res. , vol.27 , Issue.1 , pp. 55-64
    • Boyer, S.1    Maunoury, R.2
  • 26
    • 0026092419 scopus 로고
    • Recent evolutionary origin of the expression of the glial fibrillary acidic protein (GFAP) in lens epithelial cells. A molecular and genetic analysis of various mouse species
    • Boyer S., Montagutelli X., et al. Recent evolutionary origin of the expression of the glial fibrillary acidic protein (GFAP) in lens epithelial cells. A molecular and genetic analysis of various mouse species. Brain Res. Mol. Brain Res. 10 2 (1991) 159-166
    • (1991) Brain Res. Mol. Brain Res. , vol.10 , Issue.2 , pp. 159-166
    • Boyer, S.1    Montagutelli, X.2
  • 27
    • 33749365947 scopus 로고    scopus 로고
    • Involvement of cytoskeletal proteins and growth factor receptors during development of the human eye
    • Bozanic D., Bocina I., et al. Involvement of cytoskeletal proteins and growth factor receptors during development of the human eye. Anat. Embryol. (Berl.) 211 5 (2006) 367-377
    • (2006) Anat. Embryol. (Berl.) , vol.211 , Issue.5 , pp. 367-377
    • Bozanic, D.1    Bocina, I.2
  • 28
    • 0017844585 scopus 로고
    • Chain-proteins of the vertebrate lens
    • Bradley R., and Maisel H. Chain-proteins of the vertebrate lens. Experientia 34 4 (1978) 470-472
    • (1978) Experientia , vol.34 , Issue.4 , pp. 470-472
    • Bradley, R.1    Maisel, H.2
  • 29
    • 0018388019 scopus 로고
    • Age changes in the skeleton of the human lens
    • Bradley R.H., Ireland M.E., et al. Age changes in the skeleton of the human lens. Acta Ophthalmol. (Copenh.) 57 3 (1979) 461-469
    • (1979) Acta Ophthalmol. (Copenh.) , vol.57 , Issue.3 , pp. 461-469
    • Bradley, R.H.1    Ireland, M.E.2
  • 30
    • 0027095747 scopus 로고
    • Membrane-binding properties of filensin, a cytoskeletal protein of the lens fiber cells
    • Brunkener M., and Georgatos S.D. Membrane-binding properties of filensin, a cytoskeletal protein of the lens fiber cells. J. Cell Sci. 103 Pt. 3 (1992) 709-718
    • (1992) J. Cell Sci. , vol.103 , Issue.PART 3 , pp. 709-718
    • Brunkener, M.1    Georgatos, S.D.2
  • 31
    • 0032233810 scopus 로고    scopus 로고
    • Desmin cytoskeleton in muscle integrity and function
    • Herrmann H., and Harris J.R. (Eds), Plenum Press, New York and London
    • Capetanaki Y., and Milner D.J. Desmin cytoskeleton in muscle integrity and function. In: Herrmann H., and Harris J.R. (Eds). Intermediate Filaments Vol. 31 (1998), Plenum Press, New York and London 463-495
    • (1998) Intermediate Filaments , vol.31 , pp. 463-495
    • Capetanaki, Y.1    Milner, D.J.2
  • 32
    • 0024470306 scopus 로고
    • Overexpression of the vimentin gene in transgenic mice inhibits normal lens cell differentiation
    • Capetanaki Y., Smith S., et al. Overexpression of the vimentin gene in transgenic mice inhibits normal lens cell differentiation. J. Cell Biol. 109 4 Pt. 1 (1989) 1653-1664
    • (1989) J. Cell Biol. , vol.109 , Issue.4 PART 1 , pp. 1653-1664
    • Capetanaki, Y.1    Smith, S.2
  • 33
    • 0028831015 scopus 로고
    • In vitro studies on the assembly properties of the lens proteins CP49, CP115: coassembly with alpha-crystallin but not with vimentin
    • Carter J.M., Hutcheson A.M., et al. In vitro studies on the assembly properties of the lens proteins CP49, CP115: coassembly with alpha-crystallin but not with vimentin. Exp. Eye Res. 60 2 (1995) 181-192
    • (1995) Exp. Eye Res. , vol.60 , Issue.2 , pp. 181-192
    • Carter, J.M.1    Hutcheson, A.M.2
  • 34
    • 0034643291 scopus 로고    scopus 로고
    • Mapping of the human CP49 gene and identification of an intragenic polymorphic marker to allow genetic linkage analysis in autosomal dominant congenital cataract
    • Carter J.M., McLean W.H., et al. Mapping of the human CP49 gene and identification of an intragenic polymorphic marker to allow genetic linkage analysis in autosomal dominant congenital cataract. Biochem. Biophys. Res. Commun. 270 2 (2000) 432-436
    • (2000) Biochem. Biophys. Res. Commun. , vol.270 , Issue.2 , pp. 432-436
    • Carter, J.M.1    McLean, W.H.2
  • 35
    • 0030770449 scopus 로고    scopus 로고
    • Caspase cleavage of keratin 18 and reorganization of intermediate filaments during epithelial cell apoptosis
    • Caulin C., Salvesen G.S., et al. Caspase cleavage of keratin 18 and reorganization of intermediate filaments during epithelial cell apoptosis. J. Cell Biol. 138 6 (1997) 1379-1394
    • (1997) J. Cell Biol. , vol.138 , Issue.6 , pp. 1379-1394
    • Caulin, C.1    Salvesen, G.S.2
  • 36
    • 0033410222 scopus 로고    scopus 로고
    • A novel mutation in the helix termination motif of keratin K12 in a US family with Meesmann corneal dystrophy
    • Coleman C.M., Hannush S., et al. A novel mutation in the helix termination motif of keratin K12 in a US family with Meesmann corneal dystrophy. Am. J. Ophthalmol. 128 6 (1999) 687-691
    • (1999) Am. J. Ophthalmol. , vol.128 , Issue.6 , pp. 687-691
    • Coleman, C.M.1    Hannush, S.2
  • 37
    • 0028004289 scopus 로고
    • Mice lacking vimentin develop and reproduce without an obvious phenotype
    • Colucci-Guyon E., Portier M.M., et al. Mice lacking vimentin develop and reproduce without an obvious phenotype. Cell 79 4 (1994) 679-694
    • (1994) Cell , vol.79 , Issue.4 , pp. 679-694
