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Volumn 47, Issue 38, 2008, Pages 10069-10083

Structural and functional roles of deamidation and/or truncation of N- or C-Termini in human αA-crystallin

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; DESORPTION; DICHROISM; ELECTRIC INSTRUMENT TRANSFORMERS; FLUORESCENCE; LIGHT EMISSION; LUMINESCENCE; OPTICAL PROPERTIES; PROTEINS; SPECTROSCOPIC ANALYSIS; SPECTRUM ANALYZERS; SPEECH; WINDOWS OPERATING SYSTEM;

EID: 52249118740     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi8001902     Document Type: Article
Times cited : (42)

References (57)
  • 2
    • 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.
    • (1992) Proc. Natl. Acad. Sci. U.S.A , vol.89 , pp. 10449-10453
    • Horwitz, J.1
  • 3
    • 0037195949 scopus 로고    scopus 로고
    • Role of C-terminal extension of α-crystallins; Swapping the C-terminal extension of αA-crystallin with αB-crystallin results in enhanced chaperone activity
    • Pasta, S. Y., Raman, B., Ramkrishna, T., and Rao, C. M. (2002) Role of C-terminal extension of α-crystallins; Swapping the C-terminal extension of αA-crystallin with αB-crystallin results in enhanced chaperone activity. J. Biol. Chem. 277, 45821-45828.
    • (2002) J. Biol. Chem , vol.277 , pp. 45821-45828
    • Pasta, S.Y.1    Raman, B.2    Ramkrishna, T.3    Rao, C.M.4
  • 4
    • 0027316992 scopus 로고    scopus 로고
    • The C-terminal region of α-crystallin: Involvement in protection against heat-induced denaturation
    • Takemoto, L., Emmons, T., and Horwitz, J. ( 1999) The C-terminal region of α-crystallin: involvement in protection against heat-induced denaturation. Biochem. J. 294, 435-438.
    • (1999) Biochem. J , vol.294 , pp. 435-438
    • Takemoto, L.1    Emmons, T.2    Horwitz, J.3
  • 5
    • 0033972325 scopus 로고    scopus 로고
    • Subunit exchange of small heat shock proteins. Analysis of oligomer formation of αA-crystallin and HSP27 by fluorescence resonance energy transfer and site-directed truncations
    • Bova, M. P., Mchaourab, H. S., Han, Y., and Fung, B. K. K. (2000) Subunit exchange of small heat shock proteins. Analysis of oligomer formation of αA-crystallin and HSP27 by fluorescence resonance energy transfer and site-directed truncations. J. Biol. Chem. 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.K.4
  • 8
    • 0029770039 scopus 로고    scopus 로고
    • Cloning, expression, and chaperone-like activity of human αA-crystallin
    • Andley, U. P., Mathur, S., Griest, T. A., and Petrash, J. M. (1996) Cloning, expression, and chaperone-like activity of human αA-crystallin. J. Biol. Chem. 271, 31973-31980.
    • (1996) J. Biol. Chem , vol.271 , pp. 31973-31980
    • Andley, U.P.1    Mathur, S.2    Griest, T.A.3    Petrash, J.M.4
  • 9
    • 10844246436 scopus 로고    scopus 로고
    • αA-crystallin interacting regions in the small heat shock protein, αB-crystallin
    • Sreelakshmi, Y., Santhoshkumar, P., Bhattacharyya, J., and Sharma, K. K. (2004) αA-crystallin interacting regions in the small heat shock protein, αB-crystallin. Biochemistry 43, 15785-15795.
    • (2004) Biochemistry , vol.43 , pp. 15785-15795
    • Sreelakshmi, Y.1    Santhoshkumar, P.2    Bhattacharyya, J.3    Sharma, K.K.4
  • 10
    • 33646891273 scopus 로고    scopus 로고
    • The interaction between αA- and αA-crystalllin is sequence specific
    • Sreelakshmi, Y., and Sharma, K. K. (2006) The interaction between αA- and αA-crystalllin is sequence specific. Mol. Vision 12, 581-587.
