메뉴 건너뛰기




Volumn 54, Issue 38, 2015, Pages 5949-5958

Species-Specific Structural and Functional Divergence of α-Crystallins: Zebrafish αba- and Rodent αains-Crystallin Encode Activated Chaperones

Author keywords

[No Author keywords available]

Indexed keywords

BINDING SITES; BINS; EVOLUTIONARY ALGORITHMS; GENE EXPRESSION; GENES; LENSES; LIGHT SCATTERING; MAMMALS; OLIGOMERS; OPTICAL PROPERTIES; RATS; TISSUE;

EID: 84942580950     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/acs.biochem.5b00678     Document Type: Article
Times cited : (12)

References (67)
  • 1
    • 0019786296 scopus 로고
    • Lens differentiation in vertebrates. A review of cellular and molecular features
    • Piatigorsky, J. (1981) Lens differentiation in vertebrates. A review of cellular and molecular features Differentiation 19, 134-153 10.1111/j.1432-0436.1981.tb01141.x
    • (1981) Differentiation , vol.19 , pp. 134-153
    • Piatigorsky, J.1
  • 3
    • 0020678719 scopus 로고
    • Short-range order of Crystallin proteins accounts for eye lens transparency
    • Delaye, M. and Tardieu, A. (1983) Short-range order of Crystallin proteins accounts for eye lens transparency Nature 302, 415-417 10.1038/302415a0
    • (1983) Nature , vol.302 , pp. 415-417
    • Delaye, M.1    Tardieu, A.2
  • 4
    • 0023721503 scopus 로고
    • Eye lens proteins and transparency: From light transmission theory to solution X-ray structural analysis
    • Tardieu, A. (1988) Eye lens proteins and transparency: from light transmission theory to solution X-ray structural analysis Annu. Rev. Biophys. Biomol. Struct. 17, 47-70 10.1146/annurev.biophys.17.1.47
    • (1988) Annu. Rev. Biophys. Biomol. Struct. , vol.17 , pp. 47-70
    • Tardieu, A.1
  • 5
    • 0028104494 scopus 로고
    • Eye-lens proteins: Structure, superstructure, stability, genetics
    • Jaenicke, R. (1994) Eye-lens proteins: structure, superstructure, stability, genetics Naturwissenschaften 81, 423-429 10.1007/BF01136641
    • (1994) Naturwissenschaften , vol.81 , pp. 423-429
    • Jaenicke, R.1
  • 6
    • 0020063988 scopus 로고
    • Four small Drosophila heat shock proteins are related to each other and to mammalian alpha-Crystallin
    • Ingolia, T. D. and Craig, E. A. (1982) Four small Drosophila heat shock proteins are related to each other and to mammalian alpha-Crystallin Proc. Natl. Acad. Sci. U. S. A. 79, 2360-2364 10.1073/pnas.79.7.2360
    • (1982) Proc. Natl. Acad. Sci. U. S. A. , vol.79 , pp. 2360-2364
    • Ingolia, T.D.1    Craig, E.A.2
  • 7
    • 0032077156 scopus 로고    scopus 로고
    • Genealogy of the α-Crystallin - Small heat-shock protein superfamily
    • de Jong, W. W., Caspers, G. J., and Leunissen, J. A. (1998) Genealogy of the α-Crystallin - small heat-shock protein superfamily Int. J. Biol. Macromol. 22, 151-162 10.1016/S0141-8130(98)00013-0
    • (1998) Int. J. Biol. Macromol. , vol.22 , pp. 151-162
    • De Jong, W.W.1    Caspers, G.J.2    Leunissen, J.A.3
  • 8
    • 0026483279 scopus 로고
    • α-Crystallin can function as a molecular chaperone
    • Horwitz, J. (1992) α-Crystallin can function as a molecular chaperone Proc. Natl. Acad. Sci. U. S. A. 89, 10449-10453 10.1073/pnas.89.21.10449
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 10449-10453
    • Horwitz, J.1
  • 9
    • 0033829222 scopus 로고    scopus 로고
    • The major in vivo modifications of the human water-insoluble lens crystallins are disulfide bonds, deamidation, methionine oxidation and backbone cleavage
    • Hanson, S. R., Hasan, A., Smith, D. L., and Smith, J. B. (2000) The major in vivo modifications of the human water-insoluble lens crystallins are disulfide bonds, deamidation, methionine oxidation and backbone cleavage Exp. Eye Res. 71, 195-207 10.1006/exer.2000.0868
    • (2000) Exp. Eye Res. , vol.71 , pp. 195-207
    • Hanson, S.R.1    Hasan, A.2    Smith, D.L.3    Smith, J.B.4