    • Colucci-Guyon, E.1    Portier, M.M.2
  • 38
    • 0033942141 scopus 로고    scopus 로고
    • A juvenile-onset, progressive cataract locus on chromosome 3q21-q22 is associated with a missense mutation in the beaded filament structural protein-2
    • Conley Y.P., Erturk D., et al. A juvenile-onset, progressive cataract locus on chromosome 3q21-q22 is associated with a missense mutation in the beaded filament structural protein-2. Am. J. Hum. Genet. 66 4 (2000) 1426-1431
    • (2000) Am. J. Hum. Genet. , vol.66 , Issue.4 , pp. 1426-1431
    • Conley, Y.P.1    Erturk, D.2
  • 39
    • 0034073435 scopus 로고    scopus 로고
    • A novel keratin 12 mutation in a German kindred with Meesmann's corneal dystrophy
    • Corden L.D., Swensson O., et al. A novel keratin 12 mutation in a German kindred with Meesmann's corneal dystrophy. Br. J. Ophthalmol. 84 5 (2000) 527-530
    • (2000) Br. J. Ophthalmol. , vol.84 , Issue.5 , pp. 527-530
    • Corden, L.D.1    Swensson, O.2
  • 40
    • 0033958844 scopus 로고    scopus 로고
    • Molecular genetics of Meesmann's corneal dystrophy: ancestral and novel mutations in keratin 12 (K12) and complete sequence of the human KRT12 gene
    • Corden L.D., Swensson O., et al. Molecular genetics of Meesmann's corneal dystrophy: ancestral and novel mutations in keratin 12 (K12) and complete sequence of the human KRT12 gene. Exp. Eye Res. 70 1 (2000) 41-49
    • (2000) Exp. Eye Res. , vol.70 , Issue.1 , pp. 41-49
    • Corden, L.D.1    Swensson, O.2
  • 41
    • 0034740389 scopus 로고    scopus 로고
    • Requirement for TGFbeta receptor signaling during terminal lens fiber differentiation
    • de Iongh R.U., Lovicu F.J., et al. Requirement for TGFbeta receptor signaling during terminal lens fiber differentiation. Development 128 20 (2001) 3995-4010
    • (2001) Development , vol.128 , Issue.20 , pp. 3995-4010
    • de Iongh, R.U.1    Lovicu, F.J.2
  • 42
    • 22144452168 scopus 로고    scopus 로고
    • Transforming growth factor-beta-induced epithelial-mesenchymal transition in the lens: a model for cataract formation
    • de Iongh R.U., Wederell E., et al. Transforming growth factor-beta-induced epithelial-mesenchymal transition in the lens: a model for cataract formation. Cells Tissues Organs 179 1-2 (2005) 43-55
    • (2005) Cells Tissues Organs , vol.179 , Issue.1-2 , pp. 43-55
    • de Iongh, R.U.1    Wederell, E.2
  • 43
    • 0021276369 scopus 로고
    • Studies on lens vimentin
    • Ellis M., Alousi S., et al. Studies on lens vimentin. Exp. Eye Res. 38 2 (1984) 195-202
    • (1984) Exp. Eye Res. , vol.38 , Issue.2 , pp. 195-202
    • Ellis, M.1    Alousi, S.2
  • 44
    • 2642563501 scopus 로고    scopus 로고
    • Mutant small heat-shock protein 27 causes axonal Charcot-Marie-Tooth disease and distal hereditary motor neuropathy
    • Evgrafov O.V., Mersiyanova I., et al. Mutant small heat-shock protein 27 causes axonal Charcot-Marie-Tooth disease and distal hereditary motor neuropathy. Nat. Genet. 36 6 (2004) 602-606
    • (2004) Nat. Genet. , vol.36 , Issue.6 , pp. 602-606
    • Evgrafov, O.V.1    Mersiyanova, I.2
  • 45
    • 0038303766 scopus 로고    scopus 로고
    • Tropomodulin binds to filensin intermediate filaments
    • Fischer R.S., Quinlan R.A., et al. Tropomodulin binds to filensin intermediate filaments. FEBS Lett. 547 1-3 (2003) 228-232
    • (2003) FEBS Lett. , vol.547 , Issue.1-3 , pp. 228-232
    • Fischer, R.S.1    Quinlan, R.A.2
  • 46
    • 0024210122 scopus 로고
    • Age-related changes in a fiber cell-specific extrinsic membrane protein
    • FitzGerald P.G. Age-related changes in a fiber cell-specific extrinsic membrane protein. Curr. Eye Res. 7 12 (1988) 1255-1262
    • (1988) Curr. Eye Res. , vol.7 , Issue.12 , pp. 1255-1262
    • FitzGerald, P.G.1
  • 47
    • 0024166479 scopus 로고
    • Immunochemical characterization of a Mr 115 lens fiber cell-specific extrinsic membrane protein
    • FitzGerald P.G. Immunochemical characterization of a Mr 115 lens fiber cell-specific extrinsic membrane protein. Curr. Eye Res. 7 12 (1988) 1243-1253
    • (1988) Curr. Eye Res. , vol.7 , Issue.12 , pp. 1243-1253
    • FitzGerald, P.G.1
  • 48
    • 0024474174 scopus 로고
    • The Mr 115 kd fiber cell-specific protein is a component of the lens cytoskeleton
    • FitzGerald P.G., and Gottlieb W. The Mr 115 kd fiber cell-specific protein is a component of the lens cytoskeleton. Curr. Eye Res. 8 8 (1989) 801-811
    • (1989) Curr. Eye Res. , vol.8 , Issue.8 , pp. 801-811
    • FitzGerald, P.G.1    Gottlieb, W.2
  • 49
    • 0025914055 scopus 로고
    • Ultrastructural localization of alpha A-crystallin to the bovine lens fiber cell cytoskeleton
    • FitzGerald P.G., and Graham D. Ultrastructural localization of alpha A-crystallin to the bovine lens fiber cell cytoskeleton. Curr. Eye Res. 10 5 (1991) 417-436
    • (1991) Curr. Eye Res. , vol.10 , Issue.5 , pp. 417-436
    • FitzGerald, P.G.1    Graham, D.2
  • 50
    • 0031966169 scopus 로고    scopus 로고
    • Intermediate filament cytoskeletal proteins associated with bovine lens native membrane fractions
    • Fleschner C.R. Intermediate filament cytoskeletal proteins associated with bovine lens native membrane fractions. Curr. Eye Res. 17 4 (1998) 409-418
    • (1998) Curr. Eye Res. , vol.17 , Issue.4 , pp. 409-418
    • Fleschner, C.R.1
  • 51
    • 0025985774 scopus 로고