    • (2006) Mol. Vision , vol.12 , pp. 581-587
    • Sreelakshmi, Y.1    Sharma, K.K.2
  • 11
    • 14144255401 scopus 로고    scopus 로고
    • Insight into the domains required for dimerization and assembly of human αB-crystallin
    • Ghosh, J. G., and Clark, J. I. (2005) Insight into the domains required for dimerization and assembly of human αB-crystallin. Protein Sci. 14, 684-695.
    • (2005) Protein Sci , vol.14 , pp. 684-695
    • Ghosh, J.G.1    Clark, J.I.2
  • 12
    • 0032586878 scopus 로고    scopus 로고
    • Mutation R120G in αB-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function
    • Bova, M. P., Yaron, O., Huang, Q. L., Ding, L. L., Haley, D. A., Stewart, P. L., and Horwitz, J. (1999) Mutation R120G in αB-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function. Proc. Natl. Acad. Sci. U.S.A. 96, 6137-6142.
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 6137-6142
    • Bova, M.P.1    Yaron, O.2    Huang, Q.L.3    Ding, L.L.4    Haley, D.A.5    Stewart, P.L.6    Horwitz, J.7
  • 13
    • 0034719154 scopus 로고    scopus 로고
    • Structural and functional changes in the αA-crystallin R116C mutant in hereditary cataract
    • Cobb, B. A., and Petrash, M. (2000) Structural and functional changes in the αA-crystallin R116C mutant in hereditary cataract. Biochemistry 39, 15791-15798.
    • (2000) Biochemistry , vol.39 , pp. 15791-15798
    • Cobb, B.A.1    Petrash, M.2
  • 14
    • 0021359934 scopus 로고
    • The search for a solution to senile cataracts, Procter lecture
    • Spector, A. (1984) The search for a solution to senile cataracts, Procter lecture. Invest. Ophthalmol. Visual Sci. 25, 130-145.
    • (1984) Invest. Ophthalmol. Visual Sci , vol.25 , pp. 130-145
    • Spector, A.1
  • 15
    • 0025748591 scopus 로고
    • High correlation between pentosidine protein crosslinks and pigmentation implicates ascorbate oxidation in human lens senescence and cataractogenesis
    • Nagaraj, R. H., Sell, D. R., Prabhakaram, M., Ortwerth, B. J., and Monnier, V. M. (1991) High correlation between pentosidine protein crosslinks and pigmentation implicates ascorbate oxidation in human lens senescence and cataractogenesis. Proc. Natl. Acad. Sci. U.S.A. 88, 10257-10261.
    • (1991) Proc. Natl. Acad. Sci. U.S.A , vol.88 , pp. 10257-10261
    • Nagaraj, R.H.1    Sell, D.R.2    Prabhakaram, M.3    Ortwerth, B.J.4    Monnier, V.M.5
  • 16
    • 0025953440 scopus 로고
    • Photooxidation of specific residues in α-crystallin polypeptides
    • McDermott, M., Chiesa, R., Roberts, J. E., and Dillon, J. (1991) Photooxidation of specific residues in α-crystallin polypeptides. Biochemistry 30, 8653-8660.
    • (1991) Biochemistry , vol.30 , pp. 8653-8660
    • McDermott, M.1    Chiesa, R.2    Roberts, J.E.3    Dillon, J.4
  • 17
    • 34748888365 scopus 로고    scopus 로고
    • Proteomics of crystallin species present in water insoluble proteins of normal and cataractous human lenses
    • Harrington, V., and Srivastava, O. P. (2007) Proteomics of crystallin species present in water insoluble proteins of normal and cataractous human lenses. Mol. Vision 13, 1680-1694.
    • (2007) Mol. Vision , vol.13 , pp. 1680-1694
    • Harrington, V.1    Srivastava, O.P.2
  • 18
    • 0345825772 scopus 로고    scopus 로고
    • Existence of deamidated αB-crystallin fragments in normal and cataractous human lenses
    • Srivastava, O. P., and Srivastava, K. (2003) Existence of deamidated αB-crystallin fragments in normal and cataractous human lenses. Mol. Vision 9, 110-118.