  • 10
    • 33644858451 scopus 로고    scopus 로고
    • Deamidation in human lens betaB2-Crystallin destabilizes the dimer
    • Lampi, K. J., Amyx, K. K., Ahmann, P., and Steel, E. A. (2006) Deamidation in human lens betaB2-Crystallin destabilizes the dimer Biochemistry 45, 3146-3153 10.1021/bi052051k
    • (2006) Biochemistry , vol.45 , pp. 3146-3153
    • Lampi, K.J.1    Amyx, K.K.2    Ahmann, P.3    Steel, E.A.4
  • 11
    • 84862660904 scopus 로고    scopus 로고
    • The pathogenic role of Maillard reaction in the aging eye
    • Nagaraj, R. H., Linetsky, M., and Stitt, A. W. (2012) The pathogenic role of Maillard reaction in the aging eye Amino Acids 42, 1205-1220 10.1007/s00726-010-0778-x
    • (2012) Amino Acids , vol.42 , pp. 1205-1220
    • Nagaraj, R.H.1    Linetsky, M.2    Stitt, A.W.3
  • 12
    • 79955709128 scopus 로고    scopus 로고
    • AlphaA-Crystallin peptide SDRDKFVIFLDVKHF accumulating in aging lens impairs the function of alpha-Crystallin and induces lens protein aggregation
    • Santhoshkumar, P., Raju, M., and Sharma, K. K. (2011) alphaA-Crystallin peptide SDRDKFVIFLDVKHF accumulating in aging lens impairs the function of alpha-Crystallin and induces lens protein aggregation PLoS One 6, e19291 10.1371/journal.pone.0019291
    • (2011) PLoS One , vol.6 , pp. e19291
    • Santhoshkumar, P.1    Raju, M.2    Sharma, K.K.3
  • 13
    • 0033572725 scopus 로고    scopus 로고
    • Effects of macromolecular crowding on protein folding and aggregation
    • van den Berg, B., Ellis, R. J., and Dobson, C. M. (1999) Effects of macromolecular crowding on protein folding and aggregation EMBO J. 18, 6927-6933 10.1093/emboj/18.24.6927
    • (1999) EMBO J. , vol.18 , pp. 6927-6933
    • Van Den Berg, B.1    Ellis, R.J.2    Dobson, C.M.3
  • 14
    • 0034254189 scopus 로고    scopus 로고
    • Macromolecular crowding perturbs protein refolding kinetics: Implications for folding inside the cell
    • van den Berg, B., Wain, R., Dobson, C. M., and Ellis, R. J. (2000) Macromolecular crowding perturbs protein refolding kinetics: implications for folding inside the cell EMBO J. 19, 3870-3875 10.1093/emboj/19.15.3870
    • (2000) EMBO J. , vol.19 , pp. 3870-3875
    • Van Den Berg, B.1    Wain, R.2    Dobson, C.M.3    Ellis, R.J.4
  • 15
    • 0027342592 scopus 로고
    • Proctor Lecture. The function of α-Crystallin
    • Horwitz, J. (1993) Proctor Lecture. The function of α-Crystallin Invest. Ophthalmol. Visual Sci. 34, 10-22
    • (1993) Invest. Ophthalmol. Visual Sci. , vol.34 , pp. 10-22
    • Horwitz, J.1
  • 16
    • 0030954844 scopus 로고    scopus 로고
    • Cataract as a protein condensation disease: The Proctor Lecture
    • Benedek, G. B. (1997) Cataract as a protein condensation disease: the Proctor Lecture Invest. Ophthalmol. Visual Sci. 38, 1911-1921
    • (1997) Invest. Ophthalmol. Visual Sci. , vol.38 , pp. 1911-1921
    • Benedek, G.B.1
  • 17
    • 84877039811 scopus 로고    scopus 로고
    • Comparative proteomic analysis identifies age-dependent increases in the abundance of specific proteins after deletion of the small heat shock proteins alphaA- and alphaB-Crystallin
    • Andley, U. P., Malone, J. P., Hamilton, P. D., Ravi, N., and Townsend, R. R. (2013) Comparative proteomic analysis identifies age-dependent increases in the abundance of specific proteins after deletion of the small heat shock proteins alphaA- and alphaB-Crystallin Biochemistry 52, 2933-2948 10.1021/bi400180d
    • (2013) Biochemistry , vol.52 , pp. 2933-2948
    • Andley, U.P.1    Malone, J.P.2    Hamilton, P.D.3    Ravi, N.4    Townsend, R.R.5
  • 18
    • 2942750445 scopus 로고    scopus 로고
    • Morphological characterization of the Alpha A- and Alpha B-Crystallin double knockout mouse lens
    • Boyle, D. L., Takemoto, L., Brady, J. P., and Wawrousek, E. F. (2003) Morphological characterization of the Alpha A- and Alpha B-Crystallin double knockout mouse lens BMC Ophthalmol. 3, 3 10.1186/1471-2415-3-3