    • Keratin genes, epidermal differentiation and animal models for the study of human skin diseases
    • Fuchs E. Keratin genes, epidermal differentiation and animal models for the study of human skin diseases. Biochem. Soc. Trans. 19 4 (1991) 1112-1115
    • (1991) Biochem. Soc. Trans. , vol.19 , Issue.4 , pp. 1112-1115
    • Fuchs, E.1
  • 52
    • 0028287112 scopus 로고
    • Intermediate filaments and disease: mutations that cripple cell strength
    • Fuchs E. Intermediate filaments and disease: mutations that cripple cell strength. J. Cell Biol. 125 3 (1994) 511-516
    • (1994) J. Cell Biol. , vol.125 , Issue.3 , pp. 511-516
    • Fuchs, E.1
  • 53
    • 19244384754 scopus 로고
    • Genetic bases of epidermolysis bullosa simplex and epidermolytic hyperkeratosis
    • Fuchs E., Coulombe P., et al. Genetic bases of epidermolysis bullosa simplex and epidermolytic hyperkeratosis. J. Invest. Dermatol 103 5 Suppl. (1994) 25S-30S
    • (1994) J. Invest. Dermatol , vol.103 , Issue.5 SUPPL
    • Fuchs, E.1    Coulombe, P.2
  • 54
    • 0035809911 scopus 로고    scopus 로고
    • A novel interaction of the Golgi complex with the vimentin intermediate filament cytoskeleton
    • Gao Y., and Sztul E. A novel interaction of the Golgi complex with the vimentin intermediate filament cytoskeleton. J. Cell Biol. 152 5 (2001) 877-894
    • (2001) J. Cell Biol. , vol.152 , Issue.5 , pp. 877-894
    • Gao, Y.1    Sztul, E.2
  • 55
    • 0036020958 scopus 로고    scopus 로고
    • A novel type of regulation of the vimentin intermediate filament cytoskeleton by a Golgi protein
    • Gao Y.S., Vrielink A., et al. A novel type of regulation of the vimentin intermediate filament cytoskeleton by a Golgi protein. Eur. J. Cell Biol. 81 7 (2002) 391-401
    • (2002) Eur. J. Cell Biol. , vol.81 , Issue.7 , pp. 391-401
    • Gao, Y.S.1    Vrielink, A.2
  • 56
    • 0019886732 scopus 로고
    • Isolation of polymerization-competent vimentin from porcine eye lens tissue
    • Geisler N., and Weber K. Isolation of polymerization-competent vimentin from porcine eye lens tissue. FEBS Lett. 125 2 (1981) 253-256
    • (1981) FEBS Lett. , vol.125 , Issue.2 , pp. 253-256
    • Geisler, N.1    Weber, K.2
  • 57
    • 0023372471 scopus 로고
    • Two distinct attachment sites for vimentin along the plasma membrane and the nuclear envelope in avian erythrocytes: a basis for a vectorial assembly of intermediate filaments
    • Georgatos S.D., and Blobel G. Two distinct attachment sites for vimentin along the plasma membrane and the nuclear envelope in avian erythrocytes: a basis for a vectorial assembly of intermediate filaments. J. Cell Biol. 105 1 (1987) 105-115
    • (1987) J. Cell Biol. , vol.105 , Issue.1 , pp. 105-115
    • Georgatos, S.D.1    Blobel, G.2
  • 58
    • 0027153962 scopus 로고
    • Bovine filensin possesses primary and secondary structure similarity to intermediate filament proteins
    • Gounari F., Merdes A., et al. Bovine filensin possesses primary and secondary structure similarity to intermediate filament proteins. J. Cell Biol. 121 4 (1993) 847-853
    • (1993) J. Cell Biol. , vol.121 , Issue.4 , pp. 847-853
    • Gounari, F.1    Merdes, A.2
  • 59
    • 0030757156 scopus 로고    scopus 로고
    • The mouse filensin gene: structure and evolutionary relation to other intermediate filament genes
    • Gounari F., Karagianni N., et al. The mouse filensin gene: structure and evolutionary relation to other intermediate filament genes. FEBS Lett. 413 2 (1997) 371-378
    • (1997) FEBS Lett. , vol.413 , Issue.2 , pp. 371-378
    • Gounari, F.1    Karagianni, N.2
  • 60
    • 0021676702 scopus 로고
    • Expression of the intermediate-filament-associated protein synemin in chicken lens cells
    • Granger B.L., and Lazarides E. Expression of the intermediate-filament-associated protein synemin in chicken lens cells. Mol. Cell. Biol. 4 10 (1984) 1943-1950
    • (1984) Mol. Cell. Biol. , vol.4 , Issue.10 , pp. 1943-1950
    • Granger, B.L.1    Lazarides, E.2
  • 61
    • 4444230618 scopus 로고    scopus 로고
    • Kazrin, a novel periplakin-interacting protein associated with desmosomes and the keratinocyte plasma membrane
    • Groot K.R., Sevilla L.M., et al. Kazrin, a novel periplakin-interacting protein associated with desmosomes and the keratinocyte plasma membrane. J. Cell Biol. 166 5 (2004) 653-659
    • (2004) J. Cell Biol. , vol.166 , Issue.5 , pp. 653-659
    • Groot, K.R.1    Sevilla, L.M.2
  • 62
    • 0021281782 scopus 로고
    • Glial fibrillary acidic protein is localized in the lens epithelium
    • Hatfield J.S., Skoff R.P., et al. Glial fibrillary acidic protein is localized in the lens epithelium. J. Cell Biol. 98 5 (1984) 1895-1898
    • (1984) J. Cell Biol. , vol.98 , Issue.5 , pp. 1895-1898
    • Hatfield, J.S.1    Skoff, R.P.2
  • 63
    • 0021883166 scopus 로고
    • The lens epithelium contains glial fibrillary acidic protein (GFAP)
    • Hatfield J.S., Skoff R.P., et al. The lens epithelium contains glial fibrillary acidic protein (GFAP). J. Neuroimmunol 8 4-6 (1985) 347-357
    • (1985) J. Neuroimmunol , vol.8 , Issue.4-6 , pp. 347-357
    • Hatfield, J.S.1    Skoff, R.P.2
  • 64
    • 0027463042 scopus 로고
    • cDNA analysis of the 49 kDa lens fiber cell cytoskeletal protein: a new, lens-specific member of the intermediate filament family?
