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Volumn 156, Issue , 2017, Pages 58-71

The lens actin filament cytoskeleton: Diverse structures for complex functions

Author keywords

Actin binding proteins; Actin dynamics; Cytoskeleton; Fiber cell; Lens development; Membrane skeleton; Myosin; Tropomodulin

Indexed keywords

ACTIN; ACTIN BINDING PROTEIN; ACTIN RELATED PROTEIN 2-3 COMPLEX; ALPHA ACTININ; ALPHA CRYSTALLIN; BETA CRYSTALLIN; COFILIN; CORTACTIN; EZRIN; F ACTIN; GAMMA CRYSTALLIN; GELSOLIN; METHENAMINE; MYOSIN; MYOSIN II; MYOSIN LIGHT CHAIN KINASE; NERVE CELL ADHESION MOLECULE; NEURAL WISKOTT ALDRICH SYNDROME PROTEIN; PLECTIN; PROTEIN CDC42; RAC1 PROTEIN; RAP1 PROTEIN; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; RHOB GUANINE NUCLEOTIDE BINDING PROTEIN; SPECTRIN; TROPOMODULIN; TROPOMYOSIN; UVOMORULIN;

EID: 84961219239     PISSN: 00144835     EISSN: 10960007     Source Type: Journal    
DOI: 10.1016/j.exer.2016.03.005     Document Type: Article
Times cited : (49)

References (248)
  • 1
    • 79960128316 scopus 로고    scopus 로고
    • Establishment of conditional reporter mouse lines at ROSA26 locus for live cell imaging
    • Abe, T., Kiyonari, H., Shioi, G., Inoue, K., Nakao, K., Aizawa, S., Fujimori, T., Establishment of conditional reporter mouse lines at ROSA26 locus for live cell imaging. Genesis 49 (2011), 579–590.
    • (2011) Genesis , vol.49 , pp. 579-590
    • Abe, T.1    Kiyonari, H.2    Shioi, G.3    Inoue, K.4    Nakao, K.5    Aizawa, S.6    Fujimori, T.7
  • 2
    • 0038519687 scopus 로고    scopus 로고
    • Morphology and organization of posterior fiber ends during migration
    • Al-Ghoul, K.J., Kuszak, J.R., Lu, J.Y., Owens, M.J., Morphology and organization of posterior fiber ends during migration. Mol. Vis. 9 (2003), 119–128.
    • (2003) Mol. Vis. , vol.9 , pp. 119-128
    • Al-Ghoul, K.J.1    Kuszak, J.R.2    Lu, J.Y.3    Owens, M.J.4
  • 4
    • 0023668669 scopus 로고
    • Band 3 and ankyrin homologues are present in eye lens: evidence for all major erythrocyte membrane components in same non-erythroid cell
    • Allen, D.P., Low, P.S., Dola, A., Maisel, H., Band 3 and ankyrin homologues are present in eye lens: evidence for all major erythrocyte membrane components in same non-erythroid cell. Biochem. biophysical Res. Commun. 149 (1987), 266–275.
    • (1987) Biochem. biophysical Res. Commun. , vol.149 , pp. 266-275
    • Allen, D.P.1    Low, P.S.2    Dola, A.3    Maisel, H.4
  • 5
    • 33749059234 scopus 로고    scopus 로고
    • Actin-targeting natural products: structures, properties and mechanisms of action. Cellular and molecular life sciences
    • Allingham, J.S., Klenchin, V.A., Rayment, I., Actin-targeting natural products: structures, properties and mechanisms of action. Cellular and molecular life sciences. CMLS 63 (2006), 2119–2134.
    • (2006) CMLS , vol.63 , pp. 2119-2134
    • Allingham, J.S.1    Klenchin, V.A.2    Rayment, I.3
  • 6
    • 0033214493 scopus 로고    scopus 로고
    • Identification of a novel tropomodulin isoform, skeletal tropomodulin, that caps actin filament pointed ends in fast skeletal muscle
    • Almenar-Queralt, A., Lee, A., Conley, C.A., Ribas de Pouplana, L., Fowler, V.M., Identification of a novel tropomodulin isoform, skeletal tropomodulin, that caps actin filament pointed ends in fast skeletal muscle. J. Biol. Chem. 274 (1999), 28466–28475.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28466-28475
    • Almenar-Queralt, A.1    Lee, A.2    Conley, C.A.3    Ribas de Pouplana, L.4    Fowler, V.M.5
  • 7
    • 0035910096 scopus 로고    scopus 로고
    • Direct real-time observation of actin filament branching mediated by Arp2/3 complex using total internal reflection fluorescence microscopy
    • Amann, K.J., Pollard, T.D., Direct real-time observation of actin filament branching mediated by Arp2/3 complex using total internal reflection fluorescence microscopy. Proc. Natl. Acad. Sci. U. S. A. 98 (2001), 15009–15013.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 15009-15013
    • Amann, K.J.1    Pollard, T.D.2
  • 8
    • 84899755134 scopus 로고    scopus 로고
    • In vivo substrates of the lens molecular chaperones alphaA-crystallin and alphaB-crystallin
    • Andley, U.P., Malone, J.P., Townsend, R.R., In vivo substrates of the lens molecular chaperones alphaA-crystallin and alphaB-crystallin. PloS one, 9, 2014, e95507.
    • (2014) PloS one , vol.9 , pp. e95507
    • Andley, U.P.1    Malone, J.P.2    Townsend, R.R.3
  • 9
    • 0032213892 scopus 로고    scopus 로고
    • Not just scaffolding: plectin regulates actin dynamics in cultured cells
    • Andra, K., Nikolic, B., Stocher, M., Drenckhahn, D., Wiche, G., Not just scaffolding: plectin regulates actin dynamics in cultured cells. Genes & Dev. 12 (1998), 3442–3451.
    • (1998) Genes & Dev. , vol.12 , pp. 3442-3451
    • Andra, K.1    Nikolic, B.2    Stocher, M.3    Drenckhahn, D.4    Wiche, G.5
  • 10
    • 0022486518 scopus 로고
    • The 4.1-like proteins of the bovine lens: spectrin-binding proteins closely related in structure to red blood cell protein 4.1
    • Aster, J.C., Brewer, G.J., Maisel, H., The 4.1-like proteins of the bovine lens: spectrin-binding proteins closely related in structure to red blood cell protein 4.1. J. cell Biol. 103 (1986), 115–122.
    • (1986) J. cell Biol. , vol.103 , pp. 115-122
    • Aster, J.C.1    Brewer, G.J.2    Maisel, H.3
  • 13
    • 0019170917 scopus 로고
    • Partial purification and characterization of an actin depolymerizing factor from brain
    • Bamburg, J.R., Harris, H.E., Weeds, A.G., Partial purification and characterization of an actin depolymerizing factor from brain. FEBS Lett. 121 (1980), 178–182.
    • (1980) FEBS Lett. , vol.121 , pp. 178-182
    • Bamburg, J.R.1    Harris, H.E.2    Weeds, A.G.3
  • 14
    • 0027057819 scopus 로고
    • Mitochondrial dynamics in differentiating fiber cells of the mammalian lens
    • Bassnett, S., Mitochondrial dynamics in differentiating fiber cells of the mammalian lens. Curr. Eye Res. 11 (1992), 1227–1232.
    • (1992) Curr. Eye Res. , vol.11 , pp. 1227-1232
    • Bassnett, S.1
  • 15
    • 0029127167 scopus 로고
    • The fate of the Golgi apparatus and the endoplasmic reticulum during lens fiber cell differentiation
    • Bassnett, S., The fate of the Golgi apparatus and the endoplasmic reticulum during lens fiber cell differentiation. Investigative Ophthalmol. Vis. Sci. 36 (1995), 1793–1803.
    • (1995) Investigative Ophthalmol. Vis. Sci. , vol.36 , pp. 1793-1803
    • Bassnett, S.1
  • 16
    • 29044435230 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of cells in the living lens: the relationship between cell length and volume
    • Bassnett, S., Three-dimensional reconstruction of cells in the living lens: the relationship between cell length and volume. Exp. eye Res. 81 (2005), 716–723.
    • (2005) Exp. eye Res. , vol.81 , pp. 716-723
    • Bassnett, S.1
  • 17
    • 0026774623 scopus 로고
    • Coincident loss of mitochondria and nuclei during lens fiber cell differentiation
    • An official publication of the American Association of Anatomists
    • Bassnett, S., Beebe, D.C., Coincident loss of mitochondria and nuclei during lens fiber cell differentiation. An official publication of the American Association of Anatomists Dev. Dyn. 194 (1992), 85–93.
    • (1992) Dev. Dyn. , vol.194 , pp. 85-93
    • Bassnett, S.1    Beebe, D.C.2
  • 18
    • 0031002566 scopus 로고    scopus 로고
    • Chromatin degradation in differentiating fiber cells of the eye lens
    • Bassnett, S., Mataic, D., Chromatin degradation in differentiating fiber cells of the eye lens. J. cell Biol. 137 (1997), 37–49.
    • (1997) J. cell Biol. , vol.137 , pp. 37-49
    • Bassnett, S.1    Mataic, D.2
  • 19
    • 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. 112:13 (1999), 2155–2165.
    • (1999) J. cell Sci. , vol.112 , Issue.13 , pp. 2155-2165
    • Bassnett, S.1    Missey, H.2    Vucemilo, I.3
  • 20
    • 0037374457 scopus 로고    scopus 로고
    • Morphometric analysis of fibre cell growth in the developing chicken lens
    • Bassnett, S., Winzenburger, P.A., Morphometric analysis of fibre cell growth in the developing chicken lens. Exp. eye Res. 76 (2003), 291–302.
    • (2003) Exp. eye Res. , vol.76 , pp. 291-302
    • Bassnett, S.1    Winzenburger, P.A.2
  • 21
    • 0024798108 scopus 로고
    • Cytochalasin prevents cell elongation and increases potassium efflux from embryonic lens epithelial cells: implications for the mechanism of lens fiber cell elongation
    • Beebe, D.C., Cerrelli, S., Cytochalasin prevents cell elongation and increases potassium efflux from embryonic lens epithelial cells: implications for the mechanism of lens fiber cell elongation. Lens eye Toxic. Res. 6 (1989), 589–601.
    • (1989) Lens eye Toxic. Res. , vol.6 , pp. 589-601
    • Beebe, D.C.1    Cerrelli, S.2
  • 23
    • 0034958883 scopus 로고    scopus 로고
    • Spectrin and ankyrin-based pathways: metazoan inventions for integrating cells into tissues
    • Bennett, V., Baines, A.J., Spectrin and ankyrin-based pathways: metazoan inventions for integrating cells into tissues. Physiol. Rev. 81 (2001), 1353–1392.
    • (2001) Physiol. Rev. , vol.81 , pp. 1353-1392
    • Bennett, V.1    Baines, A.J.2
  • 24
    • 0018397366 scopus 로고
    • Identification and partial purification of ankyrin, the high affinity membrane attachment site for human erythrocyte spectrin
    • Bennett, V., Stenbuck, P.J., Identification and partial purification of ankyrin, the high affinity membrane attachment site for human erythrocyte spectrin. J. Biol. Chem. 254 (1979), 2533–2541.
    • (1979) J. Biol. Chem. , vol.254 , pp. 2533-2541
    • Bennett, V.1    Stenbuck, P.J.2
  • 25
    • 0019309226 scopus 로고
    • Human erythrocyte ankyrin. Purification and properties
    • Bennett, V., Stenbuck, P.J., Human erythrocyte ankyrin. Purification and properties. J. Biol. Chem. 255 (1980), 2540–2548.
    • (1980) J. Biol. Chem. , vol.255 , pp. 2540-2548
    • Bennett, V.1    Stenbuck, P.J.2
  • 26
    • 0034213327 scopus 로고    scopus 로고
    • Rho GTPases and their effector proteins
    • Bishop, A.L., Hall, A., Rho GTPases and their effector proteins. Biochem. J. 348:2 (2000), 241–255.
    • (2000) Biochem. J. , vol.348 , Issue.2 , pp. 241-255
    • Bishop, A.L.1    Hall, A.2
  • 27
    • 84950104731 scopus 로고    scopus 로고
    • Breakdown of interlocking domains may contribute to formation of membranous globules and lens opacity in ephrin-A5 mice
    • Biswas, S., Son, A., Yu, Q., Zhou, R., Lo, W.K., Breakdown of interlocking domains may contribute to formation of membranous globules and lens opacity in ephrin-A5 mice. Exp. eye Res. 145 (2015), 130–139.