    • (2003) BMC Ophthalmol. , vol.3 , pp. 3
    • Boyle, D.L.1    Takemoto, L.2    Brady, J.P.3    Wawrousek, E.F.4
  • 19
    • 0031017669 scopus 로고    scopus 로고
    • Targeted disruption of the mouse aA-Crystallin gene induces cataract and cytoplasmic inclusion bodies containing the small heat shock protein aB-Crystallin
    • Brady, J. P., Garland, D., Duglas-Tabor, Y., Robison Jr. W. G., , Groome, A., and Wawrousek, E. F. (1997) Targeted disruption of the mouse aA-Crystallin gene induces cataract and cytoplasmic inclusion bodies containing the small heat shock protein aB-Crystallin Proc. Natl. Acad. Sci. U. S. A. 94, 884-889 10.1073/pnas.94.3.884
    • (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
  • 20
    • 0031934121 scopus 로고    scopus 로고
    • Autosomal dominant congenital cataract associated with a missense mutation in the human a Crystallin gene CRYAA
    • Litt, M., Kramer, P., LaMorticella, D. M., Murphey, W., Lovrien, E. W., and Weleber, R. G. (1998) Autosomal dominant congenital cataract associated with a missense mutation in the human a Crystallin gene CRYAA Hum. Mol. Genet. 7, 471-474 10.1093/hmg/7.3.471
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 471-474
    • Litt, M.1    Kramer, P.2    LaMorticella, D.M.3    Murphey, W.4    Lovrien, E.W.5    Weleber, R.G.6
  • 21
    • 0242287938 scopus 로고    scopus 로고
    • Cell death triggered by a novel mutation in the alphaA-Crystallin gene underlies autosomal dominant cataract linked to chromosome 21q
    • Mackay, D., Andley, U., and Shiels, A. (2003) Cell death triggered by a novel mutation in the alphaA-Crystallin gene underlies autosomal dominant cataract linked to chromosome 21q Eur. J. Hum. Genet. 11, 784-793 10.1038/sj.ejhg.5201046
    • (2003) Eur. J. Hum. Genet. , vol.11 , pp. 784-793
    • Mackay, D.1    Andley, U.2    Shiels, A.3
  • 23
    • 84936952487 scopus 로고    scopus 로고
    • A conserved role of alphaA-Crystallin in the development of the zebrafish embryonic lens
    • Zou, P., Wu, S. Y., Koteiche, H. A., Mishra, S., Levic, D. S., Knapik, E., Chen, W., and McHaourab, H. S. (2015) A conserved role of alphaA-Crystallin in the development of the zebrafish embryonic lens Exp. Eye Res. 138, 104-113 10.1016/j.exer.2015.07.001
    • (2015) Exp. Eye Res. , vol.138 , pp. 104-113
    • Zou, P.1    Wu, S.Y.2    Koteiche, H.A.3    Mishra, S.4    Levic, D.S.5    Knapik, E.6    Chen, W.7    McHaourab, H.S.8
  • 24
    • 0027391629 scopus 로고
    • Small heat shock proteins are molecular chaperones
    • Jakob, U., Gaestel, M., Engel, K., and Buchner, J. (1993) Small heat shock proteins are molecular chaperones J. Biol. Chem. 268, 1517-1520
    • (1993) J. Biol. Chem. , vol.268 , pp. 1517-1520
    • Jakob, U.1    Gaestel, M.2    Engel, K.3    Buchner, J.4
  • 26
    • 0038193547 scopus 로고    scopus 로고
    • Mechanism of chaperone function in small heat-shock proteins. Phosphorylation-induced activation of two-mode binding in alphaB-Crystallin
    • Koteiche, H. A. and McHaourab, H. S. (2003) Mechanism of chaperone function in small heat-shock proteins. Phosphorylation-induced activation of two-mode binding in alphaB-Crystallin J. Biol. Chem. 278, 10361-10367 10.1074/jbc.M211851200
    • (2003) J. Biol. Chem. , vol.278 , pp. 10361-10367
    • Koteiche, H.A.1    McHaourab, H.S.2
  • 27
    • 0037174851 scopus 로고    scopus 로고
    • Mechanism of Chaperone Function in Small Heat-Shock Proteins.Two-Mode Binding of the Excited States of T4 Lysozyme Mutants by aA-Crystallin
    • Mchaourab, H. S., Dodson, E. K., and Koteiche, H. A. (2002) Mechanism of Chaperone Function in Small Heat-Shock Proteins.Two-Mode Binding of the Excited States of T4 Lysozyme Mutants by aA-Crystallin J. Biol. Chem. 277, 40557-40566 10.1074/jbc.M206250200