    • Hess J.F., Casselman J.T., et al. cDNA analysis of the 49 kDa lens fiber cell cytoskeletal protein: a new, lens-specific member of the intermediate filament family?. Curr. Eye Res. 12 1 (1993) 77-88
    • (1993) Curr. Eye Res. , vol.12 , Issue.1 , pp. 77-88
    • Hess, J.F.1    Casselman, J.T.2
  • 65
    • 0029911721 scopus 로고    scopus 로고
    • Gene structure and cDNA sequence identify the beaded filament protein CP49 as a highly divergent type I intermediate filament protein
    • Hess J.F., Casselman J.T., et al. Gene structure and cDNA sequence identify the beaded filament protein CP49 as a highly divergent type I intermediate filament protein. J. Biol. Chem. 271 12 (1996) 6729-6735
    • (1996) J. Biol. Chem. , vol.271 , Issue.12 , pp. 6729-6735
    • Hess, J.F.1    Casselman, J.T.2
  • 66
    • 0032077115 scopus 로고    scopus 로고
    • Primary sequence, secondary structure, gene structure, and assembly properties suggests that the lens-specific cytoskeletal protein filensin represents a novel class of intermediate filament protein
    • Hess J.F., Casselman J.T., et al. Primary sequence, secondary structure, gene structure, and assembly properties suggests that the lens-specific cytoskeletal protein filensin represents a novel class of intermediate filament protein. Exp. Eye Res. 66 5 (1998) 625-644
    • (1998) Exp. Eye Res. , vol.66 , Issue.5 , pp. 625-644
    • Hess, J.F.1    Casselman, J.T.2
  • 67
    • 0023239962 scopus 로고
    • Site-specific phosphorylation induces disassembly of vimentin filaments in vitro
    • Inagaki M., Nishi Y., et al. Site-specific phosphorylation induces disassembly of vimentin filaments in vitro. Nature 328 6131 (1987) 649-652
    • (1987) Nature , vol.328 , Issue.6131 , pp. 649-652
    • Inagaki, M.1    Nishi, Y.2
  • 68
    • 0021215563 scopus 로고
    • A cytoskeletal protein unique to lens fiber cell differentiation
    • Ireland M., and Maisel H. A cytoskeletal protein unique to lens fiber cell differentiation. Exp. Eye Res. 38 6 (1984) 637-645
    • (1984) Exp. Eye Res. , vol.38 , Issue.6 , pp. 637-645
    • Ireland, M.1    Maisel, H.2
  • 69
    • 0021191234 scopus 로고
    • Phosphorylation of chick lens proteins
    • Ireland M., and Maisel H. Phosphorylation of chick lens proteins. Curr. Eye Res. 3 7 (1984) 961-968
    • (1984) Curr. Eye Res. , vol.3 , Issue.7 , pp. 961-968
    • Ireland, M.1    Maisel, H.2
  • 70
    • 0024841799 scopus 로고
    • A family of lens fiber cell specific proteins
    • Ireland M., and Maisel H. A family of lens fiber cell specific proteins. Lens Eye Toxic Res. 6 4 (1989) 623-638
    • (1989) Lens Eye Toxic Res. , vol.6 , Issue.4 , pp. 623-638
    • Ireland, M.1    Maisel, H.2
  • 71
    • 0033942142 scopus 로고    scopus 로고
    • Autosomal-dominant congenital cataract associated with a deletion mutation in the human beaded filament protein gene BFSP2
    • Jakobs P.M., Hess J.F., et al. Autosomal-dominant congenital cataract associated with a deletion mutation in the human beaded filament protein gene BFSP2. Am. J. Hum. Genet. 66 4 (2000) 1432-1436
    • (2000) Am. J. Hum. Genet. , vol.66 , Issue.4 , pp. 1432-1436
    • Jakobs, P.M.1    Hess, J.F.2
  • 72
    • 3042822399 scopus 로고    scopus 로고
    • Plakins: goliaths that link cell junctions and the cytoskeleton
    • Jefferson J.J., Leung C.L., et al. Plakins: goliaths that link cell junctions and the cytoskeleton. Nat. Rev. Mol. Cell Biol. 5 7 (2004) 542-553
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , Issue.7 , pp. 542-553
    • Jefferson, J.J.1    Leung, C.L.2
  • 73
    • 0026669548 scopus 로고
    • Cytokeratin expression and early lens development
    • Kasper M., and Viebahn C. Cytokeratin expression and early lens development. Anat. Embryol. (Berl.) 186 3 (1992) 285-290
    • (1992) Anat. Embryol. (Berl.) , vol.186 , Issue.3 , pp. 285-290
    • Kasper, M.1    Viebahn, C.2
  • 74
    • 46049106122 scopus 로고    scopus 로고
    • Identification of a novel intermediate filament-linked N-cadherin/gamma-catenin complex involved in the establishment of the cytoarchitecture of differentiated lens fiber cells
    • Leonard M., Chan Y., et al. Identification of a novel intermediate filament-linked N-cadherin/gamma-catenin complex involved in the establishment of the cytoarchitecture of differentiated lens fiber cells. Dev. Biol. 319 2 (2008) 298-308
    • (2008) Dev. Biol. , vol.319 , Issue.2 , pp. 298-308
    • Leonard, M.1    Chan, Y.2
  • 75
    • 0036169110 scopus 로고    scopus 로고
    • Plakins: a family of versatile cytolinker proteins
    • Leung C.L., Green K.J., et al. Plakins: a family of versatile cytolinker proteins. Trends Cell Biol. 12 1 (2002) 37-45
    • (2002) Trends Cell Biol. , vol.12 , Issue.1 , pp. 37-45
    • Leung, C.L.1    Green, K.J.2
  • 76
    • 33744914329 scopus 로고    scopus 로고
    • Molecular identification and characterisation of the glycine transporter (GLYT1) and the glutamine/glutamate transporter (ASCT2) in the rat lens
    • Lim J., Lorentzen K.A., et al. Molecular identification and characterisation of the glycine transporter (GLYT1) and the glutamine/glutamate transporter (ASCT2) in the rat lens. Exp. Eye Res. 83 2 (2006) 447-455
