메뉴 건너뛰기




Volumn 26, Issue 1, 2007, Pages 78-98

Crystallins in the eye: Function and pathology

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA CRYSTALLIN; BETA CRYSTALLIN; CHAPERONE; CRYSTALLIN; DESMIN; HEAT SHOCK PROTEIN; STRUCTURAL PROTEIN;

EID: 33845425645     PISSN: 13509462     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.preteyeres.2006.10.003     Document Type: Review
Times cited : (376)

References (189)
  • 2
    • 0029770039 scopus 로고    scopus 로고
    • Cloning, expression, and chaperone-like activity of human alphaA-crystallin
    • Andley U.P., Mathur S., Griest T.A., and Petrash J.M. Cloning, expression, and chaperone-like activity of human alphaA-crystallin. J. Biol. Chem. 271 (1996) 31973-31980
    • (1996) J. Biol. Chem. , vol.271 , pp. 31973-31980
    • Andley, U.P.1    Mathur, S.2    Griest, T.A.3    Petrash, J.M.4
  • 3
    • 0032553123 scopus 로고    scopus 로고
    • The molecular chaperone alphaA-crystallin enhances lens epithelial cell growth and resistance to UVA stress
    • Andley U.P., Song Z., Wawrousek E.F., and Bassnett S. The molecular chaperone alphaA-crystallin enhances lens epithelial cell growth and resistance to UVA stress. J. Biol. Chem. 273 (1998) 31252-31261
    • (1998) J. Biol. Chem. , vol.273 , pp. 31252-31261
    • Andley, U.P.1    Song, Z.2    Wawrousek, E.F.3    Bassnett, S.4
  • 4
    • 0034711260 scopus 로고    scopus 로고
    • Differential protective activity of alphaA- and alphaB-crystallin in lens epithelial cells
    • Andley U.P., Song Z., Wawrousek E.F., Fleming T.P., and Bassnett S. Differential protective activity of alphaA- and alphaB-crystallin in lens epithelial cells. J. Biol. Chem. 275 (2000) 36823-36831
    • (2000) J. Biol. Chem. , vol.275 , pp. 36823-36831
    • Andley, U.P.1    Song, Z.2    Wawrousek, E.F.3    Fleming, T.P.4    Bassnett, S.5
  • 5
    • 0035169769 scopus 로고    scopus 로고
    • Lens epithelial cells derived from alphaB-crystallin knockout mice demonstrate hyperproliferation and genomic instability
    • Andley U.P., Song Z., Wawrousek E.F., Brady J.P., Bassnett S., and Fleming T.P. Lens epithelial cells derived from alphaB-crystallin knockout mice demonstrate hyperproliferation and genomic instability. Faseb J. 15 (2001) 221-229
    • (2001) Faseb J. , vol.15 , pp. 221-229
    • Andley, U.P.1    Song, Z.2    Wawrousek, E.F.3    Brady, J.P.4    Bassnett, S.5    Fleming, T.P.6
  • 6
    • 0037155819 scopus 로고    scopus 로고
    • The R116C mutation in alpha A-crystallin diminishes its protective ability against stress-induced lens epithelial cell apoptosis
    • Andley U.P., Patel H.C., and Xi J.H. The R116C mutation in alpha A-crystallin diminishes its protective ability against stress-induced lens epithelial cell apoptosis. J. Biol. Chem. 277 (2002) 10178-10186
    • (2002) J. Biol. Chem. , vol.277 , pp. 10178-10186
    • Andley, U.P.1    Patel, H.C.2    Xi, J.H.3
  • 7
    • 0141703310 scopus 로고    scopus 로고
    • Polydispersity of a mammalian chaperone: mass spectrometry reveals the population of oligomers in alphaB-crystallin
    • Aquilina J.A., Benesch J.L., Bateman O.A., Slingsby C., and Robinson C.V. Polydispersity of a mammalian chaperone: mass spectrometry reveals the population of oligomers in alphaB-crystallin. Proc. Natl. Acad. Sci. USA 100 (2003) 10611-10616
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 10611-10616
    • Aquilina, J.A.1    Benesch, J.L.2    Bateman, O.A.3    Slingsby, C.4    Robinson, C.V.5
  • 8
    • 3142543752 scopus 로고    scopus 로고
    • Phosphorylation of {alpha}B-crystallin Alters Chaperone Function through Loss of Dimeric Substructure
    • Aquilina J.A., Benesch J.L.P., Ding L.L., Yaron O., Horwitz J., and Robinson C.V. Phosphorylation of {alpha}B-crystallin Alters Chaperone Function through Loss of Dimeric Substructure. J. Biol. Chem. 279 (2004) 28675-28680
    • (2004) J. Biol. Chem. , vol.279 , pp. 28675-28680
    • Aquilina, J.A.1    Benesch, J.L.P.2    Ding, L.L.3    Yaron, O.4    Horwitz, J.5    Robinson, C.V.6
  • 9
    • 0031457379 scopus 로고    scopus 로고
    • Chaperone activity of alpha B-crystallin suppresses tubulin aggregation through complex formation
    • Arai H., and Atomi Y. Chaperone activity of alpha B-crystallin suppresses tubulin aggregation through complex formation. Cell Struct. Funct. 22 (1997) 539-544
    • (1997) Cell Struct. Funct. , vol.22 , pp. 539-544
    • Arai, H.1    Atomi, Y.2
  • 10
    • 0031962486 scopus 로고    scopus 로고
    • Small stress proteins: chaperones that act as regulators of intracellular redox state and programmed cell death
    • Arrigo A.P. Small stress proteins: chaperones that act as regulators of intracellular redox state and programmed cell death. Biol. Chem. 379 (1998) 19-26
    • (1998) Biol. Chem. , vol.379 , pp. 19-26
    • Arrigo, A.P.1
  • 12
    • 16644372078 scopus 로고    scopus 로고
    • Cell kinetic status of mouse lens epithelial cells lacking alphaA- and alphaB-crystallin
    • Bai F., Xi J., Higashikubo R., and Andley U.P. Cell kinetic status of mouse lens epithelial cells lacking alphaA- and alphaB-crystallin. Mol. Cell Biochem. 265 (2004) 115-122
    • (2004) Mol. Cell Biochem. , vol.265 , pp. 115-122
    • Bai, F.1    Xi, J.2    Higashikubo, R.3    Andley, U.P.4
  • 13
    • 11844302307 scopus 로고    scopus 로고
    • A comparative analysis of alphaA- and alphaB-crystallin expression during the cell cycle in primary mouse lens epithelial cultures
    • Bai F., Xi J., Higashikubo R., and Andley U.P. A comparative analysis of alphaA- and alphaB-crystallin expression during the cell cycle in primary mouse lens epithelial cultures. Exp. Eye Res. 79 (2004) 795-805
    • (2004) Exp. Eye Res. , vol.79 , pp. 795-805
    • Bai, F.1    Xi, J.2    Higashikubo, R.3    Andley, U.P.4
  • 14
    • 0141591735 scopus 로고    scopus 로고
    • Hyperproliferation and p53 status of lens epithelial cells derived from alphaB-crystallin knockout mice
    • Bai F., Xi J.H., Wawrousek E.F., Fleming T.P., and Andley U.P. Hyperproliferation and p53 status of lens epithelial cells derived from alphaB-crystallin knockout mice. J. Biol. Chem. 278 (2003) 36876-36886
    • (2003) J. Biol. Chem. , vol.278 , pp. 36876-36886
    • Bai, F.1    Xi, J.H.2    Wawrousek, E.F.3    Fleming, T.P.4    Andley, U.P.5
  • 15
    • 0036343618 scopus 로고    scopus 로고
    • Lens organelle degradation
    • Bassnett S. Lens organelle degradation. Exp. Eye Res. 74 (2002) 1-6
    • (2002) Exp. Eye Res. , vol.74 , pp. 1-6
    • Bassnett, S.1
  • 16
    • 0035094146 scopus 로고    scopus 로고
    • Changes in adhesion complexes define stages in the differentiation of lens fiber cells
    • Beebe D.C., Vasiliev O., Guo J., Shui Y.B., and Bassnett S. Changes in adhesion complexes define stages in the differentiation of lens fiber cells. Invest. Ophthalmol. Vis. Sci. 42 (2001) 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
  • 17
  • 18
    • 0028071812 scopus 로고
    • Phosphorylation and supramolecular organization of murine small heat shock protein HSP25 abolish its actin polymerization-inhibiting activity
    • Benndorf R., Hayess K., Ryazantsev S., Wieske M., Behlke J., and Lutsch G. Phosphorylation and supramolecular organization of murine small heat shock protein HSP25 abolish its actin polymerization-inhibiting activity. J. Biol. Chem. 269 (1994) 20780-20784
    • (1994) J. Biol. Chem. , vol.269 , pp. 20780-20784
    • Benndorf, R.1    Hayess, K.2    Ryazantsev, S.3    Wieske, M.4    Behlke, J.5    Lutsch, G.6
  • 19
    • 0024578954 scopus 로고
    • alpha B subunit of lens-specific protein alpha-crystallin is present in other ocular and non-ocular tissues
    • Bhat S.P., and Nagineni C.N. alpha B subunit of lens-specific protein alpha-crystallin is present in other ocular and non-ocular tissues. Biochem. Biophys. Res. Commun. 158 (1989) 319-325
    • (1989) Biochem. Biophys. Res. Commun. , vol.158 , pp. 319-325
    • Bhat, S.P.1    Nagineni, C.N.2
  • 20
    • 0037086447 scopus 로고    scopus 로고
    • Addressing protein localization within the nucleus
    • Bickmore W.A., and Sutherland H.G. Addressing protein localization within the nucleus. Embo J. 21 (2002) 1248-1254
    • (2002) Embo J. , vol.21 , pp. 1248-1254
    • Bickmore, W.A.1    Sutherland, H.G.2
  • 22
    • 33750857016 scopus 로고    scopus 로고
    • Specific heat shock proteins protect microtubules during simulated ischemia in cardiac myocytes
    • Bluhm W.F., Martin J.L., Mestril R., and Dillmann W.H. Specific heat shock proteins protect microtubules during simulated ischemia in cardiac myocytes. Am. J. Physiol. 275 (1998) H2243-H2249
    • (1998) Am. J. Physiol. , vol.275
    • Bluhm, W.F.1    Martin, J.L.2    Mestril, R.3    Dillmann, W.H.4
  • 23
    • 0035847115 scopus 로고    scopus 로고
    • Interaction between αB-crystallin and the human 20S proteasomal subunit C8/alpha7
    • Boelens W.C., Croes Y., and de Jong W.W. Interaction between αB-crystallin and the human 20S proteasomal subunit C8/alpha7. Biochim. Biophys. Acta 1544 (2001) 311-319
    • (2001) Biochim. Biophys. Acta , vol.1544 , pp. 311-319
    • Boelens, W.C.1    Croes, Y.2    de Jong, W.W.3
  • 25
    • 0030015111 scopus 로고    scopus 로고
    • EM immunolocalization of alpha-crystallins: association with the plasma membrane from normal and cataractous human lenses
    • Boyle D.L., and Takemoto L. EM immunolocalization of alpha-crystallins: association with the plasma membrane from normal and cataractous human lenses. Curr. Eye Res. 15 (1996) 577-582
    • (1996) Curr. Eye Res. , vol.15 , pp. 577-582
    • Boyle, D.L.1    Takemoto, L.2
  • 26
    • 0034181672 scopus 로고    scopus 로고
    • A possible role for alpha-crystallins in lens epithelial cell differentiation
    • Boyle D.L., and Takemoto L. A possible role for alpha-crystallins in lens epithelial cell differentiation. Mol. Vis. 6 (2000) 63-71
    • (2000) Mol. Vis. , vol.6 , pp. 63-71
    • Boyle, D.L.1    Takemoto, L.2
  • 27
    • 2942750445 scopus 로고    scopus 로고
    • Morphological characterization of the Alpha A- and Alpha B-crystallin double knockout mouse lens
    • Boyle D.L., Takemoto L., Brady J.P., and Wawrousek E.F. Morphological characterization of the Alpha A- and Alpha B-crystallin double knockout mouse lens. BMC Ophthalmol. 3 (2003) 3
    • (2003) BMC Ophthalmol. , vol.3 , pp. 3
    • Boyle, D.L.1    Takemoto, L.2    Brady, J.P.3    Wawrousek, E.F.4
  • 28
    • 0031017669 scopus 로고    scopus 로고
    • Targeted disruption of the mouse alpha A-crystallin gene induces cataract and cytoplasmic inclusion bodies containing the small heat shock protein alpha B-crystallin
    • Brady J.P., Garland D., Duglas-Tabor Y., Robison Jr. W.G., Groome A., and Wawrousek E.F. Targeted disruption of the mouse alpha A-crystallin gene induces cataract and cytoplasmic inclusion bodies containing the small heat shock protein alpha B-crystallin. Proc. Natl. Acad. Sci. USA 94 (1997) 884-889
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 884-889
    • Brady, J.P.1    Garland, D.2    Duglas-Tabor, Y.3    Robison Jr., W.G.4    Groome, A.5    Wawrousek, E.F.6
  • 31
    • 0033016897 scopus 로고    scopus 로고
    • The small heat shock-related protein-20 is an actin-associated protein
    • Brophy C.M., Lamb S., and Graham A. The small heat shock-related protein-20 is an actin-associated protein. J. Vasc. Res. 29 (1999) 326-333
    • (1999) J. Vasc. Res. , vol.29 , pp. 326-333
    • Brophy, C.M.1    Lamb, S.2    Graham, A.3
  • 33
    • 0028831015 scopus 로고
    • In vitro studies on the assembly properties of the lens proteins CP49, CP115: coassembly with alpha-crystallin but not with vimentin
    • Carter J.M., Hutcheson A.M., and Quinlan R.A. In vitro studies on the assembly properties of the lens proteins CP49, CP115: coassembly with alpha-crystallin but not with vimentin. Exp. Eye Res. 60 (1995) 181-192
    • (1995) Exp. Eye Res. , vol.60 , pp. 181-192
    • Carter, J.M.1    Hutcheson, A.M.2    Quinlan, R.A.3
  • 34
    • 0032078745 scopus 로고    scopus 로고
    • NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and chaperone action of small heat-shock proteins
    • Carver J.A., and Lindner R.A. NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and chaperone action of small heat-shock proteins. Int. J. Biol. Macromol. 22 (1998) 197-209
    • (1998) Int. J. Biol. Macromol. , vol.22 , pp. 197-209
    • Carver, J.A.1    Lindner, R.A.2
  • 35
    • 0036306093 scopus 로고    scopus 로고
    • The interaction of the molecular chaperone alpha-crystallin with unfolding alpha-lactalbumin: a structural and kinetic spectroscopic study
    • Carver J.A., Lindner R.A., Lyon C., Canet D., Hernandez H., Dobson C.M., and Redfield C. The interaction of the molecular chaperone alpha-crystallin with unfolding alpha-lactalbumin: a structural and kinetic spectroscopic study. J. Mol. Biol. 318 (2002) 815-827
    • (2002) J. Mol. Biol. , vol.318 , pp. 815-827
    • Carver, J.A.1    Lindner, R.A.2    Lyon, C.3    Canet, D.4    Hernandez, H.5    Dobson, C.M.6    Redfield, C.7
  • 36
    • 0024584286 scopus 로고
    • Differential synthesis and phosphorylation of the alpha-crystallin A and B chains during bovine lens fiber cell differentiation
    • Chiesa R., McDermott M.J., and Spector A. Differential synthesis and phosphorylation of the alpha-crystallin A and B chains during bovine lens fiber cell differentiation. Curr. Eye Res. 8 (1989) 151-158
    • (1989) Curr. Eye Res. , vol.8 , pp. 151-158
    • Chiesa, R.1    McDermott, M.J.2    Spector, A.3
  • 37
    • 0032773390 scopus 로고    scopus 로고
    • Lens cytoskeleton and transparency: a model
    • Clark J.I., Matsushima H., David L.L., and Clark J.M. Lens cytoskeleton and transparency: a model. Eye 13 Pt 3b (1999) 417-424
    • (1999) Eye , vol.13 , Issue.PART 3b , pp. 417-424
    • Clark, J.I.1    Matsushima, H.2    David, L.L.3    Clark, J.M.4
  • 38
  • 39
    • 0035095351 scopus 로고    scopus 로고
    • Crystal structure of the calcium-loaded spherulin 3a dimer sheds light on the evolution of the eye lens betagamma-crystallin domain fold
    • Clout N.J., Kretschmar M., Jaenicke R., and Slingsby C. Crystal structure of the calcium-loaded spherulin 3a dimer sheds light on the evolution of the eye lens betagamma-crystallin domain fold. Structure 9 (2001) 115-124
    • (2001) Structure , vol.9 , pp. 115-124
    • Clout, N.J.1    Kretschmar, M.2    Jaenicke, R.3    Slingsby, C.4
  • 40
    • 0034719154 scopus 로고    scopus 로고
    • Structural and functional changes in the alpha A-crystallin R116C mutant in hereditary cataracts
    • Cobb B.A., and Petrash J.M. Structural and functional changes in the alpha A-crystallin R116C mutant in hereditary cataracts. Biochemistry 39 (2000) 15791-15798
    • (2000) Biochemistry , vol.39 , pp. 15791-15798
    • Cobb, B.A.1    Petrash, J.M.2
  • 41
    • 0037080002 scopus 로고    scopus 로고
    • alpha-crystallin chaperone-like activity and membrane binding in age-related cataracts
    • Cobb B.A., and Petrash J.M. alpha-crystallin chaperone-like activity and membrane binding in age-related cataracts. Biochemistry 41 (2002) 483-490
    • (2002) Biochemistry , vol.41 , pp. 483-490
    • Cobb, B.A.1    Petrash, J.M.2
  • 43
    • 1642442576 scopus 로고    scopus 로고
    • Mafs, Prox1, and Pax6 can regulate chicken betaB1-crystallin gene expression
    • Cui W., Tomarev S.I., Piatigorsky J., Chepelinsky A.B., and Duncan M.K. Mafs, Prox1, and Pax6 can regulate chicken betaB1-crystallin gene expression. J. Biol. Chem. 279 (2004) 11088-11095
    • (2004) J. Biol. Chem. , vol.279 , pp. 11088-11095
    • Cui, W.1    Tomarev, S.I.2    Piatigorsky, J.3    Chepelinsky, A.B.4    Duncan, M.K.5
  • 44
    • 0030219742 scopus 로고    scopus 로고
    • Lens development and crystallin gene expression: many roles for Pax-6
    • Cvekl A., and Piatigorsky J. Lens development and crystallin gene expression: many roles for Pax-6. Bioessays 18 (1996) 621-630
    • (1996) Bioessays , vol.18 , pp. 621-630
    • Cvekl, A.1    Piatigorsky, J.2
  • 45
    • 0027999510 scopus 로고
    • A complex array of positive and negative elements regulates the chicken alpha A-crystallin gene: involvement of Pax-6, USF, CREB and/or CREM, and AP-1 proteins
    • Cvekl A., Sax C.M., Bresnick E.H., and Piatigorsky J. A complex array of positive and negative elements regulates the chicken alpha A-crystallin gene: involvement of Pax-6, USF, CREB and/or CREM, and AP-1 proteins. Mol. Cell. Biol. 14 (1994) 7363-7376
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7363-7376
    • Cvekl, A.1    Sax, C.M.2    Bresnick, E.H.3    Piatigorsky, J.4
  • 46
    • 0032077156 scopus 로고    scopus 로고
    • Genealogy of the alpha-crystallin--small heat-shock protein superfamily
    • de Jong W.W., Caspers G.J., and Leunissen J.A. Genealogy of the alpha-crystallin--small heat-shock protein superfamily. Int. J. Biol. Macromol. 22 (1998) 151-162
    • (1998) Int. J. Biol. Macromol. , vol.22 , pp. 151-162
    • de Jong, W.W.1    Caspers, G.J.2    Leunissen, J.A.3
  • 47
    • 0020678719 scopus 로고
    • Short-range order of crystallin proteins accounts for eye lens transparency
    • Delaye M., and Tardieu A. Short-range order of crystallin proteins accounts for eye lens transparency. Nature 302 (1983) 415-417
    • (1983) Nature , vol.302 , pp. 415-417
    • Delaye, M.1    Tardieu, A.2
  • 48
    • 0037648469 scopus 로고    scopus 로고
    • The small heat-shock protein αB-crystallin promotes FBX4-dependent ubiquitination
    • den Engelsman J., Keijsers V., de Jong W.W., and Boelens W.W. The small heat-shock protein αB-crystallin promotes FBX4-dependent ubiquitination. J. Biol. Chem. 278 (2003) 4699-4704
    • (2003) J. Biol. Chem. , vol.278 , pp. 4699-4704
    • den Engelsman, J.1    Keijsers, V.2    de Jong, W.W.3    Boelens, W.W.4
  • 50
    • 27744461695 scopus 로고    scopus 로고
    • Nuclear import of {alpha}B-crystallin is phosphorylation-dependent and hampered by hyperphosphorylation of the myopathy-related mutant R120G
    • den Engelsman J., Gerrits D., de Jong W.W., Robbins J., Kato K., and Boelens W.C. Nuclear import of {alpha}B-crystallin is phosphorylation-dependent and hampered by hyperphosphorylation of the myopathy-related mutant R120G. J. Biol. Chem. 280 (2005) 37139-37148
    • (2005) J. Biol. Chem. , vol.280 , pp. 37139-37148
    • den Engelsman, J.1    Gerrits, D.2    de Jong, W.W.3    Robbins, J.4    Kato, K.5    Boelens, W.C.6
  • 51
    • 0028178722 scopus 로고
    • Alpha A- and alpha B-crystallin in the retina. Association with the post-Golgi compartment of frog retinal photoreceptors
    • Deretic D., Aebersold R.H., Morrison H.D., and Papermaster D.S. Alpha A- and alpha B-crystallin in the retina. Association with the post-Golgi compartment of frog retinal photoreceptors. J. Biol. Chem. 269 (1994) 16853-16861
    • (1994) J. Biol. Chem. , vol.269 , pp. 16853-16861
    • Deretic, D.1    Aebersold, R.H.2    Morrison, H.D.3    Papermaster, D.S.4
  • 52
    • 0037096983 scopus 로고    scopus 로고
    • Effects of modifications of alpha-crystallin on its chaperone and other properties
    • Derham B.K., and Harding J.J. Effects of modifications of alpha-crystallin on its chaperone and other properties. Biochem. J. 364 (2002) 711-717
    • (2002) Biochem. J. , vol.364 , pp. 711-717
    • Derham, B.K.1    Harding, J.J.2
  • 54
    • 0030724879 scopus 로고    scopus 로고
    • AlphaB-crystallin interacts with intermediate filaments in response to stress
    • Djabali K., de Nechaud B., Landon F., and Portier M.M. AlphaB-crystallin interacts with intermediate filaments in response to stress. J. Cell Sci. 110 Pt 21 (1997) 2759-2769
    • (1997) J. Cell Sci. , vol.110 , Issue.PART 21 , pp. 2759-2769
    • Djabali, K.1    de Nechaud, B.2    Landon, F.3    Portier, M.M.4
  • 55
    • 0024580908 scopus 로고
    • Expression of the murine alpha B-crystallin gene is not restricted to the lens
    • Dubin R.A., Wawrousek E.F., and Piatigorsky J. Expression of the murine alpha B-crystallin gene is not restricted to the lens. Mol. Cell Biol. 9 (1989) 1083-1091
    • (1989) Mol. Cell Biol. , vol.9 , pp. 1083-1091
    • Dubin, R.A.1    Wawrousek, E.F.2    Piatigorsky, J.3
  • 56
    • 0343742639 scopus 로고    scopus 로고
    • Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation
    • Ehrnsperger M., Graber S., Gaestel M., and Buchner J. Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation. Embo J. 16 (1997) 221-229
    • (1997) Embo J. , vol.16 , pp. 221-229
    • Ehrnsperger, M.1    Graber, S.2    Gaestel, M.3    Buchner, J.4
  • 58
    • 2442684463 scopus 로고    scopus 로고
    • CRYBA3/A1 gene mutation associated with suture-sparing autosomal dominant congenital nuclear cataract: a novel phenotype
    • Ferrini W., Schorderet D.F., Othenin-Girard P., Uffer S., Heon E., and Munier F.L. CRYBA3/A1 gene mutation associated with suture-sparing autosomal dominant congenital nuclear cataract: a novel phenotype. Invest. Opthalmol. Vis. Sci. 45 (2004) 1436-1441
    • (2004) Invest. Opthalmol. Vis. Sci. , vol.45 , pp. 1436-1441
    • Ferrini, W.1    Schorderet, D.F.2    Othenin-Girard, P.3    Uffer, S.4    Heon, E.5    Munier, F.L.6
  • 59
    • 2342439076 scopus 로고    scopus 로고
    • alphaB-crystallin-coated MAP microtubule resists nocodazole and calcium-induced disassembly
    • Fujita Y., Ohto E., Katayama E., and Atomi Y. alphaB-crystallin-coated MAP microtubule resists nocodazole and calcium-induced disassembly. J. Cell. Sci. 117 (2004) 1719-1726
    • (2004) J. Cell. Sci. , vol.117 , pp. 1719-1726
    • Fujita, Y.1    Ohto, E.2    Katayama, E.3    Atomi, Y.4
  • 60
    • 6344241870 scopus 로고    scopus 로고
    • Small heat shock protein alphaB-crystallin is part of cell cycle-dependent Golgi reorganization
    • Gangalum R.K., Schibler M.J., and Bhat S.P. Small heat shock protein alphaB-crystallin is part of cell cycle-dependent Golgi reorganization. J. Biol. Chem. 279 (2004) 43374-43377
    • (2004) J. Biol. Chem. , vol.279 , pp. 43374-43377
    • Gangalum, R.K.1    Schibler, M.J.2    Bhat, S.P.3
  • 61
    • 14144255401 scopus 로고    scopus 로고
    • Insights into the domains required for dimerization and assembly of human alphaB crystallin
    • Ghosh J.G., and Clark J.I. Insights into the domains required for dimerization and assembly of human alphaB crystallin. Protein Sci. 14 (2005) 684-695
    • (2005) Protein Sci. , vol.14 , pp. 684-695
    • Ghosh, J.G.1    Clark, J.I.2
  • 63
    • 33746441661 scopus 로고    scopus 로고
    • {alpha}A-crystallin expression prevents {gamma}-crystallin insolubility and cataract formation in the zebrafish cloche mutant lens
    • Goishi K., Shimizu A., Najarro G., Watanabe S., Rogers R., Zon L.I., and Klagsbrun M. {alpha}A-crystallin expression prevents {gamma}-crystallin insolubility and cataract formation in the zebrafish cloche mutant lens. Development 133 (2006) 2585-2593
    • (2006) Development , vol.133 , pp. 2585-2593
    • Goishi, K.1    Shimizu, A.2    Najarro, G.3    Watanabe, S.4    Rogers, R.5    Zon, L.I.6    Klagsbrun, M.7
  • 64
    • 0026440390 scopus 로고
    • Binding of actin to lens alpha crystallins
    • Gopalakrishnan S., and 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
  • 65
    • 0032549677 scopus 로고    scopus 로고
    • The small heat-shock protein, alphaB-crystallin, has a variable quaternary structure
    • Haley D.A., Horwitz J., and Stewart P.L. The small heat-shock protein, alphaB-crystallin, has a variable quaternary structure. J. Mol. Biol. 277 (1998) 27-35
    • (1998) J. Mol. Biol. , vol.277 , pp. 27-35
    • Haley, D.A.1    Horwitz, J.2    Stewart, P.L.3
  • 66
    • 33746730605 scopus 로고    scopus 로고
    • MALDI Tissue Imaging of Ocular Lens {alpha}-crystallin
    • Han J., and Schey K.L. MALDI Tissue Imaging of Ocular Lens {alpha}-crystallin. Invest. Ophthalmol. Vis. Sci. 47 (2006) 2990-2996
    • (2006) Invest. Ophthalmol. Vis. Sci. , vol.47 , pp. 2990-2996
    • Han, J.1    Schey, K.L.2
  • 67
    • 0033829222 scopus 로고    scopus 로고
    • The major in vivo modifications of the human water-insoluble lens crystallins are disulfide bonds, deamidation, methionine oxidation and backbone cleavage
    • Hanson S.R., Hasan A., Smith D.L., and Smith J.B. The major in vivo modifications of the human water-insoluble lens crystallins are disulfide bonds, deamidation, methionine oxidation and backbone cleavage. Exp. Eye Res. 71 (2000) 195-207
    • (2000) Exp. Eye Res. , vol.71 , pp. 195-207
    • Hanson, S.R.1    Hasan, A.2    Smith, D.L.3    Smith, J.B.4
  • 68
    • 0033853066 scopus 로고    scopus 로고
    • Small heat shock proteins, the cytoskeleton, and inclusion body formation
    • Head M.W., and Goldman J.E. Small heat shock proteins, the cytoskeleton, and inclusion body formation. Neuropathol. Appl. Neurobiol. 26 (2000) 304-312
    • (2000) Neuropathol. Appl. Neurobiol. , vol.26 , pp. 304-312
    • Head, M.W.1    Goldman, J.E.2
  • 70
    • 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. USA 89 (1992) 10449-10453
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10449-10453
    • Horwitz, J.1
  • 71
    • 0037325497 scopus 로고    scopus 로고
    • Alpha-crystallin
    • Horwitz J. Alpha-crystallin. Exp. Eye Res. 76 (2003) 145-153
    • (2003) Exp. Eye Res. , vol.76 , pp. 145-153
    • Horwitz, J.1
  • 72
    • 0031918807 scopus 로고    scopus 로고
    • Lens alpha-crystallin: chaperone-like properties
    • Horwitz J., Huang Q.L., Ding L., and Bova M.P. Lens alpha-crystallin: chaperone-like properties. Methods Enzymol. 290 (1998) 365-383
    • (1998) Methods Enzymol. , vol.290 , pp. 365-383
    • Horwitz, J.1    Huang, Q.L.2    Ding, L.3    Bova, M.P.4
  • 73
    • 0032807869 scopus 로고    scopus 로고
    • Lens alpha-crystallin: function and structure
    • Horwitz J., Bova M.P., Ding L.L., Haley D.A., and Stewart P.L. Lens alpha-crystallin: function and structure. Eye 13 Pt 3b (1999) 403-408
    • (1999) Eye , vol.13 , Issue.PART 3b , pp. 403-408
    • Horwitz, J.1    Bova, M.P.2    Ding, L.L.3    Haley, D.A.4    Stewart, P.L.5
  • 74
    • 11844274723 scopus 로고    scopus 로고
    • The native oligomeric organization of alpha-crystallin, is it necessary for its chaperone function?
    • Horwitz J., Huang Q., and Ding L. The native oligomeric organization of alpha-crystallin, is it necessary for its chaperone function?. Exp. Eye Res. 79 (2004) 817-821
    • (2004) Exp. Eye Res. , vol.79 , pp. 817-821
    • Horwitz, J.1    Huang, Q.2    Ding, L.3
  • 76
    • 19444366359 scopus 로고    scopus 로고
    • Alexander-disease mutation of GFAP causes filament disorganization and decreased solubility of GFAP
    • Hsiao V.C., Tian R., Long H., Der Perng M., Brenner M., Quinlan R.A., and Goldman J.E. Alexander-disease mutation of GFAP causes filament disorganization and decreased solubility of GFAP. J. Cell Sci. 118 (2005) 2057-2065
    • (2005) J. Cell Sci. , vol.118 , pp. 2057-2065
    • Hsiao, V.C.1    Tian, R.2    Long, H.3    Der Perng, M.4    Brenner, M.5    Quinlan, R.A.6    Goldman, J.E.7
  • 77
    • 33744732089 scopus 로고    scopus 로고
    • A transgenic mouse model for human autosomal dominant cataract
    • Hsu C.D., Kymes S., and Petrash J.M. A transgenic mouse model for human autosomal dominant cataract. Invest. Ophthalmol. Vis. Sci. 47 (2006) 2036-2044
    • (2006) Invest. Ophthalmol. Vis. Sci. , vol.47 , pp. 2036-2044
    • Hsu, C.D.1    Kymes, S.2    Petrash, J.M.3
  • 78
    • 0035544297 scopus 로고    scopus 로고
    • AlphaB-crystallin phosphorylated at Ser-59 is localized in centrosomes and midbodies during mitosis
    • Inaguma Y., Ito H., Iwamoto I., Saga S., and Kato K. AlphaB-crystallin phosphorylated at Ser-59 is localized in centrosomes and midbodies during mitosis. Eur. J. Cell Biol. 80 (2001) 741-748
    • (2001) Eur. J. Cell Biol. , vol.80 , pp. 741-748
    • Inaguma, Y.1    Ito, H.2    Iwamoto, I.3    Saga, S.4    Kato, K.5
  • 79
    • 0020063988 scopus 로고
    • Four small Drosophila heat shock proteins are related to each other and to mammalian alpha-crystallin
    • Ingolia T.D., and Craig E.A. Four small Drosophila heat shock proteins are related to each other and to mammalian alpha-crystallin. Proc. Natl. Acad. Sci. USA 79 (1982) 2360-2364
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 2360-2364
    • Ingolia, T.D.1    Craig, E.A.2
  • 80
    • 0035167113 scopus 로고    scopus 로고
    • Lens crystallins and their microbial homologs: structure, stability, and function
    • Jaenicke R., and Slingsby C. Lens crystallins and their microbial homologs: structure, stability, and function. Crit. Rev. Biochem. Mol. Biol. 36 (2001) 435-499
    • (2001) Crit. Rev. Biochem. Mol. Biol. , vol.36 , pp. 435-499
    • Jaenicke, R.1    Slingsby, C.2
  • 82
    • 0034605446 scopus 로고    scopus 로고
    • Role of the heat shock response and molecular chaperones in oncogenesis and cell death
    • Jolly C., and Morimoto R.I. Role of the heat shock response and molecular chaperones in oncogenesis and cell death. J. Natl. Cancer Inst. 92 (2000) 1564-1572
    • (2000) J. Natl. Cancer Inst. , vol.92 , pp. 1564-1572
    • Jolly, C.1    Morimoto, R.I.2
  • 83
    • 0032556548 scopus 로고    scopus 로고
    • Expression of alphaB-crystallin in a mouse model of inherited retinal degeneration
    • Jones S.E., Jomary C., Grist J., Thomas M.R., and Neal M.J. Expression of alphaB-crystallin in a mouse model of inherited retinal degeneration. Neuroreport 9 (1998) 4161-4165
    • (1998) Neuroreport , vol.9 , pp. 4161-4165
    • Jones, S.E.1    Jomary, C.2    Grist, J.3    Thomas, M.R.4    Neal, M.J.5
  • 85
    • 0035844174 scopus 로고    scopus 로고
    • The small heat shock protein alpha B-crystallin negatively regulates cytochrome c- and caspase-8-dependent activation of caspase-3 by inhibiting its autoproteolytic maturation
    • Kamradt M.C., Chen F., and Cryns V.L. The small heat shock protein alpha B-crystallin negatively regulates cytochrome c- and caspase-8-dependent activation of caspase-3 by inhibiting its autoproteolytic maturation. J. Biol. Chem. 276 (2001) 16059-16063
    • (2001) J. Biol. Chem. , vol.276 , pp. 16059-16063
    • Kamradt, M.C.1    Chen, F.2    Cryns, V.L.3
  • 86
    • 0037064065 scopus 로고    scopus 로고
    • The small heat shock protein alpha B-crystallin negatively regulates apoptosis during myogenic differentiation by inhibiting caspase-3 activation
    • Kamradt M.C., Chen F., Sam S., and Cryns V.L. The small heat shock protein alpha B-crystallin negatively regulates apoptosis during myogenic differentiation by inhibiting caspase-3 activation. J. Biol. Chem. 277 (2002) 38731-38736
    • (2002) J. Biol. Chem. , vol.277 , pp. 38731-38736
    • Kamradt, M.C.1    Chen, F.2    Sam, S.3    Cryns, V.L.4
  • 88
    • 0028180509 scopus 로고
    • Alpha-crystallin/small heat shock protein has autokinase activity
    • Kantorow M., and Piatigorsky J. Alpha-crystallin/small heat shock protein has autokinase activity. Proc. Natl. Acad. Sci. USA 91 (1994) 3112-3116
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3112-3116
    • Kantorow, M.1    Piatigorsky, J.2
  • 89
    • 0346963154 scopus 로고    scopus 로고
    • Modified alpha A crystallin in the retina: altered expression and truncation with aging
    • Kapphahn R.J., Ethen C.M., Peters E.A., Higgins L., and Ferrington D.A. Modified alpha A crystallin in the retina: altered expression and truncation with aging. Biochemistry 42 (2003) 15310-15325
    • (2003) Biochemistry , vol.42 , pp. 15310-15325
    • Kapphahn, R.J.1    Ethen, C.M.2    Peters, E.A.3    Higgins, L.4    Ferrington, D.A.5
  • 92
    • 1342292267 scopus 로고    scopus 로고
    • Crystal structure of a small heat-shock protein
    • Kim K.K., Kim R., and Kim S.H. Crystal structure of a small heat-shock protein. Nature 394 (1998) 595-599
    • (1998) Nature , vol.394 , pp. 595-599
    • Kim, K.K.1    Kim, R.2    Kim, S.H.3
  • 95
    • 0033607618 scopus 로고    scopus 로고
    • Folding pattern of the alpha-crystallin domain in alphaA-crystallin determined by site-directed spin labeling
    • Koteiche H.A., and McHaourab H.S. Folding pattern of the alpha-crystallin domain in alphaA-crystallin determined by site-directed spin labeling. J. Mol. Biol. 294 (1999) 561-577
    • (1999) J. Mol. Biol. , vol.294 , pp. 561-577
    • Koteiche, H.A.1    McHaourab, H.S.2
  • 96
    • 0038193547 scopus 로고    scopus 로고
    • Mechanism of chaperone function in small heat-shock proteins. Phosphorylation-induced activation of two-mode binding in alphaB-crystallin
    • Koteiche H.A., and McHaourab H.S. Mechanism of chaperone function in small heat-shock proteins. Phosphorylation-induced activation of two-mode binding in alphaB-crystallin. J. Biol. Chem. 278 (2003) 10361-10367
    • (2003) J. Biol. Chem. , vol.278 , pp. 10361-10367
    • Koteiche, H.A.1    McHaourab, H.S.2
  • 97
    • 33744903422 scopus 로고    scopus 로고
    • Mechanism of a Hereditary Cataract Phenotype: MUTATIONS IN {alpha}A-CRYSTALLIN ACTIVATE SUBSTRATE BINDING
    • Koteiche H.A., and McHaourab H.S. Mechanism of a Hereditary Cataract Phenotype: MUTATIONS IN {alpha}A-CRYSTALLIN ACTIVATE SUBSTRATE BINDING. J. Biol. Chem. 281 (2006) 14273-14279
    • (2006) J. Biol. Chem. , vol.281 , pp. 14273-14279
    • Koteiche, H.A.1    McHaourab, H.S.2
  • 98
    • 0028967420 scopus 로고
    • Sequence of the new Drosophila melanogaster small heat-shock-related gene, lethal(2) essential for life [l(2)efl], at locus 59F4,5
    • Kurzik-Dumke U., and Lohmann E. Sequence of the new Drosophila melanogaster small heat-shock-related gene, lethal(2) essential for life [l(2)efl], at locus 59F4,5. Gene 154 (1995) 171-175
    • (1995) Gene , vol.154 , pp. 171-175
    • Kurzik-Dumke, U.1    Lohmann, E.2
  • 100
    • 0032617026 scopus 로고    scopus 로고
    • Regulation of actin dynamics by stress-activated protein kinase 2 (SAPK2)-dependent phosphorylation of heat-shock protein of 27 kDa (Hsp27)
    • Landry J., and Huot J. Regulation of actin dynamics by stress-activated protein kinase 2 (SAPK2)-dependent phosphorylation of heat-shock protein of 27 kDa (Hsp27). Biochem. Soc. Symp. 64 (1999) 79-89
    • (1999) Biochem. Soc. Symp. , vol.64 , pp. 79-89
    • Landry, J.1    Huot, J.2
  • 101
    • 0033765314 scopus 로고    scopus 로고
    • A small heat shock protein cooperates with heat shock protein 70 systems to reactivate a heat-denatured protein
    • Lee G.J., and Vierling E. A small heat shock protein cooperates with heat shock protein 70 systems to reactivate a heat-denatured protein. Plant. Physiol. 122 (2000) 189-198
    • (2000) Plant. Physiol. , vol.122 , pp. 189-198
    • Lee, G.J.1    Vierling, E.2
  • 102
    • 0030802287 scopus 로고    scopus 로고
    • Molecular chaperones and the cytoskeleton
    • Liang P., and MacRae T.H. Molecular chaperones and the cytoskeleton. J. Cell Sci. 110 Pt 13 (1997) 1431-1440
    • (1997) J. Cell Sci. , vol.110 , Issue.PART 13 , pp. 1431-1440
    • Liang, P.1    MacRae, T.H.2
  • 104
    • 0029910357 scopus 로고    scopus 로고
    • Molecular characterization of a novel, developmentally regulated small embryonic chaperone from Caenorhabditis elegans
    • Linder B., Jin Z., Freedman J.H., and Rubin C.S. Molecular characterization of a novel, developmentally regulated small embryonic chaperone from Caenorhabditis elegans. J. Biol. Chem. 271 (1996) 30158-30166
    • (1996) J. Biol. Chem. , vol.271 , pp. 30158-30166
    • Linder, B.1    Jin, Z.2    Freedman, J.H.3    Rubin, C.S.4
  • 106
    • 0031934121 scopus 로고    scopus 로고
    • Autosomal dominant congenital cataract associated with a missense mutation in the human alpha crystallin gene CRYAA
    • Litt M., Kramer P., LaMorticella D.M., Murphey W., Lovrien E.W., and Weleber R.G. Autosomal dominant congenital cataract associated with a missense mutation in the human alpha crystallin gene CRYAA. Hum. Mol. Genet. 7 (1998) 471-474
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 471-474
    • Litt, M.1    Kramer, P.2    LaMorticella, D.M.3    Murphey, W.4    Lovrien, E.W.5    Weleber, R.G.6
  • 107
    • 25444524072 scopus 로고    scopus 로고
    • Interaction and biophysical properties of human lens Q155* betaB2-crystallin mutant
    • Liu B.F., and Liang J.J. Interaction and biophysical properties of human lens Q155* betaB2-crystallin mutant. Mol .Vis. 11 (2005) 321-327
    • (2005) Mol .Vis. , vol.11 , pp. 321-327
    • Liu, B.F.1    Liang, J.J.2
  • 108
    • 33646377432 scopus 로고    scopus 로고
    • Domain interaction sites of human lens betaB2-crystallin
    • Liu B.F., and Liang J.J. Domain interaction sites of human lens betaB2-crystallin. J. Biol. Chem. 281 (2006) 2624-2630
    • (2006) J. Biol. Chem. , vol.281 , pp. 2624-2630
    • Liu, B.F.1    Liang, J.J.2
  • 109
    • 4444281383 scopus 로고    scopus 로고
    • Human alphaA- and alphaB-crystallins prevent UVA-induced apoptosis through regulation of PKCalpha, RAF/MEK/ERK and AKT signaling pathways
    • Liu J.P., Schlosser R., Ma W.Y., Dong Z., Feng H., Lui L., Huang X.Q., Liu Y., and Li D.W. Human alphaA- and alphaB-crystallins prevent UVA-induced apoptosis through regulation of PKCalpha, RAF/MEK/ERK and AKT signaling pathways. Exp. Eye Res. 79 (2004) 393-403
    • (2004) Exp. Eye Res. , vol.79 , pp. 393-403
    • Liu, J.P.1    Schlosser, R.2    Ma, W.Y.3    Dong, Z.4    Feng, H.5    Lui, L.6    Huang, X.Q.7    Liu, Y.8    Li, D.W.9
  • 112
    • 0024218965 scopus 로고
    • The evolution of lenticular proteins: the beta- and gamma-crystallin super gene family
    • Lubsen N.H., Aarts H.J., and Schoenmakers J.G. The evolution of lenticular proteins: the beta- and gamma-crystallin super gene family. Prog. Biophys. Mol. Biol. 51 (1988) 47-76
    • (1988) Prog. Biophys. Mol. Biol. , vol.51 , pp. 47-76
    • Lubsen, N.H.1    Aarts, H.J.2    Schoenmakers, J.G.3
  • 113
    • 0242287938 scopus 로고    scopus 로고
    • Cell death triggered by a novel mutation in the alphaA-crystallin gene underlies autosomal dominant cataract linked to chromosome 21q
    • Mackay D.S., Andley U.P., and Shiels A. Cell death triggered by a novel mutation in the alphaA-crystallin gene underlies autosomal dominant cataract linked to chromosome 21q. Eur. J. Hum. Genet. 11 (2003) 784-793
    • (2003) Eur. J. Hum. Genet. , vol.11 , pp. 784-793
    • Mackay, D.S.1    Andley, U.P.2    Shiels, A.3
  • 114
    • 1842452643 scopus 로고    scopus 로고
    • A missense mutation in the gammaD crystallin gene (CRYGD) associated with autosomal dominant "coral-like" cataract linked to chromosome 2q
    • Mackay D.S., Andley U.P., and Shiels A. A missense mutation in the gammaD crystallin gene (CRYGD) associated with autosomal dominant "coral-like" cataract linked to chromosome 2q. Mol. Vis. 10 (2004) 155-162
    • (2004) Mol. Vis. , vol.10 , pp. 155-162
    • Mackay, D.S.1    Andley, U.P.2    Shiels, A.3
  • 115
    • 0033927557 scopus 로고    scopus 로고
    • Structure and function of small heat shock/alpha-crystallin proteins: established concepts and emerging ideas
    • MacRae T.H. Structure and function of small heat shock/alpha-crystallin proteins: established concepts and emerging ideas. Cell Mol. Life Sci. 57 (2000) 899-913
    • (2000) Cell Mol. Life Sci. , vol.57 , pp. 899-913
    • MacRae, T.H.1
  • 116
    • 18844362688 scopus 로고    scopus 로고
    • alpha-crystallin localizes to the leading edges of migrating lens epithelial cells
    • Maddala R., and Rao V.P. alpha-crystallin localizes to the leading edges of migrating lens epithelial cells. Exp. Cell Res. 306 (2005) 203-215
    • (2005) Exp. Cell Res. , vol.306 , pp. 203-215
    • Maddala, R.1    Rao, V.P.2
  • 117
    • 0032590219 scopus 로고    scopus 로고
    • Low expression of alphaA-crystallins and rhodopsin kinase of photoreceptors in retinal dystrophy rat
    • Maeda A., Ohguro H., Maeda T., Nakagawa T., and Kuroki Y. Low expression of alphaA-crystallins and rhodopsin kinase of photoreceptors in retinal dystrophy rat. Invest. Ophthalmol. Vis. Sci. 40 (1999) 2788-2794
    • (1999) Invest. Ophthalmol. Vis. Sci. , vol.40 , pp. 2788-2794
    • Maeda, A.1    Ohguro, H.2    Maeda, T.3    Nakagawa, T.4    Kuroki, Y.5
  • 118
    • 33644874959 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and apoptosis underlie the pathogenic process in alpha-B-crystallin desmin-related cardiomyopathy
    • Maloyan A., Sanbe A., Osinska H., Westfall M., Robinson D., Imahashi K., Murphy E., and Robbins J. Mitochondrial dysfunction and apoptosis underlie the pathogenic process in alpha-B-crystallin desmin-related cardiomyopathy. Circulation 112 (2005) 3451-3461
    • (2005) Circulation , vol.112 , pp. 3451-3461
    • Maloyan, A.1    Sanbe, A.2    Osinska, H.3    Westfall, M.4    Robinson, D.5    Imahashi, K.6    Murphy, E.7    Robbins, J.8
  • 119
    • 0037174851 scopus 로고    scopus 로고
    • Mechanism of chaperone function in small heat shock proteins. Two-mode binding of the excited states of T4 lysozyme mutants by alphaA-crystallin
    • McHaourab H.S., Dodson E.K., and Koteiche H.A. Mechanism of chaperone function in small heat shock proteins. Two-mode binding of the excited states of T4 lysozyme mutants by alphaA-crystallin. J. Biol. Chem. 277 (2002) 40557-40566
    • (2002) J. Biol. Chem. , vol.277 , pp. 40557-40566
    • McHaourab, H.S.1    Dodson, E.K.2    Koteiche, H.A.3
  • 120
    • 0030014643 scopus 로고    scopus 로고
    • Small stress proteins as novel regulators of apoptosis. Heat shock protein 27 blocks Fas/APO-1- and staurosporine-induced cell death
    • Mehlen P., Schulze-Osthoff K., and Arrigo A.P. Small stress proteins as novel regulators of apoptosis. Heat shock protein 27 blocks Fas/APO-1- and staurosporine-induced cell death. J. Biol. Chem. 271 (1996) 16510-16514
    • (1996) J. Biol. Chem. , vol.271 , pp. 16510-16514
    • Mehlen, P.1    Schulze-Osthoff, K.2    Arrigo, A.P.3
  • 121
    • 0025813543 scopus 로고
    • A 25-kD inhibitor of actin polymerization is a low molecular mass heat shock protein
    • Miron T., Vancompernolle K., Vandekerckhove J., Wilchek M., and Geiger B. A 25-kD inhibitor of actin polymerization is a low molecular mass heat shock protein. J. Cell Biol. 114 (1991) 255-261
    • (1991) J. Cell Biol. , vol.114 , pp. 255-261
    • Miron, T.1    Vancompernolle, K.2    Vandekerckhove, J.3    Wilchek, M.4    Geiger, B.5
  • 122
    • 33645538666 scopus 로고    scopus 로고
    • Caspase-dependent secondary lens fiber cell disintegration in alphaA-/alphaB-crystallin double-knockout mice
    • Morozov V., and Wawrousek E.F. Caspase-dependent secondary lens fiber cell disintegration in alphaA-/alphaB-crystallin double-knockout mice. Development 133 (2006) 813-821
    • (2006) Development , vol.133 , pp. 813-821
    • Morozov, V.1    Wawrousek, E.F.2
  • 123
    • 2342651518 scopus 로고    scopus 로고
    • Molecular chaperones and the stress of oncogenesis
    • Mosser D.D., and Morimoto R.I. Molecular chaperones and the stress of oncogenesis. Oncogene 23 (2004) 2907-2918
    • (2004) Oncogene , vol.23 , pp. 2907-2918
    • Mosser, D.D.1    Morimoto, R.I.2
  • 125
    • 0032477726 scopus 로고    scopus 로고
    • ATP-enhanced molecular chaperone functions of the small heat shock protein human alphaB crystallin
    • Muchowski P.J., and Clark J.I. ATP-enhanced molecular chaperone functions of the small heat shock protein human alphaB crystallin. Proc. Natl. Acad. Sci. USA 95 (1998) 1004-1009
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 1004-1009
    • Muchowski, P.J.1    Clark, J.I.2
  • 126
    • 11144243412 scopus 로고    scopus 로고
    • Modulation of neurodegeneration by molecular chaperones
    • Muchowski P.J., and Wacker J.L. Modulation of neurodegeneration by molecular chaperones. Nat. Rev. Neurosci. 6 (2005) 11-22
    • (2005) Nat. Rev. Neurosci. , vol.6 , pp. 11-22
    • Muchowski, P.J.1    Wacker, J.L.2
  • 127
    • 20444390503 scopus 로고    scopus 로고
    • Crystallin distribution in Bruch's membrane-choroid complex from AMD and age-matched donor eyes
    • Nakata K., Crabb J.W., and Hollyfield J.G. Crystallin distribution in Bruch's membrane-choroid complex from AMD and age-matched donor eyes. Exp. Eye Res. 80 (2005) 821-826
    • (2005) Exp. Eye Res. , vol.80 , pp. 821-826
    • Nakata, K.1    Crabb, J.W.2    Hollyfield, J.G.3
  • 128
    • 0028176579 scopus 로고
    • Chaperone activity of alpha-crystallins modulates intermediate filament assembly
    • Nicholl I.D., and Quinlan R.A. Chaperone activity of alpha-crystallins modulates intermediate filament assembly. Embo J. 13 (1994) 945-953
    • (1994) Embo J. , vol.13 , pp. 945-953
    • Nicholl, I.D.1    Quinlan, R.A.2
  • 129
    • 0034743675 scopus 로고    scopus 로고
    • Structural insight into microtubule function
    • Nogales E. Structural insight into microtubule function. Annu. Rev. Biophys. Biomol. Struct. 30 (2001) 397-420
    • (2001) Annu. Rev. Biophys. Biomol. Struct. , vol.30 , pp. 397-420
    • Nogales, E.1
  • 132
    • 14044262967 scopus 로고    scopus 로고
    • Decrease in protein solubility and cataract formation caused by the Pro23 to Thr mutation in human gamma D-crystallin
    • Pande A., Annunziata O., Asherie N., Ogun O., Benedek G.B., and Pande J. Decrease in protein solubility and cataract formation caused by the Pro23 to Thr mutation in human gamma D-crystallin. Biochemistry 44 (2005) 2491-2500
    • (2005) Biochemistry , vol.44 , pp. 2491-2500
    • Pande, A.1    Annunziata, O.2    Asherie, N.3    Ogun, O.4    Benedek, G.B.5    Pande, J.6
  • 133
    • 0026709362 scopus 로고
    • Activation and repression sequences determine the lens-specific expression of the rat gamma D-crystallin gene
    • Peek R., Kraft H.J., Klok E.J., Lubsen N.H., and Schoenmakers J.G. Activation and repression sequences determine the lens-specific expression of the rat gamma D-crystallin gene. Nucleic. Acids Res. 20 (1992) 4865-4871
    • (1992) Nucleic. Acids Res. , vol.20 , pp. 4865-4871
    • Peek, R.1    Kraft, H.J.2    Klok, E.J.3    Lubsen, N.H.4    Schoenmakers, J.G.5
  • 134
    • 0026638133 scopus 로고
    • Rise and fall of crystallin gene messenger levels during fibroblast growth factor induced terminal differentiation of lens cells
    • Peek R., McAvoy J.W., Lubsen N.H., and Schoenmakers J.G. Rise and fall of crystallin gene messenger levels during fibroblast growth factor induced terminal differentiation of lens cells. Dev. Biol. 152 (1992) 152-160
    • (1992) Dev. Biol. , vol.152 , pp. 152-160
    • Peek, R.1    McAvoy, J.W.2    Lubsen, N.H.3    Schoenmakers, J.G.4
  • 135
    • 0034769611 scopus 로고    scopus 로고
    • Age-related telomere shortening occurs in lens epithelium from old rats and is slowed by caloric restriction
    • Pendergrass W.R., Penn P.E., Li J., and Wolf N.S. Age-related telomere shortening occurs in lens epithelium from old rats and is slowed by caloric restriction. Exp. Eye Res. 73 (2001) 221-228
    • (2001) Exp. Eye Res. , vol.73 , pp. 221-228
    • Pendergrass, W.R.1    Penn, P.E.2    Li, J.3    Wolf, N.S.4
  • 136
    • 0000843475 scopus 로고    scopus 로고
    • The cardiomyopathy and lens cataract mutation in alphaB-crystallin alters its protein structure, chaperone activity, and interaction with intermediate filaments in vitro
    • Perng M.D., Muchowski P.J., van Den I.P., Wu G.J., Hutcheson A.M., Clark J.I., and Quinlan R.A. The cardiomyopathy and lens cataract mutation in alphaB-crystallin alters its protein structure, chaperone activity, and interaction with intermediate filaments in vitro. J. Biol. Chem. 274 (1999) 33235-33243
    • (1999) J. Biol. Chem. , vol.274 , pp. 33235-33243
    • Perng, M.D.1    Muchowski, P.J.2    van Den, I.P.3    Wu, G.J.4    Hutcheson, A.M.5    Clark, J.I.6    Quinlan, R.A.7
  • 137
    • 33746485560 scopus 로고    scopus 로고
    • The Alexander Disease-causing glial fibrillary acidic protein mutant, R416W, accumulates into rosenthal fibers by a pathway that involves filament aggregation and the association of alpha B-crystallin and HSP27
    • Perng M.D., Su M., Wen S.F., Li R., Gibbon T., Prescott A.R., Brenner M., and Quinlan R.A. The Alexander Disease-causing glial fibrillary acidic protein mutant, R416W, accumulates into rosenthal fibers by a pathway that involves filament aggregation and the association of alpha B-crystallin and HSP27. Am. J. Hum. Genet. 79 (2006) 197-213
    • (2006) Am. J. Hum. Genet. , vol.79 , pp. 197-213
    • Perng, M.D.1    Su, M.2    Wen, S.F.3    Li, R.4    Gibbon, T.5    Prescott, A.R.6    Brenner, M.7    Quinlan, R.A.8
  • 138
    • 0031970686 scopus 로고    scopus 로고
    • Multifunctional lens crystallins and corneal enzymes. More than meets the eye
    • Piatigorsky J. Multifunctional lens crystallins and corneal enzymes. More than meets the eye. Ann. N Y Acad. Sci. 842 (1998) 7-15
    • (1998) Ann. N Y Acad. Sci. , vol.842 , pp. 7-15
    • Piatigorsky, J.1
  • 139
    • 0037270166 scopus 로고    scopus 로고
    • Crystallin genes: specialization by changes in gene regulation may precede gene duplication
    • Piatigorsky J. Crystallin genes: specialization by changes in gene regulation may precede gene duplication. J. Struct. Funct. Genom. 3 (2003) 131-137
    • (2003) J. Struct. Funct. Genom. , vol.3 , pp. 131-137
    • Piatigorsky, J.1
  • 140
    • 0030684773 scopus 로고    scopus 로고
    • Autokinase activity of alpha-crystallin inhibits its specific interaction with the DOTIS element in the murine gamma D/E/F-crystallin promoter in vitro
    • Pietrowski D., and Graw J. Autokinase activity of alpha-crystallin inhibits its specific interaction with the DOTIS element in the murine gamma D/E/F-crystallin promoter in vitro. Biol. Chem. 378 (1997) 1183-1186
    • (1997) Biol. Chem. , vol.378 , pp. 1183-1186
    • Pietrowski, D.1    Graw, J.2
  • 141
    • 0028168805 scopus 로고
    • Alpha-crystallins are involved in specific interactions with the murine gamma D/E/F-crystallin-encoding gene
    • Pietrowski D., Durante M.J., Liebstein A., Schmitt-John T., Werner T., and Graw J. Alpha-crystallins are involved in specific interactions with the murine gamma D/E/F-crystallin-encoding gene. Gene 144 (1994) 171-178
    • (1994) Gene , vol.144 , pp. 171-178
    • Pietrowski, D.1    Durante, M.J.2    Liebstein, A.3    Schmitt-John, T.4    Werner, T.5    Graw, J.6
  • 142
    • 0035159695 scopus 로고    scopus 로고
    • Cytoskeletal catastrophe causes brain degeneration
    • Quinlan R. Cytoskeletal catastrophe causes brain degeneration. Nat. Genet. 27 (2001) 10-11
    • (2001) Nat. Genet. , vol.27 , pp. 10-11
    • Quinlan, R.1
  • 143
    • 0036366525 scopus 로고    scopus 로고
    • Cytoskeletal competence requires protein chaperones
    • Quinlan R. Cytoskeletal competence requires protein chaperones. Prog. Mol. Subcell Biol. 28 (2002) 219-233
    • (2002) Prog. Mol. Subcell Biol. , vol.28 , pp. 219-233
    • Quinlan, R.1
  • 144
    • 0027973129 scopus 로고
    • Chaperone-like activity and quaternary structure of alpha-crystallin
    • Raman B., and Rao C.M. Chaperone-like activity and quaternary structure of alpha-crystallin. J. Biol. Chem. 269 (1994) 27264-27268
    • (1994) J. Biol. Chem. , vol.269 , pp. 27264-27268
    • Raman, B.1    Rao, C.M.2
  • 146
    • 0033967140 scopus 로고    scopus 로고
    • Regulation of mouse lens fiber cell development and differentiation by the Maf gene
    • Ring B.Z., Cordes S.P., Overbeek P.A., and Barsh G.S. Regulation of mouse lens fiber cell development and differentiation by the Maf gene. Development 127 (2000) 307-317
    • (2000) Development , vol.127 , pp. 307-317
    • Ring, B.Z.1    Cordes, S.P.2    Overbeek, P.A.3    Barsh, G.S.4
  • 147
    • 0029817433 scopus 로고    scopus 로고
    • Differential expression of alpha A- and alpha B-crystallin during murine ocular development
    • Robinson M.L., and Overbeek P.A. Differential expression of alpha A- and alpha B-crystallin during murine ocular development. Invest. Ophthalmol. Vis. Sci. 37 (1996) 2276-2284
    • (1996) Invest. Ophthalmol. Vis. Sci. , vol.37 , pp. 2276-2284
    • Robinson, M.L.1    Overbeek, P.A.2
  • 148
    • 33745303518 scopus 로고    scopus 로고
    • Quantitative measurement of young human eye lens crystallins by direct injection Fourier transform ion cyclotron resonance mass spectrometry
    • Robinson N.E., Lampi K.J., Speir J.P., Kruppa G., Easterling M., and Robinson A.B. Quantitative measurement of young human eye lens crystallins by direct injection Fourier transform ion cyclotron resonance mass spectrometry. Mol. Vis. 12 (2006) 704-711
    • (2006) Mol. Vis. , vol.12 , pp. 704-711
    • Robinson, N.E.1    Lampi, K.J.2    Speir, J.P.3    Kruppa, G.4    Easterling, M.5    Robinson, A.B.6
  • 149
    • 0037194897 scopus 로고    scopus 로고
    • Polyglutamine pathogenesis: emergence of unifying mechanisms for Huntington's disease and related disorders
    • Ross C.A. Polyglutamine pathogenesis: emergence of unifying mechanisms for Huntington's disease and related disorders. Neuron 35 (2002) 819-822
    • (2002) Neuron , vol.35 , pp. 819-822
    • Ross, C.A.1
  • 151
    • 21744433513 scopus 로고    scopus 로고
    • The decrease of the cytoskeleton tubulin follows the decrease of the associating molecular chaperone alphaB-crystallin in unloaded soleus muscle atrophy without stretch
    • Sakurai T., Fujita Y., Ohto E., Oguro A., and Atomi Y. The decrease of the cytoskeleton tubulin follows the decrease of the associating molecular chaperone alphaB-crystallin in unloaded soleus muscle atrophy without stretch. Faseb J. 19 (2005) 1199-1201
    • (2005) Faseb J. , vol.19 , pp. 1199-1201
    • Sakurai, T.1    Fujita, Y.2    Ohto, E.3    Oguro, A.4    Atomi, Y.5
  • 153
    • 0028254544 scopus 로고
    • Expression of the alpha-crystallin/small heat-shock protein/molecular chaperone genes in the lens and other tissues
    • Sax C.M., and Piatigorsky J. Expression of the alpha-crystallin/small heat-shock protein/molecular chaperone genes in the lens and other tissues. Adv. Enzymol. Relat. Areas. Mol. Biol. 69 (1994) 155-201
    • (1994) Adv. Enzymol. Relat. Areas. Mol. Biol. , vol.69 , pp. 155-201
    • Sax, C.M.1    Piatigorsky, J.2
  • 154
    • 0032502739 scopus 로고    scopus 로고
    • Interaction of 1,1'-bi(4-anilino)naphthalene-5,5'-disulfonic acid with alpha-crystallin
    • Sharma K.K., Kaur H., Kumar G.S., and Kester K. Interaction of 1,1'-bi(4-anilino)naphthalene-5,5'-disulfonic acid with alpha-crystallin. J. Biol. Chem. 273 (1998) 8965-8970
    • (1998) J. Biol. Chem. , vol.273 , pp. 8965-8970
    • Sharma, K.K.1    Kaur, H.2    Kumar, G.S.3    Kester, K.4
  • 155
    • 0034635397 scopus 로고    scopus 로고
    • Synthesis and characterization of a peptide identified as a functional element in alphaA-crystallin
    • Sharma K.K., Kumar R.S., Kumar G.S., and Quinn P.T. Synthesis and characterization of a peptide identified as a functional element in alphaA-crystallin. J. Biol. Chem. 275 (2000) 3767-3771
    • (2000) J. Biol. Chem. , vol.275 , pp. 3767-3771
    • Sharma, K.K.1    Kumar, R.S.2    Kumar, G.S.3    Quinn, P.T.4
  • 156
    • 0035139109 scopus 로고    scopus 로고
    • Cellular defenses against unfolded proteins: a cell biologist thinks about neurodegenerative diseases
    • Sherman M.Y., and Goldberg A.L. Cellular defenses against unfolded proteins: a cell biologist thinks about neurodegenerative diseases. Neuron 29 (2001) 15-32
    • (2001) Neuron , vol.29 , pp. 15-32
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 157
    • 0034673151 scopus 로고    scopus 로고
    • Mutation of R116C results in highly oligomerized alpha A-crystallin with modified structure and defective chaperone-like function
    • Shroff N.P., Cherian-Shaw M., Bera S., and Abraham E.C. Mutation of R116C results in highly oligomerized alpha A-crystallin with modified structure and defective chaperone-like function. Biochemistry 39 (2000) 1420-1426
    • (2000) Biochemistry , vol.39 , pp. 1420-1426
    • Shroff, N.P.1    Cherian-Shaw, M.2    Bera, S.3    Abraham, E.C.4
  • 158
    • 20044394594 scopus 로고    scopus 로고
    • Up-regulation of osteopontin and alphaBeta-crystallin in the normal-appearing white matter of multiple sclerosis: an immunohistochemical study utilizing tissue microarrays
    • Sinclair C., Mirakhur M., Kirk J., Farrell M., and McQuaid S. Up-regulation of osteopontin and alphaBeta-crystallin in the normal-appearing white matter of multiple sclerosis: an immunohistochemical study utilizing tissue microarrays. Neuropathol. Appl. Neurobiol. 31 (2005) 292-303
    • (2005) Neuropathol. Appl. Neurobiol. , vol.31 , pp. 292-303
    • Sinclair, C.1    Mirakhur, M.2    Kirk, J.3    Farrell, M.4    McQuaid, S.5
  • 159
    • 0032580087 scopus 로고    scopus 로고
    • Cloning and mapping the mouse Crygs gene and non-lens expression of [gamma]S-crystallin
    • Sinha D., Esumi N., Jaworski C., Kozak C.A., Pierce E., and Wistow G. Cloning and mapping the mouse Crygs gene and non-lens expression of [gamma]S-crystallin. Mol. Vis. 4 (1998) 8
    • (1998) Mol. Vis. , vol.4 , pp. 8
    • Sinha, D.1    Esumi, N.2    Jaworski, C.3    Kozak, C.A.4    Pierce, E.5    Wistow, G.6
  • 160
    • 0032789443 scopus 로고    scopus 로고
    • Structure of the crystallins
    • Slingsby C., and Clout N.J. Structure of the crystallins. Eye 13 Pt 3b (1999) 395-402
    • (1999) Eye , vol.13 , Issue.PART 3b , pp. 395-402
    • Slingsby, C.1    Clout, N.J.2
  • 161
    • 0034595859 scopus 로고    scopus 로고
    • Canonical heat shock element in the alpha B-crystallin gene shows tissue-specific and developmentally controlled interactions with heat shock factor
    • Somasundaram T., and Bhat S.P. Canonical heat shock element in the alpha B-crystallin gene shows tissue-specific and developmentally controlled interactions with heat shock factor. J. Biol. Chem. 275 (2000) 17154-17159
    • (2000) J. Biol. Chem. , vol.275 , pp. 17154-17159
    • Somasundaram, T.1    Bhat, S.P.2
  • 162
    • 33646891273 scopus 로고    scopus 로고
    • The interaction between alphaA- and alphaB-crystallin is sequence-specific
    • Sreelakshmi Y., and Sharma K.K. The interaction between alphaA- and alphaB-crystallin is sequence-specific. Mol. Vis. 12 (2006) 581-587
    • (2006) Mol. Vis. , vol.12 , pp. 581-587
    • Sreelakshmi, Y.1    Sharma, K.K.2
  • 163
    • 25144461582 scopus 로고    scopus 로고
    • Wrapping the alpha-crystallin domain fold in a chaperone assembly
    • Stamler R., Kappe G., Boelens W., and Slingsby C. Wrapping the alpha-crystallin domain fold in a chaperone assembly. J. Mol. Biol. 353 (2005) 68-79
    • (2005) J. Mol. Biol. , vol.353 , pp. 68-79
    • Stamler, R.1    Kappe, G.2    Boelens, W.3    Slingsby, C.4
  • 164
    • 0026457201 scopus 로고
    • Identification of MAPKAP kinase 2 as a major enzyme responsible for the phosphorylation of the small mammalian heat shock proteins
    • Stokoe D., Engel K., Campbell D.G., Cohen P., and Gaestel M. Identification of MAPKAP kinase 2 as a major enzyme responsible for the phosphorylation of the small mammalian heat shock proteins. FEBS Lett. 313 (1992) 307-313
    • (1992) FEBS Lett. , vol.313 , pp. 307-313
    • Stokoe, D.1    Engel, K.2    Campbell, D.G.3    Cohen, P.4    Gaestel, M.5
  • 165
    • 0033984092 scopus 로고    scopus 로고
    • Muscle develops a specific form of small heat shock protein complex composed of MKBP/HSPB2 and HSPB3 during myogenic differentiation
    • Sugiyama Y., Suzuki A., Kishikawa M., Akutsu R., Hirose T., Waye M.M., Tsui S.K., Yoshida S., and Ohno S. Muscle develops a specific form of small heat shock protein complex composed of MKBP/HSPB2 and HSPB3 during myogenic differentiation. J. Biol. Chem. 275 (2000) 1095-1104
    • (2000) J. Biol. Chem. , vol.275 , pp. 1095-1104
    • Sugiyama, Y.1    Suzuki, A.2    Kishikawa, M.3    Akutsu, R.4    Hirose, T.5    Waye, M.M.6    Tsui, S.K.7    Yoshida, S.8    Ohno, S.9
  • 166
    • 0030933472 scopus 로고    scopus 로고
    • Conformational and functional differences between recombinant human lens alphaA- and alphaB-crystallin
    • Sun T.X., Das B.K., and Liang J.J. Conformational and functional differences between recombinant human lens alphaA- and alphaB-crystallin. J. Biol. Chem. 272 (1997) 6220-6225
    • (1997) J. Biol. Chem. , vol.272 , pp. 6220-6225
    • Sun, T.X.1    Das, B.K.2    Liang, J.J.3
  • 167
    • 0032479355 scopus 로고    scopus 로고
    • Subunit exchange of lens alpha-crystallin: a fluorescence energy transfer study with the fluorescent labeled alphaA-crystallin mutant W9F as a probe
    • Sun T.X., Akhtar N.J., and Liang J.J. Subunit exchange of lens alpha-crystallin: a fluorescence energy transfer study with the fluorescent labeled alphaA-crystallin mutant W9F as a probe. FEBS Lett. 430 (1998) 401-404
    • (1998) FEBS Lett. , vol.430 , pp. 401-404
    • Sun, T.X.1    Akhtar, N.J.2    Liang, J.J.3
  • 168
    • 0032498791 scopus 로고    scopus 로고
    • MKBP, a novel member of the small heat shock protein family, binds and activates the myotonic dystrophy protein kinase
    • Suzuki A., Sugiyama Y., Hayashi Y., Nyu-i N., Yoshida M., Nonaka I., Ishiura S., Arahata K., and Ohno S. MKBP, a novel member of the small heat shock protein family, binds and activates the myotonic dystrophy protein kinase. J. Cell Biol. 140 (1998) 1113-1124
    • (1998) J. Cell Biol. , vol.140 , pp. 1113-1124
    • Suzuki, A.1    Sugiyama, Y.2    Hayashi, Y.3    Nyu-i, N.4    Yoshida, M.5    Nonaka, I.6    Ishiura, S.7    Arahata, K.8    Ohno, S.9
  • 169
    • 26444583909 scopus 로고    scopus 로고
    • Molecular composition of drusen and possible involvement of anti-retinal autoimmunity in two different forms of macular degeneration in cynomolgus monkey (Macaca fascicularis)
    • Umeda S., Suzuki M.T., Okamoto H., Ono F., Mizota A., Terao K., Yoshikawa Y., Tanaka Y., and Iwata T. Molecular composition of drusen and possible involvement of anti-retinal autoimmunity in two different forms of macular degeneration in cynomolgus monkey (Macaca fascicularis). Faseb J. 19 (2005) 1683-1685
    • (2005) Faseb J. , vol.19 , pp. 1683-1685
    • Umeda, S.1    Suzuki, M.T.2    Okamoto, H.3    Ono, F.4    Mizota, A.5    Terao, K.6    Yoshikawa, Y.7    Tanaka, Y.8    Iwata, T.9
  • 170
    • 0034058749 scopus 로고    scopus 로고
    • Depression of nuclear transcription and extension of mRNA half-life under anoxia in Artemia franciscana embryos
    • van Breukelen F., Maier R., and Hand S.C. Depression of nuclear transcription and extension of mRNA half-life under anoxia in Artemia franciscana embryos. J. Exp. Biol. 203 (2000) 1123-1130
    • (2000) J. Exp. Biol. , vol.203 , pp. 1123-1130
    • van Breukelen, F.1    Maier, R.2    Hand, S.C.3
  • 171
    • 0043205911 scopus 로고    scopus 로고
    • Nuclear speckle localisation of the small heat shock protein alpha B-crystallin and its inhibition by the R120G cardiomyopathy-linked mutation
    • van den Ijssel.P., Wheelock R., Prescott A., Russell P., and Quinlan R.A. Nuclear speckle localisation of the small heat shock protein alpha B-crystallin and its inhibition by the R120G cardiomyopathy-linked mutation. Exp. Cell Res. 287 (2003) 249-261
    • (2003) Exp. Cell Res. , vol.287 , pp. 249-261
    • van den, Ijssel.P.1    Wheelock, R.2    Prescott, A.3    Russell, P.4    Quinlan, R.A.5
  • 172
    • 0035718677 scopus 로고    scopus 로고
    • Structure and function of the small heat shock protein/alpha-crystallin family of molecular chaperones
    • Van Montfort R., Slingsby C., and Vierling E. Structure and function of the small heat shock protein/alpha-crystallin family of molecular chaperones. Adv. Protein Chem. 59 (2001) 105-156
    • (2001) Adv. Protein Chem. , vol.59 , pp. 105-156
    • Van Montfort, R.1    Slingsby, C.2    Vierling, E.3
  • 174
    • 0034987735 scopus 로고    scopus 로고
    • A unique form of autosomal dominant cataract explained by gene conversion between beta-crystallin B2 and its pseudogene
    • Vanita, Sarhadi V., Reis A., Jung M., Singh D., Sperling K., Singh J.R., and Burger J. A unique form of autosomal dominant cataract explained by gene conversion between beta-crystallin B2 and its pseudogene. J. Med. Genet. 38 (2001) 392-396
    • (2001) J. Med. Genet. , vol.38 , pp. 392-396
    • Vanita1    Sarhadi, V.2    Reis, A.3    Jung, M.4    Singh, D.5    Sperling, K.6    Singh, J.R.7    Burger, J.8
  • 177
    • 4644279714 scopus 로고    scopus 로고
    • Expression and regulation of alpha-, beta-, and gamma-crystallins in mammalian lens epithelial cells
    • Wang X., Garcia C.M., Shui Y.B., and Beebe D.C. Expression and regulation of alpha-, beta-, and gamma-crystallins in mammalian lens epithelial cells. Invest. Ophthalmol. Vis. Sci. 45 (2004) 3608-3619
    • (2004) Invest. Ophthalmol. Vis. Sci. , vol.45 , pp. 3608-3619
    • Wang, X.1    Garcia, C.M.2    Shui, Y.B.3    Beebe, D.C.4
  • 179
    • 33646857038 scopus 로고    scopus 로고
    • Small heat shock proteins inhibit amyloid-beta protein aggregation and cerebrovascular amyloid-beta protein toxicity
    • Wilhelmus M.M., Boelens W.C., Otte-Holler I., Kamps B., de Waal R.M., and Verbeek M.M. Small heat shock proteins inhibit amyloid-beta protein aggregation and cerebrovascular amyloid-beta protein toxicity. Brain Res. 1089 (2006) 67-78
    • (2006) Brain Res. , vol.1089 , pp. 67-78
    • Wilhelmus, M.M.1    Boelens, W.C.2    Otte-Holler, I.3    Kamps, B.4    de Waal, R.M.5    Verbeek, M.M.6
  • 181
    • 0027225772 scopus 로고
    • Lens crystallins: gene recruitment and evolutionary dynamism
    • Wistow G. Lens crystallins: gene recruitment and evolutionary dynamism. Trends Biochem. Sci. 18 (1993) 301-306
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 301-306
    • Wistow, G.1
  • 182
    • 0025890262 scopus 로고
    • Lens protein expression in mammals: taxon-specificity and the recruitment of crystallins
    • Wistow G., and Kim H. Lens protein expression in mammals: taxon-specificity and the recruitment of crystallins. J. Mol. Evol. 32 (1991) 262-269
    • (1991) J. Mol. Evol. , vol.32 , pp. 262-269
    • Wistow, G.1    Kim, H.2
  • 183
    • 0036469257 scopus 로고    scopus 로고
    • Downregulation of a unique photoreceptor protein correlates with improper outer segment assembly
    • Wohabrebbi A., Umstot E.S., Iannaccone A., Desiderio D.M., and Jablonski M.M. Downregulation of a unique photoreceptor protein correlates with improper outer segment assembly. J. Neurosci. Res. 67 (2002) 298-308
    • (2002) J. Neurosci. Res. , vol.67 , pp. 298-308
    • Wohabrebbi, A.1    Umstot, E.S.2    Iannaccone, A.3    Desiderio, D.M.4    Jablonski, M.M.5
  • 184
    • 0142056039 scopus 로고    scopus 로고
    • A comprehensive analysis of the expression of crystallins in mouse retina
    • Xi J., Farjo R., Yoshida S., Kern T.S., Swaroop A., and Andley U.P. A comprehensive analysis of the expression of crystallins in mouse retina. Mol. Vis. 9 (2003) 410-419
    • (2003) Mol. Vis. , vol.9 , pp. 410-419
    • Xi, J.1    Farjo, R.2    Yoshida, S.3    Kern, T.S.4    Swaroop, A.5    Andley, U.P.6
  • 185
    • 0037444674 scopus 로고    scopus 로고
    • Reduced survival of lens epithelial cells in the alphaA-crystallin-knockout mouse
    • Xi J.H., Bai F., and Andley U.P. Reduced survival of lens epithelial cells in the alphaA-crystallin-knockout mouse. J. Cell Sci. 116 (2003) 1073-1085
    • (2003) J. Cell Sci. , vol.116 , pp. 1073-1085
    • Xi, J.H.1    Bai, F.2    Andley, U.P.3
  • 186
    • 33744475377 scopus 로고    scopus 로고
    • Alpha-crystallin expression affects microtubule assembly and prevents their aggregation
    • Xi J.H., Bai F., McGaha R., and Andley U.P. Alpha-crystallin expression affects microtubule assembly and prevents their aggregation. Faseb J. 20 (2006) 846-857
    • (2006) Faseb J. , vol.20 , pp. 846-857
    • Xi, J.H.1    Bai, F.2    McGaha, R.3    Andley, U.P.4
  • 187
    • 33746367158 scopus 로고    scopus 로고
    • A novel function of DNA repair molecule Nbs1 in terminal differentiation of the lens fibre cells and cataractogenesis
    • Yang Y.G., Frappart P.O., Frappart L., Wang Z.Q., and Tong W.M. A novel function of DNA repair molecule Nbs1 in terminal differentiation of the lens fibre cells and cataractogenesis. DNA Repair (Amst) 5 (2006) 885-893
    • (2006) DNA Repair (Amst) , vol.5 , pp. 885-893
    • Yang, Y.G.1    Frappart, P.O.2    Frappart, L.3    Wang, Z.Q.4    Tong, W.M.5
  • 188
    • 0242416955 scopus 로고    scopus 로고
    • Differential temporal and spatial expression of immediate early genes in retinal neurons after ischemia-reperfusion injury
    • Yoshimura N., Kikuchi T., Kuroiwa S., and Gaun S. Differential temporal and spatial expression of immediate early genes in retinal neurons after ischemia-reperfusion injury. Invest. Ophthalmol. Vis. Sci. 44 (2003) 2211-2220
    • (2003) Invest. Ophthalmol. Vis. Sci. , vol.44 , pp. 2211-2220
    • Yoshimura, N.1    Kikuchi, T.2    Kuroiwa, S.3    Gaun, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.