    • (2002) J. Biol. Chem. , vol.277 , pp. 40557-40566
    • Mchaourab, H.S.1    Dodson, E.K.2    Koteiche, H.A.3
  • 28
    • 1942437441 scopus 로고    scopus 로고
    • Binding of destabilized betaB2-Crystallin mutants to alpha-Crystallin: The role of a folding intermediate
    • Sathish, H. A., Koteiche, H. A., and McHaourab, H. S. (2004) Binding of destabilized betaB2-Crystallin mutants to alpha-Crystallin: the role of a folding intermediate J. Biol. Chem. 279, 16425-16432 10.1074/jbc.M313402200
    • (2004) J. Biol. Chem. , vol.279 , pp. 16425-16432
    • Sathish, H.A.1    Koteiche, H.A.2    McHaourab, H.S.3
  • 29
    • 0242582458 scopus 로고    scopus 로고
    • Mechanism of chaperone function in small heat-shock proteins. Fluorescence studies of the conformations of T4 lysozyme bound to alphaB-Crystallin
    • Sathish, H. A., Stein, R. A., Yang, G., and Mchaourab, H. S. (2003) Mechanism of chaperone function in small heat-shock proteins. Fluorescence studies of the conformations of T4 lysozyme bound to alphaB-Crystallin J. Biol. Chem. 278, 44214-44221 10.1074/jbc.M307578200
    • (2003) J. Biol. Chem. , vol.278 , pp. 44214-44221
    • Sathish, H.A.1    Stein, R.A.2    Yang, G.3    McHaourab, H.S.4
  • 30
    • 14044272992 scopus 로고    scopus 로고
    • Mechanism of chaperone function in small heat shock proteins: Dissociation of the HSP27 oligomer is required for recognition and binding of destabilized T4 lysozyme
    • Shashidharamurthy, R., Koteiche, H. A., Dong, J., and McHaourab, H. S. (2005) Mechanism of chaperone function in small heat shock proteins: dissociation of the HSP27 oligomer is required for recognition and binding of destabilized T4 lysozyme J. Biol. Chem. 280, 5281-5289 10.1074/jbc.M407236200
    • (2005) J. Biol. Chem. , vol.280 , pp. 5281-5289
    • Shashidharamurthy, R.1    Koteiche, H.A.2    Dong, J.3    McHaourab, H.S.4
  • 31
    • 0034681446 scopus 로고    scopus 로고
    • Temperature-dependent chaperone activity and structural properties of human alphaA- and alphaB-crystallins
    • Reddy, G. B., Das, K. P., Petrash, J. M., and Surewicz, W. K. (2000) Temperature-dependent chaperone activity and structural properties of human alphaA- and alphaB-crystallins J. Biol. Chem. 275, 4565-4570 10.1074/jbc.275.7.4565
    • (2000) J. Biol. Chem. , vol.275 , pp. 4565-4570
    • Reddy, G.B.1    Das, K.P.2    Petrash, J.M.3    Surewicz, W.K.4
  • 32
    • 0028981330 scopus 로고
    • Alpha-Crystallin can act as a chaperone under conditions of oxidative stress
    • Wang, K. and Spector, A. (1995) Alpha-Crystallin can act as a chaperone under conditions of oxidative stress Invest. Ophthalmol. Visual Sci. 36, 311-321
    • (1995) Invest. Ophthalmol. Visual Sci. , vol.36 , pp. 311-321
    • Wang, K.1    Spector, A.2
  • 33
    • 37449009967 scopus 로고    scopus 로고
    • Structure and orientation of T4 lysozyme bound to the small heat shock protein alpha-Crystallin
    • Claxton, D. P., Zou, P., and McHaourab, H. S. (2008) Structure and orientation of T4 lysozyme bound to the small heat shock protein alpha-Crystallin J. Mol. Biol. 375, 1026-1039 10.1016/j.jmb.2007.11.014
    • (2008) J. Mol. Biol. , vol.375 , pp. 1026-1039
    • Claxton, D.P.1    Zou, P.2    McHaourab, H.S.3
  • 34
    • 0034724559 scopus 로고    scopus 로고
    • Small heat-shock protein structures reveal a continuum from symmetric to variable assemblies
    • Haley, D. A., Bova, M. P., Huang, Q. L., Mchaourab, H. S., and Stewart, P. L. (2000) Small heat-shock protein structures reveal a continuum from symmetric to variable assemblies J. Mol. Biol. 298, 261-272 10.1006/jmbi.2000.3657
    • (2000) J. Mol. Biol. , vol.298 , pp. 261-272
    • Haley, D.A.1    Bova, M.P.2    Huang, Q.L.3    McHaourab, H.S.4    Stewart, P.L.5
  • 35
    • 0033607618 scopus 로고    scopus 로고
    • Folding pattern of the α-Crystallin domain in aA-Crystallin determined by site-directed spin labeling