    • (2006) Exp. Eye Res. , vol.83 , Issue.2 , pp. 447-455
    • Lim, J.1    Lorentzen, K.A.2
  • 77
    • 33646000308 scopus 로고    scopus 로고
    • The C terminus of lens aquaporin 0 interacts with the cytoskeletal proteins filensin and CP49
    • Lindsey Rose K.M., Gourdie R.G., et al. The C terminus of lens aquaporin 0 interacts with the cytoskeletal proteins filensin and CP49. Invest. Ophthalmol. Vis. Sci. 47 4 (2006) 1562-1570
    • (2006) Invest. Ophthalmol. Vis. Sci. , vol.47 , Issue.4 , pp. 1562-1570
    • Lindsey Rose, K.M.1    Gourdie, R.G.2
  • 79
    • 0017362469 scopus 로고
    • Filaments of the vertebrate lens
    • Maisel H. Filaments of the vertebrate lens. Experientia 33 4 (1977) 525
    • (1977) Experientia , vol.33 , Issue.4 , pp. 525
    • Maisel, H.1
  • 80
    • 0015372386 scopus 로고
    • Electron microscope observations on some structural proteins of the chick lens
    • Maisel H., and Perry M.M. Electron microscope observations on some structural proteins of the chick lens. Exp. Eye Res. 14 1 (1972) 7-12
    • (1972) Exp. Eye Res. , vol.14 , Issue.1 , pp. 7-12
    • Maisel, H.1    Perry, M.M.2
  • 81
    • 0026571035 scopus 로고
    • Susceptibility of the bovine lens 115 kDa beaded filament protein to degradation by calcium and calpain
    • Marcantonio J.M. Susceptibility of the bovine lens 115 kDa beaded filament protein to degradation by calcium and calpain. Curr. Eye Res. 11 1 (1992) 103-108
    • (1992) Curr. Eye Res. , vol.11 , Issue.1 , pp. 103-108
    • Marcantonio, J.M.1
  • 82
    • 0029872285 scopus 로고    scopus 로고
    • Calcium-induced disruption of the lens cytoskeleton
    • Marcantonio J.M. Calcium-induced disruption of the lens cytoskeleton. Ophthalmic Res. 28 Suppl. 1 (1996) 48-50
    • (1996) Ophthalmic Res. , vol.28 , Issue.SUPPL. 1 , pp. 48-50
    • Marcantonio, J.M.1
  • 83
    • 0025931128 scopus 로고
    • Calcium-induced degradation of the lens cytoskeleton
    • Marcantonio J.M., and Duncan G. Calcium-induced degradation of the lens cytoskeleton. Biochem. Soc. Trans. 19 4 (1991) 1148-1150
    • (1991) Biochem. Soc. Trans. , vol.19 , Issue.4 , pp. 1148-1150
    • Marcantonio, J.M.1    Duncan, G.2
  • 84
    • 0030693791 scopus 로고    scopus 로고
    • Gene structure and sequence comparisons of the eye lens specific protein, filensin, from rat and mouse: implications for protein classification and assembly
    • Masaki S., and Quinlan R.A. Gene structure and sequence comparisons of the eye lens specific protein, filensin, from rat and mouse: implications for protein classification and assembly. Gene 201 1-2 (1997) 11-20
    • (1997) Gene , vol.201 , Issue.1-2 , pp. 11-20
    • Masaki, S.1    Quinlan, R.A.2
  • 85
    • 0026706184 scopus 로고
    • cDNA sequence analysis of CP94: rat lens fiber cell beaded-filament structural protein shows homology to cytokeratins
    • Masaki S., and Watanabe T. cDNA sequence analysis of CP94: rat lens fiber cell beaded-filament structural protein shows homology to cytokeratins. Biochem. Biophys. Res. Commun. 186 1 (1992) 190-198
    • (1992) Biochem. Biophys. Res. Commun. , vol.186 , Issue.1 , pp. 190-198
    • Masaki, S.1    Watanabe, T.2
  • 86
    • 0027722988 scopus 로고
    • The 47-kD lens-specific protein phakinin is a tailless intermediate filament protein and an assembly partner of filensin
    • Merdes A., Gounari F., et al. The 47-kD lens-specific protein phakinin is a tailless intermediate filament protein and an assembly partner of filensin. J. Cell Biol. 123 6 Pt. 1 (1993) 1507-1516
    • (1993) J. Cell Biol. , vol.123 , Issue.6 PART 1 , pp. 1507-1516
    • Merdes, A.1    Gounari, F.2
  • 87
    • 0031609393 scopus 로고    scopus 로고
    • Immunohistochemical detection of intermediate filament nestin
    • Mokry J., and Nemecek S. Immunohistochemical detection of intermediate filament nestin. Acta Med. (Hradec Kralove) 41 2 (1998) 73-80
    • (1998) Acta Med. (Hradec Kralove) , vol.41 , Issue.2 , pp. 73-80
    • Mokry, J.1    Nemecek, S.2
  • 88
    • 0032587169 scopus 로고    scopus 로고
    • AlphaB-crystallin selectively targets intermediate filament proteins during thermal stress
    • Muchowski P.J., Valdez M.M., et al. AlphaB-crystallin selectively targets intermediate filament proteins during thermal stress. Invest. Ophthalmol. Vis. Sci. 40 5 (1999) 951-958
    • (1999) Invest. Ophthalmol. Vis. Sci. , vol.40 , Issue.5 , pp. 951-958
    • Muchowski, P.J.1    Valdez, M.M.2
  • 89
    • 0028176579 scopus 로고
    • Chaperone activity of alpha-crystallins modulates intermediate filament assembly
    • Nicholl I.D., and Quinlan R.A. Chaperone activity of alpha-crystallins modulates intermediate filament assembly. EMBO J 13 4 (1994) 945-953
    • (1994) EMBO J , vol.13 , Issue.4 , pp. 945-953
    • Nicholl, I.D.1    Quinlan, R.A.2
  • 90
    • 6344273968 scopus 로고    scopus 로고
    • Intermediate filament proteins and their associated diseases
    • Omary M.B., Coulombe P.A., et al. Intermediate filament proteins and their associated diseases. N. Engl. J. Med. 351 20 (2004) 2087-2100
    • (2004) N. Engl. J. Med. , vol.351 , Issue.20 , pp. 2087-2100
    • Omary, M.B.1    Coulombe, P.A.2
  • 91