    • (2015) Exp. eye Res. , vol.145 , pp. 130-139
    • Biswas, S.1    Son, A.2    Yu, Q.3    Zhou, R.4    Lo, W.K.5
  • 28
    • 0034720293 scopus 로고    scopus 로고
    • Direct observation of dendritic actin filament networks nucleated by Arp2/3 complex and WASP/Scar proteins
    • Blanchoin, L., Amann, K.J., Higgs, H.N., Marchand, J.B., Kaiser, D.A., Pollard, T.D., Direct observation of dendritic actin filament networks nucleated by Arp2/3 complex and WASP/Scar proteins. Nature 404 (2000), 1007–1011.
    • (2000) Nature , vol.404 , pp. 1007-1011
    • Blanchoin, L.1    Amann, K.J.2    Higgs, H.N.3    Marchand, J.B.4    Kaiser, D.A.5    Pollard, T.D.6
  • 29
    • 72049086019 scopus 로고    scopus 로고
    • Inhibitors target actin nucleators
    • Blanchoin, L., Boujemaa-Paterski, R., Inhibitors target actin nucleators. Chem. Biol. 16 (2009), 1125–1126.
    • (2009) Chem. Biol. , vol.16 , pp. 1125-1126
    • Blanchoin, L.1    Boujemaa-Paterski, R.2
  • 30
    • 0035097221 scopus 로고    scopus 로고
    • Development- and differentiation-dependent reorganization of intermediate filaments in fiber cells
    • Blankenship, T.N., Hess, J.F., FitzGerald, P.G., Development- and differentiation-dependent reorganization of intermediate filaments in fiber cells. Investigative Ophthalmol. Vis. Sci. 42 (2001), 735–742.
    • (2001) Investigative Ophthalmol. Vis. Sci. , vol.42 , pp. 735-742
    • Blankenship, T.N.1    Hess, J.F.2    FitzGerald, P.G.3
  • 31
    • 0018038933 scopus 로고
    • Selective assay of monomeric and filamentous actin in cell extracts, using inhibition of deoxyribonuclease I
    • Blikstad, I., Markey, F., Carlsson, L., Persson, T., Lindberg, U., Selective assay of monomeric and filamentous actin in cell extracts, using inhibition of deoxyribonuclease I. Cell 15 (1978), 935–943.
    • (1978) Cell , vol.15 , pp. 935-943
    • Blikstad, I.1    Markey, F.2    Carlsson, L.3    Persson, T.4    Lindberg, U.5
  • 34
    • 0029739781 scopus 로고    scopus 로고
    • Liquefaction of cortical tissue in diabetic and galactosemic rat lenses defined by confocal laser scanning microscopy
    • Bond, J., Green, C., Donaldson, P., Kistler, J., Liquefaction of cortical tissue in diabetic and galactosemic rat lenses defined by confocal laser scanning microscopy. Investigative Ophthalmol. Vis. Sci. 37 (1996), 1557–1565.
    • (1996) Investigative Ophthalmol. Vis. Sci. , vol.37 , pp. 1557-1565
    • Bond, J.1    Green, C.2    Donaldson, P.3    Kistler, J.4
  • 35
    • 79956022112 scopus 로고    scopus 로고
    • Rho signaling pathway and apical constriction in the early lens placode
    • Borges, R.M., Lamers, M.L., Forti, F.L., Santos, M.F., Yan, C.Y., Rho signaling pathway and apical constriction in the early lens placode. Genesis 49 (2011), 368–379.
    • (2011) Genesis , vol.49 , pp. 368-379
    • Borges, R.M.1    Lamers, M.L.2    Forti, F.L.3    Santos, M.F.4    Yan, C.Y.5
  • 36
    • 0018373968 scopus 로고
    • The cytoskeleton of chick lens cells
    • Bradley, R.H., Ireland, M., Maisel, H., The cytoskeleton of chick lens cells. Exp. eye Res. 28 (1979), 441–453.
    • (1979) Exp. eye Res. , vol.28 , pp. 441-453
    • Bradley, R.H.1    Ireland, M.2    Maisel, H.3
  • 37
    • 0020804117 scopus 로고
    • Purification of an 80,000-dalton protein that is a component of the isolated microvillus cytoskeleton, and its localization in nonmuscle cells
    • Bretscher, A., Purification of an 80,000-dalton protein that is a component of the isolated microvillus cytoskeleton, and its localization in nonmuscle cells. J. cell Biol. 97 (1983), 425–432.
    • (1983) J. cell Biol. , vol.97 , pp. 425-432
    • Bretscher, A.1
  • 38
    • 0034524664 scopus 로고    scopus 로고
    • ERM-Merlin and EBP50 protein families in plasma membrane organization and function
    • Bretscher, A., Chambers, D., Nguyen, R., Reczek, D., ERM-Merlin and EBP50 protein families in plasma membrane organization and function. Annu. Rev. cell Dev. Biol. 16 (2000), 113–143.
    • (2000) Annu. Rev. cell Dev. Biol. , vol.16 , pp. 113-143
    • Bretscher, A.1    Chambers, D.2    Nguyen, R.3    Reczek, D.4
  • 40
    • 39149135555 scopus 로고    scopus 로고
    • Differential binding of mutant (R116C) and wildtype alphaA crystallin to actin
    • Brown, Z., Ponce, A., Lampi, K., Hancock, L., Takemoto, L., Differential binding of mutant (R116C) and wildtype alphaA crystallin to actin. Curr. eye Res. 32 (2007), 1051–1054.
    • (2007) Curr. eye Res. , vol.32 , pp. 1051-1054
    • Brown, Z.1    Ponce, A.2    Lampi, K.3    Hancock, L.4    Takemoto, L.5
  • 41
    • 0028244823 scopus 로고
    • Jasplakinolide, a cytotoxic natural product, induces actin polymerization and competitively inhibits the binding of phalloidin to F-actin
    • Bubb, M.R., Senderowicz, A.M., Sausville, E.A., Duncan, K.L., Korn, E.D., Jasplakinolide, a cytotoxic natural product, induces actin polymerization and competitively inhibits the binding of phalloidin to F-actin. J. Biol. Chem. 269 (1994), 14869–14871.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14869-14871
    • Bubb, M.R.1    Senderowicz, A.M.2    Sausville, E.A.3    Duncan, K.L.4    Korn, E.D.5
  • 42
    • 0034681423 scopus 로고    scopus 로고
    • Effects of jasplakinolide on the kinetics of actin polymerization. An explanation for certain in vivo observations
    • Bubb, M.R., Spector, I., Beyer, B.B., Fosen, K.M., Effects of jasplakinolide on the kinetics of actin polymerization. An explanation for certain in vivo observations. J. Biol. Chem. 275 (2000), 5163–5170.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5163-5170
    • Bubb, M.R.1    Spector, I.2    Beyer, B.B.3    Fosen, K.M.4
  • 45
    • 70350179623 scopus 로고    scopus 로고
    • Cdc42- and IRSp53-dependent contractile filopodia tether presumptive lens and retina to coordinate epithelial invagination
    • Chauhan, B.K., Disanza, A., Choi, S.Y., Faber, S.C., Lou, M., Beggs, H.E., Scita, G., Zheng, Y., Lang, R.A., Cdc42- and IRSp53-dependent contractile filopodia tether presumptive lens and retina to coordinate epithelial invagination. Development 136 (2009), 3657–3667.
    • (2009) Development , vol.136 , pp. 3657-3667
    • Chauhan, B.K.1    Disanza, A.2    Choi, S.Y.3    Faber, S.C.4    Lou, M.5    Beggs, H.E.6    Scita, G.7    Zheng, Y.8    Lang, R.A.9
  • 46
    • 33846394751 scopus 로고    scopus 로고
    • A role for Wnt/planar cell polarity signaling during lens fiber cell differentiation?
    • Chen, Y., Stump, R.J., Lovicu, F.J., McAvoy, J.W., A role for Wnt/planar cell polarity signaling during lens fiber cell differentiation?. Seminars cell & Dev. Biol. 17 (2006), 712–725.
    • (2006) Seminars cell & Dev. Biol. , vol.17 , pp. 712-725
    • Chen, Y.1    Stump, R.J.2    Lovicu, F.J.3    McAvoy, J.W.4
  • 47
    • 55749100664 scopus 로고    scopus 로고
    • Wnt signaling is required for organization of the lens fiber cell cytoskeleton and development of lens three-dimensional architecture
    • Chen, Y., Stump, R.J., Lovicu, F.J., Shimono, A., McAvoy, J.W., Wnt signaling is required for organization of the lens fiber cell cytoskeleton and development of lens three-dimensional architecture. Dev. Biol. 324 (2008), 161–176.
    • (2008) Dev. Biol. , vol.324 , pp. 161-176
    • Chen, Y.1    Stump, R.J.2    Lovicu, F.J.3    Shimono, A.4    McAvoy, J.W.5
  • 48
    • 84884970717 scopus 로고    scopus 로고
    • EphA2 and Src regulate equatorial cell morphogenesis during lens development
    • Cheng, C., Ansari, M.M., Cooper, J.A., Gong, X., EphA2 and Src regulate equatorial cell morphogenesis during lens development. Development 140 (2013), 4237–4245.
    • (2013) Development , vol.140 , pp. 4237-4245
    • Cheng, C.1    Ansari, M.M.2    Cooper, J.A.3    Gong, X.4
  • 49
    • 84930893448 scopus 로고    scopus 로고
    • Lens ion homeostasis relies on the assembly and/or stability of large connexin 46 gap junction plaques on the broad sides of differentiating fiber cells. American journal of physiology
    • Cheng, C., Nowak, R.B., Gao, J., Sun, X., Biswas, S.K., Lo, W.K., Mathias, R.T., Fowler, V.M., Lens ion homeostasis relies on the assembly and/or stability of large connexin 46 gap junction plaques on the broad sides of differentiating fiber cells. American journal of physiology. Cell physiol. 308 (2015), C835–C847.
    • (2015) Cell physiol. , vol.308 , pp. C835-C847
    • Cheng, C.1    Nowak, R.B.2    Gao, J.3    Sun, X.4    Biswas, S.K.5    Lo, W.K.6    Mathias, R.T.7    Fowler, V.M.8
  • 50
    • 84959533396 scopus 로고    scopus 로고
    • STED microscopy for nanoscale imaging in living brain slices
    • Chereau, R., Tonnesen, J., Nagerl, U.V., STED microscopy for nanoscale imaging in living brain slices. Methods, 2015.
    • (2015) Methods
    • Chereau, R.1    Tonnesen, J.2    Nagerl, U.V.3
  • 52
    • 0023142377 scopus 로고
    • Inhibition of actin polymerization by latrunculin A
    • Coue, M., Brenner, S.L., Spector, I., Korn, E.D., Inhibition of actin polymerization by latrunculin A. FEBS Lett. 213 (1987), 316–318.
    • (1987) FEBS Lett. , vol.213 , pp. 316-318
    • Coue, M.1    Brenner, S.L.2    Spector, I.3    Korn, E.D.4
  • 53
    • 84930159375 scopus 로고    scopus 로고
    • Correlated light and electron microscopy: ultrastructure lights up!
    • de Boer, P., Hoogenboom, J.P., Giepmans, B.N., Correlated light and electron microscopy: ultrastructure lights up!. Nat. methods 12 (2015), 503–513.
    • (2015) Nat. methods , vol.12 , pp. 503-513
    • de Boer, P.1    Hoogenboom, J.P.2    Giepmans, B.N.3
  • 54
    • 0028803406 scopus 로고
    • Limb deformity proteins during avian neurulation and sense organ development
    • An official publication of the American Association of Anatomists
    • de la Pompa, J.L., James, D., Zeller, R., Limb deformity proteins during avian neurulation and sense organ development. An official publication of the American Association of Anatomists Dev. Dyn. 204 (1995), 156–167.
    • (1995) Dev. Dyn. , vol.204 , pp. 156-167
    • de la Pompa, J.L.1    James, D.2    Zeller, R.3
  • 55
    • 67649409220 scopus 로고    scopus 로고
    • Calpain expression and activity during lens fiber cell differentiation
    • De Maria, A., Shi, Y., Kumar, N.M., Bassnett, S., Calpain expression and activity during lens fiber cell differentiation. J. Biol. Chem. 284 (2009), 13542–13550.
    • (2009) J. Biol. Chem. , vol.284 , pp. 13542-13550
    • De Maria, A.1    Shi, Y.2    Kumar, N.M.3    Bassnett, S.4
  • 57
    • 0021199252 scopus 로고
    • Association of alpha-crystallin with actin in cultured lens cells
    • Del Vecchio, P.J., MacElroy, K.S., Rosser, M.P., Church, R.L., Association of alpha-crystallin with actin in cultured lens cells. Curr. eye Res. 3 (1984), 1213–1219.
    • (1984) Curr. eye Res. , vol.3 , pp. 1213-1219
    • Del Vecchio, P.J.1    MacElroy, K.S.2    Rosser, M.P.3    Church, R.L.4
  • 58
    • 22144496125 scopus 로고    scopus 로고
    • Plastins: versatile modulators of actin organization in (patho)physiological cellular processes
    • Delanote, V., Vandekerckhove, J., Gettemans, J., Plastins: versatile modulators of actin organization in (patho)physiological cellular processes. Acta Pharmacol. Sin. 26 (2005), 769–779.