    • Koteiche, H. A. and Mchaourab, H. S. (1999) Folding pattern of the α-Crystallin domain in aA-Crystallin determined by site-directed spin labeling J. Mol. Biol. 294, 561-577 10.1006/jmbi.1999.3242
    • (1999) J. Mol. Biol. , vol.294 , pp. 561-577
    • Koteiche, H.A.1    McHaourab, H.S.2
  • 38
    • 77957296137 scopus 로고    scopus 로고
    • Crystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens function
    • Laganowsky, A., Benesch, J. L. P., Landau, M., Ding, L., Sawaya, M. R., Cascio, D., Huang, Q., Robinson, C. V., Horwitz, J., and Eisenberg, D. (2010) Crystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens function Protein Sci. 19, 1031-1043 10.1002/pro.380
    • (2010) Protein Sci. , vol.19 , pp. 1031-1043
    • Laganowsky, A.1    Benesch, J.L.P.2    Landau, M.3    Ding, L.4    Sawaya, M.R.5    Cascio, D.6    Huang, Q.7    Robinson, C.V.8    Horwitz, J.9    Eisenberg, D.10
  • 39
    • 77957322359 scopus 로고    scopus 로고
    • Non-3D domain swapped crystal structure of truncated zebrafish alphaA Crystallin
    • Laganowsky, A. and Eisenberg, D. (2010) Non-3D domain swapped crystal structure of truncated zebrafish alphaA Crystallin Protein Sci. 19, 1978-1984 10.1002/pro.471
    • (2010) Protein Sci. , vol.19 , pp. 1978-1984
    • Laganowsky, A.1    Eisenberg, D.2
  • 40
    • 84862905389 scopus 로고    scopus 로고
    • Crystal structure of an activated variant of small heat shock protein Hsp16.5
    • McHaourab, H. S., Lin, Y., and Spiller, B. W. (2012) Crystal structure of an activated variant of small heat shock protein Hsp16.5 Biochemistry 51, 5105-5112 10.1021/bi300525x
    • (2012) Biochemistry , vol.51 , pp. 5105-5112
    • McHaourab, H.S.1    Lin, Y.2    Spiller, B.W.3
  • 41
    • 84858003372 scopus 로고    scopus 로고
    • Small heat shock proteins and a-crystallins: Dynamic proteins with flexible functions
    • Basha, E., O'Neill, H., and Vierling, E. (2012) Small heat shock proteins and a-crystallins: dynamic proteins with flexible functions Trends Biochem. Sci. 37, 106-117 10.1016/j.tibs.2011.11.005
    • (2012) Trends Biochem. Sci. , vol.37 , pp. 106-117
    • Basha, E.1    O'Neill, H.2    Vierling, E.3
  • 42
  • 43
    • 66149117827 scopus 로고    scopus 로고
    • Structure and mechanism of protein stability sensors: Chaperone activity of small heat shock proteins
    • McHaourab, H. S., Godar, J. A., and Stewart, P. L. (2009) Structure and mechanism of protein stability sensors: chaperone activity of small heat shock proteins Biochemistry 48, 3828-3837 10.1021/bi900212j
    • (2009) Biochemistry , vol.48 , pp. 3828-3837
    • McHaourab, H.S.1    Godar, J.A.2    Stewart, P.L.3
  • 44
    • 84856820287 scopus 로고    scopus 로고
    • Sequence, structure, and dynamic determinants of Hsp27 (HspB1) equilibrium dissociation are encoded by the N-terminal domain
    • McDonald, E. T., Bortolus, M., Koteiche, H. A., and Mchaourab, H. S. (2012) Sequence, structure, and dynamic determinants of Hsp27 (HspB1) equilibrium dissociation are encoded by the N-terminal domain Biochemistry 51, 1257-1268 10.1021/bi2017624
    • (2012) Biochemistry , vol.51 , pp. 1257-1268
    • McDonald, E.T.1    Bortolus, M.2    Koteiche, H.A.3    McHaourab, H.S.4
  • 45
    • 33846019666 scopus 로고    scopus 로고
    • Cryoelectron Microscopy and EPR Analysis of Engineered Symmetric and Polydisperse Hsp16.5 Assemblies Reveals Determinants of Polydispersity and Substrate Binding
    • Shi, J., Koteiche, H. A., Mchaourab, H. S., and Stewart, P. L. (2006) Cryoelectron Microscopy and EPR Analysis of Engineered Symmetric and Polydisperse Hsp16.5 Assemblies Reveals Determinants of Polydispersity and Substrate Binding J. Biol. Chem. 281, 40420-40428 10.1074/jbc.M608322200
    • (2006) J. Biol. Chem. , vol.281 , pp. 40420-40428
    • Shi, J.1    Koteiche, H.A.2    McHaourab, H.S.3    Stewart, P.L.4