    • 0027180063 scopus 로고
    • Evidence that the chick lens cytoskeletal protein CP 49 belongs to the family of intermediate filament proteins
    • Orii H., Agata K., et al. Evidence that the chick lens cytoskeletal protein CP 49 belongs to the family of intermediate filament proteins. Curr. Eye Res. 12 6 (1993) 583-588
    • (1993) Curr. Eye Res. , vol.12 , Issue.6 , pp. 583-588
    • Orii, H.1    Agata, K.2
  • 92
    • 0036097410 scopus 로고    scopus 로고
    • Apoptosis and keratin intermediate filaments
    • Oshima R.G. Apoptosis and keratin intermediate filaments. Cell Death Differ. 9 5 (2002) 486-492
    • (2002) Cell Death Differ. , vol.9 , Issue.5 , pp. 486-492
    • Oshima, R.G.1
  • 93
    • 0032818827 scopus 로고    scopus 로고
    • Intermediate filament interactions can be altered by HSP27 and alphaB-crystallin
    • Perng M.D., Cairns L., et al. Intermediate filament interactions can be altered by HSP27 and alphaB-crystallin. J. Cell Sci. 112 Pt. 13 (1999) 2099-2112
    • (1999) J. Cell Sci. , vol.112 , Issue.PART 13 , pp. 2099-2112
    • Perng, M.D.1    Cairns, L.2
  • 94
    • 0000843475 scopus 로고    scopus 로고
    • The cardiomyopathy and lens cataract mutation in alphaB-crystallin alters its protein structure, chaperone activity, and interaction with intermediate filaments in vitro
    • Perng M.D., Muchowski P.J., et al. The cardiomyopathy and lens cataract mutation in alphaB-crystallin alters its protein structure, chaperone activity, and interaction with intermediate filaments in vitro. J. Biol. Chem. 274 47 (1999) 33235-33243
    • (1999) J. Biol. Chem. , vol.274 , Issue.47 , pp. 33235-33243
    • Perng, M.D.1    Muchowski, P.J.2
  • 95
    • 38449095529 scopus 로고    scopus 로고
    • Identifying the role of specific motifs in the lens fiber cell specific intermediate filament phakosin
    • Pittenger J.T., Hess J.F., et al. Identifying the role of specific motifs in the lens fiber cell specific intermediate filament phakosin. Invest. Ophthalmol. Vis. Sci. 48 11 (2007) 5132-5141
    • (2007) Invest. Ophthalmol. Vis. Sci. , vol.48 , Issue.11 , pp. 5132-5141
    • Pittenger, J.T.1    Hess, J.F.2
  • 96
    • 0026474383 scopus 로고
    • The 53 kDa polypeptide component of the bovine fibre cell cytoskeleton is derived from the 115 kDa beaded filament protein: evidence for a fibre cell specific intermediate filament protein
    • Quinlan R.A., Carter J.M., et al. The 53 kDa polypeptide component of the bovine fibre cell cytoskeleton is derived from the 115 kDa beaded filament protein: evidence for a fibre cell specific intermediate filament protein. Curr. Eye Res. 11 9 (1992) 909-921
    • (1992) Curr. Eye Res. , vol.11 , Issue.9 , pp. 909-921
    • Quinlan, R.A.1    Carter, J.M.2
  • 97
    • 34147101803 scopus 로고    scopus 로고
    • Autosomal recessive juvenile onset cataract associated with mutation in BFSP1
    • Ramachandran R.D., Perumalsamy V., et al. Autosomal recessive juvenile onset cataract associated with mutation in BFSP1. Hum. Genet. 121 3-4 (2007) 475-482
    • (2007) Hum. Genet. , vol.121 , Issue.3-4 , pp. 475-482
    • Ramachandran, R.D.1    Perumalsamy, V.2
  • 98
    • 0020315289 scopus 로고
    • Lenticular intermediate-sized filaments: biosynthesis and interaction with plasma membrane
    • Ramaekers F.C., Dunia I., et al. Lenticular intermediate-sized filaments: biosynthesis and interaction with plasma membrane. Proc. Natl. Acad. Sci. USA 79 10 (1982) 3208-3812
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , Issue.10 , pp. 3208-3812
    • Ramaekers, F.C.1    Dunia, I.2
  • 99
    • 0027182464 scopus 로고
    • Chicken filensin: a lens fiber cell protein that exhibits sequence similarity to intermediate filament proteins
    • Remington S.G. Chicken filensin: a lens fiber cell protein that exhibits sequence similarity to intermediate filament proteins. J. Cell Sci. 105 Pt. 4 (1993) 1057-1068
    • (1993) J. Cell Sci. , vol.105 , Issue.PART 4 , pp. 1057-1068
    • Remington, S.G.1
  • 100
    • 0030069596 scopus 로고    scopus 로고
    • Calcium ionophore induced proteolysis and cataract: inhibition by cell permeable calpain antagonists
    • Sanderson J., Marcantonio J.M., et al. Calcium ionophore induced proteolysis and cataract: inhibition by cell permeable calpain antagonists. Biochem. Biophys. Res. Commun. 218 3 (1996) 893-901
    • (1996) Biochem. Biophys. Res. Commun. , vol.218 , Issue.3 , pp. 893-901
    • Sanderson, J.1    Marcantonio, J.M.2
  • 102
    • 0028905818 scopus 로고
    • Vimentin and CP49/filensin form distinct networks in the lens which are independently modulated during lens fibre cell differentiation
    • Sandilands A., Prescott A.R., et al. Vimentin and CP49/filensin form distinct networks in the lens which are independently modulated during lens fibre cell differentiation. J. Cell Sci. 108 Pt. 4 (1995) 1397-1406
    • (1995) J. Cell Sci. , vol.108 , Issue.PART 4 , pp. 1397-1406
    • Sandilands, A.1    Prescott, A.R.2
  • 103
    • 0029148358 scopus 로고
    • Filensin is proteolytically processed during lens fiber cell differentiation by multiple independent pathways
    • Sandilands A., Prescott A.R., et al. Filensin is proteolytically processed during lens fiber cell differentiation by multiple independent pathways. Eur. J. Cell Biol. 67 3 (1995) 238-253
    • (1995) Eur. J. Cell Biol. , vol.67 , Issue.3 , pp. 238-253
    • Sandilands, A.1    Prescott, A.R.2
  • 104
    • 0037373876 scopus 로고    scopus 로고
    • Knockout of the intermediate filament protein CP49 destabilises the lens fibre cell cytoskeleton and decreases lens optical quality, but does not induce cataract
    • Sandilands A., Prescott A.R., et al. Knockout of the intermediate filament protein CP49 destabilises the lens fibre cell cytoskeleton and decreases lens optical quality, but does not induce cataract. Exp. Eye Res. 76 3 (2003) 385-391
    • (2003) Exp. Eye Res. , vol.76 , Issue.3 , pp. 385-391
    • Sandilands, A.1    Prescott, A.R.2
  • 105
    • 0345550308 scopus 로고    scopus 로고
    • Bfsp2 mutation found in mouse 129 strains causes the loss of CP49' and induces vimentin-dependent changes in the lens fibre cell cytoskeleton
    • Sandilands A., Wang X., et al. Bfsp2 mutation found in mouse 129 strains causes the loss of CP49' and induces vimentin-dependent changes in the lens fibre cell cytoskeleton. Exp. Eye Res. 78 4 (2004) 875-889
    • (2004) Exp. Eye Res. , vol.78 , Issue.4 , pp. 875-889
    • Sandilands, A.1    Wang, X.2
  • 106
    • 0029032223 scopus 로고
    • The predicted structure of chick lens CP49 and a variant thereof, CP49ins, the first vertebrate cytoplasmic intermediate filament protein with a lamin-like insertion in helix 1B
    • Sawada K., Agata J., et al. The predicted structure of chick lens CP49 and a variant thereof, CP49ins, the first vertebrate cytoplasmic intermediate filament protein with a lamin-like insertion in helix 1B. Curr. Eye Res. 14 7 (1995) 545-553
    • (1995) Curr. Eye Res. , vol.14 , Issue.7 , pp. 545-553
    • Sawada, K.1    Agata, J.2
  • 107
    • 0023784401 scopus 로고
    • Immunogold-EM localization of actin and vimentin filaments in relation to polygonal arrays in lens epithelium in situ
    • Scholz D.L., and Rafferty N.S. Immunogold-EM localization of actin and vimentin filaments in relation to polygonal arrays in lens epithelium in situ. Curr. Eye Res. 7 7 (1988) 705-719
    • (1988) Curr. Eye Res. , vol.7 , Issue.7 , pp. 705-719
    • Scholz, D.L.1    Rafferty, N.S.2
  • 108
    • 1642633830 scopus 로고    scopus 로고
    • Digital image capture and quantification of subtle lens opacities in rodents
    • Seeberger T.M., Matsumoto Y., et al. Digital image capture and quantification of subtle lens opacities in rodents. J. Biomed. Opt. 9 1 (2004) 116-120
    • (2004) J. Biomed. Opt. , vol.9 , Issue.1 , pp. 116-120
    • Seeberger, T.M.1    Matsumoto, Y.2
  • 109
    • 34247127422 scopus 로고    scopus 로고
    • Inbred FVB/N mice are mutant at the cp49/Bfsp2 locus and lack beaded filament proteins in the lens
    • Simirskii V.N., Lee R.S., et al. Inbred FVB/N mice are mutant at the cp49/Bfsp2 locus and lack beaded filament proteins in the lens. Invest. Ophthalmol. Vis. Sci. 47 11 (2006) 4931-4934
    • (2006) Invest. Ophthalmol. Vis. Sci. , vol.47 , Issue.11 , pp. 4931-4934
    • Simirskii, V.N.1    Lee, R.S.2
  • 110
    • 48949116520 scopus 로고    scopus 로고
    • Protein-protein interactions between lens vimentin and alphaB-crystallin using FRET acceptor photobleaching
    • Song S., Hanson M.J., et al. Protein-protein interactions between lens vimentin and alphaB-crystallin using FRET acceptor photobleaching. Mol. Vis. 14 (2008) 1282-1287
    • (2008) Mol. Vis. , vol.14 , pp. 1282-1287
    • Song, S.1    Hanson, M.J.2
  • 111
    • 34249685610 scopus 로고    scopus 로고
    • Plakins in development and disease
    • Sonnenberg A., and Liem R.K. Plakins in development and disease. Exp. Cell Res. 313 10 (2007) 2189-2203
    • (2007) Exp. Cell Res. , vol.313 , Issue.10 , pp. 2189-2203
    • Sonnenberg, A.1    Liem, R.K.2
  • 112
    • 0348143124 scopus 로고    scopus 로고
    • A novel cell-cell junction system: the cortex adhaerens mosaic of lens fiber cells
    • Straub B.K., Boda J., et al. A novel cell-cell junction system: the cortex adhaerens mosaic of lens fiber cells. J. Cell Sci. 116 Pt. 24 (2003) 4985-4995
    • (2003) J. Cell Sci. , vol.116 , Issue.PART 24 , pp. 4985-4995
    • Straub, B.K.1    Boda, J.2
  • 113
    • 0141672002 scopus 로고    scopus 로고
    • Synemin expression in developing normal and pathological human retina and lens
    • Tawk M., Titeux M., et al. Synemin expression in developing normal and pathological human retina and lens. Exp. Neurol. 183 2 (2003) 499-507
    • (2003) Exp. Neurol. , vol.183 , Issue.2 , pp. 499-507
    • Tawk, M.1    Titeux, M.2
  • 114
    • 27744556965 scopus 로고    scopus 로고
    • Cellular integrity plus: organelle-related and protein-targeting functions of intermediate filaments
    • Toivola D.M., Tao G.Z., et al. Cellular integrity plus: organelle-related and protein-targeting functions of intermediate filaments. Trends Cell Biol. 15 11 (2005) 608-617
    • (2005) Trends Cell Biol. , vol.15 , Issue.11 , pp. 608-617
    • Toivola, D.M.1    Tao, G.Z.2
  • 115
    • 13444260973 scopus 로고    scopus 로고
    • R120G alphaB-crystallin promotes the unfolding of reduced alpha-lactalbumin and is inherently unstable