    • (2005) Acta Pharmacol. Sin. , vol.26 , pp. 769-779
    • Delanote, V.1    Vandekerckhove, J.2    Gettemans, J.3
  • 59
    • 0015415174 scopus 로고
    • Interlocking patterns on primate lens fibers
    • Dickson, D.H., Crock, G.W., Interlocking patterns on primate lens fibers. Investig. Ophthalmol. 11 (1972), 809–815.
    • (1972) Investig. Ophthalmol. , vol.11 , pp. 809-815
    • Dickson, D.H.1    Crock, G.W.2
  • 62
    • 0036696823 scopus 로고    scopus 로고
    • Spatio-temporal regulation of Rac1 localization and lamellipodia dynamics during epithelial cell-cell adhesion
    • Ehrlich, J.S., Hansen, M.D., Nelson, W.J., Spatio-temporal regulation of Rac1 localization and lamellipodia dynamics during epithelial cell-cell adhesion. Dev. cell 3 (2002), 259–270.
    • (2002) Dev. cell , vol.3 , pp. 259-270
    • Ehrlich, J.S.1    Hansen, M.D.2    Nelson, W.J.3
  • 64
    • 84864399394 scopus 로고    scopus 로고
    • A role for gammaS-crystallin in the organization of actin and fiber cell maturation in the mouse lens
    • Fan, J., Dong, L., Mishra, S., Chen, Y., FitzGerald, P., Wistow, G., A role for gammaS-crystallin in the organization of actin and fiber cell maturation in the mouse lens. FEBS J. 279 (2012), 2892–2904.
    • (2012) FEBS J. , vol.279 , pp. 2892-2904
    • Fan, J.1    Dong, L.2    Mishra, S.3    Chen, Y.4    FitzGerald, P.5    Wistow, G.6
  • 65
    • 0023992619 scopus 로고
    • An immunoreactive form of erythrocyte protein 4.9 is present in non-erythroid cells
    • Faquin, W.C., Husain, A., Hung, J., Branton, D., An immunoreactive form of erythrocyte protein 4.9 is present in non-erythroid cells. Eur. J. cell Biol. 46 (1988), 168–175.
    • (1988) Eur. J. cell Biol. , vol.46 , pp. 168-175
    • Faquin, W.C.1    Husain, A.2    Hung, J.3    Branton, D.4
  • 66
    • 0034630316 scopus 로고    scopus 로고
    • N-cadherin function is required for differentiation-dependent cytoskeletal reorganization in lens cells in vitro
    • Ferreira-Cornwell, M.C., Veneziale, R.W., Grunwald, G.B., Menko, A.S., N-cadherin function is required for differentiation-dependent cytoskeletal reorganization in lens cells in vitro. Exp. cell Res. 256 (2000), 237–247.
    • (2000) Exp. cell Res. , vol.256 , pp. 237-247
    • Ferreira-Cornwell, M.C.1    Veneziale, R.W.2    Grunwald, G.B.3    Menko, A.S.4
  • 67
    • 0038070120 scopus 로고    scopus 로고
    • Pointed-end capping by tropomodulin3 negatively regulates endothelial cell motility
    • Fischer, R.S., Fritz-Six, K.L., Fowler, V.M., Pointed-end capping by tropomodulin3 negatively regulates endothelial cell motility. J. cell Biol. 161 (2003), 371–380.
    • (2003) J. cell Biol. , vol.161 , pp. 371-380
    • Fischer, R.S.1    Fritz-Six, K.L.2    Fowler, V.M.3
  • 68
    • 0033985955 scopus 로고    scopus 로고
    • Tropomodulin and tropomyosin mediate lens cell actin cytoskeleton reorganization in vitro
    • Fischer, R.S., Lee, A., Fowler, V.M., Tropomodulin and tropomyosin mediate lens cell actin cytoskeleton reorganization in vitro. Investigative Ophthalmol. Vis. Sci. 41 (2000), 166–174.
    • (2000) Investigative Ophthalmol. Vis. Sci. , vol.41 , pp. 166-174
    • Fischer, R.S.1    Lee, A.2    Fowler, V.M.3
  • 69
    • 0038303766 scopus 로고    scopus 로고
    • Tropomodulin binds to filensin intermediate filaments
    • Fischer, R.S., Quinlan, R.A., Fowler, V.M., Tropomodulin binds to filensin intermediate filaments. FEBS Lett. 547 (2003), 228–232.
    • (2003) FEBS Lett. , vol.547 , pp. 228-232
    • Fischer, R.S.1    Quinlan, R.A.2    Fowler, V.M.3
  • 70
    • 61849139080 scopus 로고    scopus 로고
    • Lens intermediate filaments
    • FitzGerald, P.G., Lens intermediate filaments. Exp. eye Res. 88 (2009), 165–172.
    • (2009) Exp. eye Res. , vol.88 , pp. 165-172
    • FitzGerald, P.G.1
  • 71
    • 0025147720 scopus 로고
    • Discrimination between the lens fiber cell 115 kd cytoskeletal protein and alpha-actinin
    • FitzGerald, P.G., Casselman, J., Discrimination between the lens fiber cell 115 kd cytoskeletal protein and alpha-actinin. Curr. eye Res. 9 (1990), 873–882.
    • (1990) Curr. eye Res. , vol.9 , pp. 873-882
    • FitzGerald, P.G.1    Casselman, J.2
  • 72
    • 0034953789 scopus 로고    scopus 로고
    • The interaction of plectin with actin: evidence for cross-linking of actin filaments by dimerization of the actin-binding domain of plectin
    • Fontao, L., Geerts, D., Kuikman, I., Koster, J., Kramer, D., Sonnenberg, A., The interaction of plectin with actin: evidence for cross-linking of actin filaments by dimerization of the actin-binding domain of plectin. J. cell Sci. 114 (2001), 2065–2076.
    • (2001) J. cell Sci. , vol.114 , pp. 2065-2076
    • Fontao, L.1    Geerts, D.2    Kuikman, I.3    Koster, J.4    Kramer, D.5    Sonnenberg, A.6
  • 73
    • 0023272783 scopus 로고
    • Identification and purification of a novel Mr 43,000 tropomyosin-binding protein from human erythrocyte membranes
    • Fowler, V.M., Identification and purification of a novel Mr 43,000 tropomyosin-binding protein from human erythrocyte membranes. J. Biol. Chem. 262 (1987), 12792–12800.
    • (1987) J. Biol. Chem. , vol.262 , pp. 12792-12800
    • Fowler, V.M.1
  • 74
    • 0030021105 scopus 로고    scopus 로고
    • Regulation of actin filament length in erythrocytes and striated muscle
    • Fowler, V.M., Regulation of actin filament length in erythrocytes and striated muscle. Curr. Opin. cell Biol. 8 (1996), 86–96.
    • (1996) Curr. Opin. cell Biol. , vol.8 , pp. 86-96
    • Fowler, V.M.1
  • 75
    • 84887185966 scopus 로고    scopus 로고
    • The human erythrocyte plasma membrane: a Rosetta Stone for decoding membrane-cytoskeleton structure
    • Fowler, V.M., The human erythrocyte plasma membrane: a Rosetta Stone for decoding membrane-cytoskeleton structure. Curr. Top. Membr. 72 (2013), 39–88.
    • (2013) Curr. Top. Membr. , vol.72 , pp. 39-88
    • Fowler, V.M.1
  • 76
    • 0033520387 scopus 로고    scopus 로고
    • Crossroads on cytoskeletal highways
    • Fuchs, E., Yang, Y., Crossroads on cytoskeletal highways. Cell 98 (1999), 547–550.
    • (1999) Cell , vol.98 , pp. 547-550
    • Fuchs, E.1    Yang, Y.2
  • 79
    • 84870860504 scopus 로고    scopus 로고
    • Noninvasive imaging beyond the diffraction limit of 3D dynamics in thickly fluorescent specimens
    • Gao, L., Shao, L., Higgins, C.D., Poulton, J.S., Peifer, M., Davidson, M.W., Wu, X., Goldstein, B., Betzig, E., Noninvasive imaging beyond the diffraction limit of 3D dynamics in thickly fluorescent specimens. Cell 151 (2012), 1370–1385.
    • (2012) Cell , vol.151 , pp. 1370-1385
    • Gao, L.1    Shao, L.2    Higgins, C.D.3    Poulton, J.S.4    Peifer, M.5    Davidson, M.W.6    Wu, X.7    Goldstein, B.8    Betzig, E.9
  • 80
    • 84884964957 scopus 로고    scopus 로고
    • Stain-Free total protein staining is a superior loading control to beta-actin for Western blots
    • Gilda, J.E., Gomes, A.V., Stain-Free total protein staining is a superior loading control to beta-actin for Western blots. Anal. Biochem. 440 (2013), 186–188.
    • (2013) Anal. Biochem. , vol.440 , pp. 186-188
    • Gilda, J.E.1    Gomes, A.V.2
  • 81
    • 84868697480 scopus 로고    scopus 로고
    • Tmod1 and CP49 synergize to control the fiber cell geometry, transparency, and mechanical stiffness of the mouse lens
    • Gokhin, D.S., Nowak, R.B., Kim, N.E., Arnett, E.E., Chen, A.C., Sah, R.L., Clark, J.I., Fowler, V.M., Tmod1 and CP49 synergize to control the fiber cell geometry, transparency, and mechanical stiffness of the mouse lens. PloS one, 7, 2012, e48734.
    • (2012) PloS one , vol.7 , pp. e48734
    • Gokhin, D.S.1    Nowak, R.B.2    Kim, N.E.3    Arnett, E.E.4    Chen, A.C.5    Sah, R.L.6    Clark, J.I.7    Fowler, V.M.8
  • 82
    • 34248154652 scopus 로고    scopus 로고
    • Mechanism and function of formins in the control of actin assembly
    • Goode, B.L., Eck, M.J., Mechanism and function of formins in the control of actin assembly. Annu. Rev. Biochem. 76 (2007), 593–627.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 593-627
    • Goode, B.L.1    Eck, M.J.2
  • 83
    • 0026440390 scopus 로고
    • Binding of actin to lens alpha crystallins
    • Gopalakrishnan, S., Takemoto, L., Binding of actin to lens alpha crystallins. Curr. eye Res. 11 (1992), 929–933.
    • (1992) Curr. eye Res. , vol.11 , pp. 929-933
    • Gopalakrishnan, S.1    Takemoto, L.2
  • 85
    • 33845503108 scopus 로고    scopus 로고
    • HuGE, a novel GFP-actin-expressing mouse line for studying cytoskeletal dynamics
    • Gurniak, C.B., Witke, W., HuGE, a novel GFP-actin-expressing mouse line for studying cytoskeletal dynamics. Eur. J. cell Biol. 86 (2007), 3–12.
    • (2007) Eur. J. cell Biol. , vol.86 , pp. 3-12
    • Gurniak, C.B.1    Witke, W.2
  • 86
    • 0034028826 scopus 로고    scopus 로고
    • Surpassing the lateral resolution limit by a factor of two using structured illumination microscopy
    • Gustafsson, M.G., Surpassing the lateral resolution limit by a factor of two using structured illumination microscopy. J. Microsc. 198 (2000), 82–87.
    • (2000) J. Microsc. , vol.198 , pp. 82-87
    • Gustafsson, M.G.1
  • 87
    • 84862764725 scopus 로고    scopus 로고
    • A large family with MYH9 disorder caused by E1841K mutation suffering from serious kidney and hearing impairment and cataracts
    • Hao, J., Kunishima, S., Guo, X., Hu, R., Gao, W., A large family with MYH9 disorder caused by E1841K mutation suffering from serious kidney and hearing impairment and cataracts. Ann. Hematol. 91 (2012), 1147–1148.
    • (2012) Ann. Hematol. , vol.91 , pp. 1147-1148
    • Hao, J.1    Kunishima, S.2    Guo, X.3    Hu, R.4    Gao, W.5
  • 88
    • 0017208668 scopus 로고
    • Scanning electron microscopy of the adult rabbit lens
    • Harding, C.V., Susan, S., Murphy, H., Scanning electron microscopy of the adult rabbit lens. Ophthalmic Res. 8 (1976), 443–455.
    • (1976) Ophthalmic Res. , vol.8 , pp. 443-455
    • Harding, C.V.1    Susan, S.2    Murphy, H.3
  • 89
    • 84871191358 scopus 로고    scopus 로고
    • Integrin alpha5/fibronectin1 and focal adhesion kinase are required for lens fiber morphogenesis in zebrafish
    • Hayes, J.M., Hartsock, A., Clark, B.S., Napier, H.R., Link, B.A., Gross, J.M., Integrin alpha5/fibronectin1 and focal adhesion kinase are required for lens fiber morphogenesis in zebrafish. Mol. Biol. cell 23 (2012), 4725–4738.
    • (2012) Mol. Biol. cell , vol.23 , pp. 4725-4738
    • Hayes, J.M.1    Hartsock, A.2    Clark, B.S.3    Napier, H.R.4    Link, B.A.5    Gross, J.M.6
  • 90
    • 50149083752 scopus 로고    scopus 로고
    • Mammalian Rho GTPases: new insights into their functions from in vivo studies. Nature reviews
    • Heasman, S.J., Ridley, A.J., Mammalian Rho GTPases: new insights into their functions from in vivo studies. Nature reviews. Mol. cell Biol. 9 (2008), 690–701.
    • (2008) Mol. cell Biol. , vol.9 , pp. 690-701
    • Heasman, S.J.1    Ridley, A.J.2
  • 91
    • 0028460042 scopus 로고
    • Breaking the diffraction resolution limit by stimulated emission: stimulated-emission-depletion fluorescence microscopy
    • Hell, S.W., Wichmann, J., Breaking the diffraction resolution limit by stimulated emission: stimulated-emission-depletion fluorescence microscopy. Opt. Lett. 19 (1994), 780–782.
    • (1994) Opt. Lett. , vol.19 , pp. 780-782
    • Hell, S.W.1    Wichmann, J.2
  • 93
    • 84878261069 scopus 로고    scopus 로고
    • Small molecules CK-666 and CK-869 inhibit actin-related protein 2/3 complex by blocking an activating conformational change
    • Hetrick, B., Han, M.S., Helgeson, L.A., Nolen, B.J., Small molecules CK-666 and CK-869 inhibit actin-related protein 2/3 complex by blocking an activating conformational change. Chem. Biol. 20 (2013), 701–712.
    • (2013) Chem. Biol. , vol.20 , pp. 701-712
    • Hetrick, B.1    Han, M.S.2    Helgeson, L.A.3    Nolen, B.J.4
  • 94
    • 0034911925 scopus 로고    scopus 로고
    • Regulation of actin filament network formation through ARP2/3 complex: activation by a diverse array of proteins
    • Higgs, H.N., Pollard, T.D., Regulation of actin filament network formation through ARP2/3 complex: activation by a diverse array of proteins. Annu. Rev. Biochem. 70 (2001), 649–676.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 649-676
    • Higgs, H.N.1    Pollard, T.D.2
  • 95
    • 84905192362 scopus 로고    scopus 로고
    • Molecular mechanisms underlying the force-dependent regulation of actin-to-ECM linkage at the focal adhesions
    • Hirata, H., Sokabe, M., Lim, C.T., Molecular mechanisms underlying the force-dependent regulation of actin-to-ECM linkage at the focal adhesions. Prog. Mol. Biol. Transl. Sci. 126 (2014), 135–154.
    • (2014) Prog. Mol. Biol. Transl. Sci. , vol.126 , pp. 135-154
    • Hirata, H.1    Sokabe, M.2    Lim, C.T.3
  • 97
    • 77950868813 scopus 로고    scopus 로고
    • Jasplakinolide: an actin-specific reagent that promotes actin polymerization
    • Holzinger, A., Jasplakinolide: an actin-specific reagent that promotes actin polymerization. Methods Mol. Biol. 586 (2009), 71–87.
    • (2009) Methods Mol. Biol. , vol.586 , pp. 71-87
    • Holzinger, A.1
  • 98
    • 0026483279 scopus 로고
    • Alpha-crystallin can function as a molecular chaperone
    • Horwitz, J., Alpha-crystallin can function as a molecular chaperone. Proc. Natl. Acad. Sci. U. S. A. 89 (1992), 10449–10453.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 10449-10453
    • Horwitz, J.1
  • 99
    • 0036181608 scopus 로고    scopus 로고
    • Distinct cell type-specific expression of scaffolding proteins EBP50 and E3KARP: EBP50 is generally expressed with ezrin in specific epithelia, whereas E3KARP is not
    • Ingraffea, J., Reczek, D., Bretscher, A., Distinct cell type-specific expression of scaffolding proteins EBP50 and E3KARP: EBP50 is generally expressed with ezrin in specific epithelia, whereas E3KARP is not. Eur. J. cell Biol. 81 (2002), 61–68.
    • (2002) Eur. J. cell Biol. , vol.81 , pp. 61-68
    • Ingraffea, J.1    Reczek, D.2    Bretscher, A.3
  • 100
    • 0021035990 scopus 로고
    • Lens actin: purification and localization
    • Ireland, M., Lieska, N., Maisel, H., Lens actin: purification and localization. Exp. eye Res. 37 (1983), 393–408.
    • (1983) Exp. eye Res. , vol.37 , pp. 393-408
    • Ireland, M.1    Lieska, N.2    Maisel, H.3
  • 101
    • 77956191801 scopus 로고    scopus 로고
    • Fascin: a key regulator of cytoskeletal dynamics
    • Jayo, A., Parsons, M., Fascin: a key regulator of cytoskeletal dynamics. Int. J. Biochem. cell Biol. 42 (2010), 1614–1617.
    • (2010) Int. J. Biochem. cell Biol. , vol.42 , pp. 1614-1617
    • Jayo, A.1    Parsons, M.2
  • 104
    • 0024344616 scopus 로고
    • Adducin: Ca++-dependent association with sites of cell-cell contact
    • Kaiser, H.W., O'Keefe, E., Bennett, V., Adducin: Ca++-dependent association with sites of cell-cell contact. J. cell Biol. 109 (1989), 557–569.
    • (1989) J. cell Biol. , vol.109 , pp. 557-569
    • Kaiser, H.W.1    O'Keefe, E.2    Bennett, V.3
  • 106
    • 0033280324 scopus 로고    scopus 로고
    • Adaptors for clathrin-mediated traffic
    • Kirchhausen, T., Adaptors for clathrin-mediated traffic. Annu. Rev. cell Dev. Biol. 15 (1999), 705–732.
    • (1999) Annu. Rev. cell Dev. Biol. , vol.15 , pp. 705-732
    • Kirchhausen, T.1
  • 110
    • 34548827681 scopus 로고    scopus 로고
    • Ankyrin-G is a molecular partner of E-cadherin in epithelial cells and early embryos
    • Kizhatil, K., Davis, J.Q., Davis, L., Hoffman, J., Hogan, B.L., Bennett, V., Ankyrin-G is a molecular partner of E-cadherin in epithelial cells and early embryos. J. Biol. Chem. 282 (2007), 26552–26561.
    • (2007) J. Biol. Chem. , vol.282 , pp. 26552-26561
    • Kizhatil, K.1    Davis, J.Q.2    Davis, L.3    Hoffman, J.4    Hogan, B.L.5    Bennett, V.6
  • 111
    • 0037022538 scopus 로고    scopus 로고
    • Cadherin-directed actin assembly: E-cadherin physically associates with the Arp2/3 complex to direct actin assembly in nascent adhesive contacts
    • Kovacs, E.M., Goodwin, M., Ali, R.G., Paterson, A.D., Yap, A.S., Cadherin-directed actin assembly: E-cadherin physically associates with the Arp2/3 complex to direct actin assembly in nascent adhesive contacts. Curr. Biol. CB 12 (2002), 379–382.
    • (2002) Curr. Biol. CB , vol.12 , pp. 379-382
    • Kovacs, E.M.1    Goodwin, M.2    Ali, R.G.3    Paterson, A.D.4    Yap, A.S.5
  • 113
    • 0019194787 scopus 로고
    • The surface morphology of embryonic and adult chick lens-fiber cells
    • Kuszak, J., Alcala, J., Maisel, H., The surface morphology of embryonic and adult chick lens-fiber cells. Am. J. Anat. 159 (1980), 395–410.
    • (1980) Am. J. Anat. , vol.159 , pp. 395-410
    • Kuszak, J.1    Alcala, J.2    Maisel, H.3
  • 114
    • 0029558579 scopus 로고
    • The ultrastructure of epithelial and fiber cells in the crystalline lens
    • Kuszak, J.R., The ultrastructure of epithelial and fiber cells in the crystalline lens. Int. Rev. Cytol. 163 (1995), 305–350.
    • (1995) Int. Rev. Cytol. , vol.163 , pp. 305-350
    • Kuszak, J.R.1
  • 115
  • 116
    • 0842331131 scopus 로고    scopus 로고
    • Fibre cell organization in crystalline lenses
    • Kuszak, J.R., Zoltoski, R.K., Sivertson, C., Fibre cell organization in crystalline lenses. Exp. eye Res. 78 (2004), 673–687.
    • (2004) Exp. eye Res. , vol.78 , pp. 673-687
    • Kuszak, J.R.1    Zoltoski, R.K.2    Sivertson, C.3
  • 118
    • 0014248139 scopus 로고
    • Microtubules in the lens
    • Kuwabara, T., Microtubules in the lens. Archives Ophthalmol. 79 (1968), 189–195.
    • (1968) Archives Ophthalmol. , vol.79 , pp. 189-195
    • Kuwabara, T.1
  • 119
    • 0016764737 scopus 로고
    • The maturation of the lens cell: a morphologic study
    • Kuwabara, T., The maturation of the lens cell: a morphologic study. Exp. eye Res. 20 (1975), 427–443.
    • (1975) Exp. eye Res. , vol.20 , pp. 427-443
    • Kuwabara, T.1
  • 120
    • 84905474662 scopus 로고    scopus 로고
    • p120-catenin-dependent junctional recruitment of Shroom3 is required for apical constriction during lens pit morphogenesis
    • Lang, R.A., Herman, K., Reynolds, A.B., Hildebrand, J.D., Plageman, T.F. Jr., p120-catenin-dependent junctional recruitment of Shroom3 is required for apical constriction during lens pit morphogenesis. Development 141 (2014), 3177–3187.
    • (2014) Development , vol.141 , pp. 3177-3187
    • Lang, R.A.1    Herman, K.2    Reynolds, A.B.3    Hildebrand, J.D.4    Plageman, T.F.5
  • 121
    • 0034007480 scopus 로고    scopus 로고
    • Stabilization and remodeling of the membrane skeleton during lens fiber cell differentiation and maturation
    • An official publication of the American Association of Anatomists
    • Lee, A., Fischer, R.S., Fowler, V.M., Stabilization and remodeling of the membrane skeleton during lens fiber cell differentiation and maturation. An official publication of the American Association of Anatomists Dev. Dyn. 217 (2000), 257–270.
    • (2000) Dev. Dyn. , vol.217 , pp. 257-270
    • Lee, A.1    Fischer, R.S.2    Fowler, V.M.3
  • 122
    • 0035827604 scopus 로고    scopus 로고
    • Caspase remodeling of the spectrin membrane skeleton during lens development and aging
    • Lee, A., Morrow, J.S., Fowler, V.M., Caspase remodeling of the spectrin membrane skeleton during lens development and aging. J. Biol. Chem. 276 (2001), 20735–20742.
    • (2001) J. Biol. Chem. , vol.276 , pp. 20735-20742
    • Lee, A.1    Morrow, J.S.2    Fowler, V.M.3
  • 123
    • 0014971023 scopus 로고
    • Lens of the rat eye: an electron microscope and freeze-etch study
    • Leeson, T.S., Lens of the rat eye: an electron microscope and freeze-etch study. Exp. eye Res. 11 (1971), 78–82.
    • (1971) Exp. eye Res. , vol.11 , pp. 78-82
    • Leeson, T.S.1
  • 124
    • 12844251861 scopus 로고    scopus 로고
    • Abelson-interactor-1 promotes WAVE2 membrane translocation and Abelson-mediated tyrosine phosphorylation required for WAVE2 activation
    • Leng, Y., Zhang, J., Badour, K., Arpaia, E., Freeman, S., Cheung, P., Siu, M., Siminovitch, K., Abelson-interactor-1 promotes WAVE2 membrane translocation and Abelson-mediated tyrosine phosphorylation required for WAVE2 activation. Proc. Natl. Acad. Sci. U. S. A. 102 (2005), 1098–1103.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 1098-1103
    • Leng, Y.1    Zhang, J.2    Badour, K.3    Arpaia, E.4    Freeman, S.5    Cheung, P.6    Siu, M.7    Siminovitch, K.8
  • 125
    • 78650827017 scopus 로고    scopus 로고
    • Modulation of N-cadherin junctions and their role as epicenters of differentiation-specific actin regulation in the developing lens
    • Leonard, M., Zhang, L., Zhai, N., Cader, A., Chan, Y., Nowak, R.B., Fowler, V.M., Menko, A.S., Modulation of N-cadherin junctions and their role as epicenters of differentiation-specific actin regulation in the developing lens. Dev. Biol. 349 (2011), 363–377.
    • (2011) Dev. Biol. , vol.349 , pp. 363-377
    • Leonard, M.1    Zhang, L.2    Zhai, N.3    Cader, A.4    Chan, Y.5    Nowak, R.B.6    Fowler, V.M.7    Menko, A.S.8
  • 126
    • 0033771170 scopus 로고    scopus 로고
    • Differential expression of N- and B-cadherin during lens development
    • Leong, L., Menko, A.S., Grunwald, G.B., Differential expression of N- and B-cadherin during lens development. Investigative Ophthalmol. Vis. Sci. 41 (2000), 3503–3510.
    • (2000) Investigative Ophthalmol. Vis. Sci. , vol.41 , pp. 3503-3510
    • Leong, L.1    Menko, A.S.2    Grunwald, G.B.3
  • 128
    • 84882261485 scopus 로고    scopus 로고
    • Genetic variations and polymorphisms in the ezrin gene are associated with age-related cataract
    • Lin, Q., Zhou, N., Zhang, N., Zhu, B., Hu, S., Zhou, Z., Qi, Y., Genetic variations and polymorphisms in the ezrin gene are associated with age-related cataract. Mol. Vis. 19 (2013), 1572–1579.
    • (2013) Mol. Vis. , vol.19 , pp. 1572-1579
    • Lin, Q.1    Zhou, N.2    Zhang, N.3    Zhu, B.4    Hu, S.5    Zhou, Z.6    Qi, Y.7
  • 129
    • 38449103389 scopus 로고    scopus 로고
    • Diverse roles of Rho family GTPases in neuronal development, survival, and death
    • A journal and virtual library
    • Linseman, D.A., Loucks, F.A., Diverse roles of Rho family GTPases in neuronal development, survival, and death. A journal and virtual library Front. Biosci. 13 (2008), 657–676.
    • (2008) Front. Biosci. , vol.13 , pp. 657-676
    • Linseman, D.A.1    Loucks, F.A.2
  • 130
    • 0023871863 scopus 로고
    • Actin filament patterns in mouse lens epithelium: a study of the effects of aging, injury, and genetics
    • Liou, W., Rafferty, N.S., Actin filament patterns in mouse lens epithelium: a study of the effects of aging, injury, and genetics. Cell Motil. Cytoskelet. 9 (1988), 17–29.
    • (1988) Cell Motil. Cytoskelet. , vol.9 , pp. 17-29
    • Liou, W.1    Rafferty, N.S.2
  • 131
    • 0023813915 scopus 로고
    • Adherens junctions in the ocular lens of various species: ultrastructural analysis with an improved fixation
    • Lo, W.K., Adherens junctions in the ocular lens of various species: ultrastructural analysis with an improved fixation. Cell tissue Res. 254 (1988), 31–40.
    • (1988) Cell tissue Res. , vol.254 , pp. 31-40
    • Lo, W.K.1
  • 132
    • 84897593539 scopus 로고    scopus 로고
    • Aquaporin-0 targets interlocking domains to control the integrity and transparency of the eye lens
    • Lo, W.K., Biswas, S.K., Brako, L., Shiels, A., Gu, S., Jiang, J.X., Aquaporin-0 targets interlocking domains to control the integrity and transparency of the eye lens. Investigative Ophthalmol. Vis. Sci. 55 (2014), 1202–1212.
    • (2014) Investigative Ophthalmol. Vis. Sci. , vol.55 , pp. 1202-1212
    • Lo, W.K.1    Biswas, S.K.2    Brako, L.3    Shiels, A.4    Gu, S.5    Jiang, J.X.6
  • 133
    • 0021130373 scopus 로고
    • Square arrays and their role in ridge formation in human lens fibers
    • Lo, W.K., Harding, C.V., Square arrays and their role in ridge formation in human lens fibers. J. Ultrastruct. Res. 86 (1984), 228–245.
    • (1984) J. Ultrastruct. Res. , vol.86 , pp. 228-245
    • Lo, W.K.1    Harding, C.V.2
  • 134
    • 0027517902 scopus 로고
    • Multiple structural types of gap junctions in mouse lens
    • Lo, W.K., Reese, T.S., Multiple structural types of gap junctions in mouse lens. J. cell Sci. 106:1 (1993), 227–235.
    • (1993) J. cell Sci. , vol.106 , Issue.1 , pp. 227-235
    • Lo, W.K.1    Reese, T.S.2
  • 135
    • 0030665258 scopus 로고    scopus 로고
    • Actin filament bundles in cortical fiber cells of the rat lens
    • Lo, W.K., Shaw, A.P., Wen, X.J., Actin filament bundles in cortical fiber cells of the rat lens. Exp. eye Res. 65 (1997), 691–701.
    • (1997) Exp. eye Res. , vol.65 , pp. 691-701
    • Lo, W.K.1    Shaw, A.P.2    Wen, X.J.3
  • 136
    • 0141534098 scopus 로고    scopus 로고
    • Microtubule configuration and membranous vesicle transport in elongating fiber cells of the rat lens
    • Lo, W.K., Wen, X.J., Zhou, C.J., Microtubule configuration and membranous vesicle transport in elongating fiber cells of the rat lens. Exp. eye Res. 77 (2003), 615–626.
    • (2003) Exp. eye Res. , vol.77 , pp. 615-626
    • Lo, W.K.1    Wen, X.J.2    Zhou, C.J.3
  • 137
    • 28944443596 scopus 로고    scopus 로고
    • Development of the Ocular Lens
    • Cambridge University Press Cambridge, UK; New York
    • Lovicu, F.J., Robinson, M.L., Development of the Ocular Lens. 2004, Cambridge University Press, Cambridge, UK; New York.
    • (2004)
    • Lovicu, F.J.1    Robinson, M.L.2
  • 138
    • 83055174017 scopus 로고    scopus 로고
    • Effects of a myosin light chain kinase inhibitor on the optics and accommodation of the avian crystalline lens
    • Luck, S., Choh, V., Effects of a myosin light chain kinase inhibitor on the optics and accommodation of the avian crystalline lens. Mol. Vis. 17 (2011), 2759–2764.
    • (2011) Mol. Vis. , vol.17 , pp. 2759-2764
    • Luck, S.1    Choh, V.2
  • 139
    • 0026497661 scopus 로고
    • Cytoskeleton–plasma membrane interactions
    • Luna, E.J., Hitt, A.L., Cytoskeleton–plasma membrane interactions. Science 258 (1992), 955–964.
    • (1992) Science , vol.258 , pp. 955-964
    • Luna, E.J.1    Hitt, A.L.2
  • 140
    • 80755153156 scopus 로고    scopus 로고
    • Rac1 GTPase-deficient mouse lens exhibits defects in shape, suture formation, fiber cell migration and survival
    • Maddala, R., Chauhan, B.K., Walker, C., Zheng, Y., Robinson, M.L., Lang, R.A., Rao, P.V., Rac1 GTPase-deficient mouse lens exhibits defects in shape, suture formation, fiber cell migration and survival. Dev. Biol. 360 (2011), 30–43.
    • (2011) Dev. Biol. , vol.360 , pp. 30-43
    • Maddala, R.1    Chauhan, B.K.2    Walker, C.3    Zheng, Y.4    Robinson, M.L.5    Lang, R.A.6    Rao, P.V.7
  • 141
    • 2642544131 scopus 로고    scopus 로고
    • Impaired cytoskeletal organization and membrane integrity in lens fibers of a Rho GTPase functional knockout transgenic mouse
    • A journal of technical methods and pathology
    • Maddala, R., Deng, P.F., Costello, J.M., Wawrousek, E.F., Zigler, J.S., Rao, V.P., Impaired cytoskeletal organization and membrane integrity in lens fibers of a Rho GTPase functional knockout transgenic mouse. A journal of technical methods and pathology Lab. Investig. 84 (2004), 679–692.
    • (2004) Lab. Investig. , vol.84 , pp. 679-692
    • Maddala, R.1    Deng, P.F.2    Costello, J.M.3    Wawrousek, E.F.4    Zigler, J.S.5    Rao, V.P.6
  • 142
    • 84942199093 scopus 로고    scopus 로고
    • Rap1 GTPase Is required for mouse lens epithelial maintenance and morphogenesis
    • Maddala, R., Nagendran, T., Lang, R.A., Morozov, A., Rao, P.V., Rap1 GTPase Is required for mouse lens epithelial maintenance and morphogenesis. Dev. Biol., 2015.
    • (2015) Dev. Biol.
    • Maddala, R.1    Nagendran, T.2    Lang, R.A.3    Morozov, A.4    Rao, P.V.5
  • 143
    • 35148848220 scopus 로고    scopus 로고
    • Lens fiber cell elongation and differentiation is associated with a robust increase in myosin light chain phosphorylation in the developing mouse
    • Research in Biological Diversity
    • Maddala, R., Skiba, N., Vasantha Rao, P., Lens fiber cell elongation and differentiation is associated with a robust increase in myosin light chain phosphorylation in the developing mouse. Research in Biological Diversity Differentiation 75 (2007), 713–725.
    • (2007) Differentiation , vol.75 , pp. 713-725
    • Maddala, R.1    Skiba, N.2    Vasantha Rao, P.3
  • 144
    • 80051474267 scopus 로고    scopus 로고
    • Periaxin is required for hexagonal geometry and membrane organization of mature lens fibers
    • Maddala, R., Skiba, N.P., Lalane, R. 3rd, Sherman, D.L., Brophy, P.J., Rao, P.V., Periaxin is required for hexagonal geometry and membrane organization of mature lens fibers. Dev. Biol. 357 (2011), 179–190.
    • (2011) Dev. Biol. , vol.357 , pp. 179-190
    • Maddala, R.1    Skiba, N.P.2    Lalane, R.3    Sherman, D.L.4    Brophy, P.J.5    Rao, P.V.6
  • 145
    • 84954529151 scopus 로고    scopus 로고
    • Ankyrin-B directs membrane tethering of Periaxin and is required for maintenance of lens fiber cell hexagonal shape and mechanics
    • Maddala, R., Walters, M., Brophy, P.J., Bennett, V., Rao, P.V., Ankyrin-B directs membrane tethering of Periaxin and is required for maintenance of lens fiber cell hexagonal shape and mechanics. Am. J. physiology. Cell physiology, 2015, 10.1152/ajpcell.00111.2015.
    • (2015) Am. J. physiology. Cell physiology
    • Maddala, R.1    Walters, M.2    Brophy, P.J.3    Bennett, V.4    Rao, P.V.5
  • 146
    • 16844367763 scopus 로고    scopus 로고
    • The NF2 tumor suppressor Merlin and the ERM proteins interact with N-WASP and regulate its actin polymerization function
    • Manchanda, N., Lyubimova, A., Ho, H.Y., James, M.F., Gusella, J.F., Ramesh, N., Snapper, S.B., Ramesh, V., The NF2 tumor suppressor Merlin and the ERM proteins interact with N-WASP and regulate its actin polymerization function. J. Biol. Chem. 280 (2005), 12517–12522.
    • (2005) J. Biol. Chem. , vol.280 , pp. 12517-12522
    • Manchanda, N.1    Lyubimova, A.2    Ho, H.Y.3    James, M.F.4    Gusella, J.F.5    Ramesh, N.6    Snapper, S.B.7    Ramesh, V.8
  • 147
    • 0004107123 scopus 로고
    • The Development of the Human Eye
    • third ed. Grune & Stratton New York
    • Mann, I., The Development of the Human Eye. third ed., 1964, Grune & Stratton, New York.
    • (1964)
    • Mann, I.1
  • 148
    • 0028450859 scopus 로고
    • Actin crosslinking proteins at the leading edge
    • Matsudaira, P., Actin crosslinking proteins at the leading edge. Seminars cell Biol. 5 (1994), 165–174.
    • (1994) Seminars cell Biol. , vol.5 , pp. 165-174
    • Matsudaira, P.1
  • 149
    • 0033929093 scopus 로고    scopus 로고
    • Adducin: structure, function and regulation
    • CMLS
    • Matsuoka, Y., Li, X., Bennett, V., Adducin: structure, function and regulation. CMLS Cell. Mol. Life Sci. 57 (2000), 884–895.
    • (2000) Cell. Mol. Life Sci. , vol.57 , pp. 884-895
    • Matsuoka, Y.1    Li, X.2    Bennett, V.3
  • 150
    • 0019162286 scopus 로고
    • Cytoplasmic processes interconnect lens placode and optic vesicle during eye morphogenesis
    • McAvoy, J.W., Cytoplasmic processes interconnect lens placode and optic vesicle during eye morphogenesis. Exp. eye Res. 31 (1980), 527–534.