  • 46
    • 84874101818 scopus 로고    scopus 로고
    • Cryoelectron microscopy analysis of small heat shock protein 16.5 (Hsp16.5) complexes with T4 lysozyme reveals the structural basis of multimode binding
    • Shi, J., Koteiche, H. A., McDonald, E. T., Fox, T. L., Stewart, P. L., and McHaourab, H. S. (2013) Cryoelectron microscopy analysis of small heat shock protein 16.5 (Hsp16.5) complexes with T4 lysozyme reveals the structural basis of multimode binding J. Biol. Chem. 288, 4819-4830 10.1074/jbc.M112.388132
    • (2013) J. Biol. Chem. , vol.288 , pp. 4819-4830
    • Shi, J.1    Koteiche, H.A.2    McDonald, E.T.3    Fox, T.L.4    Stewart, P.L.5    McHaourab, H.S.6
  • 47
    • 33644941793 scopus 로고    scopus 로고
    • Gene duplication and separation of functions in alphaB-Crystallin from zebrafish (Danio rerio)
    • Smith, A. A., Wyatt, K., Vacha, J., Vihtelic, T. S., Zigler Jr. J. S., , Wistow, G. J., and Posner, M. (2006) Gene duplication and separation of functions in alphaB-Crystallin from zebrafish (Danio rerio) FEBS J. 273, 481-490 10.1111/j.1742-4658.2005.05080.x
    • (2006) FEBS J. , vol.273 , pp. 481-490
    • Smith, A.A.1    Wyatt, K.2    Vacha, J.3    Vihtelic, T.S.4    Zigler, J.S.5    Wistow, G.J.6    Posner, M.7
  • 48
    • 0021249693 scopus 로고
    • Alternative splicing of alpha A-Crystallin RNA. Structural and quantitative analyses of the mRNAs for the alpha A2- and alpha Ains-Crystallin polypeptides
    • King, C. R. and Piatigorsky, J. (1984) Alternative splicing of alpha A-Crystallin RNA. Structural and quantitative analyses of the mRNAs for the alpha A2- and alpha Ains-Crystallin polypeptides J. Biol. Chem. 259, 1822-1826
    • (1984) J. Biol. Chem. , vol.259 , pp. 1822-1826
    • King, C.R.1    Piatigorsky, J.2
  • 49
    • 0030741276 scopus 로고    scopus 로고
    • Structure and function of the conserved domain in aA-Crystallin. Site-directed spin labeling identifies a b-strand located near a subunit interface
    • Berengian, A. R., Bova, M. P., and Mchaourab, H. S. (1997) Structure and function of the conserved domain in aA-Crystallin. Site-directed spin labeling identifies a b-strand located near a subunit interface Biochemistry 36, 9951-9957 10.1021/bi9712347
    • (1997) Biochemistry , vol.36 , pp. 9951-9957
    • Berengian, A.R.1    Bova, M.P.2    McHaourab, H.S.3
  • 50
    • 0029905422 scopus 로고    scopus 로고
    • Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics
    • Mchaourab, H. S., Lietzow, M. A., Hideg, K., and Hubbell, W. L. (1996) Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics Biochemistry 35, 7692-7704 10.1021/bi960482k
    • (1996) Biochemistry , vol.35 , pp. 7692-7704
    • McHaourab, H.S.1    Lietzow, M.A.2    Hideg, K.3    Hubbell, W.L.4
  • 51
    • 0027394606 scopus 로고
    • Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences
    • Eriksson, A. E., Baase, W. A., and Matthews, B. W. (1993) Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences J. Mol. Biol. 229, 747-769 10.1006/jmbi.1993.1077
    • (1993) J. Mol. Biol. , vol.229 , pp. 747-769
    • Eriksson, A.E.1    Baase, W.A.2    Matthews, B.W.3
  • 52
    • 34247580177 scopus 로고    scopus 로고
    • Specificity of alphaA-Crystallin binding to destabilized mutants of betaB1-Crystallin
    • Mchaourab, H. S., Kumar, M. S., and Koteiche, H. A. (2007) Specificity of alphaA-Crystallin binding to destabilized mutants of betaB1-Crystallin FEBS Lett. 581, 1939-1943 10.1016/j.febslet.2007.04.005
    • (2007) FEBS Lett. , vol.581 , pp. 1939-1943
    • McHaourab, H.S.1    Kumar, M.S.2    Koteiche, H.A.3
  • 53
    • 84857048837 scopus 로고    scopus 로고
    • Cataract-linked gammaD-Crystallin mutants have weak affinity to lens chaperones alpha-crystallins
    • Mishra, S., Stein, R. A., and McHaourab, H. S. (2012) Cataract-linked gammaD-Crystallin mutants have weak affinity to lens chaperones alpha-crystallins FEBS Lett. 586, 330-336 10.1016/j.febslet.2012.01.019
    • (2012) FEBS Lett. , vol.586 , pp. 330-336
    • Mishra, S.1    Stein, R.A.2    McHaourab, H.S.3
  • 54
    • 33744903422 scopus 로고    scopus 로고
    • Mechanism of a Hereditary Cataract Phenotype: Mutations in aA-Crystallin activate substrate binding
    • Koteiche, H. A. and McHaourab, H. S. (2006) Mechanism of a Hereditary Cataract Phenotype: Mutations in aA-Crystallin activate substrate binding J. Biol. Chem. 281, 14273-14279 10.1074/jbc.M512938200
    • (2006) J. Biol. Chem. , vol.281 , pp. 14273-14279
    • Koteiche, H.A.1    McHaourab, H.S.2
  • 55
    • 25444515199 scopus 로고    scopus 로고
    • Zebrafish alpha-crystallins: Protein structure and chaperone-like activity compared to their mammalian orthologs
    • Dahlman, J. M., Margot, K. L., Ding, L., Horwitz, J., and Posner, M. (2005) Zebrafish alpha-crystallins: protein structure and chaperone-like activity compared to their mammalian orthologs Mol. Vis. 11, 88-96
    • (2005) Mol. Vis. , vol.11 , pp. 88-96
    • Dahlman, J.M.1    Margot, K.L.2    Ding, L.3    Horwitz, J.4    Posner, M.5
  • 56
    • 0029067530 scopus 로고
    • Reduced chaperone-like activity of alpha A(ins)-Crystallin, an alternative splicing product containing a large insert peptide
    • Smulders, R. H., van Geel, I. G., Gerards, W. L., Bloemendal, H., and de Jong, W. W. (1995) Reduced chaperone-like activity of alpha A(ins)-Crystallin, an alternative splicing product containing a large insert peptide J. Biol. Chem. 270, 13916-13924 10.1074/jbc.270.23.13916
    • (1995) J. Biol. Chem. , vol.270 , pp. 13916-13924
    • Smulders, R.H.1    Van Geel, I.G.2    Gerards, W.L.3    Bloemendal, H.4    De Jong, W.W.5
  • 57
    • 0023946667 scopus 로고
    • Monoclonal antibodies reveal evolutionary conservation of alternative splicing of the alpha A-Crystallin primary transcript
    • Hendriks, W., Sanders, J., de Leij, L., Ramaekers, F., Bloemendal, H., and de Jong, W. W. (1988) Monoclonal antibodies reveal evolutionary conservation of alternative splicing of the alpha A-Crystallin primary transcript Eur. J. Biochem. 174, 133-137 10.1111/j.1432-1033.1988.tb14072.x
    • (1988) Eur. J. Biochem. , vol.174 , pp. 133-137
    • Hendriks, W.1    Sanders, J.2    De Leij, L.3    Ramaekers, F.4    Bloemendal, H.5    De Jong, W.W.6
  • 58
    • 43149088753 scopus 로고    scopus 로고
    • A proteome map of the zebrafish (Danio rerio) lens reveals similarities between zebrafish and mammalian Crystallin expression
    • Posner, M., Hawke, M., Lacava, C., Prince, C. J., Bellanco, N. R., and Corbin, R. W. (2008) A proteome map of the zebrafish (Danio rerio) lens reveals similarities between zebrafish and mammalian Crystallin expression Mol. Vis. 14, 806-814
    • (2008) Mol. Vis. , vol.14 , pp. 806-814
    • Posner, M.1    Hawke, M.2    Lacava, C.3    Prince, C.J.4    Bellanco, N.R.5    Corbin, R.W.6
  • 59
    • 84874357911 scopus 로고    scopus 로고
    • Changes in zebrafish (Danio rerio) lens Crystallin content during development
    • Wages, P., Horwitz, J., Ding, L., Corbin, R. W., and Posner, M. (2013) Changes in zebrafish (Danio rerio) lens Crystallin content during development Mol. Vis. 19, 408-417
    • (2013) Mol. Vis. , vol.19 , pp. 408-417
    • Wages, P.1    Horwitz, J.2    Ding, L.3    Corbin, R.W.4    Posner, M.5
  • 60
    • 0036139647 scopus 로고    scopus 로고
    • Lens proteomics: The accumulation of Crystallin modifications in the mouse lens with age
    • Ueda, Y., Duncan, M. K., and David, L. L. (2002) Lens proteomics: the accumulation of Crystallin modifications in the mouse lens with age Invest. Ophthalmol. Visual Sci. 43, 205-215
    • (2002) Invest. Ophthalmol. Visual Sci. , vol.43 , pp. 205-215
    • Ueda, Y.1    Duncan, M.K.2    David, L.L.3
  • 61
    • 0033771704 scopus 로고    scopus 로고
    • The effect of stress on the pattern of phosphorylation of aA and aB Crystallin in the rat lens
    • Wang, K., Gawinowicz, M. A., and Spector, A. (2000) The effect of stress on the pattern of phosphorylation of aA and aB Crystallin in the rat lens Exp. Eye Res. 71, 385-393 10.1006/exer.2000.0890
    • (2000) Exp. Eye Res. , vol.71 , pp. 385-393
    • Wang, K.1    Gawinowicz, M.A.2    Spector, A.3
  • 62
    • 0028216737 scopus 로고
    • Post-translational modifications of water-soluble human lens crystallins from young adults
    • Miesbauer, L. R., Zhou, X., Yang, Z., Sun, Y., Smith, D. L., and Smith, J. B. (1994) Post-translational modifications of water-soluble human lens crystallins from young adults J. Biol. Chem. 269, 12494-12502
    • (1994) J. Biol. Chem. , vol.269 , pp. 12494-12502
    • Miesbauer, L.R.1    Zhou, X.2    Yang, Z.3    Sun, Y.4    Smith, D.L.5    Smith, J.B.6
  • 63
    • 0033515597 scopus 로고    scopus 로고
    • HSP27 multimerization mediated by phosphorylation-sensitive intermolecular interactions at the amino terminus
    • Lambert, H., Charette, S. J., Bernier, A. F., Guimond, A., and Landry, J. (1999) HSP27 multimerization mediated by phosphorylation-sensitive intermolecular interactions at the amino terminus J. Biol. Chem. 274, 9378-9385 10.1074/jbc.274.14.9378
    • (1999) J. Biol. Chem. , vol.274 , pp. 9378-9385
    • Lambert, H.1    Charette, S.J.2    Bernier, A.F.3    Guimond, A.4    Landry, J.5
  • 64
    • 70349263467 scopus 로고    scopus 로고
    • Age-related changes in the spatial distribution of human lens alpha-Crystallin products by MALDI imaging mass spectrometry
    • Grey, A. C. and Schey, K. L. (2009) Age-related changes in the spatial distribution of human lens alpha-Crystallin products by MALDI imaging mass spectrometry Invest. Ophthalmol. Visual Sci. 50, 4319-4329 10.1167/iovs.09-3522
    • (2009) Invest. Ophthalmol. Visual Sci. , vol.50 , pp. 4319-4329
    • Grey, A.C.1    Schey, K.L.2
  • 65
    • 77958146830 scopus 로고    scopus 로고
    • Tissue localization and solubilities of alphaA-Crystallin and its numerous C-terminal truncation products in pre- and postcataractous ICR/f rat lenses
    • Stella, D. R., Floyd, K. A., Grey, A. C., Renfrow, M. B., Schey, K. L., and Barnes, S. (2010) Tissue localization and solubilities of alphaA-Crystallin and its numerous C-terminal truncation products in pre- and postcataractous ICR/f rat lenses Invest. Ophthalmol. Visual Sci. 51, 5153-5161 10.1167/iovs.10-5302
    • (2010) Invest. Ophthalmol. Visual Sci. , vol.51 , pp. 5153-5161
    • Stella, D.R.1    Floyd, K.A.2    Grey, A.C.3    Renfrow, M.B.4    Schey, K.L.5    Barnes, S.6
  • 66
    • 0036137567 scopus 로고    scopus 로고
    • Lens proteomics: Analysis of rat Crystallin sequences and two-dimensional electrophoresis map
    • Lampi, K. J., Shih, M., Ueda, Y., Shearer, T. R., and David, L. L. (2002) Lens proteomics: analysis of rat Crystallin sequences and two-dimensional electrophoresis map Invest. Ophthalmol. Visual Sci. 43, 216-224
    • (2002) Invest. Ophthalmol. Visual Sci. , vol.43 , pp. 216-224
    • Lampi, K.J.1    Shih, M.2    Ueda, Y.3    Shearer, T.R.4    David, L.L.5
  • 67
    • 33746441661 scopus 로고    scopus 로고
    • AlphaA-Crystallin expression prevents gamma-Crystallin insolubility and cataract formation in the zebrafish cloche mutant lens
    • Goishi, K., Shimizu, A., Najarro, G., Watanabe, S., Rogers, R., Zon, L. I., and Klagsbrun, M. (2006) AlphaA-Crystallin expression prevents gamma-Crystallin insolubility and cataract formation in the zebrafish cloche mutant lens Development 133, 2585-2593 10.1242/dev.02424
    • (2006) Development , vol.133 , pp. 2585-2593
    • Goishi, K.1    Shimizu, A.2    Najarro, G.3    Watanabe, S.4    Rogers, R.5    Zon, L.I.6    Klagsbrun, M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.