    • (2003) Mol. Vision , vol.9 , pp. 110-118
    • Srivastava, O.P.1    Srivastava, K.2
  • 19
    • 0023704687 scopus 로고
    • Transglutaminase mediated cross-linking of proteins and cell aging: The erythrocyte and lens models
    • Zappia, V, Ed, pp, Plenum Press, New York
    • Lorand L. (1988) Transglutaminase mediated cross-linking of proteins and cell aging: the erythrocyte and lens models, in Advances in post-translational modifications of proteins and aging (Zappia, V., Ed.) pp 79-94, Plenum Press, New York.
    • (1988) Advances in post-translational modifications of proteins and aging , pp. 79-94
    • Lorand, L.1
  • 20
    • 33750142707 scopus 로고    scopus 로고
    • Age-related changes in human crystallins determined from comparative analysis of post-translational modifications in young and aged lens: Does deamidation contribute to crystallin insolubility?
    • Wilmarth, P. A., Tanner, S., Dasari, S., Nagalla, S. R., Riviere, M. A., Bafna, V., Pevzner, P. A., and David, L. L. (2006) Age-related changes in human crystallins determined from comparative analysis of post-translational modifications in young and aged lens: Does deamidation contribute to crystallin insolubility? J. Proteome Res. 5, 2554-2566.
    • (2006) J. Proteome Res , vol.5 , pp. 2554-2566
    • Wilmarth, P.A.1    Tanner, S.2    Dasari, S.3    Nagalla, S.R.4    Riviere, M.A.5    Bafna, V.6    Pevzner, P.A.7    David, L.L.8
  • 21
    • 33644858451 scopus 로고    scopus 로고
    • Deamidation in human lens βB2 crystallin destabilizes the dimer
    • Lampi, K. J., Amyx, K. K., Ahmann, P., and Steel, E. A. (2006) Deamidation in human lens βB2 crystallin destabilizes the dimer. Biochemistry 14, 3146-3153.
    • (2006) Biochemistry , vol.14 , pp. 3146-3153
    • Lampi, K.J.1    Amyx, K.K.2    Ahmann, P.3    Steel, E.A.4
  • 22
    • 7244227985 scopus 로고    scopus 로고
    • Deamidation affects structural and functional properties of human αA-crystallin and its oligomerization with αB-crystallin
    • Gupta, R., and Srivastava, O. P. (2004) Deamidation affects structural and functional properties of human αA-crystallin and its oligomerization with αB-crystallin. J. Biol. Chem. 276, 44258-44269.
    • (2004) J. Biol. Chem , vol.276 , pp. 44258-44269
    • Gupta, R.1    Srivastava, O.P.2
  • 23
    • 0347358073 scopus 로고    scopus 로고
    • Effect of deamidation of asparagine 146 on functional and structural properties of human lens αB-crystallin
    • Gupta, R., and Srivastava, O. P. (2004) Effect of deamidation of asparagine 146 on functional and structural properties of human lens αB-crystallin. Invest. Ophthalmol. Visual Sci. 45, 206-214.
    • (2004) Invest. Ophthalmol. Visual Sci , vol.45 , pp. 206-214
    • Gupta, R.1    Srivastava, O.P.2
  • 25
    • 0016219368 scopus 로고
    • Sequence-dependent deamidation rates for model peptides of cytochrome c
    • Robinson, A. B., McKerrow, J. H., and Legaz, M. (1974) Sequence-dependent deamidation rates for model peptides of cytochrome c. Int. J. Pept. Protein Res. 6, 31-35.
    • (1974) Int. J. Pept. Protein Res , vol.6 , pp. 31-35
    • Robinson, A.B.1    McKerrow, J.H.2    Legaz, M.3
  • 26
    • 0015373660 scopus 로고
    • Deamidation in vivo of an asparagine residue of rabbit muscle aldolase
    • Midelfort, C. F., and Mehler, A. H. (1972) Deamidation in vivo of an asparagine residue of rabbit muscle aldolase. Proc Natl. Acad. Sci. U.S.A 69, 1816-1819.
    • (1972) Proc Natl. Acad. Sci. U.S.A , vol.69 , pp. 1816-1819
    • Midelfort, C.F.1    Mehler, A.H.2
  • 28
    • 0026719184 scopus 로고
    • Deamidation of human erythrocyte protein 4.1: Possible role in aging
    • Inaba, M., