메뉴 건너뛰기




Volumn 190, Issue , 2009, Pages 265-297

Structural function of mip/aquaporin 0 in the eye lens; Genetic defects lead to congenital inherited cataracts

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; AQUAPORIN; ASPARTIC ACID; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE KINASE; CELL ADHESION MOLECULE; CONNEXIN 46; CONNEXIN 47; CRYSTALLIN; FILENSIN; GAMMA CRYSTALLIN; GAMMA E CRYSTALLIN; GAMMA F CRYSTALLIN; MEMBRANE PROTEIN; PHAKININ; PROLINE; UNCLASSIFIED DRUG; ZINC ION; AQUAPORIN 0; EYE PROTEIN; WATER;

EID: 61449279992     PISSN: 01712004     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-3-540-79885-9_14     Document Type: Review
Times cited : (83)

References (217)
  • 1
    • 0025333990 scopus 로고
    • Hydrodynamic characterization of the major intrinsic protein from the bovine lens fiber membranes. Extraction in n-octyl-beta-Dglucopyranoside and evidence for a tetrameric structure
    • Aerts T, Xia JZ, Slegers H, de Block J, Clauwaert J (1990) Hydrodynamic characterization of the major intrinsic protein from the bovine lens fiber membranes. Extraction in n-octyl-beta-Dglucopyranoside and evidence for a tetrameric structure. J Biol Chem 265:8675-8680
    • (1990) J Biol Chem , vol.265 , pp. 8675-8680
    • Aerts, T.1    Xia, J.Z.2    Slegers, H.3    de Block, J.4    Clauwaert, J.5
  • 3
  • 5
    • 0033017496 scopus 로고    scopus 로고
    • Anterior polar cataracts in CS rats: A predictor of mature cataract formation
    • Al-Ghoul KJ, Kuszak JR (1999) Anterior polar cataracts in CS rats: a predictor of mature cataract formation. Invest Ophthalmol Vis Sci 40:668-679
    • (1999) Invest Ophthalmol Vis Sci , vol.40 , pp. 668-679
    • Al-Ghoul, K.J.1    Kuszak, J.R.2
  • 6
    • 0032144269 scopus 로고    scopus 로고
    • The structure of posterior subcapsular cataracts in the Royal College of Surgeons (RCS) rats
    • Al-Ghoul KJ, Novak LA, Kuszak JR (1998) The structure of posterior subcapsular cataracts in the Royal College of Surgeons (RCS) rats. Exp Eye Res 67:163-177
    • (1998) Exp Eye Res , vol.67 , pp. 163-177
    • Al-Ghoul, K.J.1    Novak, L.A.2    Kuszak, J.R.3
  • 8
    • 0038519687 scopus 로고    scopus 로고
    • Morphology and organization of posterior fiber ends during migration
    • Al-Ghoul KJ, Kuszak JR, Lu JY, Owens MJ (2003b) Morphology and organization of posterior fiber ends during migration. Mol Vis 9:119-128
    • (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
  • 14
    • 3342946768 scopus 로고    scopus 로고
    • Post-translational modifications of aquaporin O (AQP0) in the normal human lens: Spatial and temporal occurrence
    • Ball LE, Garland DL, Crouch RK, Schey KL (2004) Post-translational modifications of aquaporin O (AQP0) in the normal human lens: spatial and temporal occurrence. Biochemistry 43:9856-9865
    • (2004) Biochemistry , vol.43 , pp. 9856-9865
    • Ball, L.E.1    Garland, D.L.2    Crouch, R.K.3    Schey, K.L.4
  • 15
    • 0030771954 scopus 로고    scopus 로고
    • Fiber cell denucleation in the primate lens
    • Bassnett S (1997) Fiber cell denucleation in the primate lens. Invest Ophthalmol Vis Sci 38:1678-1687
    • (1997) Invest Ophthalmol Vis Sci , vol.38 , pp. 1678-1687
    • Bassnett, S.1
  • 16
    • 0036343618 scopus 로고    scopus 로고
    • Lens organelle degradation
    • Bassnett S (2002) Lens organelle degradation. Exp Eye Res 74:1-6
    • (2002) Exp Eye Res , vol.74 , pp. 1-6
    • Bassnett, S.1
  • 17
    • 29044435230 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of cells in the living lens: The relationship between cell length and volume
    • Bassnett S (2005) Three-dimensional reconstruction of cells in the living lens: the relationship between cell length and volume. Exp Eye Res 81:716-723
    • (2005) Exp Eye Res , vol.81 , pp. 716-723
    • Bassnett, S.1
  • 18
    • 0022322979 scopus 로고
    • Direct measurement of pH in the rat lens by ion-sensitive microelectrodes
    • Bassnett S, Duncan G (1985) Direct measurement of pH in the rat lens by ion-sensitive microelectrodes. Exp Eye Res 40:585-590
    • (1985) Exp Eye Res , vol.40 , pp. 585-590
    • Bassnett, S.1    Duncan, G.2
  • 19
    • 0031002566 scopus 로고    scopus 로고
    • Chromatin degradation in differentiating fiber cells of the eye lens
    • Bassnett S, Mataic D (1997) Chromatin degradation in differentiating fiber cells of the eye lens. J Cell Biol 137:37-49
    • (1997) J Cell Biol , vol.137 , pp. 37-49
    • Bassnett, S.1    Mataic, D.2
  • 20
    • 0028348508 scopus 로고
    • Intercellular communication between epithelial and fiber cells of the eye lens
    • Bassnett S, Kuszak JR, Reinisch L, Brown HG, Beebe DC (1994) Intercellular communication between epithelial and fiber cells of the eye lens. J Cell Sci 107:(Pt 4):799-811
    • (1994) J Cell Sci , vol.107 , Issue.PART 4 , pp. 799-811
    • Bassnett, S.1    Kuszak, J.R.2    Reinisch, L.3    Brown, H.G.4    Beebe, D.C.5
  • 21
    • 0035094146 scopus 로고    scopus 로고
    • Changes in adhesion complexes define stages in the differentiation of lens fiber cells
    • Beebe DC, Vasiliev O, Guo J, Shui YB, Bassnett S (2001) Changes in adhesion complexes define stages in the differentiation of lens fiber cells. Invest Ophthalmol Vis Sci 42:727-734
    • (2001) Invest Ophthalmol Vis Sci , vol.42 , pp. 727-734
    • Beebe, D.C.1    Vasiliev, O.2    Guo, J.3    Shui, Y.B.4    Bassnett, S.5
  • 22
    • 0034118380 scopus 로고    scopus 로고
    • Missense mutations in MIP underlie autosomal dominant 'polymorphic' and lamellar cataracts linked to 12q
    • Berry V, Francis P, Kaushal S, Moore A, Bhattacharya S (2000) Missense mutations in MIP underlie autosomal dominant 'polymorphic' and lamellar cataracts linked to 12q. Nat Genet 25:15-17
    • (2000) Nat Genet , vol.25 , pp. 15-17
    • Berry, V.1    Francis, P.2    Kaushal, S.3    Moore, A.4    Bhattacharya, S.5
  • 23
    • 0019408136 scopus 로고
    • Studies on human cataracts. III. Structural elements in nuclear cataracts and their contribution to the turbidity
    • Bettelheim FA, Siew EL, Chylack LT Jr (1981) Studies on human cataracts. III. Structural elements in nuclear cataracts and their contribution to the turbidity. Invest Ophthalmol Vis Sci 20:348-354
    • (1981) Invest Ophthalmol Vis Sci , vol.20 , pp. 348-354
    • Bettelheim, F.A.1    Siew, E.L.2    Chylack Jr, L.T.3
  • 24
    • 0028837059 scopus 로고
    • Calcium cataract: A model for optical anisotropy fluctuations
    • Bettelheim FA, Qin C, Zigler JS Jr (1995) Calcium cataract: a model for optical anisotropy fluctuations. Exp Eye Res 60:153-157
    • (1995) Exp Eye Res , vol.60 , pp. 153-157
    • Bettelheim, F.A.1    Qin, C.2    Zigler Jr, J.S.3
  • 25
    • 0030934017 scopus 로고    scopus 로고
    • On the nature of hereditary cataract in strain 13/N guinea pigs
    • Bettelheim FA, Churchill AC, Zigler JS Jr (1997) On the nature of hereditary cataract in strain 13/N guinea pigs. Curr Eye Res 16:917-924
    • (1997) Curr Eye Res , vol.16 , pp. 917-924
    • Bettelheim, F.A.1    Churchill, A.C.2    Zigler Jr, J.S.3
  • 26
    • 0035097221 scopus 로고    scopus 로고
    • Development- and differentiation-dependent reorganization of intermediate filaments in fiber cells
    • Blankenship TN, Hess JF, FitzGerald PG (2001) Development- and differentiation-dependent reorganization of intermediate filaments in fiber cells. Invest Ophthalmol Vis Sci 42:735-742
    • (2001) Invest Ophthalmol Vis Sci , vol.42 , pp. 735-742
    • Blankenship, T.N.1    Hess, J.F.2    FitzGerald, P.G.3
  • 30
    • 0020078925 scopus 로고
    • Immunocytochemical localization of the lens main intrinsic polypeptide (MIP26) in communicating junctions
    • Bok D, Dockstader J, Horwitz J (1982) Immunocytochemical localization of the lens main intrinsic polypeptide (MIP26) in communicating junctions. J Cell Biol 92:213-220
    • (1982) J Cell Biol , vol.92 , pp. 213-220
    • Bok, D.1    Dockstader, J.2    Horwitz, J.3
  • 31
    • 0031459385 scopus 로고    scopus 로고
    • Confocal microscopy of human lens membranes in aged normal and nuclear cataracts
    • Boyle DL, Takemoto LJ (1997) Confocal microscopy of human lens membranes in aged normal and nuclear cataracts. Invest Ophthalmol Vis Sci 38:2826-2832
    • (1997) Invest Ophthalmol Vis Sci , vol.38 , pp. 2826-2832
    • Boyle, D.L.1    Takemoto, L.J.2
  • 32
    • 0032968787 scopus 로고    scopus 로고
    • Localization of MIP 26 in nuclear fiber cells from aged normal and age-related nuclear cataractous human lenses
    • Boyle DL, Takemoto LJ (1999) Localization of MIP 26 in nuclear fiber cells from aged normal and age-related nuclear cataractous human lenses. Exp Eye Res 68:41-49
    • (1999) Exp Eye Res , vol.68 , pp. 41-49
    • Boyle, D.L.1    Takemoto, L.J.2
  • 33
    • 0031126322 scopus 로고    scopus 로고
    • Confocal microscopy of cataracts from animal model systems: Relevance to human nuclear cataract
    • Boyle DL, Blunt DS, Takemoto LJ (1997) Confocal microscopy of cataracts from animal model systems: relevance to human nuclear cataract. Exp Eye Res 64:565-572
    • (1997) Exp Eye Res , vol.64 , pp. 565-572
    • Boyle, D.L.1    Blunt, D.S.2    Takemoto, L.J.3
  • 34
    • 0017189486 scopus 로고
    • Lens membranes II. Isolation and characterization of the main intrinsic polypeptide (MIP) of bovine lens fiber membranes
    • Broekhuyse RM, Kuhlmann ED, Stols AL (1976) Lens membranes II. Isolation and characterization of the main intrinsic polypeptide (MIP) of bovine lens fiber membranes. Exp Eye Res 23:365-371
    • (1976) Exp Eye Res , vol.23 , pp. 365-371
    • Broekhuyse, R.M.1    Kuhlmann, E.D.2    Stols, A.L.3
  • 35
    • 0018615178 scopus 로고
    • Lens membranes VII. MIP is an immunologically specific component of lens fiber membranes and is identical with 26K band protein
    • Broekhuyse RM, Kuhlmann ED,Winkens HJ (1979) Lens membranes VII. MIP is an immunologically specific component of lens fiber membranes and is identical with 26K band protein. Exp Eye Res 29:303-313
    • (1979) Exp Eye Res , vol.29 , pp. 303-313
    • Broekhuyse, R.M.1    Kuhlmann, E.D.2    Winkens, H.J.3
  • 36
    • 33846014316 scopus 로고    scopus 로고
    • The supramolecular architecture of junctional microdomains in native lens membranes
    • 8:51-55
    • Buzhynskyy N, Hite RK,Walz T, Scheuring S (2007) The supramolecular architecture of junctional microdomains in native lens membranes. EMBO Reports 8:51-55
    • (2007) EMBO Reports
    • Buzhynskyy, N.1    Hite, R.K.2    Walz, T.3    Scheuring, S.4
  • 37
    • 0030883373 scopus 로고    scopus 로고
    • Comparison of the water transporting properties of MIP and AQP1
    • Chandy G, Zampighi GA, Kreman M, Hall JE (1997) Comparison of the water transporting properties of MIP and AQP1. J Membr Biol 159:29-39
    • (1997) J Membr Biol , vol.159 , pp. 29-39
    • Chandy, G.1    Zampighi, G.A.2    Kreman, M.3    Hall, J.E.4
  • 39
    • 0024309098 scopus 로고
    • Distribution of gap junctions and square array junctions in the mammalian lens
    • Costello MJ, McIntosh TJ, Robertson JD (1989) Distribution of gap junctions and square array junctions in the mammalian lens. Invest Ophthalmol Vis Sci 30:975-989
    • (1989) Invest Ophthalmol Vis Sci , vol.30 , pp. 975-989
    • Costello, M.J.1    McIntosh, T.J.2    Robertson, J.D.3
  • 40
    • 0030219742 scopus 로고    scopus 로고
    • Lens development and crystallin gene expression: Many roles for Pax-6
    • Cvekl A, Piatigorsky J (1996) Lens development and crystallin gene expression: many roles for Pax-6. Bioessays 18:621-630
    • (1996) Bioessays , vol.18 , pp. 621-630
    • Cvekl, A.1    Piatigorsky, J.2
  • 41
    • 0023919492 scopus 로고
    • Proteolytic changes in main intrinsic polypeptide (MIP26) from membranes in selenite cataract
    • David LL, Takemoto LJ, Anderson RS, Shearer TR (1988) Proteolytic changes in main intrinsic polypeptide (MIP26) from membranes in selenite cataract. Curr Eye Res 7:411-417
    • (1988) Curr Eye Res , vol.7 , pp. 411-417
    • David, L.L.1    Takemoto, L.J.2    Anderson, R.S.3    Shearer, T.R.4
  • 43
    • 33750589568 scopus 로고    scopus 로고
    • Functional characterization of a naturally occurring C×50 truncation
    • DeRosa AM, Mui R, Srinivas M, White TW (2006) Functional characterization of a naturally occurring C×50 truncation. Invest Ophthalmol Vis Sci 47:4474-4481
    • (2006) Invest Ophthalmol Vis Sci , vol.47 , pp. 4474-4481
    • DeRosa, A.M.1    Mui, R.2    Srinivas, M.3    White, T.W.4
  • 44
    • 38349054558 scopus 로고    scopus 로고
    • The cataract-inducing S50P mutation in C×50 dominantly alters the channel gating of wild-type lens connexins
    • DeRosa AM, Xia CH, Gong X, White TW (2007) The cataract-inducing S50P mutation in C×50 dominantly alters the channel gating of wild-type lens connexins. J Cell Sci 120:4107-4116
    • (2007) J Cell Sci , vol.120 , pp. 4107-4116
    • DeRosa, A.M.1    Xia, C.H.2    Gong, X.3    White, T.W.4
  • 45
    • 0026722204 scopus 로고
    • Reconstitution of channels from preparations enriched in lens gap junction protein MP70
    • Donaldson P, Kistler J (1992) Reconstitution of channels from preparations enriched in lens gap junction protein MP70. J Membr Biol 129:155-165
    • (1992) J Membr Biol , vol.129 , pp. 155-165
    • Donaldson, P.1    Kistler, J.2
  • 46
    • 0035354578 scopus 로고    scopus 로고
    • Molecular solutions to mammalian lens transparency
    • Donaldson P, Kistler J, Mathias RT (2001) Molecular solutions to mammalian lens transparency. News Physiol Sci 16:118-123
    • (2001) News Physiol Sci , vol.16 , pp. 118-123
    • Donaldson, P.1    Kistler, J.2    Mathias, R.T.3
  • 48
    • 0037070180 scopus 로고    scopus 로고
    • pH-Dependent channel activity of heterologously-expressed main intrinsic protein (MIP) from rat lens
    • Drake KD, Schuette D, Chepelinsky AB, Jacob TJ, Crabbe MJ (2002) pH-Dependent channel activity of heterologously-expressed main intrinsic protein (MIP) from rat lens. FEBS Lett 512:199-204
    • (2002) FEBS Lett , vol.512 , pp. 199-204
    • Drake, K.D.1    Schuette, D.2    Chepelinsky, A.B.3    Jacob, T.J.4    Crabbe, M.J.5
  • 49
    • 0031709970 scopus 로고    scopus 로고
    • Assembly of connexins andMP26 in lens fiber plasma membranes studied by SDS-fracture immunolabeling
    • Dunia I, Recouvreur M, Nicolas P, Kumar N, Bloemendal H, Benedetti EL (1998) Assembly of connexins andMP26 in lens fiber plasma membranes studied by SDS-fracture immunolabeling. J Cell Sci 111:(Pt 15):2109-2120
    • (1998) J Cell Sci , vol.111 , Issue.PART 15 , pp. 2109-2120
    • Dunia, I.1    Recouvreur, M.2    Nicolas, P.3    Kumar, N.4    Bloemendal, H.5    Benedetti, E.L.6
  • 52
    • 0025120896 scopus 로고
    • Properties of channels reconstituted from the major intrinsic protein of lens fiber membranes
    • Ehring GR, Zampighi G, Horwitz J, Bok D, Hall JE (1990) Properties of channels reconstituted from the major intrinsic protein of lens fiber membranes. J Gen Physiol 96:631-664
    • (1990) J Gen Physiol , vol.96 , pp. 631-664
    • Ehring, G.R.1    Zampighi, G.2    Horwitz, J.3    Bok, D.4    Hall, J.E.5
  • 53
    • 0026518644 scopus 로고
    • Phosphorylation modulates the voltage dependence of channels reconstituted from the major intrinsic protein of lens fiber membranes
    • Ehring GR, Lagos N, Zampighi GA, Hall JE (1992) Phosphorylation modulates the voltage dependence of channels reconstituted from the major intrinsic protein of lens fiber membranes. J Membr Biol 126:75-88
    • (1992) J Membr Biol , vol.126 , pp. 75-88
    • Ehring, G.R.1    Lagos, N.2    Zampighi, G.A.3    Hall, J.E.4
  • 54
    • 0034161393 scopus 로고    scopus 로고
    • The importance of aquaporin water channel protein structures
    • Engel A, Fujiyoshi Y, Agre P (2000) The importance of aquaporin water channel protein structures. EMBO J 19:800-806
    • (2000) EMBO J , vol.19 , pp. 800-806
    • Engel, A.1    Fujiyoshi, Y.2    Agre, P.3
  • 56
    • 1542427226 scopus 로고    scopus 로고
    • gammaEcrystallin recruitment to the plasma membrane by specific interaction between lens MIP/aquaporin-0 and gammaE-crystallin
    • Fan J, Donovan AK, Ledee DR, Zelenka PS, Fariss RN, Chepelinsky AB (2004) gammaEcrystallin recruitment to the plasma membrane by specific interaction between lens MIP/aquaporin-0 and gammaE-crystallin. Invest Ophthalmol Vis Sci 45:863-871
    • (2004) Invest Ophthalmol Vis Sci , vol.45 , pp. 863-871
    • Fan, J.1    Donovan, A.K.2    Ledee, D.R.3    Zelenka, P.S.4    Fariss, R.N.5    Chepelinsky, A.B.6
  • 58
    • 0021064311 scopus 로고
    • Immunocytochemical localization of the main intrinsic polypeptide (MIP) in ultrathin frozen sections of rat lens
    • Fitzgerald PG, Bok D, Horwitz J (1983) Immunocytochemical localization of the main intrinsic polypeptide (MIP) in ultrathin frozen sections of rat lens. J Cell Biol 97:1491-1499
    • (1983) J Cell Biol , vol.97 , pp. 1491-1499
    • Fitzgerald, P.G.1    Bok, D.2    Horwitz, J.3
  • 59
    • 0022218284 scopus 로고
    • The distribution of the main intrinsic membrane polypeptide in ocular lens
    • FitzGerald PG, Bok D, Horwitz J (1985) The distribution of the main intrinsic membrane polypeptide in ocular lens. Curr Eye Res 4:1203-1218
    • (1985) Curr Eye Res , vol.4 , pp. 1203-1218
    • FitzGerald, P.G.1    Bok, D.2    Horwitz, J.3
  • 60
  • 62
    • 0033675222 scopus 로고    scopus 로고
    • Congenital progressive polymorphic cataract caused by a mutation in the major intrinsic protein of the lens, MIP (AQP0)
    • Francis P, Berry V, Bhattacharya S, Moore A (2000a) Congenital progressive polymorphic cataract caused by a mutation in the major intrinsic protein of the lens, MIP (AQP0). Br J Ophthalmol 84:1376-1379
    • (2000) Br J Ophthalmol , vol.84 , pp. 1376-1379
    • Francis, P.1    Berry, V.2    Bhattacharya, S.3    Moore, A.4
  • 66
    • 0021969813 scopus 로고
    • Lens cell-to-cell channel protein: I. Self-assembly into liposomes and permeability regulation by calmodulin
    • Girsch SJ, Peracchia C (1985a) Lens cell-to-cell channel protein: I. Self-assembly into liposomes and permeability regulation by calmodulin. J Membr Biol 83:217-225
    • (1985) J Membr Biol , vol.83 , pp. 217-225
    • Girsch, S.J.1    Peracchia, C.2
  • 67
    • 0021954166 scopus 로고
    • Lens cell-to-cell channel protein: II. Conformational change in the presence of calmodulin
    • Girsch SJ, Peracchia C (1985b) Lens cell-to-cell channel protein: II. Conformational change in the presence of calmodulin. J Membr Biol 83:227-233
    • (1985) J Membr Biol , vol.83 , pp. 227-233
    • Girsch, S.J.1    Peracchia, C.2
  • 68
    • 0025826151 scopus 로고
    • Calmodulin interacts with a C-terminus peptide from the lens membrane protein MIP26
    • Girsch SJ, Peracchia C (1991) Calmodulin interacts with a C-terminus peptide from the lens membrane protein MIP26. Curr Eye Res 10:839-849
    • (1991) Curr Eye Res , vol.10 , pp. 839-849
    • Girsch, S.J.1    Peracchia, C.2
  • 69
    • 3843103698 scopus 로고    scopus 로고
    • Lens major intrinsic protein (MIP)/aquaporin 0 expression in rat lens epithelia explants requires fibroblast growth factor-induced ERK and JNK signaling
    • Golestaneh N, Fan J, Fariss RN, Lo WK, Zelenka PS, Chepelinsky AB (2004) Lens major intrinsic protein (MIP)/aquaporin 0 expression in rat lens epithelia explants requires fibroblast growth factor-induced ERK and JNK signaling. J Biol Chem 279:31813-31822
    • (2004) J Biol Chem , vol.279 , pp. 31813-31822
    • Golestaneh, N.1    Fan, J.2    Fariss, R.N.3    Lo, W.K.4    Zelenka, P.S.5    Chepelinsky, A.B.6
  • 70
    • 44949151180 scopus 로고    scopus 로고
    • PKC putative phosphorylation site Ser235 is required for MIP/AQP0 translocation to the plasma membrane
    • Golestaneh N, Fan J, Zelenka P, Chepelinsky AB (2008) PKC putative phosphorylation site Ser235 is required for MIP/AQP0 translocation to the plasma membrane. Mol Vis 14:1006-1014
    • (2008) Mol Vis , vol.14 , pp. 1006-1014
    • Golestaneh, N.1    Fan, J.2    Zelenka, P.3    Chepelinsky, A.B.4
  • 71
    • 33845669996 scopus 로고    scopus 로고
    • Gonen T, Walz T (2006) The structure of aquaporins. Q Rev Biophys 39:361-396 Gonen T, Cheng Y, Kistler J, Walz T (2004a) Aquaporin-0 membrane junctions form upon proteolytic cleavage. J Mol Biol 342:1337-1345
    • Gonen T, Walz T (2006) The structure of aquaporins. Q Rev Biophys 39:361-396 Gonen T, Cheng Y, Kistler J, Walz T (2004a) Aquaporin-0 membrane junctions form upon proteolytic cleavage. J Mol Biol 342:1337-1345
  • 72
    • 2442659197 scopus 로고    scopus 로고
    • Aquaporin-O membrane junctions reveal the structure of a closed water pore
    • Gonen T, Sliz P, Kistler J, Cheng Y, Walz T (2004b) Aquaporin-O membrane junctions reveal the structure of a closed water pore. Nature 429:193-197
    • (2004) Nature , vol.429 , pp. 193-197
    • Gonen, T.1    Sliz, P.2    Kistler, J.3    Cheng, Y.4    Walz, T.5
  • 74
    • 36249012485 scopus 로고    scopus 로고
    • Connexins in lens development and cataractogenesis
    • Gong X, Cheng C, Xia CH (2007) Connexins in lens development and cataractogenesis. J Membr Biol 218:9-12
    • (2007) J Membr Biol , vol.218 , pp. 9-12
    • Gong, X.1    Cheng, C.2    Xia, C.H.3
  • 75
    • 0021789405 scopus 로고
    • Major intrinsic polypeptide (MIP26K) from lens membrane: Reconstitution into vesicles and inhibition of channel forming activity by peptide antiserum
    • Gooden M, Rintoul D, Takehana M, Takemoto L (1985a) Major intrinsic polypeptide (MIP26K) from lens membrane: reconstitution into vesicles and inhibition of channel forming activity by peptide antiserum. Biochem Biophys Res Commun 128:993-999
    • (1985) Biochem Biophys Res Commun , vol.128 , pp. 993-999
    • Gooden, M.1    Rintoul, D.2    Takehana, M.3    Takemoto, L.4
  • 76
    • 0022214472 scopus 로고
    • Reconstitution of MIP26 from single human lenses into artificial membranes. I. Differences in pH sensitivity of cataractous vs. normal human lens fiber cell proteins
    • Gooden MM, Takemoto LJ, Rintoul DA (1985b) Reconstitution of MIP26 from single human lenses into artificial membranes. I. Differences in pH sensitivity of cataractous vs. normal human lens fiber cell proteins. Curr Eye Res 4:1107-1115
    • (1985) Curr Eye Res , vol.4 , pp. 1107-1115
    • Gooden, M.M.1    Takemoto, L.J.2    Rintoul, D.A.3
  • 77
    • 0021712623 scopus 로고
    • The major intrinsic protein (MIP) of the bovine lens fiber membrane: Characterization and structure based on cDNA cloning
    • Gorin MB, Yancey SB, Cline J, Revel JP, Horwitz J (1984) The major intrinsic protein (MIP) of the bovine lens fiber membrane: characterization and structure based on cDNA cloning. Cell 39:49-59
    • (1984) Cell , vol.39 , pp. 49-59
    • Gorin, M.B.1    Yancey, S.B.2    Cline, J.3    Revel, J.P.4    Horwitz, J.5
  • 78
    • 0024372245 scopus 로고
    • Covalent change in the major intrinsic polypeptide (MIP26K) during cataract development in the streptozotocin-induced diabetic rat
    • Granstrom D, Swamy M, Abraham E, Takemoto L (1989) Covalent change in the major intrinsic polypeptide (MIP26K) during cataract development in the streptozotocin-induced diabetic rat. Curr Eye Res 8:589-593
    • (1989) Curr Eye Res , vol.8 , pp. 589-593
    • Granstrom, D.1    Swamy, M.2    Abraham, E.3    Takemoto, L.4
  • 79
    • 0242322773 scopus 로고    scopus 로고
    • The genetic and molecular basis of congenital eye defects
    • Graw J (2003) The genetic and molecular basis of congenital eye defects. Nat Rev 4:876-888
    • (2003) Nat Rev , vol.4 , pp. 876-888
    • Graw, J.1
  • 80
    • 11144298645 scopus 로고    scopus 로고
    • Congenital hereditary cataracts
    • Graw J (2004) Congenital hereditary cataracts. Int J Dev Biol 48:1031-1044
    • (2004) Int J Dev Biol , vol.48 , pp. 1031-1044
    • Graw, J.1
  • 81
    • 0037351438 scopus 로고    scopus 로고
    • Developmental genetics in ophthalmology
    • Graw J, Loster J (2003) Developmental genetics in ophthalmology. Ophthalmic Genet 24:1-33
    • (2003) Ophthalmic Genet , vol.24 , pp. 1-33
    • Graw, J.1    Loster, J.2
  • 82
    • 0141757144 scopus 로고    scopus 로고
    • Insertion of MP20 into lens fiber cell plasma membranes correlates with the formation of an extracellular diffusion barrier
    • Grey AC, Jacobs MD, Gonen T, Kistler J, Donaldson PJ (2003) Insertion of MP20 into lens fiber cell plasma membranes correlates with the formation of an extracellular diffusion barrier. Exp Eye Res 77:567-574
    • (2003) Exp Eye Res , vol.77 , pp. 567-574
    • Grey, A.C.1    Jacobs, M.D.2    Gonen, T.3    Kistler, J.4    Donaldson, P.J.5
  • 83
    • 0024308379 scopus 로고
    • A non-connexon protein (MIP) is involved in eye lens gap-junction formation
    • GruijtersWT
    • GruijtersWT (1989) A non-connexon protein (MIP) is involved in eye lens gap-junction formation. J Cell Sci 93:(Pt 3):509-513
    • (1989) J Cell Sci , vol.93 , Issue.PART 3 , pp. 509-513
  • 84
    • 0023158364 scopus 로고
    • Immunolocalization of MP70 in lens fiber 16-17-nm intercellular junctions
    • Gruijters WT, Kistler J, Bullivant S, Goodenough DA (1987) Immunolocalization of MP70 in lens fiber 16-17-nm intercellular junctions. J Cell Biol 104:565-572
    • (1987) J Cell Biol , vol.104 , pp. 565-572
    • Gruijters, W.T.1    Kistler, J.2    Bullivant, S.3    Goodenough, D.A.4
  • 85
    • 34548840252 scopus 로고    scopus 로고
    • A novel mutation in major intrinsic protein of the lens gene (MIP) underlies autosomal dominant cataract in a Chinese family
    • Gu F, Zhai H, Li D, Zhao L, Li C, Huang S, Ma X (2007) A novel mutation in major intrinsic protein of the lens gene (MIP) underlies autosomal dominant cataract in a Chinese family. Mol Vis 13:1651-1656
    • (2007) Mol Vis , vol.13 , pp. 1651-1656
    • Gu, F.1    Zhai, H.2    Li, D.3    Zhao, L.4    Li, C.5    Huang, S.6    Ma, X.7
  • 86
    • 0016815316 scopus 로고
    • Early cytologic changes of Fraser cataract. An electron microscopic study
    • Hamai Y, Kuwabara T (1975) Early cytologic changes of Fraser cataract. An electron microscopic study. Invest Ophthalmol 14:517-527
    • (1975) Invest Ophthalmol , vol.14 , pp. 517-527
    • Hamai, Y.1    Kuwabara, T.2
  • 90
    • 0032546752 scopus 로고    scopus 로고
    • Purified lens major intrinsic protein (MIP) forms highly ordered tetragonal two-dimensional arrays by reconstitution
    • Hasler L, Walz T, Tittmann P, Gross H, Kistler J, Engel A (1998) Purified lens major intrinsic protein (MIP) forms highly ordered tetragonal two-dimensional arrays by reconstitution. J Mol Biol 279:855-864
    • (1998) J Mol Biol , vol.279 , pp. 855-864
    • Hasler, L.1    Walz, T.2    Tittmann, P.3    Gross, H.4    Kistler, J.5    Engel, A.6
  • 91
    • 35748948975 scopus 로고    scopus 로고
    • In and out of the ER: Protein folding, quality control, degradation, and related human diseases
    • Hebert DN, Molinari M (2007) In and out of the ER: protein folding, quality control, degradation, and related human diseases. Physiol Rev 87:1377-1408
    • (2007) Physiol Rev , vol.87 , pp. 1377-1408
    • Hebert, D.N.1    Molinari, M.2
  • 92
    • 39149086399 scopus 로고    scopus 로고
    • Congenital cataracts and their molecular genetics
    • Hejtmancik JF (2008) Congenital cataracts and their molecular genetics. Semin Cell Dev Biol 19:134-149
    • (2008) Semin Cell Dev Biol , vol.19 , pp. 134-149
    • Hejtmancik, J.F.1
  • 93
    • 2942532502 scopus 로고    scopus 로고
    • Molecular genetics of age-related cataract
    • Hejtmancik JF, Kantorow M (2004) Molecular genetics of age-related cataract. Exp Eye Res 79:3-9
    • (2004) Exp Eye Res , vol.79 , pp. 3-9
    • Hejtmancik, J.F.1    Kantorow, M.2
  • 95
    • 0346096980 scopus 로고    scopus 로고
    • Gap junction processing and redistribution revealed by quantitative optical measurements of connexin46 epitopes in the lens
    • Jacobs MD, Soeller C, Sisley AM, Cannell MB, Donaldson PJ (2004) Gap junction processing and redistribution revealed by quantitative optical measurements of connexin46 epitopes in the lens. Invest Ophthalmol Vis Sci 45:191-199
    • (2004) Invest Ophthalmol Vis Sci , vol.45 , pp. 191-199
    • Jacobs, M.D.1    Soeller, C.2    Sisley, A.M.3    Cannell, M.B.4    Donaldson, P.J.5
  • 96
    • 0028318868 scopus 로고
    • Molecular structure of the water channel through aquaporin CHIP. The hourglass model
    • Jung JS, Preston GM, Smith BL, Guggino WB, Agre P (1994) Molecular structure of the water channel through aquaporin CHIP. The hourglass model. J Biol Chem 269:14648-14654
    • (1994) J Biol Chem , vol.269 , pp. 14648-14654
    • Jung, J.S.1    Preston, G.M.2    Smith, B.L.3    Guggino, W.B.4    Agre, P.5
  • 97
    • 33748543959 scopus 로고    scopus 로고
    • AQP0-LTR of the Cat Fr mouse alters water permeability and calcium regulation of wild type AQP0
    • Kalman K, Nemeth-Cahalan KL, Froger A, Hall JE (2006) AQP0-LTR of the Cat Fr mouse alters water permeability and calcium regulation of wild type AQP0. Biochim Biophys Acta 1758:1094-1099
    • (2006) Biochim Biophys Acta , vol.1758 , pp. 1094-1099
    • Kalman, K.1    Nemeth-Cahalan, K.L.2    Froger, A.3    Hall, J.E.4
  • 99
    • 0025336985 scopus 로고
    • Nucleotide and derived amino-acid sequence of the major intrinsic protein of rat eye-lens
    • Kent NA, Shiels A (1990) Nucleotide and derived amino-acid sequence of the major intrinsic protein of rat eye-lens. Nucleic Acids Res 18:4256
    • (1990) Nucleic Acids Res , vol.18 , pp. 4256
    • Kent, N.A.1    Shiels, A.2
  • 100
    • 0033152657 scopus 로고    scopus 로고
    • Transcription factors for lens development assessed in vivo
    • Kondoh H (1999) Transcription factors for lens development assessed in vivo. Curr Opin Genet Dev 9:301-308
    • (1999) Curr Opin Genet Dev , vol.9 , pp. 301-308
    • Kondoh, H.1
  • 101
    • 0029086075 scopus 로고
    • Ion, water and neutral solute transport in Xenopus oocytes expressing frog lens MIP
    • Kushmerick C, Rice SJ, Baldo GJ, Haspel HC, Mathias RT (1995) Ion, water and neutral solute transport in Xenopus oocytes expressing frog lens MIP. Exp Eye Res 61:351-362
    • (1995) Exp Eye Res , vol.61 , pp. 351-362
    • Kushmerick, C.1    Rice, S.J.2    Baldo, G.J.3    Haspel, H.C.4    Mathias, R.T.5
  • 102
    • 0029035395 scopus 로고
    • The development of lens sutures
    • Kuszak JR (1995a) The development of lens sutures. Prog Retin Eye Res 14:567-591
    • (1995) Prog Retin Eye Res , vol.14 , pp. 567-591
    • Kuszak, J.R.1
  • 103
    • 0029558579 scopus 로고
    • The ultrastructure of epithelial and fiber cells in the crystalline lens
    • Kuszak JR (1995b) The ultrastructure of epithelial and fiber cells in the crystalline lens. Int Rev Cytol 163:305-350
    • (1995) Int Rev Cytol , vol.163 , pp. 305-350
    • Kuszak, J.R.1
  • 104
    • 0036118283 scopus 로고    scopus 로고
    • A quantitative analysis of sutural contributions to variability in back vertex distance and transmittance in rabbit lenses as a function of development, growth, and age
    • Kuszak JR, Al-Ghoul KJ (2002) A quantitative analysis of sutural contributions to variability in back vertex distance and transmittance in rabbit lenses as a function of development, growth, and age. Optom Vis Sci 79:193-204
    • (2002) Optom Vis Sci , vol.79 , pp. 193-204
    • Kuszak, J.R.1    Al-Ghoul, K.J.2
  • 105
    • 0025860445 scopus 로고
    • Lens optical quality is a direct function of lens sutural architecture
    • Kuszak JR, Sivak JG, Weerheim JA (1991) Lens optical quality is a direct function of lens sutural architecture. Invest Ophthalmol Vis Sci 32:2119-2129
    • (1991) Invest Ophthalmol Vis Sci , vol.32 , pp. 2119-2129
    • Kuszak, J.R.1    Sivak, J.G.2    Weerheim, J.A.3
  • 106
    • 0027987358 scopus 로고
    • The interrelationship of lens anatomy and optical quality. II. Primate lenses
    • Kuszak JR, Peterson KL, Sivak JG, Herbert KL (1994) The interrelationship of lens anatomy and optical quality. II. Primate lenses. Exp Eye Res 59:521-535
    • (1994) Exp Eye Res , vol.59 , pp. 521-535
    • Kuszak, J.R.1    Peterson, K.L.2    Sivak, J.G.3    Herbert, K.L.4
  • 107
    • 0029874569 scopus 로고    scopus 로고
    • Electron microscopic observations of the crystalline lens
    • Kuszak JR, Peterson KL, Brown HG (1996) Electron microscopic observations of the crystalline lens. Microsc Res Tech 33:441-479
    • (1996) Microsc Res Tech , vol.33 , pp. 441-479
    • Kuszak, J.R.1    Peterson, K.L.2    Brown, H.G.3
  • 108
    • 0842331131 scopus 로고    scopus 로고
    • Fiber cell organization in crystalline lenses
    • Kuszak JR, Zoltoski RK, Sivertson C (2004a) Fiber cell organization in crystalline lenses. Exp Eye Res 78:673-687
    • (2004) Exp Eye Res , vol.78 , pp. 673-687
    • Kuszak, J.R.1    Zoltoski, R.K.2    Sivertson, C.3
  • 110
    • 33747885879 scopus 로고    scopus 로고
    • Quantitative analysis of animal model lens anatomy: Accommodative range is related to fiber structure and organization
    • Kuszak JR, Mazurkiewicz M, Jison L, Madurski A, Ngando A, Zoltoski RK (2006a) Quantitative analysis of animal model lens anatomy: accommodative range is related to fiber structure and organization. Vet Ophthalmol 9:266-280
    • (2006) Vet Ophthalmol , vol.9 , pp. 266-280
    • Kuszak, J.R.1    Mazurkiewicz, M.2    Jison, L.3    Madurski, A.4    Ngando, A.5    Zoltoski, R.K.6
  • 111
    • 33645463379 scopus 로고    scopus 로고
    • Computer modeling of secondary fiber development and growth: I. Nonprimate lenses
    • Kuszak JR, Mazurkiewicz M, Zoltoski R (2006b) Computer modeling of secondary fiber development and growth: I. Nonprimate lenses. Mol Vis 12:251-270
    • (2006) Mol Vis , vol.12 , pp. 251-270
    • Kuszak, J.R.1    Mazurkiewicz, M.2    Zoltoski, R.3
  • 112
    • 0031664396 scopus 로고    scopus 로고
    • Spatial differences in gap junction gating in the lens are a consequence of connexin cleavage
    • Lin JS, Eckert R, Kistler J, Donaldson P (1998) Spatial differences in gap junction gating in the lens are a consequence of connexin cleavage. Eur J Cell Biol 76:246-250
    • (1998) Eur J Cell Biol , vol.76 , pp. 246-250
    • Lin, J.S.1    Eckert, R.2    Kistler, J.3    Donaldson, P.4
  • 113
    • 34948835215 scopus 로고    scopus 로고
    • A substitution of arginine to lysine at the COOH-terminus of MIP caused a different binocular phenotype in a congenital cataract family
    • Lin H, Hejtmancik JF, Qi Y (2007) A substitution of arginine to lysine at the COOH-terminus of MIP caused a different binocular phenotype in a congenital cataract family. Mol Vis 13:1822-1827
    • (2007) Mol Vis , vol.13 , pp. 1822-1827
    • Lin, H.1    Hejtmancik, J.F.2    Qi, Y.3
  • 115
    • 46449123212 scopus 로고    scopus 로고
    • Confocal fluorescence microscopy study of interaction between lens MIP26/AQP0 and crystallins in living cells
    • Liu BF, Liang JJ (2008) Confocal fluorescence microscopy study of interaction between lens MIP26/AQP0 and crystallins in living cells. J Cell Biochem 104:51-58
    • (2008) J Cell Biochem , vol.104 , pp. 51-58
    • Liu, B.F.1    Liang, J.J.2
  • 116
    • 0025339151 scopus 로고
    • Identity of the calmodulin-binding proteins in bovine lens plasma membranes
    • Louis CF, Hogan P, Visco L, Strasburg G (1990) Identity of the calmodulin-binding proteins in bovine lens plasma membranes. Exp Eye Res 50:495-503
    • (1990) Exp Eye Res , vol.50 , pp. 495-503
    • Louis, C.F.1    Hogan, P.2    Visco, L.3    Strasburg, G.4
  • 117
    • 0035691974 scopus 로고    scopus 로고
    • FGF-induced lens cell proliferation and differentiation is dependent on MAPK (ERK1/2) signaling
    • Lovicu FJ,McAvoy JW(2001) FGF-induced lens cell proliferation and differentiation is dependent on MAPK (ERK1/2) signaling. Development (Cambridge, England) 128:5075-5084
    • (2001) Development (Cambridge, England) , vol.128 , pp. 5075-5084
    • Lovicu, F.J.1    McAvoy, J.W.2
  • 118
    • 14844323116 scopus 로고    scopus 로고
    • Growth factor regulation of lens development
    • Lovicu FJ, McAvoy JW (2005) Growth factor regulation of lens development. Dev Biol 280:1-14
    • (2005) Dev Biol , vol.280 , pp. 1-14
    • Lovicu, F.J.1    McAvoy, J.W.2
  • 120
    • 0842266338 scopus 로고    scopus 로고
    • The lens: Local transport and global transparency
    • Mathias RT, Rae JL (2004) The lens: local transport and global transparency. Exp Eye Res 78:689-698
    • (2004) Exp Eye Res , vol.78 , pp. 689-698
    • Mathias, R.T.1    Rae, J.L.2
  • 121
    • 0026348012 scopus 로고
    • Cell to cell communication and pH in the frog lens
    • Mathias RT, Riquelme G, Rae JL (1991) Cell to cell communication and pH in the frog lens. J Gen Physiol 98:1085-1103
    • (1991) J Gen Physiol , vol.98 , pp. 1085-1103
    • Mathias, R.T.1    Riquelme, G.2    Rae, J.L.3
  • 122
    • 0031014473 scopus 로고    scopus 로고
    • Physiological properties of the normal lens
    • Mathias RT, Rae JL, Baldo GJ (1997) Physiological properties of the normal lens. Physiol Rev 77:21-50
    • (1997) Physiol Rev , vol.77 , pp. 21-50
    • Mathias, R.T.1    Rae, J.L.2    Baldo, G.J.3
  • 124
    • 0019132166 scopus 로고
    • Induction of the eye lens
    • McAvoy JW (1980) Induction of the eye lens. Differentiation 17:137-149
    • (1980) Differentiation , vol.17 , pp. 137-149
    • McAvoy, J.W.1
  • 125
    • 0019513841 scopus 로고
    • The spatial relationship between presumptive lens and optic vesicle/cup during early eye morphogenesis in the rat
    • McAvoy JW (1981) The spatial relationship between presumptive lens and optic vesicle/cup during early eye morphogenesis in the rat. Exp Eye Res 33:447-458
    • (1981) Exp Eye Res , vol.33 , pp. 447-458
    • McAvoy, J.W.1
  • 127
    • 0032811276 scopus 로고    scopus 로고
    • McAvoy JW, Chamberlain CG, de Iongh RU, Hales AM, Lovicu FJ (1999) Lens development. Eye (London, England) 13:(Pt 3b):425-437
    • McAvoy JW, Chamberlain CG, de Iongh RU, Hales AM, Lovicu FJ (1999) Lens development. Eye (London, England) 13:(Pt 3b):425-437
  • 128
    • 0028243491 scopus 로고
    • Lens major intrinsic protein (MIP) promotes adhesion when reconstituted into large unilamellar liposomes
    • Michea LF, de la Fuente M, Lagos N (1994) Lens major intrinsic protein (MIP) promotes adhesion when reconstituted into large unilamellar liposomes. Biochemistry 33:7663-7669
    • (1994) Biochemistry , vol.33 , pp. 7663-7669
    • Michea, L.F.1    de la Fuente, M.2    Lagos, N.3
  • 129
    • 0029095804 scopus 로고
    • Biochemical evidence for adhesion-promoting role of major intrinsic protein isolated from both normal and cataractous human lenses
    • Michea LF, Andrinolo D, Ceppi H, Lagos N (1995) Biochemical evidence for adhesion-promoting role of major intrinsic protein isolated from both normal and cataractous human lenses. Exp Eye Res 61:293-301
    • (1995) Exp Eye Res , vol.61 , pp. 293-301
    • Michea, L.F.1    Andrinolo, D.2    Ceppi, H.3    Lagos, N.4
  • 132
    • 0023358851 scopus 로고
    • A gene location for the inheritance of the cataract Fraser (CatFr) mouse congenital cataract
    • Muggleton-Harris AL, Festing MF, Hall M (1987) A gene location for the inheritance of the cataract Fraser (CatFr) mouse congenital cataract. Genet Res 49:235-238
    • (1987) Genet Res , vol.49 , pp. 235-238
    • Muggleton-Harris, A.L.1    Festing, M.F.2    Hall, M.3
  • 136
    • 43149096666 scopus 로고    scopus 로고
    • Nakatsukasa K, Brodsky JL (2008) The recognition and retrotranslocation of misfolded proteins from the endoplasmic reticulum. Traffic (Copenhagen, Denmark) 9:861-870
    • Nakatsukasa K, Brodsky JL (2008) The recognition and retrotranslocation of misfolded proteins from the endoplasmic reticulum. Traffic (Copenhagen, Denmark) 9:861-870
  • 137
    • 0041721625 scopus 로고    scopus 로고
    • pH and calcium regulate the water permeability of aquaporin 0
    • Nemeth-Cahalan KL, Hall JE (2000) pH and calcium regulate the water permeability of aquaporin 0. J Biol Chem 275:6777-6782
    • (2000) J Biol Chem , vol.275 , pp. 6777-6782
    • Nemeth-Cahalan, K.L.1    Hall, J.E.2
  • 139
    • 35649011018 scopus 로고    scopus 로고
    • Zinc modulation of water permeability reveals that aquaporin 0 functions as a cooperative tetramer
    • Nemeth-Cahalan KL, Kalman K, Froger A, Hall JE (2007) Zinc modulation of water permeability reveals that aquaporin 0 functions as a cooperative tetramer. J Gen Physiol 130:457-464
    • (2007) J Gen Physiol , vol.130 , pp. 457-464
    • Nemeth-Cahalan, K.L.1    Kalman, K.2    Froger, A.3    Hall, J.E.4
  • 140
    • 43149087359 scopus 로고    scopus 로고
    • The function of filensin and phakinin in lens transparency
    • Oka M, Kudo H, Sugama N, Asami Y, Takehana M (2008) The function of filensin and phakinin in lens transparency. Mol Vis 14:815-822
    • (2008) Mol Vis , vol.14 , pp. 815-822
    • Oka, M.1    Kudo, H.2    Sugama, N.3    Asami, Y.4    Takehana, M.5
  • 141
    • 0037379798 scopus 로고    scopus 로고
    • Bilateral congenital cataracts result from a gain-of-function mutation in the gene for aquaporin-O in mice
    • Okamura T, Miyoshi I, Takahashi K, Mototani Y, Ishigaki S, Kon Y, Kasai N (2003) Bilateral congenital cataracts result from a gain-of-function mutation in the gene for aquaporin-O in mice. Genomics 81:361-368
    • (2003) Genomics , vol.81 , pp. 361-368
    • Okamura, T.1    Miyoshi, I.2    Takahashi, K.3    Mototani, Y.4    Ishigaki, S.5    Kon, Y.6    Kasai, N.7
  • 143
    • 29144496893 scopus 로고    scopus 로고
    • Co-axial association of recombinant eye lens aquaporin-0 observed in loosely packed 3D crystals
    • Palanivelu DV, Kozono DE, Engel A, Suda K, Lustig A, Agre P, Schirmer T (2006) Co-axial association of recombinant eye lens aquaporin-0 observed in loosely packed 3D crystals. J Mol Biol 355:605-611
    • (2006) J Mol Biol , vol.355 , pp. 605-611
    • Palanivelu, D.V.1    Kozono, D.E.2    Engel, A.3    Suda, K.4    Lustig, A.5    Agre, P.6    Schirmer, T.7
  • 145
    • 0029910115 scopus 로고    scopus 로고
    • Phylogenetic characterization of the MIP family of transmembrane channel proteins
    • Park JH, Saier MH Jr (1996) Phylogenetic characterization of the MIP family of transmembrane channel proteins. J Membr Biology 153:171-180
    • (1996) J Membr Biology , vol.153 , pp. 171-180
    • Park, J.H.1    Saier Jr, M.H.2
  • 146
    • 0020535397 scopus 로고
    • In vitro synthesis and membrane insertion of bovine MP26, an integral protein from lens fiber plasma membrane
    • Paul DL, Goodenough DA (1983a) In vitro synthesis and membrane insertion of bovine MP26, an integral protein from lens fiber plasma membrane. J Cell Biol 96:633-638
    • (1983) J Cell Biol , vol.96 , pp. 633-638
    • Paul, D.L.1    Goodenough, D.A.2
  • 147
    • 0020561113 scopus 로고
    • Preparation, characterization, and localization of antisera against bovine MP26, an integral protein from lens fiber plasma membrane
    • Paul DL, Goodenough DA (1983b) Preparation, characterization, and localization of antisera against bovine MP26, an integral protein from lens fiber plasma membrane. J Cell Biol 96:625-632
    • (1983) J Cell Biol , vol.96 , pp. 625-632
    • Paul, D.L.1    Goodenough, D.A.2
  • 148
    • 0026352039 scopus 로고
    • Connexin46, a novel lens gap junction protein, induces voltage-gated currents in nonjunctional plasma membrane of Xenopus oocytes
    • Paul DL, Ebihara L, Takemoto LJ, Swenson KI, Goodenough DA (1991) Connexin46, a novel lens gap junction protein, induces voltage-gated currents in nonjunctional plasma membrane of Xenopus oocytes. J Cell Biol 115:1077-1089
    • (1991) J Cell Biol , vol.115 , pp. 1077-1089
    • Paul, D.L.1    Ebihara, L.2    Takemoto, L.J.3    Swenson, K.I.4    Goodenough, D.A.5
  • 150
    • 15044347034 scopus 로고    scopus 로고
    • Seeing is believing! The optical properties of the eye lens are dependent upon a functional intermediate filament cytoskeleton
    • Perng MD, Quinlan RA (2005) Seeing is believing! The optical properties of the eye lens are dependent upon a functional intermediate filament cytoskeleton. Exp Cell Res 305:1-9
    • (2005) Exp Cell Res , vol.305 , pp. 1-9
    • Perng, M.D.1    Quinlan, R.A.2
  • 151
    • 34249663915 scopus 로고    scopus 로고
    • Insights into the beaded filament of the eye lens
    • Perng MD, Zhang Q, Quinlan RA (2007) Insights into the beaded filament of the eye lens. Exp Cell Res 313:2180-2188
    • (2007) Exp Cell Res , vol.313 , pp. 2180-2188
    • Perng, M.D.1    Zhang, Q.2    Quinlan, R.A.3
  • 152
    • 0019786296 scopus 로고
    • Lens differentiation in vertebrates. A review of cellular and molecular features
    • Piatigorsky J (1981) Lens differentiation in vertebrates. A review of cellular and molecular features. Differentiation 19:134-153
    • (1981) Differentiation , vol.19 , pp. 134-153
    • Piatigorsky, J.1
  • 153
    • 0026325136 scopus 로고
    • Genomic cloning, complete nucleotide sequence, and structure of the human gene encoding the major intrinsic protein (MIP) of the lens
    • Pisano MM, Chepelinsky AB (1991) Genomic cloning, complete nucleotide sequence, and structure of the human gene encoding the major intrinsic protein (MIP) of the lens. Genomics 11:981-990
    • (1991) Genomics , vol.11 , pp. 981-990
    • Pisano, M.M.1    Chepelinsky, A.B.2
  • 154
    • 0026503030 scopus 로고    scopus 로고
    • Preston GM, Carroll TP, Guggino WB, Agre P (1992) Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein. Science (New York, NY) 256:385-387
    • Preston GM, Carroll TP, Guggino WB, Agre P (1992) Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein. Science (New York, NY) 256:385-387
  • 155
    • 0032812753 scopus 로고    scopus 로고
    • Quinlan RA, Sandilands A, Procter JE, Prescott AR, Hutcheson AM, Dahm R, Gribbon C, Wallace P, Carter JM (1999) The eye lens cytoskeleton. Eye (London, England) 13:(Pt 3b):409-416
    • Quinlan RA, Sandilands A, Procter JE, Prescott AR, Hutcheson AM, Dahm R, Gribbon C, Wallace P, Carter JM (1999) The eye lens cytoskeleton. Eye (London, England) 13:(Pt 3b):409-416
  • 156
    • 0018909395 scopus 로고
    • Interaction of newly synthesized alpha-crystallin with isolated lens plasma membranes
    • Ramaekers FC, Selten-Versteegen AM, Bloemendal H (1980) Interaction of newly synthesized alpha-crystallin with isolated lens plasma membranes. Biochim Biophys Acta 596:57-63
    • (1980) Biochim Biophys Acta , vol.596 , pp. 57-63
    • Ramaekers, F.C.1    Selten-Versteegen, A.M.2    Bloemendal, H.3
  • 157
    • 0027233420 scopus 로고
    • The MIP family of integral membrane channel proteins: Sequence comparisons, evolutionary relationships, reconstructed pathway of evolution, and proposed functional differentiation of the two repeated halves of the proteins
    • Reizer J, Reizer A, Saier MH Jr (1993) The MIP family of integral membrane channel proteins: sequence comparisons, evolutionary relationships, reconstructed pathway of evolution, and proposed functional differentiation of the two repeated halves of the proteins. Crit Rev Biochem Mol Biol 28:235-257
    • (1993) Crit Rev Biochem Mol Biol , vol.28 , pp. 235-257
    • Reizer, J.1    Reizer, A.2    Saier Jr, M.H.3
  • 158
    • 11144304548 scopus 로고    scopus 로고
    • Lens differentiation and crystallin regulation: A chick model
    • Reza HM, Yasuda K (2004a) Lens differentiation and crystallin regulation: a chick model. Int J Dev Biol 48:805-817
    • (2004) Int J Dev Biol , vol.48 , pp. 805-817
    • Reza, H.M.1    Yasuda, K.2
  • 159
    • 1542288230 scopus 로고    scopus 로고
    • Roles of Maf family proteins in lens development
    • Reza HM, Yasuda K (2004b) Roles of Maf family proteins in lens development. Dev Dyn 229:440-448
    • (2004) Dev Dyn , vol.229 , pp. 440-448
    • Reza, H.M.1    Yasuda, K.2
  • 160
    • 33846401811 scopus 로고    scopus 로고
    • An essential role for FGF receptor signaling in lens development
    • Robinson ML (2006) An essential role for FGF receptor signaling in lens development. Semin Cell Dev Biol 17:726-740
    • (2006) Semin Cell Dev Biol , vol.17 , pp. 726-740
    • Robinson, M.L.1
  • 162
    • 0036023359 scopus 로고    scopus 로고
    • Disruption of Gja8 (alpha8 connexin) in mice leads to microphthalmia associated with retardation of lens growth and lens fiber maturation
    • Rong P, Wang X, Niesman I, Wu Y, Benedetti LE, Dunia I, Levy E, Gong X (2002) Disruption of Gja8 (alpha8 connexin) in mice leads to microphthalmia associated with retardation of lens growth and lens fiber maturation. Development (Cambridge, England) 129:167-174
    • (2002) Development (Cambridge, England) , vol.129 , pp. 167-174
    • Rong, P.1    Wang, X.2    Niesman, I.3    Wu, Y.4    Benedetti, L.E.5    Dunia, I.6    Levy, E.7    Gong, X.8
  • 166
    • 0037373876 scopus 로고    scopus 로고
    • Knockout of the intermediate filament protein CP49 destabilizes the lens fiber cell cytoskeleton and decreases lens optical quality, but does not induce cataract
    • Sandilands A, Prescott AR, Wegener A, Zoltoski RK, Hutcheson AM, Masaki S, Kuszak JR, Quinlan RA (2003) Knockout of the intermediate filament protein CP49 destabilizes the lens fiber cell cytoskeleton and decreases lens optical quality, but does not induce cataract. Exp Eye Res 76:385-391
    • (2003) Exp Eye Res , vol.76 , pp. 385-391
    • Sandilands, A.1    Prescott, A.R.2    Wegener, A.3    Zoltoski, R.K.4    Hutcheson, A.M.5    Masaki, S.6    Kuszak, J.R.7    Quinlan, R.A.8
  • 167
    • 0024390696 scopus 로고
    • A fluorescence-quenching assay for measuring permeability of reconstituted lens MIP26
    • Scaglione BA, Rintoul DA (1989) A fluorescence-quenching assay for measuring permeability of reconstituted lens MIP26. Invest Ophthalmol Vis Sci 30:961-966
    • (1989) Invest Ophthalmol Vis Sci , vol.30 , pp. 961-966
    • Scaglione, B.A.1    Rintoul, D.A.2
  • 168
    • 36049012024 scopus 로고    scopus 로고
    • Structural models of the supramolecular organization of AQP0 and connexons in junctional microdomains
    • Scheuring S, Buzhynskyy N, Jaroslawski S, Goncalves RP, Hite RK, Walz T (2007) Structural models of the supramolecular organization of AQP0 and connexons in junctional microdomains. J Struct Biol 160:385-394
    • (2007) J Struct Biol , vol.160 , pp. 385-394
    • Scheuring, S.1    Buzhynskyy, N.2    Jaroslawski, S.3    Goncalves, R.P.4    Hite, R.K.5    Walz, T.6
  • 171
    • 0033054261 scopus 로고    scopus 로고
    • Modifications to rat lens major intrinsic protein in selenite-induced cataract
    • Schey KL, Fowler JG, Shearer TR, David L (1999) Modifications to rat lens major intrinsic protein in selenite-induced cataract. Invest Ophthalmol Vis Sci 40:657-667
    • (1999) Invest Ophthalmol Vis Sci , vol.40 , pp. 657-667
    • Schey, K.L.1    Fowler, J.G.2    Shearer, T.R.3    David, L.4
  • 173
    • 45549088852 scopus 로고    scopus 로고
    • Posttranslational modifications in lens fiber connexins identified by off-line-HPLC MALDI-quadrupole time-of-flight mass spectroscopy
    • Shearer D, EnsW, Standing K, Valdimarsson G (2008) Posttranslational modifications in lens fiber connexins identified by off-line-HPLC MALDI-quadrupole time-of-flight mass spectroscopy. Invest Ophthalmol Vis Sci 49:1553-1562
    • (2008) Invest Ophthalmol Vis Sci , vol.49 , pp. 1553-1562
    • Shearer, D.1    Ens, W.2    Standing, K.3    Valdimarsson, G.4
  • 174
    • 0026070186 scopus 로고
    • Channel reconstitution in liposomes and planar bilayers with HPLC-purified MIP26 of bovine lens
    • Shen L, Shrager P, Girsch SJ, Donaldson PJ, Peracchia C (1991) Channel reconstitution in liposomes and planar bilayers with HPLC-purified MIP26 of bovine lens. JMembr Biol 124:21-32
    • (1991) JMembr Biol , vol.124 , pp. 21-32
    • Shen, L.1    Shrager, P.2    Girsch, S.J.3    Donaldson, P.J.4    Peracchia, C.5
  • 175
    • 0242319631 scopus 로고    scopus 로고
    • Development of a macromolecular diffusion pathway in the lens
    • Shestopalov VI, Bassnett S (2003) Development of a macromolecular diffusion pathway in the lens. J Cell Sci 116:4191-4199
    • (2003) J Cell Sci , vol.116 , pp. 4191-4199
    • Shestopalov, V.I.1    Bassnett, S.2
  • 176
    • 0030031158 scopus 로고    scopus 로고
    • Mutations in the founder of the MIP gene family underlie cataract development in the mouse
    • Shiels A, Bassnett S (1996) Mutations in the founder of the MIP gene family underlie cataract development in the mouse. Nat Genet 12:212-215
    • (1996) Nat Genet , vol.12 , pp. 212-215
    • Shiels, A.1    Bassnett, S.2
  • 177
    • 0027437259 scopus 로고
    • Aberrant expression of the gene for lens major intrinsic protein in the CAT mouse
    • Shiels A, Griffin CS (1993) Aberrant expression of the gene for lens major intrinsic protein in the CAT mouse. Curr Eye Res 12:913-921
    • (1993) Curr Eye Res , vol.12 , pp. 913-921
    • Shiels, A.1    Griffin, C.S.2
  • 179
    • 0026094642 scopus 로고
    • Immunochemical comparison of the major intrinsic protein of eye-lens fiber cell membranes in mice with hereditary cataracts
    • Shiels A, Griffin CS, Muggleton-Harris AL (1991) Immunochemical comparison of the major intrinsic protein of eye-lens fiber cell membranes in mice with hereditary cataracts. Biochim Biophys Acta 1097:318-324
    • (1991) Biochim Biophys Acta , vol.1097 , pp. 318-324
    • Shiels, A.1    Griffin, C.S.2    Muggleton-Harris, A.L.3
  • 180
    • 0033729222 scopus 로고    scopus 로고
    • Disruption of lens fiber cell architecture in mice expressing a chimeric AQP0-LTR protein
    • Shiels A, Mackay D, Bassnett S, Al-Ghoul K, Kuszak J (2000) Disruption of lens fiber cell architecture in mice expressing a chimeric AQP0-LTR protein. FASEB J 14:2207-2212
    • (2000) FASEB J , vol.14 , pp. 2207-2212
    • Shiels, A.1    Mackay, D.2    Bassnett, S.3    Al-Ghoul, K.4    Kuszak, J.5
  • 183
    • 0027973615 scopus 로고
    • The interrelationship of lens anatomy and optical quality. I. Non-primate lenses
    • Sivak JG, Herbert KL, Peterson KL, Kuszak JR (1994) The interrelationship of lens anatomy and optical quality. I. Non-primate lenses. Exp Eye Res 59:505-520
    • (1994) Exp Eye Res , vol.59 , pp. 505-520
    • Sivak, J.G.1    Herbert, K.L.2    Peterson, K.L.3    Kuszak, J.R.4
  • 184
    • 0027984623 scopus 로고
    • Localization of aquaporin CHIP in the human eye: Implications in the pathogenesis of glaucoma and other disorders of ocular fluid balance
    • Stamer WD, Snyder RW, Smith BL, Agre P, Regan JW (1994) Localization of aquaporin CHIP in the human eye: implications in the pathogenesis of glaucoma and other disorders of ocular fluid balance. Invest Ophthalmol Vis Sci 35:3867-3872
    • (1994) Invest Ophthalmol Vis Sci , vol.35 , pp. 3867-3872
    • Stamer, W.D.1    Snyder, R.W.2    Smith, B.L.3    Agre, P.4    Regan, J.W.5
  • 185
    • 0026774929 scopus 로고
    • Glycation of lensMIP26 affects the permeability in reconstituted liposomes
    • SwamyMS, Abraham EC (1992) Glycation of lensMIP26 affects the permeability in reconstituted liposomes. Biochem Biophys Res Commun 186:632-638
    • (1992) Biochem Biophys Res Commun , vol.186 , pp. 632-638
    • Swamy, M.S.1    Abraham, E.C.2
  • 186
    • 0035971736 scopus 로고    scopus 로고
    • Glycation decreases calmodulin binding to lens transmembrane protein, MIP
    • Swamy-Mruthinti S (2001) Glycation decreases calmodulin binding to lens transmembrane protein, MIP. Biochim Biophys Acta 1536:64-72
    • (2001) Biochim Biophys Acta , vol.1536 , pp. 64-72
    • Swamy-Mruthinti, S.1
  • 187
    • 0030928806 scopus 로고    scopus 로고
    • Mass spectroscopic identification of in vitro glycated sites of MIP
    • Swamy-Mruthinti S, Schey KL (1997) Mass spectroscopic identification of in vitro glycated sites of MIP. Curr Eye Res 16:936-941
    • (1997) Curr Eye Res , vol.16 , pp. 936-941
    • Swamy-Mruthinti, S.1    Schey, K.L.2
  • 188
    • 0024560509 scopus 로고
    • Formation of gap junctions by expression of connexins in Xenopus oocyte pairs
    • Swenson KI, Jordan JR, Beyer EC, Paul DL (1989) Formation of gap junctions by expression of connexins in Xenopus oocyte pairs. Cell 57:145-155
    • (1989) Cell , vol.57 , pp. 145-155
    • Swenson, K.I.1    Jordan, J.R.2    Beyer, E.C.3    Paul, D.L.4
  • 189
    • 0022500721 scopus 로고
    • Covalent change of major intrinsic polypeptide (MIP26K) of lens membrane during human senile cataractogenesis
    • Takemoto L, Takehana M (1986a) Covalent change of major intrinsic polypeptide (MIP26K) of lens membrane during human senile cataractogenesis. Biochem Biophys Res Commun 135:965-971
    • (1986) Biochem Biophys Res Commun , vol.135 , pp. 965-971
    • Takemoto, L.1    Takehana, M.2
  • 190
    • 0022978546 scopus 로고
    • Major intrinsic polypeptide (MIP26K) from human lens membrane: Characterization of low-molecular-weight forms in the aging human lens
    • Takemoto L, Takehana M (1986b) Major intrinsic polypeptide (MIP26K) from human lens membrane: characterization of low-molecular-weight forms in the aging human lens. Exp Eye Res 43:661-667
    • (1986) Exp Eye Res , vol.43 , pp. 661-667
    • Takemoto, L.1    Takehana, M.2
  • 191
    • 0022607768 scopus 로고
    • Antisera to synthetic peptides of MIP26K as probes of membrane changes during human cataractogenesis
    • Takemoto L, Takehana M, Horwitz J (1986a) Antisera to synthetic peptides of MIP26K as probes of membrane changes during human cataractogenesis. Exp Eye Res 42:497-501
    • (1986) Exp Eye Res , vol.42 , pp. 497-501
    • Takemoto, L.1    Takehana, M.2    Horwitz, J.3
  • 192
    • 0022587559 scopus 로고
    • Covalent changes in MIP26K during aging of the human lens membrane
    • Takemoto L, Takehana M, Horwitz J (1986b) Covalent changes in MIP26K during aging of the human lens membrane. Invest Ophthalmol Vis Sci 27:443-446
    • (1986) Invest Ophthalmol Vis Sci , vol.27 , pp. 443-446
    • Takemoto, L.1    Takehana, M.2    Horwitz, J.3
  • 193
    • 0023223347 scopus 로고
    • Antisera to synthetic peptides of MIP26K as probes of changes in opaque vs. transparent regions within the same human cataractous lens
    • Takemoto L, Kodama T, Takemoto D (1987a) Antisera to synthetic peptides of MIP26K as probes of changes in opaque vs. transparent regions within the same human cataractous lens. Exp Eye Res 45:179-183
    • (1987) Exp Eye Res , vol.45 , pp. 179-183
    • Takemoto, L.1    Kodama, T.2    Takemoto, D.3
  • 194
    • 0023143942 scopus 로고
    • Major intrinsic polypeptide (MIP26K) of the lens membrane: Covalent change in an internal sequence during human senile cataractogenesis
    • Takemoto L, Smith J, Kodama T (1987b) Major intrinsic polypeptide (MIP26K) of the lens membrane: covalent change in an internal sequence during human senile cataractogenesis. Biochem Biophys Res Commun 142:761-766
    • (1987) Biochem Biophys Res Commun , vol.142 , pp. 761-766
    • Takemoto, L.1    Smith, J.2    Kodama, T.3
  • 195
    • 0023810717 scopus 로고
    • Changes in the major intrinsic polypeptide (MIP26K) during opacification of the Emory mouse lens
    • Takemoto L, Kuck J, Kuck K (1988) Changes in the major intrinsic polypeptide (MIP26K) during opacification of the Emory mouse lens. Exp Eye Res 47:329-336
    • (1988) Exp Eye Res , vol.47 , pp. 329-336
    • Takemoto, L.1    Kuck, J.2    Kuck, K.3
  • 196
    • 0026024254 scopus 로고
    • Changes in lens membrane major intrinsic polypeptide during cataractogenesis in aged Hannover Wistar rats
    • Takemoto LJ, GorthyWC, Morin CL, Steward DE (1991) Changes in lens membrane major intrinsic polypeptide during cataractogenesis in aged Hannover Wistar rats. Invest Ophthalmol Vis Sci 32:556-561
    • (1991) Invest Ophthalmol Vis Sci , vol.32 , pp. 556-561
    • Takemoto, L.J.1    Gorthy, W.C.2    Morin, C.L.3    Steward, D.E.4
  • 199
    • 34248547579 scopus 로고    scopus 로고
    • Functional expression of aquaporins in embryonic, postnatal, and adult mouse lenses
    • Varadaraj K, Kumari SS, Mathias RT (2007) Functional expression of aquaporins in embryonic, postnatal, and adult mouse lenses. Dev Dyn 236:1319-1328
    • (2007) Dev Dyn , vol.236 , pp. 1319-1328
    • Varadaraj, K.1    Kumari, S.S.2    Mathias, R.T.3
  • 200
    • 46049085584 scopus 로고    scopus 로고
    • Functional characterization of a human aquaporin 0 mutation that leads to a congenital dominant lens cataract
    • Varadaraj K, Kumari SS, Patil R, Wax MB, Mathias RT (2008) Functional characterization of a human aquaporin 0 mutation that leads to a congenital dominant lens cataract. Exp Eye Res 87:9-21
    • (2008) Exp Eye Res , vol.87 , pp. 9-21
    • Varadaraj, K.1    Kumari, S.S.2    Patil, R.3    Wax, M.B.4    Mathias, R.T.5
  • 203
    • 0035665531 scopus 로고    scopus 로고
    • Virkki LV, Cooper GJ, Boron WF (2001) Cloning and functional expression of an MIP (AQP0) homolog from killifish (Fundulus heteroclitus) lens. Am J Physiol Regul Integr Comp Physiol 281:R1994-R2003
    • Virkki LV, Cooper GJ, Boron WF (2001) Cloning and functional expression of an MIP (AQP0) homolog from killifish (Fundulus heteroclitus) lens. Am J Physiol Regul Integr Comp Physiol 281:R1994-R2003
  • 205
    • 48249092089 scopus 로고    scopus 로고
    • Differentiation-dependent changes in the membrane properties of fiber cells isolated from the rat lens
    • Webb KF, Donaldson PJ (2008) Differentiation-dependent changes in the membrane properties of fiber cells isolated from the rat lens. Am J Physiol 294:C1133-C1145
    • (2008) Am J Physiol , vol.294
    • Webb, K.F.1    Donaldson, P.J.2
  • 206
    • 0037059499 scopus 로고    scopus 로고
    • White TW (2002) Unique and redundant connexin contributions to lens development. Science (New York, NY) 295:319-320
    • White TW (2002) Unique and redundant connexin contributions to lens development. Science (New York, NY) 295:319-320
  • 207
    • 0027070644 scopus 로고
    • Mouse C×50, a functional member of the connexin family of gap junction proteins, is the lens fiber protein MP70
    • White TW, Bruzzone R, Goodenough DA, Paul DL (1992) Mouse C×50, a functional member of the connexin family of gap junction proteins, is the lens fiber protein MP70. Mol Biol Cell 3:711-720
    • (1992) Mol Biol Cell , vol.3 , pp. 711-720
    • White, T.W.1    Bruzzone, R.2    Goodenough, D.A.3    Paul, D.L.4
  • 209
    • 33745170655 scopus 로고    scopus 로고
    • Absence of alpha3 (C×46) and alpha8 (C×50) connexins leads to cataracts by affecting lens inner fiber cells
    • Xia CH, Cheng C, Huang Q, Cheung D, Li L, Dunia I, Benedetti LE, Horwitz J, Gong X (2006a) Absence of alpha3 (C×46) and alpha8 (C×50) connexins leads to cataracts by affecting lens inner fiber cells. Exp Eye Res 83:688-696
    • (2006) Exp Eye Res , vol.83 , pp. 688-696
    • Xia, C.H.1    Cheng, C.2    Huang, Q.3    Cheung, D.4    Li, L.5    Dunia, I.6    Benedetti, L.E.7    Horwitz, J.8    Gong, X.9
  • 211
    • 0023856874 scopus 로고
    • Expression of the gene for main intrinsic polypeptide (MIP): Separate spatial distributions of MIP and beta-crystallin gene transcripts in rat lens development
    • Yancey SB, Koh K, Chung J, Revel JP (1988) Expression of the gene for main intrinsic polypeptide (MIP): separate spatial distributions of MIP and beta-crystallin gene transcripts in rat lens development. J Cell Biol 106:705-714
    • (1988) J Cell Biol , vol.106 , pp. 705-714
    • Yancey, S.B.1    Koh, K.2    Chung, J.3    Revel, J.P.4
  • 212
    • 1642365478 scopus 로고    scopus 로고
    • Interaction of major intrinsic protein (aquaporin-0) with fiber connexins in lens development
    • Yu XS, Jiang JX (2004) Interaction of major intrinsic protein (aquaporin-0) with fiber connexins in lens development. J Cell Sci 117:871-880
    • (2004) J Cell Sci , vol.117 , pp. 871-880
    • Yu, X.S.1    Jiang, J.X.2
  • 213
    • 20444505236 scopus 로고    scopus 로고
    • Developmental regulation of the direct interaction between the intracellular loop of connexin 45.6 and the C terminus of major intrinsic protein (aquaporin-0)
    • Yu XS, Yin X, Lafer EM, Jiang JX (2005) Developmental regulation of the direct interaction between the intracellular loop of connexin 45.6 and the C terminus of major intrinsic protein (aquaporin-0). J Cell Biol 280:22081-22090
    • (2005) J Cell Biol , vol.280 , pp. 22081-22090
    • Yu, X.S.1    Yin, X.2    Lafer, E.M.3    Jiang, J.X.4
  • 215
    • 0024312337 scopus 로고
    • The structural organization and protein composition of lens fiber junctions
    • Zampighi GA, Hall JE, Ehring GR, Simon SA (1989) The structural organization and protein composition of lens fiber junctions. J Cell Biol 108:2255-2275
    • (1989) J Cell Biol , vol.108 , pp. 2255-2275
    • Zampighi, G.A.1    Hall, J.E.2    Ehring, G.R.3    Simon, S.A.4
  • 217
    • 0014385272 scopus 로고
    • Morphogenesis of the eye lens in a mouse strain with hereditary cataracts
    • Zwaan J, Williams RM (1968) Morphogenesis of the eye lens in a mouse strain with hereditary cataracts. J Exp Zool 169:407-421
    • (1968) J Exp Zool , vol.169 , pp. 407-421
    • Zwaan, J.1    Williams, R.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.