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Volumn 31, Issue 6, 2012, Pages 576-604

Novel roles for α-crystallins in retinal function and disease

Author keywords

B Crystallin; Angiogenesis; Apoptosis; Chaperone; Exosomes; Retinal pigment epithelium

Indexed keywords

ALPHA CRYSTALLIN; AMYLOID BETA PROTEIN; ANGIOGENIC FACTOR; CHAPERONE; GROWTH FACTOR; HEAT SHOCK PROTEIN; UBIQUITIN; VASCULOTROPIN;

EID: 84867401896     PISSN: 13509462     EISSN: 18731635     Source Type: Journal    
DOI: 10.1016/j.preteyeres.2012.06.001     Document Type: Review
Times cited : (114)

References (328)
  • 1
    • 84864492897 scopus 로고    scopus 로고
    • Small heat shock proteins HSP27 (HspB1), αB-crystallin (HspB5) and HSP22 (HspB8) as regulators of cell death
    • Apr 13. (Epub ahead of print)
    • Acunzo J., Katsogiannou M., Rocchi P. Small heat shock proteins HSP27 (HspB1), αB-crystallin (HspB5) and HSP22 (HspB8) as regulators of cell death. Int. J. Biochem. Cell Biol 2012, Apr 13. (Epub ahead of print).
    • (2012) Int. J. Biochem. Cell Biol
    • Acunzo, J.1    Katsogiannou, M.2    Rocchi, P.3
  • 2
    • 4444246913 scopus 로고    scopus 로고
    • Heat stress-induced localization of small heat shock proteins in mouse myoblasts: intranuclear lamin A/C speckles as target for alphaB-crystallin and Hsp25
    • Adhikari A.S., SridharRao K., Rangaraj N., Parnaik V.K., Rao Ch.M. Heat stress-induced localization of small heat shock proteins in mouse myoblasts: intranuclear lamin A/C speckles as target for alphaB-crystallin and Hsp25. Exp. Cell. Res. 2004, 299:393-403.
    • (2004) Exp. Cell. Res. , vol.299 , pp. 393-403
    • Adhikari, A.S.1    SridharRao, K.2    Rangaraj, N.3    Parnaik, V.K.4    Rao, C.5
  • 3
    • 79959362400 scopus 로고    scopus 로고
    • αB-crystallin, a small heat shock protein, modulates NF-κB activity in a phosphorylation-dependent manner and protects muscle myoblasts from TNF-α induced cytotoxicity
    • Adhikari A.S., Singh B.N., Rao K.S., Rao Ch.M. αB-crystallin, a small heat shock protein, modulates NF-κB activity in a phosphorylation-dependent manner and protects muscle myoblasts from TNF-α induced cytotoxicity. Biochim. Biophys. Acta 2011, 1813:1532-1542.
    • (2011) Biochim. Biophys. Acta , vol.1813 , pp. 1532-1542
    • Adhikari, A.S.1    Singh, B.N.2    Rao, K.S.3    Rao, C.4
  • 4
    • 43049183420 scopus 로고    scopus 로고
    • Oxidative stress and calpain inhibition induce alpha B-crystallin phosphorylation via p38-MAPK and calcium signalling pathways in H9c2 cells
    • Aggeli I.K., Beis I., Gaitanaki C. Oxidative stress and calpain inhibition induce alpha B-crystallin phosphorylation via p38-MAPK and calcium signalling pathways in H9c2 cells. Cell Signal. 2008, 20:1292-1302.
    • (2008) Cell Signal. , vol.20 , pp. 1292-1302
    • Aggeli, I.K.1    Beis, I.2    Gaitanaki, C.3
  • 5
    • 37349032463 scopus 로고    scopus 로고
    • Effect of phosphorylation on alpha B-crystallin: differences in stability, subunit exchange and chaperone activity of homo and mixed oligomers of alpha B-crystallin and its phosphorylation-mimicking mutant
    • Ahmad M.F., Raman B., Ramakrishna T., Rao Ch.M. Effect of phosphorylation on alpha B-crystallin: differences in stability, subunit exchange and chaperone activity of homo and mixed oligomers of alpha B-crystallin and its phosphorylation-mimicking mutant. J. Mol. Biol. 2008, 375:1040-1051.
    • (2008) J. Mol. Biol. , vol.375 , pp. 1040-1051
    • Ahmad, M.F.1    Raman, B.2    Ramakrishna, T.3    Rao, C.4
  • 6
    • 0345760069 scopus 로고    scopus 로고
    • Characterization of beta amyloid assemblies in drusen: the deposits associated with aging and age-related macular degeneration
    • Anderson D.H., Talaga K.C., Rivest A.J., Barron E., Hageman G.S., Johnson L.V. Characterization of beta amyloid assemblies in drusen: the deposits associated with aging and age-related macular degeneration. Exp. Eye Res. 2004, 78:243-256.
    • (2004) Exp. Eye Res. , vol.78 , pp. 243-256
    • Anderson, D.H.1    Talaga, K.C.2    Rivest, A.J.3    Barron, E.4    Hageman, G.S.5    Johnson, L.V.6
  • 7
    • 0032553123 scopus 로고    scopus 로고
    • The molecular chaperone αA-crystallin enhances lens epithelial cell growth and resistance to UVA stress
    • Andley U.P., Song Z., Wawrousek E.F., Bassnett S. The molecular chaperone αA-crystallin enhances lens epithelial cell growth and resistance to UVA stress. J. Biol. Chem. 1998, 273:31252-31261.
    • (1998) J. Biol. Chem. , vol.273 , pp. 31252-31261
    • Andley, U.P.1    Song, Z.2    Wawrousek, E.F.3    Bassnett, S.4
  • 8
    • 0034711260 scopus 로고    scopus 로고
    • Differential protective activity of αA- and αB-crystallin in lens epithelial cells
    • Andley U.P., Song Z., Wawrousek E.F., Fleming T.P., Bassnett S. Differential protective activity of αA- and αB-crystallin in lens epithelial cells. J. Biol. Chem. 2000, 275:36823-36831.
    • (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
  • 9
    • 33845425645 scopus 로고    scopus 로고
    • Crystallins in the eye: function and pathology
    • Andley U.P. Crystallins in the eye: function and pathology. Prog. Retin. Eye Res. 2007, 26:78-98.
    • (2007) Prog. Retin. Eye Res. , vol.26 , pp. 78-98
    • Andley, U.P.1
  • 10
    • 3142543752 scopus 로고    scopus 로고
    • Phosphorylation of alphaB-crystallin alters chaperone function through loss of dimeric substructure
    • Aquilina J.A., Benesch J.L., Ding L.L., Yaron O., Horwitz J., Robinson C.V. Phosphorylation of alphaB-crystallin alters chaperone function through loss of dimeric substructure. J. Biol. Chem. 2004, 279:28675-28680.
    • (2004) J. Biol. Chem. , vol.279 , pp. 28675-28680
    • Aquilina, J.A.1    Benesch, J.L.2    Ding, L.L.3    Yaron, O.4    Horwitz, J.5    Robinson, C.V.6
  • 14
    • 77951686244 scopus 로고    scopus 로고
    • Extracellular matrix, inflammation, and the angiogenic response
    • Arroyo A.G., Iruela-Arispe M.L. Extracellular matrix, inflammation, and the angiogenic response. Cardiovasc. Res. 2010, 86:226-235.
    • (2010) Cardiovasc. Res. , vol.86 , pp. 226-235
    • Arroyo, A.G.1    Iruela-Arispe, M.L.2
  • 15
    • 80053019029 scopus 로고    scopus 로고
    • Structural and functional properties of NH2-terminal domain, core domain, and COOH-terminal extensions of αA- and αB-crystallins
    • Asomugha C.O., Gupta R., Srivastava O.P. Structural and functional properties of NH2-terminal domain, core domain, and COOH-terminal extensions of αA- and αB-crystallins. Mol. Vis. 2011, 17:2356-2367.
    • (2011) Mol. Vis. , vol.17 , pp. 2356-2367
    • Asomugha, C.O.1    Gupta, R.2    Srivastava, O.P.3
  • 16
    • 39349083915 scopus 로고    scopus 로고
    • Adapting proteostasis for disease intervention
    • Balch W.E., Morimoto R.I., Dillin A., Kelly J.W. Adapting proteostasis for disease intervention. Science 2008, 319:916-919.
    • (2008) Science , vol.319 , pp. 916-919
    • Balch, W.E.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4
  • 17
    • 66149126023 scopus 로고    scopus 로고
    • Interactions between small heat shock protein alpha-crystallin and galectin-related interfiber protein (GRIFIN) in the ocular lens
    • Barton K.A., Hsu C.D., Petrash J.M. Interactions between small heat shock protein alpha-crystallin and galectin-related interfiber protein (GRIFIN) in the ocular lens. Biochemistry 2009, 48:3956-3966.
    • (2009) Biochemistry , vol.48 , pp. 3956-3966
    • Barton, K.A.1    Hsu, C.D.2    Petrash, J.M.3
  • 18
    • 33748475316 scopus 로고    scopus 로고
    • The dynamic instability of microtubules is required for aggresome formation in oligodendroglial cells after proteolytic stress
    • Bauer N.G., Richter-Landsberg C. The dynamic instability of microtubules is required for aggresome formation in oligodendroglial cells after proteolytic stress. J. Mol. Neurosci. 2006, 29:153-168.
    • (2006) J. Mol. Neurosci. , vol.29 , pp. 153-168
    • Bauer, N.G.1    Richter-Landsberg, C.2
  • 19
    • 0026694490 scopus 로고
    • Alpha B-crystallin in cardiac tissue. Association with actin and desmin filaments
    • Bennardini F., Wrzosek A., Chiesi M. Alpha B-crystallin in cardiac tissue. Association with actin and desmin filaments. Circ. Res. 1992, 71:288-294.
    • (1992) Circ. Res. , vol.71 , pp. 288-294
    • Bennardini, F.1    Wrzosek, A.2    Chiesi, M.3
  • 20
    • 0033525723 scopus 로고    scopus 로고
    • Site-directed spin labeling study of subunit interactions in the alpha-crystallin domain of small heat-shock proteins. Comparison of the oligomer symmetry in alphaA-crystallin, HSP 27, and HSP 16.3
    • Berengian A.R., Parfenova M., Mchaourab H.S. Site-directed spin labeling study of subunit interactions in the alpha-crystallin domain of small heat-shock proteins. Comparison of the oligomer symmetry in alphaA-crystallin, HSP 27, and HSP 16.3. J. Biol. Chem. 1999, 274:6305-6314.
    • (1999) J. Biol. Chem. , vol.274 , pp. 6305-6314
    • Berengian, A.R.1    Parfenova, M.2    Mchaourab, H.S.3
  • 21
    • 0024578954 scopus 로고
    • Alpha B subunit of lens-specific protein alpha-crystallin is present in other ocular and non-ocular tissues
    • Bhat S.P., 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. 1989, 158:319-325.
    • (1989) Biochem. Biophys. Res. Commun. , vol.158 , pp. 319-325
    • Bhat, S.P.1    Nagineni, C.N.2
  • 22
    • 33644690454 scopus 로고    scopus 로고
    • Mini-αB-crystallin: a functional element of αB-crystallin with chaperone-like activity
    • Bhattacharyya J., Padmanabha Udupa E.G., Wang J., Sharma K.K. Mini-αB-crystallin: a functional element of αB-crystallin with chaperone-like activity. Biochemistry 2006, 45:3069-3076.
    • (2006) Biochemistry , vol.45 , pp. 3069-3076
    • Bhattacharyya, J.1    Padmanabha Udupa, E.G.2    Wang, J.3    Sharma, K.K.4
  • 23
    • 5644275139 scopus 로고    scopus 로고
    • Role of ATP on the interaction of alpha-crystallin with its substrates and its implications for the molecular chaperone function
    • Biswas A., Das K.P. Role of ATP on the interaction of alpha-crystallin with its substrates and its implications for the molecular chaperone function. J. Biol. Chem. 2004, 279:42648-42657.
    • (2004) J. Biol. Chem. , vol.279 , pp. 42648-42657
    • Biswas, A.1    Das, K.P.2
  • 24
    • 38849139632 scopus 로고    scopus 로고
    • Zn2+ enhances the molecular chaperone function and stability of alpha-crystallin
    • Biswas A., Das K.P. Zn2+ enhances the molecular chaperone function and stability of alpha-crystallin. Biochemistry 2008, 47:804-816.
    • (2008) Biochemistry , vol.47 , pp. 804-816
    • Biswas, A.1    Das, K.P.2
  • 25
    • 42449091462 scopus 로고    scopus 로고
    • Small heat shock proteins Hsp27 or alphaB-crystallin and the protein components of neurofibrillary tangles: tau and neurofilaments
    • Björkdahl C., Sjögren M.J., Zhou X., Concha H., Avila J., Winblad B., Pei J.J. Small heat shock proteins Hsp27 or alphaB-crystallin and the protein components of neurofibrillary tangles: tau and neurofilaments. J. Neurosci. Res. 2008, 86:1343-1352.
    • (2008) J. Neurosci. Res. , vol.86 , pp. 1343-1352
    • Björkdahl, C.1    Sjögren, M.J.2    Zhou, X.3    Concha, H.4    Avila, J.5    Winblad, B.6    Pei, J.J.7
  • 26
    • 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., Dillmann W.H. Specific heat shock proteins protect microtubules during simulated ischemia in cardiac myocytes. Am. J. Physiol. 1998, 275:H2243-H2249.
    • (1998) Am. J. Physiol. , vol.275
    • Bluhm, W.F.1    Martin, J.L.2    Mestril, R.3    Dillmann, W.H.4
  • 27
    • 0035847115 scopus 로고    scopus 로고
    • Interaction between alphaB-crystallin and the human 20S proteasomal subunit C8/alpha7
    • Boelens W.C., Croes Y., de Jong W.W. Interaction between alphaB-crystallin and the human 20S proteasomal subunit C8/alpha7. Biochim. Biophys. Acta 2001, 1544:311-319.
    • (2001) Biochim. Biophys. Acta , vol.1544 , pp. 311-319
    • Boelens, W.C.1    Croes, Y.2    de Jong, W.W.3
  • 30
    • 0033972325 scopus 로고    scopus 로고
    • Subunit exchange of small heat shock proteins. Analysis of oligomer formation of alphaA-crystallin and Hsp27 by fluorescence resonance energy transfer and site-directed truncations
    • Bova M.P., McHaourab H.S., Han Y., Fung B.K. Subunit exchange of small heat shock proteins. Analysis of oligomer formation of alphaA-crystallin and Hsp27 by fluorescence resonance energy transfer and site-directed truncations. J. Biol. Chem. 2000, 275:1035-1042.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1035-1042
    • Bova, M.P.1    McHaourab, H.S.2    Han, Y.3    Fung, B.K.4
  • 31
    • 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., Wawrousek E.F. Morphological characterization of the Alpha A- and Alpha B-crystallin double knockout mouse lens. BMC. Ophthalmol. 2003, 3:3.
    • (2003) BMC. Ophthalmol. , vol.3 , pp. 3
    • Boyle, D.L.1    Takemoto, L.2    Brady, J.P.3    Wawrousek, E.F.4
  • 32
    • 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 W.G., Groome A., 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. U. S. A. 1997, 94:884-889.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 884-889
    • Brady, J.P.1    Garland, D.2    Duglas-Tabor, Y.3    Robison, W.G.4    Groome, A.5    Wawrousek, E.F.6
  • 34
    • 71549124963 scopus 로고    scopus 로고
    • Methionine sulfoxide reductase A (MsrA) restores alpha-crystallin chaperone activity lost upon methionine oxidation
    • Brennan L.A., Lee W., Giblin F.J., David L.L., Kantorow M. Methionine sulfoxide reductase A (MsrA) restores alpha-crystallin chaperone activity lost upon methionine oxidation. Biochim. Biophys. Acta 2009, 1790:1665-1672.
    • (2009) Biochim. Biophys. Acta , vol.1790 , pp. 1665-1672
    • Brennan, L.A.1    Lee, W.2    Giblin, F.J.3    David, L.L.4    Kantorow, M.5
  • 36
    • 0344012568 scopus 로고    scopus 로고
    • Stress-induced extracellular Hsp72 is a functionally significant danger signal to the immune system
    • Campisi J., Leem T.H., Fleshner M. Stress-induced extracellular Hsp72 is a functionally significant danger signal to the immune system. Cell Stress Chaperones 2003, 8:272-286.
    • (2003) Cell Stress Chaperones , vol.8 , pp. 272-286
    • Campisi, J.1    Leem, T.H.2    Fleshner, M.3
  • 37
    • 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., 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. 1998, 22:197-209.
    • (1998) Int. J. Biol. Macromol. , vol.22 , pp. 197-209
    • Carver, J.A.1    Lindner, R.A.2
  • 39
    • 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., Redfield C. The interaction of the molecular chaperone alpha-crystallin with unfolding alpha-lactalbumin: a structural and kinetic spectroscopic study. J. Mol. Biol. 2002, 318:815-827.
    • (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
  • 41
    • 27944450427 scopus 로고    scopus 로고
    • Intrasarcoplasmic amyloidosis impairs proteolytic function of proteasomes in cardiomyocytes by compromising substrate uptake
    • Chen Q., Liu J.B., Horak K.M., Zheng H., Kumarapeli A.R., Li J., Li F., Gerdes A.M., Wawrousek E.F., Wang X. Intrasarcoplasmic amyloidosis impairs proteolytic function of proteasomes in cardiomyocytes by compromising substrate uptake. Circ. Res. 2005, 97:1018-1026.
    • (2005) Circ. Res. , vol.97 , pp. 1018-1026
    • Chen, Q.1    Liu, J.B.2    Horak, K.M.3    Zheng, H.4    Kumarapeli, A.R.5    Li, J.6    Li, F.7    Gerdes, A.M.8    Wawrousek, E.F.9    Wang, X.10
  • 42
    • 78650342494 scopus 로고    scopus 로고
    • Altered chaperone-like activity of alpha-crystallins promotes cataractogenesis
    • Cheng C., Xia C.H., Huang Q., Ding L., Horwitz J., Gong X. Altered chaperone-like activity of alpha-crystallins promotes cataractogenesis. J. Biol. Chem. 2010, 285:41187-41193.
    • (2010) J. Biol. Chem. , vol.285 , pp. 41187-41193
    • Cheng, C.1    Xia, C.H.2    Huang, Q.3    Ding, L.4    Horwitz, J.5    Gong, X.6
  • 43
    • 0023644471 scopus 로고
    • The phosphorylation of the primary gene products of alpha-crystallin
    • Chiesa R., Gawinowicz-Kolks M.A., Spector A. The phosphorylation of the primary gene products of alpha-crystallin. J. Biol. Chem. 1987, 262:1438-1441.
    • (1987) J. Biol. Chem. , vol.262 , pp. 1438-1441
    • Chiesa, R.1    Gawinowicz-Kolks, M.A.2    Spector, A.3
  • 44
    • 77952314934 scopus 로고    scopus 로고
    • Identification of in vivo phosphorylation sites of lens proteins from porcine eye lenses by a gel-free phosphoproteomics approach
    • Chiou S.H., Huang C.H., Lee I.L., Wang Y.T., Liu N.Y., Tsay Y.G., Chen Y.J. Identification of in vivo phosphorylation sites of lens proteins from porcine eye lenses by a gel-free phosphoproteomics approach. Mol. Vis. 2010, 16:294-302.
    • (2010) Mol. Vis. , vol.16 , pp. 294-302
    • Chiou, S.H.1    Huang, C.H.2    Lee, I.L.3    Wang, Y.T.4    Liu, N.Y.5    Tsay, Y.G.6    Chen, Y.J.7
  • 45
    • 0033846766 scopus 로고    scopus 로고
    • Insulin and IGF-I affect the protein composition of the lens fibre cell with possible consequences for cataract
    • Civil A., van Genesen S.T., Klok E.J., Lubsen N.H. Insulin and IGF-I affect the protein composition of the lens fibre cell with possible consequences for cataract. Exp. Eye Res. 2000, 70:785-794.
    • (2000) Exp. Eye Res. , vol.70 , pp. 785-794
    • Civil, A.1    van Genesen, S.T.2    Klok, E.J.3    Lubsen, N.H.4
  • 46
    • 34548150402 scopus 로고    scopus 로고
    • Angiogenesis and chronic inflammation: cause or consequence?
    • Costa C., Incio J., Soares R. Angiogenesis and chronic inflammation: cause or consequence?. Angiogenesis 2007, 10:149-166.
    • (2007) Angiogenesis , vol.10 , pp. 149-166
    • Costa, C.1    Incio, J.2    Soares, R.3
  • 48
    • 77949328788 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy: selectivity pays off
    • Cuervo A.M. Chaperone-mediated autophagy: selectivity pays off. Trends Endocrinol. Metab. 2010, 21:142-150.
    • (2010) Trends Endocrinol. Metab. , vol.21 , pp. 142-150
    • Cuervo, A.M.1
  • 49
    • 0029124685 scopus 로고
    • Temperature induced exposure of hydrophobic surfaces and its effect on the chaperone activity of alpha-crystallin
    • Das K.P., Surewicz W.K. Temperature induced exposure of hydrophobic surfaces and its effect on the chaperone activity of alpha-crystallin. FEBS Lett. 1995, 369:321-325.
    • (1995) FEBS Lett. , vol.369 , pp. 321-325
    • Das, K.P.1    Surewicz, W.K.2
  • 50
    • 34248553886 scopus 로고    scopus 로고
    • Human retinal pigment epithelium cell changes and expression of alphaB-crystallin: a biomarker for retinal pigment epithelium cell change in age-related macular degeneration
    • De S., Rabin D.M., Salero E., Lederman P.L., Temple S., Stern J.H. Human retinal pigment epithelium cell changes and expression of alphaB-crystallin: a biomarker for retinal pigment epithelium cell change in age-related macular degeneration. Arch. Ophthalmol. 2007, 125:641-645.
    • (2007) Arch. Ophthalmol. , vol.125 , pp. 641-645
    • De, S.1    Rabin, D.M.2    Salero, E.3    Lederman, P.L.4    Temple, S.5    Stern, J.H.6
  • 51
    • 0027472047 scopus 로고
    • Evolution of the alpha-crystallin/small heat-shock protein family
    • de Jong W.W., Leunissen J.A., Voorter C.E. Evolution of the alpha-crystallin/small heat-shock protein family. Mol. Biol. Evol. 1993, 10,103-10,126.
    • (1993) Mol. Biol. Evol. , pp. 10103-10126
    • de Jong, W.W.1    Leunissen, J.A.2    Voorter, C.E.3
  • 52
    • 0032077156 scopus 로고    scopus 로고
    • Genealogy of the alpha-crystallin - small heat-shock protein superfamily
    • de Jong W.W., Caspers G.J., Leunissen J.A. Genealogy of the alpha-crystallin - small heat-shock protein superfamily. Int. J. Biol. Macromol. 1998, 22:151-162.
    • (1998) Int. J. Biol. Macromol. , vol.22 , pp. 151-162
    • de Jong, W.W.1    Caspers, G.J.2    Leunissen, J.A.3
  • 53
    • 78149466716 scopus 로고    scopus 로고
    • αB-Crystallin inhibits the cell toxicity associated with amyloid fibril formation by κ-casein and the amyloid-β peptide
    • Dehle F.C., Ecroyd H., Musgrave I.F., Carver J.A. αB-Crystallin inhibits the cell toxicity associated with amyloid fibril formation by κ-casein and the amyloid-β peptide. Cell Stress Chaperones 2010, 15:1013-1026.
    • (2010) Cell Stress Chaperones , vol.15 , pp. 1013-1026
    • Dehle, F.C.1    Ecroyd, H.2    Musgrave, I.F.3    Carver, J.A.4
  • 54
    • 0037648469 scopus 로고    scopus 로고
    • The small heat-shock protein alpha B-crystallin promotes FBX4-dependent ubiquitination
    • den Engelsman J., Keijsers V., de Jong W.W., Boelens W.C. The small heat-shock protein alpha B-crystallin promotes FBX4-dependent ubiquitination. J. Biol. Chem. 2003, 278:4699-4704.
    • (2003) J. Biol. Chem. , vol.278 , pp. 4699-4704
    • den Engelsman, J.1    Keijsers, V.2    de Jong, W.W.3    Boelens, W.C.4
  • 56
    • 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., 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. 2005, 280:37139-37148.
    • (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
  • 57
    • 0037975774 scopus 로고    scopus 로고
    • Amyloid-beta is found in drusen from some age-related macular degeneration retinas, but not in drusen from normal retinas
    • Dentchev T., Milam A.H., Lee V.M., Trojanowski J.Q., Dunaief J.L. Amyloid-beta is found in drusen from some age-related macular degeneration retinas, but not in drusen from normal retinas. Mol. Vis. 2003, 9:84-90.
    • (2003) Mol. Vis. , vol.9 , pp. 84-90
    • Dentchev, T.1    Milam, A.H.2    Lee, V.M.3    Trojanowski, J.Q.4    Dunaief, J.L.5
  • 58
    • 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., 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. 1994, 269:16853-16861.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16853-16861
    • Deretic, D.1    Aebersold, R.H.2    Morrison, H.D.3    Papermaster, D.S.4
  • 59
    • 0032986520 scopus 로고    scopus 로고
    • Alpha-crystallin as a molecular chaperone
    • Derham B.K., Harding J.J. Alpha-crystallin as a molecular chaperone. Prog. Retin. Eye Res. 1999, 18:463-509.
    • (1999) Prog. Retin. Eye Res. , vol.18 , pp. 463-509
    • Derham, B.K.1    Harding, J.J.2
  • 61
    • 34250822281 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy
    • Dice J.F. Chaperone-mediated autophagy. Autophagy 2007, 3:295-299.
    • (2007) Autophagy , vol.3 , pp. 295-299
    • Dice, J.F.1
  • 64
    • 0030724879 scopus 로고    scopus 로고
    • AlphaB-crystallin interacts with intermediate filaments in response to stress
    • Djabali K., de Néchaud B., Landon F., Portier M.M. AlphaB-crystallin interacts with intermediate filaments in response to stress. J. Cell Sci. 1997, 110(Pt. 21):2759-2769.
    • (1997) J. Cell Sci. , vol.110 , Issue.PART. 21 , pp. 2759-2769
    • Djabali, K.1    de Néchaud, B.2    Landon, F.3    Portier, M.M.4
  • 65
    • 0033571984 scopus 로고    scopus 로고
    • AlphaB-crystallin interacts with cytoplasmic intermediate filament bundles during mitosis
    • Djabali K., Piron G., de Néchaud B., Portier M.M. alphaB-crystallin interacts with cytoplasmic intermediate filament bundles during mitosis. Exp. Cell Res. 1999, 253:649-662.
    • (1999) Exp. Cell Res. , vol.253 , pp. 649-662
    • Djabali, K.1    Piron, G.2    de Néchaud, B.3    Portier, M.M.4
  • 66
    • 11944272407 scopus 로고    scopus 로고
    • Sequence and functional conservation of the intergenic region between the head-to-head genes encoding the small heat shock proteins alphaB-crystallin and HspB2 in the mammalian lineage
    • Doerwald L., van Rheede T., Dirks R.P., Madsen O., Rexwinkel R., van Genesen S.T., Martens G.J., de Jong W.W., Lubsen N.H. Sequence and functional conservation of the intergenic region between the head-to-head genes encoding the small heat shock proteins alphaB-crystallin and HspB2 in the mammalian lineage. J. Mol. Evol. 2004, 59:674-686.
    • (2004) J. Mol. Evol. , vol.59 , pp. 674-686
    • Doerwald, L.1    van Rheede, T.2    Dirks, R.P.3    Madsen, O.4    Rexwinkel, R.5    van Genesen, S.T.6    Martens, G.J.7    de Jong, W.W.8    Lubsen, N.H.9
  • 67
    • 84861812691 scopus 로고    scopus 로고
    • AlphaB-Crystallin expression in epiretinal membrane of human proliferative diabetic retinopathy
    • Feb 24. 32, 1190-1196.
    • Dong Z., Kase S., Ando R., Fukuhara J., Saito W., Kanda A., Murata M., Noda K., Ishida S. AlphaB-Crystallin expression in epiretinal membrane of human proliferative diabetic retinopathy. Retina 2012, Feb 24. 32, 1190-1196.
    • (2012) Retina
    • Dong, Z.1    Kase, S.2    Ando, R.3    Fukuhara, J.4    Saito, W.5    Kanda, A.6    Murata, M.7    Noda, K.8    Ishida, S.9
  • 68
    • 84876201467 scopus 로고    scopus 로고
    • Deficiency of αB-crystallin augments ER stress-induced apoptosis by accentuating mitochondrial dysfunction in RPE cells
    • (E-Abstract)
    • Dou G., Sreekumar P.G., Spee C., He S., Ryan S.J., Kannan R., Hinton D.R. Deficiency of αB-crystallin augments ER stress-induced apoptosis by accentuating mitochondrial dysfunction in RPE cells. Invest. Ophthalmol. Vis. Sci. 2010, 51:1438. (E-Abstract).
    • (2010) Invest. Ophthalmol. Vis. Sci. , vol.51 , pp. 1438
    • Dou, G.1    Sreekumar, P.G.2    Spee, C.3    He, S.4    Ryan, S.J.5    Kannan, R.6    Hinton, D.R.7
  • 69
    • 77955920499 scopus 로고    scopus 로고
    • In vitro renaturation of alkaline family G/11 xylanase via a folding intermediate: alpha-crystallin facilitates refolding in an ATP-independent manner
    • Dutta T., Bhattacharjee A., Majumdar U., Ray S.S., Sahoo R., Ghosh S. In vitro renaturation of alkaline family G/11 xylanase via a folding intermediate: alpha-crystallin facilitates refolding in an ATP-independent manner. Appl. Biochem. Biotechnol. 2010, 162:1238-1248.
    • (2010) Appl. Biochem. Biotechnol. , vol.162 , pp. 1238-1248
    • Dutta, T.1    Bhattacharjee, A.2    Majumdar, U.3    Ray, S.S.4    Sahoo, R.5    Ghosh, S.6
  • 70
    • 58149506229 scopus 로고    scopus 로고
    • Crystallin proteins and amyloid fibrils
    • Ecroyd H., Carver J.A. Crystallin proteins and amyloid fibrils. Cell Mol. Life Sci. 2009, 66:62-81.
    • (2009) Cell Mol. Life Sci. , vol.66 , pp. 62-81
    • Ecroyd, H.1    Carver, J.A.2
  • 72
    • 0035450191 scopus 로고    scopus 로고
    • Complex effects of molecular chaperones on the aggregation and refolding of fibroblast growth factor-1
    • Edwards K.L., Kueltzo L.A., Fisher M.T., Middaugh C.R. Complex effects of molecular chaperones on the aggregation and refolding of fibroblast growth factor-1. Arch. Biochem. Biophys. 2001, 393:14-21.
    • (2001) Arch. Biochem. Biophys. , vol.393 , pp. 14-21
    • Edwards, K.L.1    Kueltzo, L.A.2    Fisher, M.T.3    Middaugh, C.R.4
  • 75
    • 77953538551 scopus 로고    scopus 로고
    • Induction of the small heat shock protein alpha B crystallin genotoxic stress is mediated by p53 and p73
    • Evans J.R., Bosman J.D., Brown-Endres L., Yehiely F., Cryns V.L. Induction of the small heat shock protein alpha B crystallin genotoxic stress is mediated by p53 and p73. Breast Cancer Res. Treat. 2010, 122:159-168.
    • (2010) Breast Cancer Res. Treat. , vol.122 , pp. 159-168
    • Evans, J.R.1    Bosman, J.D.2    Brown-Endres, L.3    Yehiely, F.4    Cryns, V.L.5
  • 77
    • 0025914055 scopus 로고
    • Ultrastructural localization of alpha A-crystallin to the bovine lens fiber cell cytoskeleton
    • FitzGerald P.G., Graham D. Ultrastructural localization of alpha A-crystallin to the bovine lens fiber cell cytoskeleton. Curr. Eye Res. 1991, 10:417-436.
    • (1991) Curr. Eye Res. , vol.10 , pp. 417-436
    • FitzGerald, P.G.1    Graham, D.2
  • 79
    • 66149122699 scopus 로고    scopus 로고
    • The retinal proteome in experimental diabetic retinopathy: up-regulation of crystallins and reversal by systemic and periocular insulin
    • Fort P.E., Freeman W.M., Losiewicz M.K., Singh R.S., Gardner T.W. The retinal proteome in experimental diabetic retinopathy: up-regulation of crystallins and reversal by systemic and periocular insulin. Mol. Cell Proteomics 2009, 8:767-779.
    • (2009) Mol. Cell Proteomics , vol.8 , pp. 767-779
    • Fort, P.E.1    Freeman, W.M.2    Losiewicz, M.K.3    Singh, R.S.4    Gardner, T.W.5
  • 80
    • 0034924812 scopus 로고    scopus 로고
    • Folding of newly translated proteins in vivo: the role of molecular chaperones
    • Frydman J. Folding of newly translated proteins in vivo: the role of molecular chaperones. Annu. Rev. Biochem. 2001, 70:603-647.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 603-647
    • Frydman, J.1
  • 81
    • 0037040277 scopus 로고    scopus 로고
    • Detection of protein-protein interactions among lens crystallins in a mammalian two-hybrid system assay
    • Fu L., Liang J.J. Detection of protein-protein interactions among lens crystallins in a mammalian two-hybrid system assay. J. Biol. Chem. 2002, 277:4255-4260.
    • (2002) J. Biol. Chem. , vol.277 , pp. 4255-4260
    • Fu, L.1    Liang, J.J.2
  • 82
    • 2342439076 scopus 로고    scopus 로고
    • AlphaB-Crystallin-coated MAP microtubule resists nocodazole and calcium-induced disassembly
    • Fujita Y., Ohto E., Katayama E., Atomi Y. alphaB-Crystallin-coated MAP microtubule resists nocodazole and calcium-induced disassembly. J. Cell Sci. 2004, 117:1719-1726.
    • (2004) J. Cell Sci. , vol.117 , pp. 1719-1726
    • Fujita, Y.1    Ohto, E.2    Katayama, E.3    Atomi, Y.4
  • 83
    • 33646745737 scopus 로고    scopus 로고
    • Increased neuronal expression of alpha B-crystallin in human olivary hypertrophy
    • Fukushima K., Mizuno Y., Takatama M., Okamoto K. Increased neuronal expression of alpha B-crystallin in human olivary hypertrophy. Neuropathology 2006, 26:196-200.
    • (2006) Neuropathology , vol.26 , pp. 196-200
    • Fukushima, K.1    Mizuno, Y.2    Takatama, M.3    Okamoto, K.4
  • 84
    • 2442453433 scopus 로고    scopus 로고
    • Effects of divalent metal ions on the alphaB-crystallin chaperone-like activity: spectroscopic evidence for a complex between copper(II) and protein
    • Ganadu M.L., Aru M., Mura G.M., Coi A., Mlynarz P., Kozlowski H. Effects of divalent metal ions on the alphaB-crystallin chaperone-like activity: spectroscopic evidence for a complex between copper(II) and protein. J. Inorg. Biochem. 2004, 98:1103-1109.
    • (2004) J. Inorg. Biochem. , vol.98 , pp. 1103-1109
    • Ganadu, M.L.1    Aru, M.2    Mura, G.M.3    Coi, A.4    Mlynarz, P.5    Kozlowski, H.6
  • 85
    • 0029025765 scopus 로고
    • Molecular chaperones protect against glycation-induced inactivation of glucose-6-phosphate dehydrogenase
    • Ganea E., Harding J.J. Molecular chaperones protect against glycation-induced inactivation of glucose-6-phosphate dehydrogenase. Eur. J. Biochem. 1995, 231:181-185.
    • (1995) Eur. J. Biochem. , vol.231 , pp. 181-185
    • Ganea, E.1    Harding, J.J.2
  • 86
    • 0030585373 scopus 로고    scopus 로고
    • Inhibition of 6-phosphogluconate dehydrogenase by carbamylation and protection by alpha-crystallin, a chaperone-like protein
    • Ganea E., Harding J.J. Inhibition of 6-phosphogluconate dehydrogenase by carbamylation and protection by alpha-crystallin, a chaperone-like protein. Biochem. Biophys. Res. Commun. 1996, 222:626-631.
    • (1996) Biochem. Biophys. Res. Commun. , vol.222 , pp. 626-631
    • Ganea, E.1    Harding, J.J.2
  • 87
    • 67649949013 scopus 로고    scopus 로고
    • AlphaB-crystallin: a Golgi-associated membrane protein in the developing ocular lens
    • Gangalum R.K., Bhat S.P. AlphaB-crystallin: a Golgi-associated membrane protein in the developing ocular lens. Invest. Ophthalmol. Vis. Sci. 2009, 50:3283-3290.
    • (2009) Invest. Ophthalmol. Vis. Sci. , vol.50 , pp. 3283-3290
    • Gangalum, R.K.1    Bhat, S.P.2
  • 88
    • 79952802009 scopus 로고    scopus 로고
    • AlphaB-crystallin is found in detergent-resistant membrane microdomains and is secreted via exosomes from human retinal pigment epithelial cells
    • Gangalum R.K., Atanasov I.C., Zhou Z.H., Bhat S.P. AlphaB-crystallin is found in detergent-resistant membrane microdomains and is secreted via exosomes from human retinal pigment epithelial cells. J. Biol. Chem. 2011, 286:3261-3269.
    • (2011) J. Biol. Chem. , vol.286 , pp. 3261-3269
    • Gangalum, R.K.1    Atanasov, I.C.2    Zhou, Z.H.3    Bhat, S.P.4
  • 89
    • 27744485379 scopus 로고    scopus 로고
    • Interactive domains for chaperone activity in the small heat shock protein, human alphaB crystallin
    • Ghosh J.G., Estrada M.R., Clark J.I. Interactive domains for chaperone activity in the small heat shock protein, human alphaB crystallin. Biochemistry 2005, 44:14854-14869.
    • (2005) Biochemistry , vol.44 , pp. 14854-14869
    • Ghosh, J.G.1    Estrada, M.R.2    Clark, J.I.3
  • 90
    • 33750887004 scopus 로고    scopus 로고
    • The beta4-beta8 groove is an ATP-interactive site in the alpha crystallin core domain of the small heat shock protein, human alphaB crystallin
    • Ghosh J.G., Houck S.A., Doneanu C.E., Clark J.I. The beta4-beta8 groove is an ATP-interactive site in the alpha crystallin core domain of the small heat shock protein, human alphaB crystallin. J. Mol. Biol. 2006, 364:364-375.
    • (2006) J. Mol. Biol. , vol.364 , pp. 364-375
    • Ghosh, J.G.1    Houck, S.A.2    Doneanu, C.E.3    Clark, J.I.4
  • 91
    • 34249749409 scopus 로고    scopus 로고
    • Interactions between important regulatory proteins and human alpha B crystallin
    • Ghosh J.G., Shenoy A.K., Clark J.I. Interactions between important regulatory proteins and human alpha B crystallin. Biochemistry 2007, 46:6308-6317.
    • (2007) Biochemistry , vol.46 , pp. 6308-6317
    • Ghosh, J.G.1    Shenoy, A.K.2    Clark, J.I.3
  • 92
    • 34548241302 scopus 로고    scopus 로고
    • Interactive sequences in the stress protein and molecular chaperone human alphaB crystallin recognize and modulate the assembly of filaments
    • Ghosh J.G., Houck S.A., Clark J.I. Interactive sequences in the stress protein and molecular chaperone human alphaB crystallin recognize and modulate the assembly of filaments. Int. J. Biochem. Cell Biol. 2007, 39:1804-1815.
    • (2007) Int. J. Biochem. Cell Biol. , vol.39 , pp. 1804-1815
    • Ghosh, J.G.1    Houck, S.A.2    Clark, J.I.3
  • 94
    • 33750806555 scopus 로고    scopus 로고
    • Ischemia-induced phosphorylation and translocation of stress protein alpha B-crystallin to Z lines of myocardium
    • Golenhofen N., Ness W., Koob R., Htun P., Schaper W., Drenckhahn D. Ischemia-induced phosphorylation and translocation of stress protein alpha B-crystallin to Z lines of myocardium. Am. J. Physiol. 1998, 274:H1457-H1464.
    • (1998) Am. J. Physiol. , vol.274
    • Golenhofen, N.1    Ness, W.2    Koob, R.3    Htun, P.4    Schaper, W.5    Drenckhahn, D.6
  • 96
    • 0030936847 scopus 로고    scopus 로고
    • Protein quality control: triage by chaperones and proteases
    • Gottesman S., Wickner S., Maurizi M.R. Protein quality control: triage by chaperones and proteases. Genes Dev. 1997, 11:815-823.
    • (1997) Genes Dev. , vol.11 , pp. 815-823
    • Gottesman, S.1    Wickner, S.2    Maurizi, M.R.3
  • 97
    • 61849122908 scopus 로고    scopus 로고
    • Genetics of crystallins: cataract and beyond
    • Graw J. Genetics of crystallins: cataract and beyond. Exp. Eye Res. 2009, 88:173-189.
    • (2009) Exp. Eye Res. , vol.88 , pp. 173-189
    • Graw, J.1
  • 99
    • 77949692461 scopus 로고    scopus 로고
    • Alzheimer's disease and retinal neurodegeneration
    • Guo L., Duggan J., Cordeiro M.F. Alzheimer's disease and retinal neurodegeneration. Curr. Alzheimer Res. 2010, 7:3-14.
    • (2010) Curr. Alzheimer Res. , vol.7 , pp. 3-14
    • Guo, L.1    Duggan, J.2    Cordeiro, M.F.3
  • 100
    • 67650528792 scopus 로고    scopus 로고
    • Identification of interaction sites between human betaA3- and alphaA/alphaB-crystallins by mammalian two-hybrid and fluorescence resonance energy transfer acceptor photobleaching methods
    • Gupta R., Srivastava O.P. Identification of interaction sites between human betaA3- and alphaA/alphaB-crystallins by mammalian two-hybrid and fluorescence resonance energy transfer acceptor photobleaching methods. J. Biol. Chem. 2009, 284:18481-18492.
    • (2009) J. Biol. Chem. , vol.284 , pp. 18481-18492
    • Gupta, R.1    Srivastava, O.P.2
  • 101
    • 0036558366 scopus 로고    scopus 로고
    • Structure and properties of small heat shock proteins (sHsp) and their interaction with cytoskeleton proteins
    • Gusev N.B., Bogatcheva N.V., Marston S.B. Structure and properties of small heat shock proteins (sHsp) and their interaction with cytoskeleton proteins. Biochemistry (Mosc) 2002, 67:511-519.
    • (2002) Biochemistry (Mosc) , vol.67 , pp. 511-519
    • Gusev, N.B.1    Bogatcheva, N.V.2    Marston, S.B.3
  • 103
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl F.U., Bracher A., Hayer-Hartl M. Molecular chaperones in protein folding and proteostasis. Nature 2011, 475:324-332.
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 106
    • 0033621703 scopus 로고    scopus 로고
    • AlphaB-crystallin regulates intermediate filament organization in situ
    • Head M.W., Hurwitz L., Kegel K., Goldman J.E. AlphaB-crystallin regulates intermediate filament organization in situ. Neuroreport 2000, 11:361-365.
    • (2000) Neuroreport , vol.11 , pp. 361-365
    • Head, M.W.1    Hurwitz, L.2    Kegel, K.3    Goldman, J.E.4
  • 107
    • 0029968456 scopus 로고    scopus 로고
    • Glycation induced inactivation of malate dehydrogenase protection by aspirin and a lens molecular chaperone, alpha-crystallin
    • Heath M.M., Rixon K.C., Harding J.J. Glycation induced inactivation of malate dehydrogenase protection by aspirin and a lens molecular chaperone, alpha-crystallin. Biochim. Biophys. Acta 1996, 1315:176-184.
    • (1996) Biochim. Biophys. Acta , vol.1315 , pp. 176-184
    • Heath, M.M.1    Rixon, K.C.2    Harding, J.J.3
  • 108
    • 77954248724 scopus 로고    scopus 로고
    • Anti-alpha B-crystallin immunoreactivity in Guillain-Barré syndrome and chronic inflammatory demyelinating polyneuropathy
    • Hegen H., Wanschitz J., Ehling R., Deisenhammer F., Löscher W.N., Reindl M., Berger T. Anti-alpha B-crystallin immunoreactivity in Guillain-Barré syndrome and chronic inflammatory demyelinating polyneuropathy. J. Peripher. Nerv. Syst. 2010, 15:150-152.
    • (2010) J. Peripher. Nerv. Syst. , vol.15 , pp. 150-152
    • Hegen, H.1    Wanschitz, J.2    Ehling, R.3    Deisenhammer, F.4    Löscher, W.N.5    Reindl, M.6    Berger, T.7
  • 110
    • 79952635812 scopus 로고    scopus 로고
    • BAG3 directly interacts with mutated alphaB-crystallin to suppress its aggregation and toxicity
    • Hishiya A., Salman M.N., Carra S., Kampinga H.H., Takayama S. BAG3 directly interacts with mutated alphaB-crystallin to suppress its aggregation and toxicity. PLoS One 2011, 6:e16828.
    • (2011) PLoS One , vol.6
    • Hishiya, A.1    Salman, M.N.2    Carra, S.3    Kampinga, H.H.4    Takayama, S.5
  • 111
    • 0029878451 scopus 로고    scopus 로고
    • Alpha-crystallin acting as a molecular chaperone protects catalase against steroid-induced inactivation
    • Hook D.W., Harding J.J. Alpha-crystallin acting as a molecular chaperone protects catalase against steroid-induced inactivation. FEBS Lett. 1996, 382:281-284.
    • (1996) FEBS Lett. , vol.382 , pp. 281-284
    • Hook, D.W.1    Harding, J.J.2
  • 112
    • 0034604721 scopus 로고    scopus 로고
    • Alpha B-crystallin gene induction and phosphorylation by MKK6-activated p38. A potential role for alpha B-crystallin as a target of the p38 branch of the cardiac stress response
    • Hoover H.E., Thuerauf D.J., Martindale J.J., Glembotski C.C. alpha B-crystallin gene induction and phosphorylation by MKK6-activated p38. A potential role for alpha B-crystallin as a target of the p38 branch of the cardiac stress response. J. Biol. Chem. 2000, 275:23825-23833.
    • (2000) J. Biol. Chem. , vol.275 , pp. 23825-23833
    • Hoover, H.E.1    Thuerauf, D.J.2    Martindale, J.J.3    Glembotski, C.C.4
  • 114
    • 0026483279 scopus 로고
    • Alpha-crystallin can function as a molecular chaperone
    • Horwitz J. Alpha-crystallin can function as a molecular chaperone. Proc. Natl. Acad. Sci. U. S. A. 1992, 89:10449-10453.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 10449-10453
    • Horwitz, J.1
  • 115
    • 0037325497 scopus 로고    scopus 로고
    • Alpha-crystallin
    • Horwitz J. Alpha-crystallin. Exp. Eye Res. 2003, 76:145-153.
    • (2003) Exp. Eye Res. , vol.76 , pp. 145-153
    • Horwitz, J.1
  • 116
    • 33646122452 scopus 로고    scopus 로고
    • An algorithm for predicting protein-protein interaction sites: abnormally exposed amino acid residues and secondary structure elements
    • Hoskins J., Lovell S., Blundell T.L. An algorithm for predicting protein-protein interaction sites: abnormally exposed amino acid residues and secondary structure elements. Protein Sci. 2006, 15:1017-1029.
    • (2006) Protein Sci. , vol.15 , pp. 1017-1029
    • Hoskins, J.1    Lovell, S.2    Blundell, T.L.3
  • 118
    • 0029004307 scopus 로고
    • Induction of the synthesis of hsp27 and alpha B crystallin in tissues of heat-stressed rats and its suppression by ethanol or an alpha 1-adrenergic antagonist
    • Inaguma Y., Hasegawa K., Goto S., Ito H., Kato K. Induction of the synthesis of hsp27 and alpha B crystallin in tissues of heat-stressed rats and its suppression by ethanol or an alpha 1-adrenergic antagonist. J. Biochem. (Tokyo) 1995, 117:1238-1243.
    • (1995) J. Biochem. (Tokyo) , vol.117 , pp. 1238-1243
    • Inaguma, Y.1    Hasegawa, K.2    Goto, S.3    Ito, H.4    Kato, K.5
  • 119
    • 0035544297 scopus 로고    scopus 로고
    • αB-crystallin phosphorylated at Ser-59 is localized in centrosomes and midbodies during mitosis
    • Inaguma Y., Ito H., Iwamoto I., Saga S., Kato K. αB-crystallin phosphorylated at Ser-59 is localized in centrosomes and midbodies during mitosis. Eur. J. Cell Biol. 2001, 80:741-748.
    • (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
  • 121
    • 0030613774 scopus 로고    scopus 로고
    • Phosphorylation of alphaB-crystallin in response to various types of stress
    • Ito H., Okamoto K., Nakayama H., Isobe T., Kato K. Phosphorylation of alphaB-crystallin in response to various types of stress. J. Biol. Chem. 1997, 272:29934-29941.
    • (1997) J. Biol. Chem. , vol.272 , pp. 29934-29941
    • Ito, H.1    Okamoto, K.2    Nakayama, H.3    Isobe, T.4    Kato, K.5
  • 122
    • 0035895908 scopus 로고    scopus 로고
    • Phosphorylation-induced change of the oligomerization state of alpha B-crystallin
    • Ito H., Kamei K., Iwamoto I., Inaguma Y., Nohara D., Kato K. Phosphorylation-induced change of the oligomerization state of alpha B-crystallin. J. Biol. Chem. 2001, 276:5346-5352.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5346-5352
    • Ito, H.1    Kamei, K.2    Iwamoto, I.3    Inaguma, Y.4    Nohara, D.5    Kato, K.6
  • 123
    • 0036239489 scopus 로고    scopus 로고
    • Inhibition of proteasomes induces accumulation, phosphorylation, and recruitment of Hsp27and αB-crystallin to aggresomes
    • Ito H., Kamei K., Iwamoto I., Inaguma Y., Garcia-Mata R., Sztul E., Kato K. Inhibition of proteasomes induces accumulation, phosphorylation, and recruitment of Hsp27and αB-crystallin to aggresomes. J. Biochem. (Tokyo) 2002, 131:593-603.
    • (2002) J. Biochem. (Tokyo) , vol.131 , pp. 593-603
    • Ito, H.1    Kamei, K.2    Iwamoto, I.3    Inaguma, Y.4    Garcia-Mata, R.5    Sztul, E.6    Kato, K.7
  • 124
    • 0024521440 scopus 로고
    • Alpha B-crystallin is expressed in non-lenticular tissues and accumulates in Alexander's disease brain
    • Iwaki T., Kume-Iwaki A., Liem R.K., Goldman J.E. Alpha B-crystallin is expressed in non-lenticular tissues and accumulates in Alexander's disease brain. Cell 1989, 57:71-78.
    • (1989) Cell , vol.57 , pp. 71-78
    • Iwaki, T.1    Kume-Iwaki, A.2    Liem, R.K.3    Goldman, J.E.4
  • 125
    • 0025101570 scopus 로고
    • Cellular distribution of alpha B-crystallin in non-lenticular tissues
    • Iwaki T., Kume-Iwaki A., Goldman J.E. Cellular distribution of alpha B-crystallin in non-lenticular tissues. J. Histochem. Cytochem. 1990, 38:31-39.
    • (1990) J. Histochem. Cytochem. , vol.38 , pp. 31-39
    • Iwaki, T.1    Kume-Iwaki, A.2    Goldman, J.E.3
  • 126
    • 0023506457 scopus 로고
    • Folding and association of proteins
    • Jaenicke R. Folding and association of proteins. Prog. Biophys. Mol. Biol. 1987, 49:117-237.
    • (1987) Prog. Biophys. Mol. Biol. , vol.49 , pp. 117-237
    • Jaenicke, R.1
  • 131
    • 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., Neal M.J. Expression of alphaB-crystallin in a mouse model of inherited retinal degeneration. Neuroreport 1998, 9:4161-4165.
    • (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
  • 132
    • 60949098753 scopus 로고    scopus 로고
    • Heat shock proteins as gatekeepers of proteolytic pathways-Implications for age-related macular degeneration (AMD)
    • Kaarniranta K., Salminen A., Eskelinen E.L., Kopitz J. Heat shock proteins as gatekeepers of proteolytic pathways-Implications for age-related macular degeneration (AMD). Ageing Res. Rev. 2009, 8:128-139.
    • (2009) Ageing Res. Rev. , vol.8 , pp. 128-139
    • Kaarniranta, K.1    Salminen, A.2    Eskelinen, E.L.3    Kopitz, J.4
  • 134
    • 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., 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. 2001, 276:16059-16063.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16059-16063
    • Kamradt, M.C.1    Chen, F.2    Cryns, V.L.3
  • 135
    • 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., 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. 2002, 277:38731-38736.
    • (2002) J. Biol. Chem. , vol.277 , pp. 38731-38736
    • Kamradt, M.C.1    Chen, F.2    Sam, S.3    Cryns, V.L.4
  • 137
    • 84863308955 scopus 로고    scopus 로고
    • Transcriptome analysis using next generation sequencing reveals molecular signatures of diabetic retinopathy and efficacy of candidate drugs
    • Kandpal R.P., Rajasimha H.K., Brooks M.J., Nellissery J., Wan J., Qian J., Kern T.S., Swaroop A. Transcriptome analysis using next generation sequencing reveals molecular signatures of diabetic retinopathy and efficacy of candidate drugs. Mol. Vis. 2012, 18:1123-1146.
    • (2012) Mol. Vis. , vol.18 , pp. 1123-1146
    • Kandpal, R.P.1    Rajasimha, H.K.2    Brooks, M.J.3    Nellissery, J.4    Wan, J.5    Qian, J.6    Kern, T.S.7    Swaroop, A.8
  • 138
    • 0034746493 scopus 로고    scopus 로고
    • Regulation of GSH in alphaA-expressing human lens epithelial cell lines and in alphaA knockout mouse lenses
    • Kannan R., Ouyang B., Wawrousek E., Kaplowitz N., Andley U.P. Regulation of GSH in alphaA-expressing human lens epithelial cell lines and in alphaA knockout mouse lenses. Invest. Ophthalmol. Vis. Sci. 2001, 42:409-416.
    • (2001) Invest. Ophthalmol. Vis. Sci. , vol.42 , pp. 409-416
    • Kannan, R.1    Ouyang, B.2    Wawrousek, E.3    Kaplowitz, N.4    Andley, U.P.5
  • 140
    • 0028180509 scopus 로고
    • Alpha-crystallin/small heat shock protein has autokinase activity
    • Kantorow M., Piatigorsky J. Alpha-crystallin/small heat shock protein has autokinase activity. Proc. Natl. Acad. Sci. U. S. A. 1994, 91:3112-3116.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 3112-3116
    • Kantorow, M.1    Piatigorsky, J.2
  • 141
    • 0029083170 scopus 로고
    • Conversion from oligomers to tetramers enhances autophosphorylation by lens alpha A-crystallin. Specificity between alpha A- and alpha B-crystallin subunits
    • Kantorow M., Horwitz J., van Boekel M.A., de Jong W.W., Piatigorsky J. Conversion from oligomers to tetramers enhances autophosphorylation by lens alpha A-crystallin. Specificity between alpha A- and alpha B-crystallin subunits. J. Biol. Chem. 1995, 1995(270):17215-17220.
    • (1995) J. Biol. Chem. , vol.1995 , Issue.270 , pp. 17215-17220
    • Kantorow, M.1    Horwitz, J.2    van Boekel, M.A.3    de Jong, W.W.4    Piatigorsky, J.5
  • 142
  • 143
    • 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., Ferrington D.A. Modified alpha A crystallin in the retina: altered expression and truncation with aging. Biochemistry 2003, 42:15310-15325.
    • (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
  • 144
    • 60549102517 scopus 로고    scopus 로고
    • Expression of alpha-crystallin in retinoblastoma
    • Kase S., Parikh J.G., Rao N.A. Expression of alpha-crystallin in retinoblastoma. Arch. Ophthalmol. 2009, 127:187-192.
    • (2009) Arch. Ophthalmol. , vol.127 , pp. 187-192
    • Kase, S.1    Parikh, J.G.2    Rao, N.A.3
  • 146
    • 79960765391 scopus 로고    scopus 로고
    • Increased expression of αA-crystallin in human diabetic eye
    • Kase S., Ishida S., Rao N.A. Increased expression of αA-crystallin in human diabetic eye. Int. J. Mol. Med. 2011, 28:505-511.
    • (2011) Int. J. Mol. Med. , vol.28 , pp. 505-511
    • Kase, S.1    Ishida, S.2    Rao, N.A.3
  • 147
    • 84855667050 scopus 로고    scopus 로고
    • Expression of α-crystallin in the retina of human sympathetic ophthalmia
    • Kase S., Meghpara B.B., Ishida S., Rao N.A. Expression of α-crystallin in the retina of human sympathetic ophthalmia. Mol. Med. Rep. 2012, 5:395-399.
    • (2012) Mol. Med. Rep. , vol.5 , pp. 395-399
    • Kase, S.1    Meghpara, B.B.2    Ishida, S.3    Rao, N.A.4
  • 148
    • 0026040828 scopus 로고
    • Immunoreactive alpha A crystallin in rat non-lenticular tissues detected with a sensitive immunoassay method
    • Kato K., Shinohara H., Kurobe N., Goto S., Inaguma Y., Ohshima K. Immunoreactive alpha A crystallin in rat non-lenticular tissues detected with a sensitive immunoassay method. Biochim. Biophys. Acta 1991, 1080:173-180.
    • (1991) Biochim. Biophys. Acta , vol.1080 , pp. 173-180
    • Kato, K.1    Shinohara, H.2    Kurobe, N.3    Goto, S.4    Inaguma, Y.5    Ohshima, K.6
  • 149
    • 0026774629 scopus 로고
    • Copurification of small heat shock protein with alpha B crystallin from human skeletal muscle
    • Kato K., Shinohara H., Goto S., Inaguma Y., Morishita R., Asano T. Copurification of small heat shock protein with alpha B crystallin from human skeletal muscle. J. Biol. Chem. 1992, 267:7718-7725.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7718-7725
    • Kato, K.1    Shinohara, H.2    Goto, S.3    Inaguma, Y.4    Morishita, R.5    Asano, T.6
  • 150
    • 0032561079 scopus 로고    scopus 로고
    • Phosphorylation of αB-crystallin in mitotic cells and identification of enzymatic activities responsible for phosphorylation
    • Kato K., Ito H., Kamei K., Inaguma Y., Iwamoto I., Saga S. Phosphorylation of αB-crystallin in mitotic cells and identification of enzymatic activities responsible for phosphorylation. J. Biol. Chem. 1998, 273:28346-28354.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28346-28354
    • Kato, K.1    Ito, H.2    Kamei, K.3    Inaguma, Y.4    Iwamoto, I.5    Saga, S.6
  • 151
    • 0032837149 scopus 로고    scopus 로고
    • Selective stimulation of Hsp27 and alphaB-crystallin but not Hsp70 expression by p38 MAP kinase activation
    • Kato K., Ito H., Kamei K., Iwamoto I. Selective stimulation of Hsp27 and alphaB-crystallin but not Hsp70 expression by p38 MAP kinase activation. Cell Stress Chaperones 1999, 4:94-101.
    • (1999) Cell Stress Chaperones , vol.4 , pp. 94-101
    • Kato, K.1    Ito, H.2    Kamei, K.3    Iwamoto, I.4
  • 152
    • 0035146830 scopus 로고    scopus 로고
    • Ser-59 is the major phosphorylation site in alphaB-crystallin accumulated in the brains of patients with Alexander's disease
    • Kato K., Inaguma Y., Ito H., Iida K., Iwamoto I., Kamei K., Ochi N., Ohta H., Kishikawa M. Ser-59 is the major phosphorylation site in alphaB-crystallin accumulated in the brains of patients with Alexander's disease. J. Neurochem. 2001, 76:730-736.
    • (2001) J. Neurochem. , vol.76 , pp. 730-736
    • Kato, K.1    Inaguma, Y.2    Ito, H.3    Iida, K.4    Iwamoto, I.5    Kamei, K.6    Ochi, N.7    Ohta, H.8    Kishikawa, M.9
  • 153
    • 0141953996 scopus 로고    scopus 로고
    • Angiogenesis inhibitors target the endothelial cell cytoskeleton through altered regulation of heat shock protein 27 and cofilin
    • Keezer S.M., Ivie S.E., Krutzsch H.C., Tandle A., Libutti S.K., Roberts D.D. Angiogenesis inhibitors target the endothelial cell cytoskeleton through altered regulation of heat shock protein 27 and cofilin. Cancer Res. 2003, 63:6405-6412.
    • (2003) Cancer Res. , vol.63 , pp. 6405-6412
    • Keezer, S.M.1    Ivie, S.E.2    Krutzsch, H.C.3    Tandle, A.4    Libutti, S.K.5    Roberts, D.D.6
  • 157
    • 78650832181 scopus 로고    scopus 로고
    • Identification of amyloid plaques in retinas from Alzheimer's patients and noninvasive in vivo optical imaging of retinal plaques in a mouse model
    • Koronyo-Hamaoui M., Koronyo Y., Ljubimov A.V., Miller C.A., Ko M.K., Black K.L., Schwartz M., Farkas D.L. Identification of amyloid plaques in retinas from Alzheimer's patients and noninvasive in vivo optical imaging of retinal plaques in a mouse model. Neuroimage 2011, 54:S204-S217.
    • (2011) Neuroimage , vol.54
    • Koronyo-Hamaoui, M.1    Koronyo, Y.2    Ljubimov, A.V.3    Miller, C.A.4    Ko, M.K.5    Black, K.L.6    Schwartz, M.7    Farkas, D.L.8
  • 158
    • 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., 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. 2003, 278:10361-10367.
    • (2003) J. Biol. Chem. , vol.278 , pp. 10361-10367
    • Koteiche, H.A.1    McHaourab, H.S.2
  • 159
    • 0034744931 scopus 로고    scopus 로고
    • AlphaB-crystallin, a low-molecular-weight heat shock protein, acts as a regulator of platelet function
    • Kozawa O., Matsuno H., Niwa M., Hatakeyama D., Kato K., Uematsu T. AlphaB-crystallin, a low-molecular-weight heat shock protein, acts as a regulator of platelet function. Cell Stress Chaperones 2001, 6:21-28.
    • (2001) Cell Stress Chaperones , vol.6 , pp. 21-28
    • Kozawa, O.1    Matsuno, H.2    Niwa, M.3    Hatakeyama, D.4    Kato, K.5    Uematsu, T.6
  • 164
    • 33749123682 scopus 로고    scopus 로고
    • Cell signaling pathways to alphaB-crystallin following stresses of the cytoskeleton
    • Launay N., Goudeau B., Kato K., Vicart P., Lilienbaum A. Cell signaling pathways to alphaB-crystallin following stresses of the cytoskeleton. Exp. Cell Res. 2006, 312:3570-3584.
    • (2006) Exp. Cell Res. , vol.312 , pp. 3570-3584
    • Launay, N.1    Goudeau, B.2    Kato, K.3    Vicart, P.4    Lilienbaum, A.5
  • 165
    • 78549288555 scopus 로고    scopus 로고
    • Serine 59 phosphorylation of {alpha}B-crystallin down-regulates its anti-apoptotic function by binding and sequestering Bcl-2 in breast cancer cells
    • Launay N., Tarze A., Vicart P., Lilienbaum A. Serine 59 phosphorylation of {alpha}B-crystallin down-regulates its anti-apoptotic function by binding and sequestering Bcl-2 in breast cancer cells. J. Biol. Chem. 2010, 285:37324-37332.
    • (2010) J. Biol. Chem. , vol.285 , pp. 37324-37332
    • Launay, N.1    Tarze, A.2    Vicart, P.3    Lilienbaum, A.4
  • 166
    • 79960287784 scopus 로고    scopus 로고
    • Phosphorylation of Ser45 and Ser59 of αB-crystallin and p38/extracellular regulated kinase activity determine αB-crystallin-mediated protection of rat brain astrocytes from C2-ceramide- and staurosporine-induced cell death
    • Li R., Reiser G. Phosphorylation of Ser45 and Ser59 of αB-crystallin and p38/extracellular regulated kinase activity determine αB-crystallin-mediated protection of rat brain astrocytes from C2-ceramide- and staurosporine-induced cell death. J. Neurochem. 2011, 118:354-364.
    • (2011) J. Neurochem. , vol.118 , pp. 354-364
    • Li, R.1    Reiser, G.2
  • 167
    • 68949198337 scopus 로고    scopus 로고
    • Alpha A-crystallin and alpha B-crystallin, newly identified interaction proteins of protease-activated receptor-2, rescue astrocytes from C2-ceramide- and staurosporine-induced cell death
    • Li R., Rohatgi T., Hanck T., Reiser G. Alpha A-crystallin and alpha B-crystallin, newly identified interaction proteins of protease-activated receptor-2, rescue astrocytes from C2-ceramide- and staurosporine-induced cell death. J. Neurochem. 2009, 110:1433-1444.
    • (2009) J. Neurochem. , vol.110 , pp. 1433-1444
    • Li, R.1    Rohatgi, T.2    Hanck, T.3    Reiser, G.4
  • 168
    • 0034602513 scopus 로고    scopus 로고
    • Interaction between beta-amyloid and lens alphaB-crystallin
    • Liang J.J. Interaction between beta-amyloid and lens alphaB-crystallin. FEBS Lett. 2000, 484:98-101.
    • (2000) FEBS Lett. , vol.484 , pp. 98-101
    • Liang, J.J.1
  • 170
    • 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., 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. 2004, 79:393-403.
    • (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
  • 171
    • 3543039430 scopus 로고    scopus 로고
    • AlphaB-crystallin inhibits glucose-induced apoptosis in vascular endothelial cells
    • Liu B., Bhat M., Nagaraj R.H. AlphaB-crystallin inhibits glucose-induced apoptosis in vascular endothelial cells. Biochem. Biophys. Res. Commun. 2004, 321:254-258.
    • (2004) Biochem. Biophys. Res. Commun. , vol.321 , pp. 254-258
    • Liu, B.1    Bhat, M.2    Nagaraj, R.H.3
  • 172
    • 33846297971 scopus 로고    scopus 로고
    • Small heat shock protein alphaB-crystallin binds to p53 to sequester its translocation to mitochondria during hydrogen peroxide-induced apoptosis
    • Liu S., Li J., Tao Y., Xiao X. Small heat shock protein alphaB-crystallin binds to p53 to sequester its translocation to mitochondria during hydrogen peroxide-induced apoptosis. Biochem. Biophys. Res. Commun. 2007, 354:109-114.
    • (2007) Biochem. Biophys. Res. Commun. , vol.354 , pp. 109-114
    • Liu, S.1    Li, J.2    Tao, Y.3    Xiao, X.4
  • 173
    • 80054788049 scopus 로고    scopus 로고
    • Diabetes impairs the neuroprotective properties of retinal alpha-crystallins
    • Losiewicz M.K., Fort P.E. Diabetes impairs the neuroprotective properties of retinal alpha-crystallins. Invest. Ophthalmol. Vis. Sci. 2011, 52:5034-5042.
    • (2011) Invest. Ophthalmol. Vis. Sci. , vol.52 , pp. 5034-5042
    • Losiewicz, M.K.1    Fort, P.E.2
  • 174
    • 0026541969 scopus 로고
    • Alpha B crystallin expression in non-lenticular tissues and selective presence in ubiquitinated inclusion bodies in human disease
    • Lowe J., McDermott H., Pike I., Spendlove I., Landon M., Mayer R.J. alpha B crystallin expression in non-lenticular tissues and selective presence in ubiquitinated inclusion bodies in human disease. J. Pathol. 1992, 166:61-68.
    • (1992) J. Pathol. , vol.166 , pp. 61-68
    • Lowe, J.1    McDermott, H.2    Pike, I.3    Spendlove, I.4    Landon, M.5    Mayer, R.J.6
  • 175
    • 32444450909 scopus 로고    scopus 로고
    • Drusen deposits associated with aging and age-related macular degeneration contain nonfibrillar amyloid oligomers
    • Luibl V., Isas J.M., Kayed R., Glabe C.G., Langen R., Chen J. Drusen deposits associated with aging and age-related macular degeneration contain nonfibrillar amyloid oligomers. J. Clin. Invest. 2006, 116:378-385.
    • (2006) J. Clin. Invest. , vol.116 , pp. 378-385
    • Luibl, V.1    Isas, J.M.2    Kayed, R.3    Glabe, C.G.4    Langen, R.5    Chen, J.6
  • 176
    • 0030475908 scopus 로고    scopus 로고
    • Modifications of the water-insoluble human lens alpha-crystallins
    • Lund A.L., Smith J.B., Smith D.L. Modifications of the water-insoluble human lens alpha-crystallins. Exp. Eye Res. 1996, 63:661-672.
    • (1996) Exp. Eye Res. , vol.63 , pp. 661-672
    • Lund, A.L.1    Smith, J.B.2    Smith, D.L.3
  • 177
    • 18844362688 scopus 로고    scopus 로고
    • Alpha-Crystallin localizes to the leading edges of migrating lens epithelial cells
    • Maddala R., Rao V.P. alpha-Crystallin localizes to the leading edges of migrating lens epithelial cells. Exp. Cell Res. 2005, 306:203-215.
    • (2005) Exp. Cell Res. , vol.306 , pp. 203-215
    • Maddala, R.1    Rao, V.P.2
  • 178
    • 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., Kurok i.Y. Low expression of alphaA-crystallins and rhodopsin kinase of photoreceptors in retinal dystrophy rat. Invest. Ophthalmol. Vis. Sci. 1999, 40:2788-2794.
    • (1999) Invest. Ophthalmol. Vis. Sci. , vol.40 , pp. 2788-2794
    • Maeda, A.1    Ohguro, H.2    Maeda, T.3    Nakagawa, T.4    Kurok, I.5
  • 179
    • 78649515958 scopus 로고    scopus 로고
    • αB-crystallin (HspB5) in familial amyloidotic polyneuropathy
    • Magalhães J., Santos S.D., Saraiva M.J. αB-crystallin (HspB5) in familial amyloidotic polyneuropathy. Int. J. Exp. Pathol. 2010, 91:515-521.
    • (2010) Int. J. Exp. Pathol. , vol.91 , pp. 515-521
    • Magalhães, J.1    Santos, S.D.2    Saraiva, M.J.3
  • 180
    • 77953811925 scopus 로고    scopus 로고
    • Kynurenine inhibits fibroblast growth factor 2-mediated expression of crystallins and MIP26 in lens epithelial cells
    • Mailankot M., Howell S., Nagaraj R.H. Kynurenine inhibits fibroblast growth factor 2-mediated expression of crystallins and MIP26 in lens epithelial cells. Biochim. Biophys. Acta 2010, 1802:609-620.
    • (2010) Biochim. Biophys. Acta , vol.1802 , pp. 609-620
    • Mailankot, M.1    Howell, S.2    Nagaraj, R.H.3
  • 182
    • 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., Robbins J. Mitochondrial dysfunction and apoptosis underlie the pathogenic process in alpha-B-crystallin desmin-related cardiomyopathy. Circulation 2005, 112:3451-3461.
    • (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
  • 183
    • 0035900776 scopus 로고    scopus 로고
    • Human bcl-2 gene attenuates the ability of rabbit lens epithelial cells against H2O2-inducedapoptosis through down-regulation of the alpha B-crystallin gene
    • Mao Y.W., Xiang H., Wang J., Korsmeyer S., Reddan J., Li D.W. Human bcl-2 gene attenuates the ability of rabbit lens epithelial cells against H2O2-inducedapoptosis through down-regulation of the alpha B-crystallin gene. J. Biol. Chem. 2001, 276:43435-43445.
    • (2001) J. Biol. Chem. , vol.276 , pp. 43435-43445
    • Mao, Y.W.1    Xiang, H.2    Wang, J.3    Korsmeyer, S.4    Reddan, J.5    Li, D.W.6
  • 184
    • 2442681777 scopus 로고    scopus 로고
    • Human alphaA- and alphaB-crystallins bind to Bax and Bcl-X(S) to sequester their translocation during staurosporine-induced apoptosis
    • Mao Y.W., Liu J.P., Xiang H., Li D.W. Human alphaA- and alphaB-crystallins bind to Bax and Bcl-X(S) to sequester their translocation during staurosporine-induced apoptosis. Cell Death Differ. 2004, 11:512-526.
    • (2004) Cell Death Differ. , vol.11 , pp. 512-526
    • Mao, Y.W.1    Liu, J.P.2    Xiang, H.3    Li, D.W.4
  • 185
    • 0031469110 scopus 로고    scopus 로고
    • Small heat shock proteins and protection against ischemic injury in cardiac myocytes
    • Martin J.L., Mestril R., Hilal-Dandan R., Brunton L.L., Dillmann W.H. Small heat shock proteins and protection against ischemic injury in cardiac myocytes. Circulation 1997, 96:4343-4348.
    • (1997) Circulation , vol.96 , pp. 4343-4348
    • Martin, J.L.1    Mestril, R.2    Hilal-Dandan, R.3    Brunton, L.L.4    Dillmann, W.H.5
  • 188
    • 77956404647 scopus 로고    scopus 로고
    • Exosomes: extracellular organelles important in intercellular communication
    • Mathivanan S., Ji H., Simpson R.J. Exosomes: extracellular organelles important in intercellular communication. J. Proteomics 2010, 73:1907-1920.
    • (2010) J. Proteomics , vol.73 , pp. 1907-1920
    • Mathivanan, S.1    Ji, H.2    Simpson, R.J.3
  • 190
    • 84860877643 scopus 로고    scopus 로고
    • αB-crystallin/sHSP protects cytochrome c and mitochondrial function against oxidative stress in lens and retinal cells
    • McGreal R.S., Lee Kantorow W., Chauss D.C., Wei J., Brennan L.A., Kantorow M. αB-crystallin/sHSP protects cytochrome c and mitochondrial function against oxidative stress in lens and retinal cells. Biochim. Biophys. Acta 2012, 1820:921-930.
    • (2012) Biochim. Biophys. Acta , vol.1820 , pp. 921-930
    • McGreal, R.S.1    Lee Kantorow, W.2    Chauss, D.C.3    Wei, J.4    Brennan, L.A.5    Kantorow, M.6
  • 191
    • 0035478709 scopus 로고    scopus 로고
    • Analysis of phosphorylated proteins and peptides by mass spectrometry
    • McLachlin D.T., Chait B.T. Analysis of phosphorylated proteins and peptides by mass spectrometry. Curr. Opin. Chem. Biol. 2001, 5:591-602.
    • (2001) Curr. Opin. Chem. Biol. , vol.5 , pp. 591-602
    • McLachlin, D.T.1    Chait, B.T.2
  • 192
    • 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., 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. 1996, 271:16510-16514.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16510-16514
    • Mehlen, P.1    Schulze-Osthoff, K.2    Arrigo, A.P.3
  • 193
    • 47249164452 scopus 로고    scopus 로고
    • The autophagic machinery is necessary for removal of cell corpses from the developing retinal neuroepithelium
    • Mellén M.A., de la Rosa E.J., Boya P. The autophagic machinery is necessary for removal of cell corpses from the developing retinal neuroepithelium. Cell Death Differ. 2008, 15:1279-1290.
    • (2008) Cell Death Differ. , vol.15 , pp. 1279-1290
    • Mellén, M.A.1    de la Rosa, E.J.2    Boya, P.3
  • 194
    • 78049490015 scopus 로고    scopus 로고
    • αA-Crystallin associates with α6 integrin receptor complexes and regulates cellular signaling
    • Menko A.S., Andley U.P. αA-Crystallin associates with α6 integrin receptor complexes and regulates cellular signaling. Exp. Eye Res. 2010, 91:640-651.
    • (2010) Exp. Eye Res. , vol.91 , pp. 640-651
    • Menko, A.S.1    Andley, U.P.2
  • 195
    • 77954142571 scopus 로고    scopus 로고
    • AlphaB-crystallin is involved in oxidative stress protection determined by VEGF in skeletal myoblasts
    • Mercatelli N., Dimauro I., Ciafré S.A., Farace M.G., Caporossi D. AlphaB-crystallin is involved in oxidative stress protection determined by VEGF in skeletal myoblasts. Free Radic. Biol. Med. 2010, 49:374-378.
    • (2010) Free Radic. Biol. Med. , vol.49 , pp. 374-378
    • Mercatelli, N.1    Dimauro, I.2    Ciafré, S.A.3    Farace, M.G.4    Caporossi, D.5
  • 196
    • 43049092658 scopus 로고    scopus 로고
    • Proteomic analysis of rat retina in a steroid-induced ocular hypertension model: potential vulnerability to oxidative stress
    • Miyara N., Shinzato M., Yamashiro Y., Iwamatsu A., Kariya K., Sawaguchi S. Proteomic analysis of rat retina in a steroid-induced ocular hypertension model: potential vulnerability to oxidative stress. Jpn. J. Ophthalmol. 2008, 52:84-90.
    • (2008) Jpn. J. Ophthalmol. , vol.52 , pp. 84-90
    • Miyara, N.1    Shinzato, M.2    Yamashiro, Y.3    Iwamatsu, A.4    Kariya, K.5    Sawaguchi, S.6
  • 197
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • Mizushima N., Levine B., Cuervo A.M., Klionsky D.J. Autophagy fights disease through cellular self-digestion. Nature 2008, 451:1069-1075.
    • (2008) Nature , vol.451 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4
  • 198
    • 33645538666 scopus 로고    scopus 로고
    • Caspase-dependent secondary lens fiber cell disintegration in alphaA-/alphaB-crystallin double-knockout mice
    • Morozov V., Wawrousek E.F. Caspase-dependent secondary lens fiber cell disintegration in alphaA-/alphaB-crystallin double-knockout mice. Development 2006, 133:813-821.
    • (2006) Development , vol.133 , pp. 813-821
    • Morozov, V.1    Wawrousek, E.F.2
  • 199
    • 0037422859 scopus 로고    scopus 로고
    • Mimicking phosphorylation of alphaB-crystallin on serine-59 is necessary and sufficient to provide maximal protection of cardiac myocytes from apoptosis
    • Morrison L.E., Hoover H.E., Thuerauf D.J., Glembotski C.C. Mimicking phosphorylation of alphaB-crystallin on serine-59 is necessary and sufficient to provide maximal protection of cardiac myocytes from apoptosis. Circ. Res. 2003, 92:203-211.
    • (2003) Circ. Res. , vol.92 , pp. 203-211
    • Morrison, L.E.1    Hoover, H.E.2    Thuerauf, D.J.3    Glembotski, C.C.4
  • 200
    • 33750600329 scopus 로고    scopus 로고
    • Chaperone-like activity of alpha-crystallin toward aldose reductase oxidatively stressed by copper ion
    • Moschini R., Marini I., Malerba M., Cappiello M., Del Corso A., Mura U. Chaperone-like activity of alpha-crystallin toward aldose reductase oxidatively stressed by copper ion. Arch. Biochem. Biophys. 2006, 453:13-17.
    • (2006) Arch. Biochem. Biophys. , vol.453 , pp. 13-17
    • Moschini, R.1    Marini, I.2    Malerba, M.3    Cappiello, M.4    Del Corso, A.5    Mura, U.6
  • 201
    • 0032477726 scopus 로고    scopus 로고
    • ATP-enhanced molecular chaperone functions of the small heat shock protein human alphaB crystallin
    • Muchowski P.J., Clark J.I. ATP-enhanced molecular chaperone functions of the small heat shock protein human alphaB crystallin. Proc. Natl. Acad. Sci. U. S. A. 1998, 95:1004-1009.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 1004-1009
    • Muchowski, P.J.1    Clark, J.I.2
  • 202
    • 11144243412 scopus 로고    scopus 로고
    • Modulation of neurodegeneration by molecular chaperones
    • Muchowski P.J., Wacker J.L. Modulation of neurodegeneration by molecular chaperones. Nat. Rev. Neurosci. 2005, 6:11-22.
    • (2005) Nat. Rev. Neurosci. , vol.6 , pp. 11-22
    • Muchowski, P.J.1    Wacker, J.L.2
  • 203
    • 0032587169 scopus 로고    scopus 로고
    • AlphaB-crystallin selectively targets intermediate filament proteins during thermal stress
    • Muchowski P.J., Valdez M.M., Clark J.I. AlphaB-crystallin selectively targets intermediate filament proteins during thermal stress. Invest. Ophthalmol. Vis. Sci. 1999, 40:951-958.
    • (1999) Invest. Ophthalmol. Vis. Sci. , vol.40 , pp. 951-958
    • Muchowski, P.J.1    Valdez, M.M.2    Clark, J.I.3
  • 204
    • 68349103136 scopus 로고    scopus 로고
    • The role of alphaA- and alphaB-crystallins in the survival of retinal ganglion cells after optic nerve axotomy
    • Munemasa Y., Kwong J.M., Caprioli J., Piri N. The role of alphaA- and alphaB-crystallins in the survival of retinal ganglion cells after optic nerve axotomy. Invest. Ophthalmol. Vis. Sci. 2009, 50:3869-3875.
    • (2009) Invest. Ophthalmol. Vis. Sci. , vol.50 , pp. 3869-3875
    • Munemasa, Y.1    Kwong, J.M.2    Caprioli, J.3    Piri, N.4
  • 205
    • 23744438797 scopus 로고    scopus 로고
    • Dicarbonyl stress and apoptosis of vascular cells: prevention by alphaB-crystallin
    • Nagaraj R.H., Oya-Ito T., Bhat M., Liu B. Dicarbonyl stress and apoptosis of vascular cells: prevention by alphaB-crystallin. Ann. N. Y. Acad. Sci. 2005, 1043:158-165.
    • (2005) Ann. N. Y. Acad. Sci. , vol.1043 , pp. 158-165
    • Nagaraj, R.H.1    Oya-Ito, T.2    Bhat, M.3    Liu, B.4
  • 206
    • 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., Hollyfield J.G. Crystallin distribution in Bruch's membrane-choroid complex from AMD and age-matched donor eyes. Exp. Eye Res. 2005, 80:821-826.
    • (2005) Exp. Eye Res. , vol.80 , pp. 821-826
    • Nakata, K.1    Crabb, J.W.2    Hollyfield, J.G.3
  • 207
    • 33750053608 scopus 로고    scopus 로고
    • AlphaB-crystallin competes with Alzheimer's disease beta-amyloid peptide for peptide-peptide interactions and induces oxidation of Abeta-Met35
    • Narayanan S., Kamps B., Boelens W.C., Reif B. alphaB-crystallin competes with Alzheimer's disease beta-amyloid peptide for peptide-peptide interactions and induces oxidation of Abeta-Met35. FEBS Lett. 2006, 580:5941-5946.
    • (2006) FEBS Lett. , vol.580 , pp. 5941-5946
    • Narayanan, S.1    Kamps, B.2    Boelens, W.C.3    Reif, B.4
  • 209
    • 0028176579 scopus 로고
    • Chaperone activity of α-crystallins modulates intermediate fi{ligature}lament assembly
    • Nicholl I.D., Quinlan R.A. Chaperone activity of α-crystallins modulates intermediate fi{ligature}lament assembly. EMBO J. 1994, 13:945-953.
    • (1994) EMBO J. , vol.13 , pp. 945-953
    • Nicholl, I.D.1    Quinlan, R.A.2
  • 210
    • 56149120271 scopus 로고    scopus 로고
    • Sensitization of RPE cells by alphaB-crystallin siRNA to SAHA-induced stage 1 apoptosis through abolishing the association of alphaB-crystallin with HDAC1 in SC35 speckles
    • Noh S.J., Jeong W.J., Rho J.H., Shin D.M., Ahn H.B., Park W.C., Rho S.H., Soung Y.H., Kim T.H., Park B.S., Yoo Y.H. Sensitization of RPE cells by alphaB-crystallin siRNA to SAHA-induced stage 1 apoptosis through abolishing the association of alphaB-crystallin with HDAC1 in SC35 speckles. Invest. Ophthalmol. Vis. Sci. 2008, 49:4753-4759.
    • (2008) Invest. Ophthalmol. Vis. Sci. , vol.49 , pp. 4753-4759
    • Noh, S.J.1    Jeong, W.J.2    Rho, J.H.3    Shin, D.M.4    Ahn, H.B.5    Park, W.C.6    Rho, S.H.7    Soung, Y.H.8    Kim, T.H.9    Park, B.S.10    Yoo, Y.H.11
  • 211
    • 84860520943 scopus 로고    scopus 로고
    • Identification of the HSPB4/TLR2/NF-κB axis in macrophage as a therapeutic target for sterile inflammation of the cornea
    • Oh J.Y., Choi H., Lee R.H., Roddy G.W., Ylöstalo J.H., Wawrousek E., Prockop D.J. Identification of the HSPB4/TLR2/NF-κB axis in macrophage as a therapeutic target for sterile inflammation of the cornea. EMBO. Mol. Med. Feb 22 2012, 4:435-440.
    • (2012) EMBO. Mol. Med. , vol.4 , pp. 435-440
    • Oh, J.Y.1    Choi, H.2    Lee, R.H.3    Roddy, G.W.4    Ylöstalo, J.H.5    Wawrousek, E.6    Prockop, D.J.7
  • 212
    • 79958098579 scopus 로고    scopus 로고
    • Parallel findings in age-related macular degeneration and Alzheimer's disease
    • Ohno-Matsui K. Parallel findings in age-related macular degeneration and Alzheimer's disease. Prog. Retin. Eye Res. 2011, 30:217-238.
    • (2011) Prog. Retin. Eye Res. , vol.30 , pp. 217-238
    • Ohno-Matsui, K.1
  • 215
    • 0031870836 scopus 로고    scopus 로고
    • The effect of glutathione upon chaperone activity of alpha-crystallin is probably mediated through target modulation
    • Pal J., Bera S., Ghosh S.K. The effect of glutathione upon chaperone activity of alpha-crystallin is probably mediated through target modulation. Ophthalmic Res. 1998, 30:271-279.
    • (1998) Ophthalmic Res. , vol.30 , pp. 271-279
    • Pal, J.1    Bera, S.2    Ghosh, S.K.3
  • 216
    • 79958761661 scopus 로고    scopus 로고
    • Functional rescue of experimental ischemic optic neuropathy with αB-crystallin
    • Pangratz-Fuehrer S., Kaur K., Ousman S.S., Steinman L., Liao Y.J. Functional rescue of experimental ischemic optic neuropathy with αB-crystallin. Eye (Lond) 2011, 25:809-817.
    • (2011) Eye (Lond) , vol.25 , pp. 809-817
    • Pangratz-Fuehrer, S.1    Kaur, K.2    Ousman, S.S.3    Steinman, L.4    Liao, Y.J.5
  • 219
    • 80053422619 scopus 로고    scopus 로고
    • Autophagy and proteotoxicity in cardiomyocytes
    • Pattison J.S., Robbins J. Autophagy and proteotoxicity in cardiomyocytes. Autophagy 2011, 7:1259-1260.
    • (2011) Autophagy , vol.7 , pp. 1259-1260
    • Pattison, J.S.1    Robbins, J.2
  • 222
    • 79960664223 scopus 로고    scopus 로고
    • Activation of autophagy in a rat model of retinal ischemia following high intraocular pressure
    • Piras A., Gianetto D., Conte D., Bosone A., Vercelli A. Activation of autophagy in a rat model of retinal ischemia following high intraocular pressure. PLoS One 2011, 6:e22514.
    • (2011) PLoS One , vol.6
    • Piras, A.1    Gianetto, D.2    Conte, D.3    Bosone, A.4    Vercelli, A.5
  • 223
    • 33847677726 scopus 로고    scopus 로고
    • Modulation of alpha and beta crystallin expression in rat retinas with ocular hypertension-induced ganglion cell degeneration
    • Piri N., Song M., Kwong J.M., Caprioli J. Modulation of alpha and beta crystallin expression in rat retinas with ocular hypertension-induced ganglion cell degeneration. Brain Res. 2007, 1141:1-9.
    • (2007) Brain Res. , vol.1141 , pp. 1-9
    • Piri, N.1    Song, M.2    Kwong, J.M.3    Caprioli, J.4
  • 224
    • 0029956553 scopus 로고    scopus 로고
    • Effects of site-directed mutations on the chaperone-like activity of alphaB-crystallin
    • Plater M.L., Goode D., Crabbe M.J. Effects of site-directed mutations on the chaperone-like activity of alphaB-crystallin. J. Biol. Chem. 1996, 271:28558-28566.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28558-28566
    • Plater, M.L.1    Goode, D.2    Crabbe, M.J.3
  • 225
    • 1542646989 scopus 로고    scopus 로고
    • A comparative view of alpha crystallins: the contribution of comparative studies to understanding function
    • Posner M. A comparative view of alpha crystallins: the contribution of comparative studies to understanding function. Integr. Comp. Biol. 2003, 43:481-491.
    • (2003) Integr. Comp. Biol. , vol.43 , pp. 481-491
    • Posner, M.1
  • 227
    • 0029929571 scopus 로고    scopus 로고
    • The intermediate filament cytoskeleton of the lens: an ever changing network through development and differentiation. A minireview
    • Prescott A.R., Sandilands A., Hutcheson A.M., Carter J.M., Quinlan R.A. The intermediate filament cytoskeleton of the lens: an ever changing network through development and differentiation. A minireview. Ophthalmic Res. 1996, 28:58-61.
    • (1996) Ophthalmic Res. , vol.28 , pp. 58-61
    • Prescott, A.R.1    Sandilands, A.2    Hutcheson, A.M.3    Carter, J.M.4    Quinlan, R.A.5
  • 228
    • 58149141478 scopus 로고    scopus 로고
    • Stimulation of the insulin/mTOR pathway delays cone death in a mouse model of retinitis pigmentosa
    • Punzo C., Kornacker K., Cepko C.L. Stimulation of the insulin/mTOR pathway delays cone death in a mouse model of retinitis pigmentosa. Nat. Neurosci. 2009, 12:44-52.
    • (2009) Nat. Neurosci. , vol.12 , pp. 44-52
    • Punzo, C.1    Kornacker, K.2    Cepko, C.L.3
  • 229
    • 0010503986 scopus 로고
    • Complete structure of the alpha B-crystallin gene: conservation of the exon-intron distribution in the two nonlinked alpha-crystallin genes
    • Quax-Jeuken Y., Quax W., van Rens G., Khan P.M., Bloemendal H. Complete structure of the alpha B-crystallin gene: conservation of the exon-intron distribution in the two nonlinked alpha-crystallin genes. Proc. Natl. Acad. Sci. U. S. A. 1985, 82:5819-5823.
    • (1985) Proc. Natl. Acad. Sci. U. S. A. , vol.82 , pp. 5819-5823
    • Quax-Jeuken, Y.1    Quax, W.2    van Rens, G.3    Khan, P.M.4    Bloemendal, H.5
  • 231
    • 79955471279 scopus 로고    scopus 로고
    • Identification and characterization of a copper-binding site in αA-crystallin
    • Raju M., Santhoshkumar P., Henzl T.M., Sharma K.K. Identification and characterization of a copper-binding site in αA-crystallin. Free Radic. Biol. Med. 2011, 50:1429-1436.
    • (2011) Free Radic. Biol. Med. , vol.50 , pp. 1429-1436
    • Raju, M.1    Santhoshkumar, P.2    Henzl, T.M.3    Sharma, K.K.4
  • 232
    • 0027973129 scopus 로고
    • Chaperone-like activity and quaternary structure of alpha-crystallin
    • Raman B., Rao C.M. Chaperone-like activity and quaternary structure of alpha-crystallin. J. Biol. Chem. 1994, 269:27264-27268.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27264-27268
    • Raman, B.1    Rao, C.M.2
  • 233
    • 0029117227 scopus 로고
    • Rapid refolding studies on the chaperone-like alpha-crystallin. Effect of alpha-crystallin on refolding of beta- and gamma-crystallins
    • Raman B., Ramakrishna T., Rao C.M. Rapid refolding studies on the chaperone-like alpha-crystallin. Effect of alpha-crystallin on refolding of beta- and gamma-crystallins. J. Biol. Chem. 1995, 270:19888-19892.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19888-19892
    • Raman, B.1    Ramakrishna, T.2    Rao, C.M.3
  • 234
    • 29644445485 scopus 로고    scopus 로고
    • AlphaB-crystallin, a small heat-shock protein, prevents the amyloid fibril growth of an amyloid beta-peptide and beta2-microglobulin
    • Raman B., Ban T., Sakai M., Pasta S.Y., Ramakrishna T., Naiki H., Goto Y., Rao Ch.M. AlphaB-crystallin, a small heat-shock protein, prevents the amyloid fibril growth of an amyloid beta-peptide and beta2-microglobulin. Biochem. J. 2005, 392:573-581.
    • (2005) Biochem. J. , vol.392 , pp. 573-581
    • Raman, B.1    Ban, T.2    Sakai, M.3    Pasta, S.Y.4    Ramakrishna, T.5    Naiki, H.6    Goto, Y.7    Rao, C.8
  • 235
    • 84867395428 scopus 로고    scopus 로고
    • Alpha A crystallin down regulates innate and adaptive immune response in experimental autoimmune uveitis
    • (E-Abstract)
    • Rao N.A., Saraswathy S. Alpha A crystallin down regulates innate and adaptive immune response in experimental autoimmune uveitis. Invest. Ophthalmol. Vis. Sci. 2009, 50:6025. (E-Abstract).
    • (2009) Invest. Ophthalmol. Vis. Sci. , vol.50 , pp. 6025
    • Rao, N.A.1    Saraswathy, S.2
  • 236
    • 41949083991 scopus 로고    scopus 로고
    • Elevated retina-specific expression of the small heat shock protein, alphaA-crystallin, is associated with photoreceptor protection in experimental uveitis
    • Rao N.A., Saraswathy S., Wu G.S., Katselis G.S., Wawrousek E.F., Bhat S. Elevated retina-specific expression of the small heat shock protein, alphaA-crystallin, is associated with photoreceptor protection in experimental uveitis. Invest. Ophthalmol. Vis. Sci. 2008, 49:1161-1171.
    • (2008) Invest. Ophthalmol. Vis. Sci. , vol.49 , pp. 1161-1171
    • Rao, N.A.1    Saraswathy, S.2    Wu, G.S.3    Katselis, G.S.4    Wawrousek, E.F.5    Bhat, S.6
  • 237
    • 84859114916 scopus 로고    scopus 로고
    • Small heat shock protein alpha crystallin prevents photoreceptor degeneration in experimental autoimmune uveitis
    • (Epub 2012 March 30)
    • Rao N.A., Saraswathy S., Pararajasegaram G., Bhat S.P. Small heat shock protein alpha crystallin prevents photoreceptor degeneration in experimental autoimmune uveitis. PLoS One 2012, 7(3):e33582. (Epub 2012 March 30).
    • (2012) PLoS One , vol.7 , Issue.3
    • Rao, N.A.1    Saraswathy, S.2    Pararajasegaram, G.3    Bhat, S.P.4
  • 238
    • 58149202714 scopus 로고    scopus 로고
    • Superoxide dismutase loaded PLGA nanoparticles protect cultured human neurons under oxidative stress
    • Reddy M.K., Wu L., Kou W., Ghorpade A., Labhasetwar V. Superoxide dismutase loaded PLGA nanoparticles protect cultured human neurons under oxidative stress. Appl. Biochem. Biotechnol. 2008, 151:565-577.
    • (2008) Appl. Biochem. Biotechnol. , vol.151 , pp. 565-577
    • Reddy, M.K.1    Wu, L.2    Kou, W.3    Ghorpade, A.4    Labhasetwar, V.5
  • 239
    • 1242339668 scopus 로고    scopus 로고
    • Structural changes in alpha-crystallin and whole eye lens during heating, observed by low-angle X-ray diffraction
    • Regini J.W., Grossmann J.G., Burgio M.R., Malik N.S., Koretz J.F., Hodson S.A., Elliott G.F. Structural changes in alpha-crystallin and whole eye lens during heating, observed by low-angle X-ray diffraction. J. Mol. Biol. 2004, 336:1185-1194.
    • (2004) J. Mol. Biol. , vol.336 , pp. 1185-1194
    • Regini, J.W.1    Grossmann, J.G.2    Burgio, M.R.3    Malik, N.S.4    Koretz, J.F.5    Hodson, S.A.6    Elliott, G.F.7
  • 243
    • 0029817433 scopus 로고    scopus 로고
    • Differential expression of alpha A- and alpha B-crystallin during murine ocular development
    • Robinson M.L., Overbeek P.A. Differential expression of alpha A- and alpha B-crystallin during murine ocular development. Invest. Ophthalmol. Vis. Sci. 1996, 37:2276-2284.
    • (1996) Invest. Ophthalmol. Vis. Sci. , vol.37 , pp. 2276-2284
    • Robinson, M.L.1    Overbeek, P.A.2
  • 244
    • 84856760438 scopus 로고    scopus 로고
    • Autophagy promotes survival of retinal ganglion cells after optic nerve axotomy in mice
    • Rodríguez-Muela N., Germain F., Mariño G., Fitze P.S., Boya P. Autophagy promotes survival of retinal ganglion cells after optic nerve axotomy in mice. Cell Death Differ. 2012, 19:162-169.
    • (2012) Cell Death Differ. , vol.19 , pp. 162-169
    • Rodríguez-Muela, N.1    Germain, F.2    Mariño, G.3    Fitze, P.S.4    Boya, P.5
  • 247
    • 84055216939 scopus 로고    scopus 로고
    • αB-crystallin, an effector of unfolded protein response, confers anti-VEGF resistance to breast cancer via maintenance of intracrine VEGF in endothelial cells
    • Ruan Q., Han S., Jiang W.G., Boulton M.E., Chen Z.J., Law B.K., Cai J. αB-crystallin, an effector of unfolded protein response, confers anti-VEGF resistance to breast cancer via maintenance of intracrine VEGF in endothelial cells. Mol. Cancer Res. 2011, 9:1632-1643.
    • (2011) Mol. Cancer Res. , vol.9 , pp. 1632-1643
    • Ruan, Q.1    Han, S.2    Jiang, W.G.3    Boulton, M.E.4    Chen, Z.J.5    Law, B.K.6    Cai, J.7
  • 253
    • 0035476853 scopus 로고    scopus 로고
    • Expression of small heat shock proteins and intermediate filaments in the human optic nerve head astrocytes exposed to elevated hydrostatic pressure in vitro
    • Salvador-Silva M., Ricard C.S., Agapova O.A., Yang P., Hernandez M.R. Expression of small heat shock proteins and intermediate filaments in the human optic nerve head astrocytes exposed to elevated hydrostatic pressure in vitro. J. Neurosci. Res. 2001, 66:59-73.
    • (2001) J. Neurosci. Res. , vol.66 , pp. 59-73
    • Salvador-Silva, M.1    Ricard, C.S.2    Agapova, O.A.3    Yang, P.4    Hernandez, M.R.5
  • 255
    • 0035861759 scopus 로고    scopus 로고
    • Phe71 is essential for chaperone-like function in alpha A-crystallin
    • Santhoshkumar P., Sharma K.K. Phe71 is essential for chaperone-like function in alpha A-crystallin. J. Biol. Chem. 2001, 276:47094-47099.
    • (2001) J. Biol. Chem. , vol.276 , pp. 47094-47099
    • Santhoshkumar, P.1    Sharma, K.K.2
  • 256
    • 9444229933 scopus 로고    scopus 로고
    • Inhibition of amyloid fibrillogenesis and toxicity by a peptide chaperone
    • Santhoshkumar P., Sharma K.K. Inhibition of amyloid fibrillogenesis and toxicity by a peptide chaperone. Mol. Cell Biochem. 2004, 267:147-155.
    • (2004) Mol. Cell Biochem. , vol.267 , pp. 147-155
    • Santhoshkumar, P.1    Sharma, K.K.2
  • 257
    • 79955709128 scopus 로고    scopus 로고
    • αA-crystallin peptide SDRDKFVIFLDVKHF accumulating in aging lens impairs the function of α-crystallin and induces lens protein aggregation
    • Santhoshkumar P., Raju M., Sharma K.K. αA-crystallin peptide SDRDKFVIFLDVKHF accumulating in aging lens impairs the function of α-crystallin and induces lens protein aggregation. PLoS One 2011, 6:e19291.
    • (2011) PLoS One , vol.6
    • Santhoshkumar, P.1    Raju, M.2    Sharma, K.K.3
  • 258
    • 73349101064 scopus 로고    scopus 로고
    • Mitochondrial proteomics in experimental autoimmune uveitis oxidative stress
    • Saraswathy S., Rao N.A. Mitochondrial proteomics in experimental autoimmune uveitis oxidative stress. Invest. Ophthalmol. Vis. Sci. 2009, 50:5559-5566.
    • (2009) Invest. Ophthalmol. Vis. Sci. , vol.50 , pp. 5559-5566
    • Saraswathy, S.1    Rao, N.A.2
  • 259
    • 69549134412 scopus 로고    scopus 로고
    • Alpha-B-crystallin as a tissue marker of epileptic foci in paediatric resections
    • Sarnat H.B., Flores-Sarnat L. Alpha-B-crystallin as a tissue marker of epileptic foci in paediatric resections. Can. J. Neurol. Sci. 2009, 36:566-574.
    • (2009) Can. J. Neurol. Sci. , vol.36 , pp. 566-574
    • Sarnat, H.B.1    Flores-Sarnat, L.2
  • 262
    • 84867331182 scopus 로고    scopus 로고
    • Phosphorylation-dependent subcellular localization of the small heat shock proteins HspB1/Hsp25 and HspB5/αB-crystallin in cultured hippocampal neurons
    • May 23. (Epub ahead of print)
    • Schmidt T., Bartelt-Kirbach B., Golenhofen N. Phosphorylation-dependent subcellular localization of the small heat shock proteins HspB1/Hsp25 and HspB5/αB-crystallin in cultured hippocampal neurons. Histochem. Cell. Biol 2012, May 23. (Epub ahead of print).
    • (2012) Histochem. Cell. Biol
    • Schmidt, T.1    Bartelt-Kirbach, B.2    Golenhofen, N.3
  • 263
    • 79951941623 scopus 로고    scopus 로고
    • Myofibrillar myopathies
    • Selcen D. Myofibrillar myopathies. Neuromuscul. Disord. 2011, 21:161-171.
    • (2011) Neuromuscul. Disord. , vol.21 , pp. 161-171
    • Selcen, D.1
  • 265
    • 0031561418 scopus 로고    scopus 로고
    • Functional elements in molecular chaperone α-crystallin: Identification of binding sites in αB-crystallin
    • Sharma K.K., Kaur H., Kester K. Functional elements in molecular chaperone α-crystallin: Identification of binding sites in αB-crystallin. Biochem. Biophys. Res. Commun. 1997, 239:217-222.
    • (1997) Biochem. Biophys. Res. Commun. , vol.239 , pp. 217-222
    • Sharma, K.K.1    Kaur, H.2    Kester, K.3
  • 266
    • 0034635397 scopus 로고    scopus 로고
    • Synthesis and characterization of a peptide identified as a functional element in αA-crystallin
    • Sharma K.K., Kumar R.S., Kumar G.S., Quinn P.T. Synthesis and characterization of a peptide identified as a functional element in αA-crystallin. J. Biol. Chem. 2000, 275:3767-3771.
    • (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
  • 267
    • 67349215120 scopus 로고    scopus 로고
    • AlphaB-crystallin suppresses oxidative stress induced astrocyte apoptosis by inhibiting caspase-3 activation
    • Shin J.H., Kim S.W., Lim C.M., Jeong J.Y., Piao C.S., Lee J.K. alphaB-crystallin suppresses oxidative stress induced astrocyte apoptosis by inhibiting caspase-3 activation. Neurosci. Res. 2009, 64:355-361.
    • (2009) Neurosci. Res. , vol.64 , pp. 355-361
    • Shin, J.H.1    Kim, S.W.2    Lim, C.M.3    Jeong, J.Y.4    Piao, C.S.5    Lee, J.K.6
  • 268
    • 0027330972 scopus 로고
    • Alpha B crystallin and HSP28 are enhanced in the cerebral cortex of patients with Alzheimer's disease
    • Shinohara H., Inaguma Y., Goto S., Inagaki T., Kato K. Alpha B crystallin and HSP28 are enhanced in the cerebral cortex of patients with Alzheimer's disease. J. Neurol. Sci. 1993, 119:203-208.
    • (1993) J. Neurol. Sci. , vol.119 , pp. 203-208
    • Shinohara, H.1    Inaguma, Y.2    Goto, S.3    Inagaki, T.4    Kato, K.5
  • 270
    • 55749112807 scopus 로고    scopus 로고
    • Proteomic profiling of exosomes: current perspectives
    • Simpson R.J., Jensen S.S., Lim J.W. Proteomic profiling of exosomes: current perspectives. Proteomics 2008, 8:4083-4099.
    • (2008) Proteomics , vol.8 , pp. 4083-4099
    • Simpson, R.J.1    Jensen, S.S.2    Lim, J.W.3
  • 272
    • 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., 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. 2005, 31:292-303.
    • (2005) Neuropathol. Appl. Neurobiol. , vol.31 , pp. 292-303
    • Sinclair, C.1    Mirakhur, M.2    Kirk, J.3    Farrell, M.4    McQuaid, S.5
  • 273
    • 33846618592 scopus 로고    scopus 로고
    • Association of alphaB crystallin, a small heat shock protein, with actin: role in modulating actin filament dynamics in vivo
    • Singh B.N., Rao K.S., Ramakrishna T., Rangaraj N., Rao ChM. Association of alphaB crystallin, a small heat shock protein, with actin: role in modulating actin filament dynamics in vivo. J. Mol. Biol. 2007, 366:756-767.
    • (2007) J. Mol. Biol. , vol.366 , pp. 756-767
    • Singh, B.N.1    Rao, K.S.2    Ramakrishna, T.3    Rangaraj, N.4    Rao, C.5
  • 274
    • 77649272915 scopus 로고    scopus 로고
    • Ubiquitin-proteasome-mediated degradation and synthesis of MyoD is modulated by alphaB-crystallin, a small heat shockprotein, during muscle differentiation
    • Singh B.N., Rao K.S., Rao Ch.M. Ubiquitin-proteasome-mediated degradation and synthesis of MyoD is modulated by alphaB-crystallin, a small heat shockprotein, during muscle differentiation. Biochim. Biophys. Acta 2010, 1803:288-299.
    • (2010) Biochim. Biophys. Acta , vol.1803 , pp. 288-299
    • Singh, B.N.1    Rao, K.S.2    Rao, C.3
  • 275
    • 0027074090 scopus 로고
    • Identification of the posttranslational modifications of bovine lens alpha B-crystallins by mass spectrometry
    • Smith J.B., Sun Y., Smith D.L., Green B. Identification of the posttranslational modifications of bovine lens alpha B-crystallins by mass spectrometry. Protein Sci. 1992, 1:601-608.
    • (1992) Protein Sci. , vol.1 , pp. 601-608
    • Smith, J.B.1    Sun, Y.2    Smith, D.L.3    Green, B.4
  • 279
    • 78149428751 scopus 로고    scopus 로고
    • αB crystallin is apically secreted within exosomes by polarized human retinal pigment epithelium and provides neuroprotection to adjacent cells
    • Sreekumar P.G., Kannan R., Kitamura M., Spee C., Barron E., Ryan S.J., Hinton D.R. αB crystallin is apically secreted within exosomes by polarized human retinal pigment epithelium and provides neuroprotection to adjacent cells. PLoS One 2010, 5(10):e12578.
    • (2010) PLoS One , vol.5 , Issue.10
    • Sreekumar, P.G.1    Kannan, R.2    Kitamura, M.3    Spee, C.4    Barron, E.5    Ryan, S.J.6    Hinton, D.R.7
  • 280
    • 84867402530 scopus 로고    scopus 로고
    • Methionine sulfoxide reductase A: structure, function and role in ocular pathology
    • Sreekumar P.G., Hinton D.R., Kannan R. Methionine sulfoxide reductase A: structure, function and role in ocular pathology. World J. Biol. Chem. 2011, 2:184-192.
    • (2011) World J. Biol. Chem. , vol.2 , pp. 184-192
    • Sreekumar, P.G.1    Hinton, D.R.2    Kannan, R.3
  • 281
    • 84858611567 scopus 로고    scopus 로고
    • Mechanism of RPE cell death in α-crystallin deficient mice: a novel and critical role for MRP1-mediated GSH efflux
    • Sreekumar P.G., Spee C., Ryan S.J., Cole S.P.C., Kannan R., Hinton D.R. Mechanism of RPE cell death in α-crystallin deficient mice: a novel and critical role for MRP1-mediated GSH efflux. PLoS One 2012, 7(3):e33420.
    • (2012) PLoS One , vol.7 , Issue.3
    • Sreekumar, P.G.1    Spee, C.2    Ryan, S.J.3    Cole, S.P.C.4    Kannan, R.5    Hinton, D.R.6
  • 283
    • 24644480940 scopus 로고    scopus 로고
    • Recognition sequence 2 (residues 60-71) plays a role in oligomerization and exchange dynamics of alphaB-crystallin
    • Sreelakshmi Y., Sharma K.K. Recognition sequence 2 (residues 60-71) plays a role in oligomerization and exchange dynamics of alphaB-crystallin. Biochemistry 2005, 44:12245-12252.
    • (2005) Biochemistry , vol.44 , pp. 12245-12252
    • Sreelakshmi, Y.1    Sharma, K.K.2
  • 284
    • 10844246436 scopus 로고    scopus 로고
    • AlphaA-crystallin interacting regions in the small heat shock protein, alphaB-crystallin
    • Sreelakshmi Y., Santhoshkumar P., Bhattacharyya J., Sharma K.K. AlphaA-crystallin interacting regions in the small heat shock protein, alphaB-crystallin. Biochemistry 2004, 43:15785-15795.
    • (2004) Biochemistry , vol.43 , pp. 15785-15795
    • Sreelakshmi, Y.1    Santhoshkumar, P.2    Bhattacharyya, J.3    Sharma, K.K.4
  • 285
    • 52649112681 scopus 로고    scopus 로고
    • Effect of trifluoroethanol on the structural and functional properties of alpha-crystallin
    • Srinivas V., Santhoshkumar P., Sharma K.K. Effect of trifluoroethanol on the structural and functional properties of alpha-crystallin. J. Protein Chem. 2002, 21:87-95.
    • (2002) J. Protein Chem. , vol.21 , pp. 87-95
    • Srinivas, V.1    Santhoshkumar, P.2    Sharma, K.K.3
  • 286
    • 0026470980 scopus 로고
    • Alpha A-crystallin is expressed in non-ocular tissues
    • Srinivasan A.N., Nagineni C.N., Bhat S.P. alpha A-crystallin is expressed in non-ocular tissues. J. Biol. Chem. 1992, 267:23337-23341.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23337-23341
    • Srinivasan, A.N.1    Nagineni, C.N.2    Bhat, S.P.3
  • 288
    • 29144527460 scopus 로고    scopus 로고
    • Small heat shock proteins: molecular structure and chaperone function
    • Sun Y., MacRae T.H. Small heat shock proteins: molecular structure and chaperone function. Cell Mol. Life Sci. 2005, 62:2460-2476.
    • (2005) Cell Mol. Life Sci. , vol.62 , pp. 2460-2476
    • Sun, Y.1    MacRae, T.H.2
  • 289
    • 12444341944 scopus 로고    scopus 로고
    • Toll-like receptors in innate immunity
    • Takeda K., Akira S. Toll-like receptors in innate immunity. Int. Immunol. 2005, 17:1-14.
    • (2005) Int. Immunol. , vol.17 , pp. 1-14
    • Takeda, K.1    Akira, S.2
  • 290
    • 0029992808 scopus 로고    scopus 로고
    • Differential phosphorylation of alpha-A crystallin in human lens of different age
    • Takemoto L.J. Differential phosphorylation of alpha-A crystallin in human lens of different age. Exp. Eye Res. 1996, 62:499-504.
    • (1996) Exp. Eye Res. , vol.62 , pp. 499-504
    • Takemoto, L.J.1
  • 291
    • 40149109190 scopus 로고    scopus 로고
    • Amyloid fibril formation and chaperone-like activity of peptides from alphaA-crystallin
    • Tanaka N., Tanaka R., Tokuhara M., Kunugi S., Lee Y.F., Hamada D. Amyloid fibril formation and chaperone-like activity of peptides from alphaA-crystallin. Biochemistry 2008, 47:2961-2967.
    • (2008) Biochemistry , vol.47 , pp. 2961-2967
    • Tanaka, N.1    Tanaka, R.2    Tokuhara, M.3    Kunugi, S.4    Lee, Y.F.5    Hamada, D.6
  • 292
    • 41149138739 scopus 로고    scopus 로고
    • Alpha B-crystallin is a cytoplasmic interaction partner of the kidney-specific cadherin-16
    • Thedieck C., Kalbacher H., Kratzer U., Lammers R., Stevanovic S., Klein G. alpha B-crystallin is a cytoplasmic interaction partner of the kidney-specific cadherin-16. J. Mol. Biol. 2008, 378:145-153.
    • (2008) J. Mol. Biol. , vol.378 , pp. 145-153
    • Thedieck, C.1    Kalbacher, H.2    Kratzer, U.3    Lammers, R.4    Stevanovic, S.5    Klein, G.6
  • 293
    • 43249109372 scopus 로고    scopus 로고
    • Isolation and characterization of exosomes from cell culture supernatants and biological fluids
    • (Chapter 3): Unit 3.22
    • Théry C., Amigorena S., Raposo G., Clayton A. Isolation and characterization of exosomes from cell culture supernatants and biological fluids. Curr. Protoc. Cell Biol. 2006, (Chapter 3): Unit 3.22.
    • (2006) Curr. Protoc. Cell Biol.
    • Théry, C.1    Amigorena, S.2    Raposo, G.3    Clayton, A.4
  • 294
    • 68849129712 scopus 로고    scopus 로고
    • Membrane vesicles as conveyors of immune responses
    • Théry C., Ostrowski M., Segura E. Membrane vesicles as conveyors of immune responses. Nat. Rev. Immunol. 2009, 9:581-593.
    • (2009) Nat. Rev. Immunol. , vol.9 , pp. 581-593
    • Théry, C.1    Ostrowski, M.2    Segura, E.3
  • 295
    • 0025869777 scopus 로고
    • Rosenthal fibers share epitopes with alpha B-crystallin, glial fibrillary acidic protein, and ubiquitin, but not with vimentin. Immunoelectron microscopy with colloidal gold
    • Tomokane N., Iwaki T., Tateishi J., Iwaki A., Goldman J.E. Rosenthal fibers share epitopes with alpha B-crystallin, glial fibrillary acidic protein, and ubiquitin, but not with vimentin. Immunoelectron microscopy with colloidal gold. Am. J. Pathol. 1991, 138:875-885.
    • (1991) Am. J. Pathol. , vol.138 , pp. 875-885
    • Tomokane, N.1    Iwaki, T.2    Tateishi, J.3    Iwaki, A.4    Goldman, J.E.5
  • 303
    • 33947359008 scopus 로고    scopus 로고
    • Identification of differentially regulated proteins in a patient with Leber's Congenital Amaurosis-aproteomic study
    • Vorum H., Østergaard M., Rice G.E., Honoré B., Bek T. Identification of differentially regulated proteins in a patient with Leber's Congenital Amaurosis-aproteomic study. Proteome Sci. 2007, 5:5.
    • (2007) Proteome Sci. , vol.5 , pp. 5
    • Vorum, H.1    Østergaard, M.2    Rice, G.E.3    Honoré, B.4    Bek, T.5
  • 304
    • 46849116411 scopus 로고    scopus 로고
    • Structural and functional diversities between members of the human HSPB, HSPH, HSPA, and DNAJ chaperone families
    • Vos M.J., Hageman J., Carra S., Kampinga H.H. Structural and functional diversities between members of the human HSPB, HSPH, HSPA, and DNAJ chaperone families. Biochemistry 2008, 47:7001-7011.
    • (2008) Biochemistry , vol.47 , pp. 7001-7011
    • Vos, M.J.1    Hageman, J.2    Carra, S.3    Kampinga, H.H.4
  • 305
    • 0033863553 scopus 로고    scopus 로고
    • Alpha-crystallin prevents irreversible protein denaturation and acts cooperatively with other heat-shock proteins to renature the stabilized partially denatured protein in an ATP-dependent manner
    • Wang K., Spector A. alpha-crystallin prevents irreversible protein denaturation and acts cooperatively with other heat-shock proteins to renature the stabilized partially denatured protein in an ATP-dependent manner. Eur. J. Biochem. 2000, 267:4705-4712.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4705-4712
    • Wang, K.1    Spector, A.2
  • 306
    • 0029018625 scopus 로고
    • 2 but phosphorylation has no effect on chaperone activity
    • 2 but phosphorylation has no effect on chaperone activity. Exp. Eye Res. 1995, 61:115-124.
    • (1995) Exp. Eye Res. , vol.61 , pp. 115-124
    • Wang, K.1    Ma, W.2    Spector, A.3
  • 307
    • 35649011558 scopus 로고    scopus 로고
    • Comparative proteome analysis of neural retinas from type 2 diabetic rats by two-dimensional electrophoresis
    • Wang Y.D., Wu J.D., Jiang Z.L., Wang Y.B., Wang X.H., Liu C., Tong M.Q. Comparative proteome analysis of neural retinas from type 2 diabetic rats by two-dimensional electrophoresis. Curr. Eye Res. 2007, 32:891-901.
    • (2007) Curr. Eye Res. , vol.32 , pp. 891-901
    • Wang, Y.D.1    Wu, J.D.2    Jiang, Z.L.3    Wang, Y.B.4    Wang, X.H.5    Liu, C.6    Tong, M.Q.7
  • 309
    • 58349109733 scopus 로고    scopus 로고
    • Autophagy and exosomes in the aged retinal pigment epithelium: possible relevance to drusen formation and age-related macular degeneration
    • Wang A.L., Lukas T.J., Yuan M., Du N., Tso M.O., Neufeld A.H. Autophagy and exosomes in the aged retinal pigment epithelium: possible relevance to drusen formation and age-related macular degeneration. PLoS One 2009, 4:e4160.
    • (2009) PLoS One , vol.4
    • Wang, A.L.1    Lukas, T.J.2    Yuan, M.3    Du, N.4    Tso, M.O.5    Neufeld, A.H.6
  • 310
    • 65549156409 scopus 로고    scopus 로고
    • Amyloid-beta up-regulates complement factor B in retinal pigment epithelial cells through cytokines released from recruited macrophages/microglia: another mechanism of complement activation in age-related macular degeneration
    • Wang J., Ohno-Matsui K., Yoshida T., Shimada N., Ichinose S., Sato T., Mochizuki M., Morita I. Amyloid-beta up-regulates complement factor B in retinal pigment epithelial cells through cytokines released from recruited macrophages/microglia: another mechanism of complement activation in age-related macular degeneration. J. Cell Physiol. 2009, 220:119-128.
    • (2009) J. Cell Physiol. , vol.220 , pp. 119-128
    • Wang, J.1    Ohno-Matsui, K.2    Yoshida, T.3    Shimada, N.4    Ichinose, S.5    Sato, T.6    Mochizuki, M.7    Morita, I.8
  • 311
    • 69949180640 scopus 로고    scopus 로고
    • TOR-mediated autophagy regulates cell death in Drosophila neurodegenerative disease
    • Wang T., Lao U., Edgar B.A. TOR-mediated autophagy regulates cell death in Drosophila neurodegenerative disease. J. Cell Biol. 2009, 186:703-711.
    • (2009) J. Cell Biol. , vol.186 , pp. 703-711
    • Wang, T.1    Lao, U.2    Edgar, B.A.3
  • 317
    • 0031887317 scopus 로고    scopus 로고
    • Alpha B-crystallin is associated with intermediate filaments in astrocytoma cells
    • Wisniewski T., Goldman J.E. Alpha B-crystallin is associated with intermediate filaments in astrocytoma cells. Neurochem. Res. 1998, 23:385-392.
    • (1998) Neurochem. Res. , vol.23 , pp. 385-392
    • Wisniewski, T.1    Goldman, J.E.2
  • 318
    • 66149103249 scopus 로고    scopus 로고
    • Alpha-Crystallin downregulates the expression of TNF-alpha and iNOS by activated rat retinal microglia in vitro and in vivo
    • Wu N., Wang Y.H., Zhao H.S., Liu D.N., Ying X., Yin Z.Q., Wang Y. alpha-Crystallin downregulates the expression of TNF-alpha and iNOS by activated rat retinal microglia in vitro and in vivo. Ophthalmic Res. 2009, 42:21-28.
    • (2009) Ophthalmic Res. , vol.42 , pp. 21-28
    • Wu, N.1    Wang, Y.H.2    Zhao, H.S.3    Liu, D.N.4    Ying, X.5    Yin, Z.Q.6    Wang, Y.7
  • 319
    • 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., Andley U.P. A comprehensive analysis of the expression of crystallins in mouse retina. Mol. Vis. 2003, 9:410-419.
    • (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
  • 320
    • 33744475377 scopus 로고    scopus 로고
    • Alpha-crystallin expression affects microtubule assembly and prevents their aggregation
    • Xi J.H., Bai F., McGaha R., Andley U.P. Alpha-crystallin expression affects microtubule assembly and prevents their aggregation. FASEB J. 2006, 20:846-857.
    • (2006) FASEB J. , vol.20 , pp. 846-857
    • Xi, J.H.1    Bai, F.2    McGaha, R.3    Andley, U.P.4
  • 321
    • 34147145520 scopus 로고    scopus 로고
    • Alpha-Crystallin distribution in retinal pigment epithelium and effect of gene knockouts on sensitivity to oxidative stress
    • Yaung J., Jin M., Barron E., Spee C., Wawrousek E.F., Kannan R., Hinton D.R. alpha-Crystallin distribution in retinal pigment epithelium and effect of gene knockouts on sensitivity to oxidative stress. Mol. Vis. 2007, 13:566-577.
    • (2007) Mol. Vis. , vol.13 , pp. 566-577
    • Yaung, J.1    Jin, M.2    Barron, E.3    Spee, C.4    Wawrousek, E.F.5    Kannan, R.6    Hinton, D.R.7
  • 322
    • 39149145829 scopus 로고    scopus 로고
    • Exacerbation of retinal degeneration in the absence of alpha crystallins in an in vivo model of chemically induced hypoxia
    • Yaung J., Kannan R., Wawrousek E.F., Spee C., Sreekumar P.G., Hinton D.R. Exacerbation of retinal degeneration in the absence of alpha crystallins in an in vivo model of chemically induced hypoxia. Exp. Eye Res. 2008, 86:355-365.
    • (2008) Exp. Eye Res. , vol.86 , pp. 355-365
    • Yaung, J.1    Kannan, R.2    Wawrousek, E.F.3    Spee, C.4    Sreekumar, P.G.5    Hinton, D.R.6
  • 325
    • 0026632361 scopus 로고
    • Heat shock protein 27 and alpha B-crystallin can form a complex, which dissociates by heat shock
    • Zantema A., Verlaan-De Vries M., Maasdam D., Bol S., van der Eb A. Heat shock protein 27 and alpha B-crystallin can form a complex, which dissociates by heat shock. J. Biol. Chem. 1992, 267:12936-12941.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12936-12941
    • Zantema, A.1    Verlaan-De Vries, M.2    Maasdam, D.3    Bol, S.4    van der Eb, A.5
  • 326
    • 84866057223 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of retina in oxygen-induced retinopathy mice using iTRAQ with 2D NanoLC-nanoESI-MS/MS
    • Zhou L., Xinling L., Koh S.K., Xiaorong L., Beuerman R.W. Quantitative proteomic analysis of retina in oxygen-induced retinopathy mice using iTRAQ with 2D NanoLC-nanoESI-MS/MS. JIOMICS 2011, 1:226-235.
    • (2011) JIOMICS , vol.1 , pp. 226-235
    • Zhou, L.1    Xinling, L.2    Koh, S.K.3    Xiaorong, L.4    Beuerman, R.W.5
  • 327
    • 84860230383 scopus 로고    scopus 로고
    • AlphaA crystallin in the pathogenesis and intervention of experimental murine corneal neovascularization
    • Zhu W., Qi X., Ren S., Jia C., Song Z., Wang Y. AlphaA crystallin in the pathogenesis and intervention of experimental murine corneal neovascularization. Exp. Eye Res. 2012, 98C:44-51.
    • (2012) Exp. Eye Res. , vol.98 C , pp. 44-51
    • Zhu, W.1    Qi, X.2    Ren, S.3    Jia, C.4    Song, Z.5    Wang, Y.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.