    • (1980) Exp. eye Res. , vol.31 , pp. 527-534
    • McAvoy, J.W.1
  • 151
    • 1842426730 scopus 로고    scopus 로고
    • Cell shape, cytoskeletal tension, and RhoA regulate stem cell lineage commitment
    • McBeath, R., Pirone, D.M., Nelson, C.M., Bhadriraju, K., Chen, C.S., Cell shape, cytoskeletal tension, and RhoA regulate stem cell lineage commitment. Dev. cell 6 (2004), 483–495.
    • (2004) Dev. cell , vol.6 , pp. 483-495
    • McBeath, R.1    Pirone, D.M.2    Nelson, C.M.3    Bhadriraju, K.4    Chen, C.S.5
  • 152
    • 0142026447 scopus 로고    scopus 로고
    • Regulation of actin dynamics by WASP family proteins
    • Miki, H., Takenawa, T., Regulation of actin dynamics by WASP family proteins. J. Biochem. 134 (2003), 309–313.
    • (2003) J. Biochem. , vol.134 , pp. 309-313
    • Miki, H.1    Takenawa, T.2
  • 153
    • 57349197819 scopus 로고    scopus 로고
    • Morphogenetic cell movements: diversity from modular mechanical properties
    • Montell, D.J., Morphogenetic cell movements: diversity from modular mechanical properties. Science 322 (2008), 1502–1505.
    • (2008) Science , vol.322 , pp. 1502-1505
    • Montell, D.J.1
  • 154
    • 0035833250 scopus 로고    scopus 로고
    • Targeted ablation of NrCAM or ankyrin-B results in disorganized lens fibers leading to cataract formation
    • More, M.I., Kirsch, F.P., Rathjen, F.G., Targeted ablation of NrCAM or ankyrin-B results in disorganized lens fibers leading to cataract formation. J. cell Biol. 154 (2001), 187–196.
    • (2001) J. cell Biol. , vol.154 , pp. 187-196
    • More, M.I.1    Kirsch, F.P.2    Rathjen, F.G.3
  • 155
    • 0033775855 scopus 로고    scopus 로고
    • Latrunculin alters the actin-monomer subunit interface to prevent polymerization
    • Morton, W.M., Ayscough, K.R., McLaughlin, P.J., Latrunculin alters the actin-monomer subunit interface to prevent polymerization. Nat. cell Biol. 2 (2000), 376–378.
    • (2000) Nat. cell Biol. , vol.2 , pp. 376-378
    • Morton, W.M.1    Ayscough, K.R.2    McLaughlin, P.J.3
  • 156
    • 0017707029 scopus 로고
    • Differentiation of rat lens epithelial cells in tissue culture. II. Effects of cytochalasins B and D on actin organization and differentiation
    • Mousa, G.Y., Trevithick, J.R., Differentiation of rat lens epithelial cells in tissue culture. II. Effects of cytochalasins B and D on actin organization and differentiation. Dev. Biol. 60 (1977), 14–25.
    • (1977) Dev. Biol. , vol.60 , pp. 14-25
    • Mousa, G.Y.1    Trevithick, J.R.2
  • 157
    • 77957735364 scopus 로고    scopus 로고
    • Tropomodulin 1-null mice have a mild spherocytic elliptocytosis with appearance of tropomodulin 3 in red blood cells and disruption of the membrane skeleton
    • Moyer, J.D., Nowak, R.B., Kim, N.E., Larkin, S.K., Peters, L.L., Hartwig, J., Kuypers, F.A., Fowler, V.M., Tropomodulin 1-null mice have a mild spherocytic elliptocytosis with appearance of tropomodulin 3 in red blood cells and disruption of the membrane skeleton. Blood 116 (2010), 2590–2599.
    • (2010) Blood , vol.116 , pp. 2590-2599
    • Moyer, J.D.1    Nowak, R.B.2    Kim, N.E.3    Larkin, S.K.4    Peters, L.L.5    Hartwig, J.6    Kuypers, F.A.7    Fowler, V.M.8
  • 158
    • 84961603849 scopus 로고    scopus 로고
    • Lens placode planar cell polarity is dependent on Cdc42-mediated junctional contraction inhibition
    • Muccioli, M., Qaisi, D., Herman, K., Plageman, T.F. Jr., Lens placode planar cell polarity is dependent on Cdc42-mediated junctional contraction inhibition. Dev. Biol., 2016.
    • (2016) Dev. Biol.
    • Muccioli, M.1    Qaisi, D.2    Herman, K.3    Plageman, T.F.4
  • 159
    • 0032568650 scopus 로고    scopus 로고
    • The interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments
    • Mullins, R.D., Heuser, J.A., Pollard, T.D., The interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments. Proc. Natl. Acad. Sci. U. S. A. 95 (1998), 6181–6186.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 6181-6186
    • Mullins, R.D.1    Heuser, J.A.2    Pollard, T.D.3
  • 161
    • 0028087729 scopus 로고
    • The roles of catenins in the cadherin-mediated cell adhesion: functional analysis of E-cadherin-alpha catenin fusion molecules
    • Nagafuchi, A., Ishihara, S., Tsukita, S., The roles of catenins in the cadherin-mediated cell adhesion: functional analysis of E-cadherin-alpha catenin fusion molecules. J. cell Biol. 127 (1994), 235–245.
    • (1994) J. cell Biol. , vol.127 , pp. 235-245
    • Nagafuchi, A.1    Ishihara, S.2    Tsukita, S.3
  • 162
    • 84928381160 scopus 로고    scopus 로고
    • Length regulation of mechanosensitive stereocilia depends on very slow actin dynamics and filament-severing proteins
    • Narayanan, P., Chatterton, P., Ikeda, A., Ikeda, S., Corey, D.P., Ervasti, J.M., Perrin, B.J., Length regulation of mechanosensitive stereocilia depends on very slow actin dynamics and filament-severing proteins. Nat. Commun., 6, 2015, 6855.
    • (2015) Nat. Commun. , vol.6 , pp. 6855
    • Narayanan, P.1    Chatterton, P.2    Ikeda, A.3    Ikeda, S.4    Corey, D.P.5    Ervasti, J.M.6    Perrin, B.J.7
  • 163
    • 29644435320 scopus 로고    scopus 로고
    • Localization of PDZ domain containing proteins Discs Large-1 and Scribble in the mouse eye
    • Nguyen, M.M., Rivera, C., Griep, A.E., Localization of PDZ domain containing proteins Discs Large-1 and Scribble in the mouse eye. Mol. Vis. 11 (2005), 1183–1199.
    • (2005) Mol. Vis. , vol.11 , pp. 1183-1199
    • Nguyen, M.M.1    Rivera, C.2    Griep, A.E.3
  • 164
    • 0021749110 scopus 로고
    • Cofilin, a protein in porcine brain that binds to actin filaments and inhibits their interactions with myosin and tropomyosin
    • Nishida, E., Maekawa, S., Sakai, H., Cofilin, a protein in porcine brain that binds to actin filaments and inhibits their interactions with myosin and tropomyosin. Biochemistry 23 (1984), 5307–5313.
    • (1984) Biochemistry , vol.23 , pp. 5307-5313
    • Nishida, E.1    Maekawa, S.2    Sakai, H.3
  • 165
    • 0028157729 scopus 로고
    • Regulation and function of the Rho subfamily of small GTPases
    • Nobes, C., Hall, A., Regulation and function of the Rho subfamily of small GTPases. Curr. Opin. Genet. Dev. 4 (1994), 77–81.
    • (1994) Curr. Opin. Genet. Dev. , vol.4 , pp. 77-81
    • Nobes, C.1    Hall, A.2
  • 166
    • 0033594123 scopus 로고    scopus 로고
    • Rho GTPases control polarity, protrusion, and adhesion during cell movement
    • Nobes, C.D., Hall, A., Rho GTPases control polarity, protrusion, and adhesion during cell movement. J. cell Biol. 144 (1999), 1235–1244.
    • (1999) J. cell Biol. , vol.144 , pp. 1235-1244
    • Nobes, C.D.1    Hall, A.2
  • 168
    • 70349926142 scopus 로고    scopus 로고
    • Tropomodulin1 is required for membrane skeleton organization and hexagonal geometry of fiber cells in the mouse lens
    • Nowak, R.B., Fischer, R.S., Zoltoski, R.K., Kuszak, J.R., Fowler, V.M., Tropomodulin1 is required for membrane skeleton organization and hexagonal geometry of fiber cells in the mouse lens. J. cell Biol. 186 (2009), 915–928.
    • (2009) J. cell Biol. , vol.186 , pp. 915-928
    • Nowak, R.B.1    Fischer, R.S.2    Zoltoski, R.K.3    Kuszak, J.R.4    Fowler, V.M.5
  • 169
    • 84864102947 scopus 로고    scopus 로고
    • Tropomodulin 1 constrain fiber cell geometry during elongation and maturation in the lens cortex
    • Official Journal of the Histochemistry Society
    • Nowak, R.B., Fowler, V.M., Tropomodulin 1 constrain fiber cell geometry during elongation and maturation in the lens cortex. Official Journal of the Histochemistry Society J. Histochem. Cytochem. 60 (2012), 414–427.
    • (2012) J. Histochem. Cytochem. , vol.60 , pp. 414-427
    • Nowak, R.B.1    Fowler, V.M.2
  • 170
    • 43149087359 scopus 로고    scopus 로고
    • The function of filensin and phakinin in lens transparency
    • Oka, M., Kudo, H., Sugama, N., Asami, Y., Takehana, M., The function of filensin and phakinin in lens transparency. Mol. Vis. 14 (2008), 815–822.
    • (2008) Mol. Vis. , vol.14 , pp. 815-822
    • Oka, M.1    Kudo, H.2    Sugama, N.3    Asami, Y.4    Takehana, M.5
  • 171
    • 33847295719 scopus 로고    scopus 로고
    • Mechanism of depolymerization and severing of actin filaments and its significance in cytoskeletal dynamics
    • Ono, S., Mechanism of depolymerization and severing of actin filaments and its significance in cytoskeletal dynamics. Int. Rev. Cytol. 258 (2007), 1–82.
    • (2007) Int. Rev. Cytol. , vol.258 , pp. 1-82
    • Ono, S.1
  • 172
    • 77958521897 scopus 로고    scopus 로고
    • Dynamic regulation of sarcomeric actin filaments in striated muscle
    • Ono, S., Dynamic regulation of sarcomeric actin filaments in striated muscle. Cytoskeleton 67 (2010), 677–692.
    • (2010) Cytoskeleton , vol.67 , pp. 677-692
    • Ono, S.1
  • 173
    • 0029588356 scopus 로고
    • A putative effector of Ral has homology to Rho/Rac GTPase activating proteins
    • Park, S.H., Weinberg, R.A., A putative effector of Ral has homology to Rho/Rac GTPase activating proteins. Oncogene 11 (1995), 2349–2355.
    • (1995) Oncogene , vol.11 , pp. 2349-2355
    • Park, S.H.1    Weinberg, R.A.2
  • 175
    • 0016587161 scopus 로고
    • Lens cell elongation in vitro and microtubules
    • Piatigorsky, J., Lens cell elongation in vitro and microtubules. Ann. N. Y. Acad. Sci. 253 (1975), 333–347.
    • (1975) Ann. N. Y. Acad. Sci. , vol.253 , pp. 333-347
    • Piatigorsky, J.1
  • 176
    • 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. Differ. Res. Biol. Divers. 19 (1981), 134–153.
    • (1981) Differ. Res. Biol. Divers. , vol.19 , pp. 134-153
    • Piatigorsky, J.1
  • 177
    • 84860320628 scopus 로고    scopus 로고
    • Functions of p120ctn in development and disease
    • Pieters, T., van Hengel, J., van Roy, F., Functions of p120ctn in development and disease. Front. Biosci. 17 (2012), 760–783.
    • (2012) Front. Biosci. , vol.17 , pp. 760-783
    • Pieters, T.1    van Hengel, J.2    van Roy, F.3
  • 179
  • 180
    • 84913525095 scopus 로고    scopus 로고
    • Cellular and molecular mechanisms of single and collective cell migrations in Drosophila: themes and variations
    • Pocha, S.M., Montell, D.J., Cellular and molecular mechanisms of single and collective cell migrations in Drosophila: themes and variations. Annu. Rev. Genet. 48 (2014), 295–318.
    • (2014) Annu. Rev. Genet. , vol.48 , pp. 295-318
    • Pocha, S.M.1    Montell, D.J.2
  • 181
    • 34247644614 scopus 로고    scopus 로고
    • Regulation of actin filament assembly by Arp2/3 complex and formins
    • Pollard, T.D., Regulation of actin filament assembly by Arp2/3 complex and formins. Annu. Rev. biophysics Biomol. Struct. 36 (2007), 451–477.
    • (2007) Annu. Rev. biophysics Biomol. Struct. , vol.36 , pp. 451-477
    • Pollard, T.D.1
  • 183
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • Pollard, T.D., Borisy, G.G., Cellular motility driven by assembly and disassembly of actin filaments. Cell 112 (2003), 453–465.
    • (2003) Cell , vol.112 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 184
    • 70849098888 scopus 로고    scopus 로고
    • Actin, a central player in cell shape and movement
    • Pollard, T.D., Cooper, J.A., Actin, a central player in cell shape and movement. Science 326 (2009), 1208–1212.
    • (2009) Science , vol.326 , pp. 1208-1212
    • Pollard, T.D.1    Cooper, J.A.2
  • 185
    • 58649124705 scopus 로고    scopus 로고
    • Co-operative roles for E-cadherin and N-cadherin during lens vesicle separation and lens epithelial cell survival
    • Pontoriero, G.F., Smith, A.N., Miller, L.A., Radice, G.L., West-Mays, J.A., Lang, R.A., Co-operative roles for E-cadherin and N-cadherin during lens vesicle separation and lens epithelial cell survival. Dev. Biol. 326 (2009), 403–417.
    • (2009) Dev. Biol. , vol.326 , pp. 403-417
    • Pontoriero, G.F.1    Smith, A.N.2    Miller, L.A.3    Radice, G.L.4    West-Mays, J.A.5    Lang, R.A.6
  • 186
  • 187
    • 42649123661 scopus 로고    scopus 로고
    • Epithelial morphogenesis in embryos: asymmetries, motors and brakes
    • Quintin, S., Gally, C., Labouesse, M., Epithelial morphogenesis in embryos: asymmetries, motors and brakes. Trends Genet. TIG 24 (2008), 221–230.
    • (2008) Trends Genet. TIG , vol.24 , pp. 221-230
    • Quintin, S.1    Gally, C.2    Labouesse, M.3
  • 188
    • 85018008101 scopus 로고
    • Lens Morphology
    • Dekker New York
    • Rafferty, N.S., Lens Morphology. 1985, Dekker, New York.
    • (1985)
    • Rafferty, N.S.1
  • 189
    • 0021162329 scopus 로고
    • Polygonal arrays of microfilaments in epithelial cells of the intact lens
    • Rafferty, N.S., Scholz, D.L., Polygonal arrays of microfilaments in epithelial cells of the intact lens. Curr. eye Res. 3 (1984), 1141–1149.
    • (1984) Curr. eye Res. , vol.3 , pp. 1141-1149
    • Rafferty, N.S.1    Scholz, D.L.2
  • 190
    • 0021844109 scopus 로고
    • Actin in polygonal arrays of microfilaments and sequestered actin bundles (SABs) in lens epithelial cells of rabbits and mice
    • Rafferty, N.S., Scholz, D.L., Actin in polygonal arrays of microfilaments and sequestered actin bundles (SABs) in lens epithelial cells of rabbits and mice. Curr. eye Res. 4 (1985), 713–718.
    • (1985) Curr. eye Res. , vol.4 , pp. 713-718
    • Rafferty, N.S.1    Scholz, D.L.2
  • 191
    • 0024362019 scopus 로고
    • Comparative study of actin filament patterns in lens epithelial cells. Are these determined by the mechanisms of lens accommodation?
    • Rafferty, N.S., Scholz, D.L., Comparative study of actin filament patterns in lens epithelial cells. Are these determined by the mechanisms of lens accommodation?. Curr. eye Res. 8 (1989), 569–579.
    • (1989) Curr. eye Res. , vol.8 , pp. 569-579
    • Rafferty, N.S.1    Scholz, D.L.2
  • 192
    • 0025018042 scopus 로고
    • Immunocytochemical evidence for an actin-myosin system in lens epithelial cells
    • Rafferty, N.S., Scholz, D.L., Goldberg, M., Lewyckyj, M., Immunocytochemical evidence for an actin-myosin system in lens epithelial cells. Exp. eye Res. 51 (1990), 591–600.
    • (1990) Exp. eye Res. , vol.51 , pp. 591-600
    • Rafferty, N.S.1    Scholz, D.L.2    Goldberg, M.3    Lewyckyj, M.4
  • 193
    • 0019833489 scopus 로고
    • Cytoskeletal and contractile structures in bovine lens cell differentiation
    • Ramaekers, F.C., Boomkens, T.R., Bloemendal, H., Cytoskeletal and contractile structures in bovine lens cell differentiation. Exp. cell Res. 135 (1981), 454–461.
    • (1981) Exp. cell Res. , vol.135 , pp. 454-461
    • Ramaekers, F.C.1    Boomkens, T.R.2    Bloemendal, H.3
  • 194
    • 39749173669 scopus 로고    scopus 로고
    • Characterization of lens fiber cell triton insoluble fraction reveals ERM (ezrin, radixin, moesin) proteins as major cytoskeletal-associated proteins
    • Rao, P.V., Ho, T., Skiba, N.P., Maddala, R., Characterization of lens fiber cell triton insoluble fraction reveals ERM (ezrin, radixin, moesin) proteins as major cytoskeletal-associated proteins. Biochem. biophysical Res. Commun. 368 (2008), 508–514.
    • (2008) Biochem. biophysical Res. Commun. , vol.368 , pp. 508-514
    • Rao, P.V.1    Ho, T.2    Skiba, N.P.3    Maddala, R.4
  • 195
    • 0036172408 scopus 로고    scopus 로고
    • Rho GTPase inactivation impairs lens growth and integrity
    • A Journal of Technical Methods and Pathology
    • Rao, V., Wawrousek, E., Tamm, E.R., Zigler, S. Jr., Rho GTPase inactivation impairs lens growth and integrity. A Journal of Technical Methods and Pathology Lab. Investig. 82 (2002), 231–239.
    • (2002) Lab. Investig. , vol.82 , pp. 231-239
    • Rao, V.1    Wawrousek, E.2    Tamm, E.R.3    Zigler, S.4
  • 196
    • 70349422245 scopus 로고    scopus 로고
    • Cortactin: Coordinating adhesion and the actin cytoskeleton at cellular protrusions
    • Ren, G., Crampton, M.S., Yap, A.S., Cortactin: Coordinating adhesion and the actin cytoskeleton at cellular protrusions. Cell Motil. Cytoskelet. 66 (2009), 865–873.
    • (2009) Cell Motil. Cytoskelet. , vol.66 , pp. 865-873
    • Ren, G.1    Crampton, M.S.2    Yap, A.S.3
  • 197
    • 79959677602 scopus 로고    scopus 로고
    • Life at the leading edge
    • Ridley, A.J., Life at the leading edge. Cell 145 (2011), 1012–1022.
    • (2011) Cell , vol.145 , pp. 1012-1022
    • Ridley, A.J.1
  • 199
    • 70349160842 scopus 로고    scopus 로고
    • Cell-autonomous requirements for Dlg-1 for lens epithelial cell structure and fiber cell morphogenesis
    • An official publication of the American Association of Anatomists
    • Rivera, C., Yamben, I.F., Shatadal, S., Waldof, M., Robinson, M.L., Griep, A.E., Cell-autonomous requirements for Dlg-1 for lens epithelial cell structure and fiber cell morphogenesis. An official publication of the American Association of Anatomists Dev. Dyn. 238 (2009), 2292–2308.
    • (2009) Dev. Dyn. , vol.238 , pp. 2292-2308
    • Rivera, C.1    Yamben, I.F.2    Shatadal, S.3    Waldof, M.4    Robinson, M.L.5    Griep, A.E.6
  • 200
    • 72049090358 scopus 로고    scopus 로고
    • Identification and characterization of a small molecule inhibitor of formin-mediated actin assembly
    • Rizvi, S.A., Neidt, E.M., Cui, J., Feiger, Z., Skau, C.T., Gardel, M.L., Kozmin, S.A., Kovar, D.R., Identification and characterization of a small molecule inhibitor of formin-mediated actin assembly. Chem. Biol. 16 (2009), 1158–1168.
    • (2009) Chem. Biol. , vol.16 , pp. 1158-1168
    • Rizvi, S.A.1    Neidt, E.M.2    Cui, J.3    Feiger, Z.4    Skau, C.T.5    Gardel, M.L.6    Kozmin, S.A.7    Kovar, D.R.8
  • 201
    • 38949149336 scopus 로고    scopus 로고
    • Enabled (Xena) regulates neural plate morphogenesis, apical constriction, and cellular adhesion required for neural tube closure in Xenopus
    • Roffers-Agarwal, J., Xanthos, J.B., Kragtorp, K.A., Miller, J.R., Enabled (Xena) regulates neural plate morphogenesis, apical constriction, and cellular adhesion required for neural tube closure in Xenopus. Dev. Biol. 314 (2008), 393–403.
    • (2008) Dev. Biol. , vol.314 , pp. 393-403
    • Roffers-Agarwal, J.1    Xanthos, J.B.2    Kragtorp, K.A.3    Miller, J.R.4
  • 202
    • 63049113736 scopus 로고    scopus 로고
    • Regulation of cell-cell adhesion by Abi/Diaphanous complexes
    • Ryu, J.R., Echarri, A., Li, R., Pendergast, A.M., Regulation of cell-cell adhesion by Abi/Diaphanous complexes. Mol. Cell. Biol. 29 (2009), 1735–1748.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 1735-1748
    • Ryu, J.R.1    Echarri, A.2    Li, R.3    Pendergast, A.M.4
  • 205
    • 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., Carter, J.M., Hutcheson, A.M., Quinlan, R.A., Richards, J., FitzGerald, P.G., 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 , pp. 1397-1406
    • Sandilands, A.1    Prescott, A.R.2    Carter, J.M.3    Hutcheson, A.M.4    Quinlan, R.A.5    Richards, J.6    FitzGerald, P.G.7
  • 207
    • 0032911020 scopus 로고    scopus 로고
    • Bidirectional signaling between the cytoskeleton and integrins
    • Schoenwaelder, S.M., Burridge, K., Bidirectional signaling between the cytoskeleton and integrins. Curr. Opin. cell Biol. 11 (1999), 274–286.
    • (1999) Curr. Opin. cell Biol. , vol.11 , pp. 274-286
    • Schoenwaelder, S.M.1    Burridge, K.2
  • 208
    • 0023784401 scopus 로고
    • Immunogold-EM localization of actin and vimentin filaments in relation to polygonal arrays in lens epithelium in situ
    • Scholz, D.L., 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 (1988), 705–719.
    • (1988) Curr. eye Res. , vol.7 , pp. 705-719
    • Scholz, D.L.1    Rafferty, N.S.2
  • 211
    • 51349091855 scopus 로고    scopus 로고
    • Alpha-actinin structure and regulation. Cellular and molecular life sciences
    • Sjoblom, B., Salmazo, A., Djinovic-Carugo, K., Alpha-actinin structure and regulation. Cellular and molecular life sciences. CMLS 65 (2008), 2688–2701.
    • (2008) CMLS , vol.65 , pp. 2688-2701
    • Sjoblom, B.1    Salmazo, A.2    Djinovic-Carugo, K.3
  • 212
    • 0032878703 scopus 로고    scopus 로고
    • Clathrin: anatomy of a coat protein
    • Smith, C.J., Pearse, B.M., Clathrin: anatomy of a coat protein. Trends cell Biol. 9 (1999), 335–338.
    • (1999) Trends cell Biol. , vol.9 , pp. 335-338
    • Smith, C.J.1    Pearse, B.M.2
  • 213
    • 0024360298 scopus 로고
    • Latrunculins–novel marine macrolides that disrupt microfilament organization and affect cell growth: I. Comparison with cytochalasin D
    • Spector, I., Shochet, N.R., Blasberger, D., Kashman, Y., Latrunculins–novel marine macrolides that disrupt microfilament organization and affect cell growth: I. Comparison with cytochalasin D. Cell Motil. Cytoskelet. 13 (1989), 127–144.
    • (1989) Cell Motil. Cytoskelet. , vol.13 , pp. 127-144
    • Spector, I.1    Shochet, N.R.2    Blasberger, D.3    Kashman, Y.4
  • 214
    • 84929666410 scopus 로고    scopus 로고
    • Expanding the Biologist's toolkit with CRISPR-Cas9
    • Sternberg, S.H., Doudna, J.A., Expanding the Biologist's toolkit with CRISPR-Cas9. Mol. cell 58 (2015), 568–574.
    • (2015) Mol. cell , vol.58 , pp. 568-574
    • Sternberg, S.H.1    Doudna, J.A.2
  • 217
    • 33845986367 scopus 로고    scopus 로고
    • c-Abl interacts with the WAVE2 signaling complex to induce membrane ruffling and cell spreading
    • Stuart, J.R., Gonzalez, F.H., Kawai, H., Yuan, Z.M., c-Abl interacts with the WAVE2 signaling complex to induce membrane ruffling and cell spreading. J. Biol. Chem. 281 (2006), 31290–31297.