    • Treweek T.M., Rekas A., et al. R120G alphaB-crystallin promotes the unfolding of reduced alpha-lactalbumin and is inherently unstable. FEBS J. 272 3 (2005) 711-724
    • (2005) FEBS J. , vol.272 , Issue.3 , pp. 711-724
    • Treweek, T.M.1    Rekas, A.2
  • 116
    • 0025205118 scopus 로고
    • Calcium-induced opacification and proteolysis in the intact rat lens
    • Truscott R.J., Marcantonio J.M., et al. Calcium-induced opacification and proteolysis in the intact rat lens. Invest. Ophthalmol. Vis. Sci. 31 11 (1990) 2405-2411
    • (1990) Invest. Ophthalmol. Vis. Sci. , vol.31 , Issue.11 , pp. 2405-2411
    • Truscott, R.J.1    Marcantonio, J.M.2
  • 117
    • 17344361902 scopus 로고    scopus 로고
    • A missense mutation in the alphaB-crystallin chaperone gene causes a desmin-related myopathy
    • Vicart P., Caron A., et al. A missense mutation in the alphaB-crystallin chaperone gene causes a desmin-related myopathy. Nat. Genet. 20 1 (1998) 92-95
    • (1998) Nat. Genet. , vol.20 , Issue.1 , pp. 92-95
    • Vicart, P.1    Caron, A.2
  • 118
    • 0032574667 scopus 로고    scopus 로고
    • The chicken CP49 gene contains an extra exon compared to the human CP49 gene which identifies an important step in the evolution of the eye lens intermediate filament proteins
    • Wallace P., Signer E., et al. The chicken CP49 gene contains an extra exon compared to the human CP49 gene which identifies an important step in the evolution of the eye lens intermediate filament proteins. Gene 211 1 (1998) 19-27
    • (1998) Gene , vol.211 , Issue.1 , pp. 19-27
    • Wallace, P.1    Signer, E.2
  • 119
    • 34249059782 scopus 로고    scopus 로고
    • The Mrj co-chaperone mediates keratin turnover and prevents the formation of toxic inclusion bodies in trophoblast cells of the placenta
    • Watson E.D., Geary-Joo C., et al. The Mrj co-chaperone mediates keratin turnover and prevents the formation of toxic inclusion bodies in trophoblast cells of the placenta. Development 134 9 (2007) 1809-1817
    • (2007) Development , vol.134 , Issue.9 , pp. 1809-1817
    • Watson, E.D.1    Geary-Joo, C.2
  • 120
    • 28544437813 scopus 로고    scopus 로고
    • Nesprin-3, a novel outer nuclear membrane protein, associates with the cytoskeletal linker protein plectin
    • Wilhelmsen K., Litjens S.H., et al. Nesprin-3, a novel outer nuclear membrane protein, associates with the cytoskeletal linker protein plectin. J. Cell Biol. 171 5 (2005) 799-810
    • (2005) J. Cell Biol. , vol.171 , Issue.5 , pp. 799-810
    • Wilhelmsen, K.1    Litjens, S.H.2
  • 121
    • 2342481180 scopus 로고    scopus 로고
    • Identification of novel principles of keratin filament network turnover in living cells
    • Windoffer R., Woll S., et al. Identification of novel principles of keratin filament network turnover in living cells. Mol. Biol. Cell 15 5 (2004) 2436-2448
    • (2004) Mol. Biol. Cell , vol.15 , Issue.5 , pp. 2436-2448
    • Windoffer, R.1    Woll, S.2
  • 122
    • 33646433420 scopus 로고    scopus 로고
    • Focal adhesions are hotspots for keratin filament precursor formation
    • Windoffer R., Kolsch A., et al. Focal adhesions are hotspots for keratin filament precursor formation. J. Cell Biol. 173 3 (2006) 341-348
    • (2006) J. Cell Biol. , vol.173 , Issue.3 , pp. 341-348
    • Windoffer, R.1    Kolsch, A.2
  • 123
    • 42749096587 scopus 로고    scopus 로고
    • A role for lengsin, a recruited enzyme, in terminal differentiation in the vertebrate lens
    • Wyatt K., Gao C., et al. A role for lengsin, a recruited enzyme, in terminal differentiation in the vertebrate lens. J. Biol. Chem. 283 10 (2008) 6607-6615
    • (2008) J. Biol. Chem. , vol.283 , Issue.10 , pp. 6607-6615
    • Wyatt, K.1    Gao, C.2
  • 124
    • 0034214304 scopus 로고    scopus 로고
    • Nestin expression during mouse eye and lens development
    • Yang J., Bian W., et al. Nestin expression during mouse eye and lens development. Mech. Dev. 94 1-2 (2000) 287-291
    • (2000) Mech. Dev. , vol.94 , Issue.1-2 , pp. 287-291
    • Yang, J.1    Bian, W.2
  • 125
    • 41949122572 scopus 로고    scopus 로고
    • Resisting the effects of aging: a function for the fiber cell beaded filament
    • Yoon K.H., Blankenship T., et al. Resisting the effects of aging: a function for the fiber cell beaded filament. Invest. Ophthalmol. Vis. Sci. 49 3 (2008) 1030-1036
    • (2008) Invest. Ophthalmol. Vis. Sci. , vol.49 , Issue.3 , pp. 1030-1036
    • Yoon, K.H.1    Blankenship, T.2
  • 127
    • 0021141629 scopus 로고
    • 2+-dependent cysteine proteinase, in bovine lens
    • 2+-dependent cysteine proteinase, in bovine lens. FEBS Lett. 170 2 (1984) 259-262
    • (1984) FEBS Lett. , vol.170 , Issue.2 , pp. 259-262
    • Yoshida, H.1    Murachi, T.2
  • 128
    • 33846012542 scopus 로고    scopus 로고
    • Progressive sutural cataract associated with a BFSP2 mutation in a Chinese family
    • 1626-1231
    • Zhang L., Gao L., et al. Progressive sutural cataract associated with a BFSP2 mutation in a Chinese family. Mol. Vis 12 (2006) 1626-1231
    • (2006) Mol. Vis , vol.12
    • Zhang, L.1    Gao, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.