    • (2006) J. Biol. Chem. , vol.281 , pp. 31290-31297
    • Stuart, J.R.1    Gonzalez, F.H.2    Kawai, H.3    Yuan, Z.M.4
  • 218
    • 70449526292 scopus 로고    scopus 로고
    • A cell polarity protein aPKClambda is required for eye lens formation and growth
    • Sugiyama, Y., Akimoto, K., Robinson, M.L., Ohno, S., Quinlan, R.A., A cell polarity protein aPKClambda is required for eye lens formation and growth. Dev. Biol. 336 (2009), 246–256.
    • (2009) Dev. Biol. , vol.336 , pp. 246-256
    • Sugiyama, Y.1    Akimoto, K.2    Robinson, M.L.3    Ohno, S.4    Quinlan, R.A.5
  • 219
    • 0030696042 scopus 로고    scopus 로고
    • Immunodetection of membrane skeletal protein 4.2 in bovine and chicken eye lenses and erythrocytes
    • Sung, L.A., Lo, W.K., Immunodetection of membrane skeletal protein 4.2 in bovine and chicken eye lenses and erythrocytes. Curr. eye Res. 16 (1997), 1127–1133.
    • (1997) Curr. eye Res. , vol.16 , pp. 1127-1133
    • Sung, L.A.1    Lo, W.K.2
  • 224
    • 0034695656 scopus 로고    scopus 로고
    • Directed actin polymerization is the driving force for epithelial cell-cell adhesion
    • Vasioukhin, V., Bauer, C., Yin, M., Fuchs, E., Directed actin polymerization is the driving force for epithelial cell-cell adhesion. Cell 100 (2000), 209–219.
    • (2000) Cell , vol.100 , pp. 209-219
    • Vasioukhin, V.1    Bauer, C.2    Yin, M.3    Fuchs, E.4
  • 225
    • 33750548443 scopus 로고    scopus 로고
    • Rho GTPases and cell cycle control
    • Villalonga, P., Ridley, A.J., Rho GTPases and cell cycle control. Growth factors 24 (2006), 159–164.
    • (2006) Growth factors , vol.24 , pp. 159-164
    • Villalonga, P.1    Ridley, A.J.2
  • 226
    • 80052521522 scopus 로고    scopus 로고
    • Aquaporin-0 interacts with the FERM domain of ezrin/radixin/moesin proteins in the ocular lens
    • Wang, Z., Schey, K.L., Aquaporin-0 interacts with the FERM domain of ezrin/radixin/moesin proteins in the ocular lens. Investigative Ophthalmol. Vis. Sci. 52 (2011), 5079–5087.
    • (2011) Investigative Ophthalmol. Vis. Sci. , vol.52 , pp. 5079-5087
    • Wang, Z.1    Schey, K.L.2
  • 228
    • 0028099996 scopus 로고
    • Tropomodulin caps the pointed ends of actin filaments
    • Weber, A., Pennise, C.R., Babcock, G.G., Fowler, V.M., Tropomodulin caps the pointed ends of actin filaments. J. cell Biol. 127 (1994), 1627–1635.
    • (1994) J. cell Biol. , vol.127 , pp. 1627-1635
    • Weber, A.1    Pennise, C.R.2    Babcock, G.G.3    Fowler, V.M.4
  • 229
    • 33746944022 scopus 로고    scopus 로고
    • Actin filament organization regulates the induction of lens cell differentiation and survival
    • Weber, G.F., Menko, A.S., Actin filament organization regulates the induction of lens cell differentiation and survival. Dev. Biol. 295 (2006), 714–729.
    • (2006) Dev. Biol. , vol.295 , pp. 714-729
    • Weber, G.F.1    Menko, A.S.2
  • 230
    • 0023657934 scopus 로고
    • Plectin from bovine lenses. Chemical properties, structural analysis and initial identification of interaction partners
    • Weitzer, G., Wiche, G., Plectin from bovine lenses. Chemical properties, structural analysis and initial identification of interaction partners. Eur. J. Biochem./FEBS 169 (1987), 41–52.
    • (1987) Eur. J. Biochem./FEBS , vol.169 , pp. 41-52
    • Weitzer, G.1    Wiche, G.2
  • 231
    • 84908637040 scopus 로고    scopus 로고
    • Networking and anchoring through plectin: a key to IF functionality and mechanotransduction
    • Wiche, G., Osmanagic-Myers, S., Castanon, M.J., Networking and anchoring through plectin: a key to IF functionality and mechanotransduction. Curr. Opin. cell Biol. 32 (2015), 21–29.
    • (2015) Curr. Opin. cell Biol. , vol.32 , pp. 21-29
    • Wiche, G.1    Osmanagic-Myers, S.2    Castanon, M.J.3
  • 232
    • 84992236576 scopus 로고    scopus 로고
    • Plectin isoforms as organizers of intermediate filament cytoarchitecture
    • Wiche, G., Winter, L., Plectin isoforms as organizers of intermediate filament cytoarchitecture. Bioarchitecture 1 (2011), 14–20.
    • (2011) Bioarchitecture , vol.1 , pp. 14-20
    • Wiche, G.1    Winter, L.2
  • 233
    • 0019443727 scopus 로고
    • The three-dimensional organization of lens fibers in the rabbit. A scanning electron microscopic reinvestigation
    • Albrecht von Graefes Archiv fur klinische und experimentelle Ophthalmologie
    • Willekens, B., Vrensen, G., The three-dimensional organization of lens fibers in the rabbit. A scanning electron microscopic reinvestigation. Albrecht von Graefes Archiv fur klinische und experimentelle Ophthalmologie Albrecht von Graefe's archive Clin. Exp. Ophthalmol. 216 (1981), 275–289.
    • (1981) Albrecht von Graefe's archive Clin. Exp. Ophthalmol. , vol.216 , pp. 275-289
    • Willekens, B.1    Vrensen, G.2
  • 234
    • 0019952709 scopus 로고
    • The three-dimensional organization of lens fibers in the rhesus monkey
    • Albrecht von Graefes Archiv fur klinische und experimentelle Ophthalmologie
    • Willekens, B., Vrensen, G., The three-dimensional organization of lens fibers in the rhesus monkey. Albrecht von Graefes Archiv fur klinische und experimentelle Ophthalmologie Graefe's archive Clin. Exp. Ophthalmol. 219 (1982), 112–120.
    • (1982) Graefe's archive Clin. Exp. Ophthalmol. , vol.219 , pp. 112-120
    • Willekens, B.1    Vrensen, G.2
  • 235
    • 0021813483 scopus 로고
    • Lens fiber organization in four avian species: a scanning electron microscopic study
    • Willekens, B., Vrensen, G., Lens fiber organization in four avian species: a scanning electron microscopic study. Tissue & cell 17 (1985), 359–377.
    • (1985) Tissue & cell , vol.17 , pp. 359-377
    • Willekens, B.1    Vrensen, G.2
  • 236
    • 84922345439 scopus 로고    scopus 로고
    • The effects of actomyosin disruptors on the mechanical integrity of the avian crystalline lens
    • Won, G.J., Fudge, D.S., Choh, V., The effects of actomyosin disruptors on the mechanical integrity of the avian crystalline lens. Mol. Vis. 21 (2015), 98–109.
    • (2015) Mol. Vis. , vol.21 , pp. 98-109
    • Won, G.J.1    Fudge, D.S.2    Choh, V.3
  • 237
    • 0028233519 scopus 로고
    • Identification and characterization of tropomodulin and tropomyosin in the adult rat lens
    • Woo, M.K., Fowler, V.M., Identification and characterization of tropomodulin and tropomyosin in the adult rat lens. J. cell Sci. 107:5 (1994), 1359–1367.
    • (1994) J. cell Sci. , vol.107 , Issue.5 , pp. 1359-1367
    • Woo, M.K.1    Fowler, V.M.2
  • 238
    • 0033817136 scopus 로고    scopus 로고
    • The lens membrane skeleton contains structures preferentially enriched in spectrin-actin or tropomodulin-actin complexes
    • Woo, M.K., Lee, A., Fischer, R.S., Moyer, J., Fowler, V.M., The lens membrane skeleton contains structures preferentially enriched in spectrin-actin or tropomodulin-actin complexes. Cell Motil. Cytoskelet. 46 (2000), 257–268.
    • (2000) Cell Motil. Cytoskelet. , vol.46 , pp. 257-268
    • Woo, M.K.1    Lee, A.2    Fischer, R.S.3    Moyer, J.4    Fowler, V.M.5
  • 239
    • 15744375543 scopus 로고    scopus 로고
    • RhoA/ROCK signaling regulates Sox9 expression and actin organization during chondrogenesis
    • Woods, A., Wang, G., Beier, F., RhoA/ROCK signaling regulates Sox9 expression and actin organization during chondrogenesis. J. Biol. Chem. 280 (2005), 11626–11634.
    • (2005) J. Biol. Chem. , vol.280 , pp. 11626-11634
    • Woods, A.1    Wang, G.2    Beier, F.3
  • 241
    • 84936752673 scopus 로고    scopus 로고
    • A dimensionless ordered pull-through model of the mammalian lens epithelium evidences scaling across species and explains the age-dependent changes in cell density in the human lens
    • Wu, J.J., Wu, W., Tholozan, F.M., Saunter, C.D., Girkin, J.M., Quinlan, R.A., A dimensionless ordered pull-through model of the mammalian lens epithelium evidences scaling across species and explains the age-dependent changes in cell density in the human lens. J. R. Soc. Interface/R. Soc., 12, 2015, 20150391.
    • (2015) J. R. Soc. Interface/R. Soc. , vol.12 , pp. 20150391
    • Wu, J.J.1    Wu, W.2    Tholozan, F.M.3    Saunter, C.D.4    Girkin, J.M.5    Quinlan, R.A.6
  • 242
    • 0036349776 scopus 로고    scopus 로고
    • Systematic analysis of E-, N- and P-cadherin expression in mouse eye development
    • Xu, L., Overbeek, P.A., Reneker, L.W., Systematic analysis of E-, N- and P-cadherin expression in mouse eye development. Exp. eye Res. 74 (2002), 753–760.
    • (2002) Exp. eye Res. , vol.74 , pp. 753-760
    • Xu, L.1    Overbeek, P.A.2    Reneker, L.W.3
  • 243
    • 85027946629 scopus 로고    scopus 로고
    • Tropomodulins: pointed-end capping proteins that regulate actin filament architecture in diverse cell types
    • Yamashiro, S., Gokhin, D.S., Kimura, S., Nowak, R.B., Fowler, V.M., Tropomodulins: pointed-end capping proteins that regulate actin filament architecture in diverse cell types. Cytoskeleton 69 (2012), 337–370.
    • (2012) Cytoskeleton , vol.69 , pp. 337-370
    • Yamashiro, S.1    Gokhin, D.S.2    Kimura, S.3    Nowak, R.B.4    Fowler, V.M.5
  • 244
    • 0022455661 scopus 로고
    • Polygonal arrays of actin filaments in human lens epithelial cells. An aging study
    • Yeh, S., Scholz, D.L., Liou, W., Rafferty, N.S., Polygonal arrays of actin filaments in human lens epithelial cells. An aging study. Investigative Ophthalmol. Vis. Sci. 27 (1986), 1535–1540.
    • (1986) Investigative Ophthalmol. Vis. Sci. , vol.27 , pp. 1535-1540
    • Yeh, S.1    Scholz, D.L.2    Liou, W.3    Rafferty, N.S.4
  • 245
    • 0019321663 scopus 로고
    • Purification and structural properties of gelsolin, a Ca2+-activated regulatory protein of macrophages
    • Yin, H.L., Stossel, T.P., Purification and structural properties of gelsolin, a Ca2+-activated regulatory protein of macrophages. J. Biol. Chem. 255 (1980), 9490–9493.
    • (1980) J. Biol. Chem. , vol.255 , pp. 9490-9493
    • Yin, H.L.1    Stossel, T.P.2
  • 246
    • 0033776421 scopus 로고    scopus 로고
    • Epithelial organization of the mammalian lens
    • Zampighi, G.A., Eskandari, S., Kreman, M., Epithelial organization of the mammalian lens. Exp. eye Res. 71 (2000), 415–435.
    • (2000) Exp. eye Res. , vol.71 , pp. 415-435
    • Zampighi, G.A.1    Eskandari, S.2    Kreman, M.3
  • 248
    • 0041883572 scopus 로고    scopus 로고
    • Association of clathrin, AP-2 adaptor and actin cytoskeleton with developing interlocking membrane domains of lens fibre cells
    • Zhou, C.J., Lo, W.K., Association of clathrin, AP-2 adaptor and actin cytoskeleton with developing interlocking membrane domains of lens fibre cells. Exp. eye Res. 77 (2003), 423–432.
    • (2003) Exp. eye Res. , vol.77 , pp. 423-432
    • Zhou, C.J.1    Lo, W.K.2


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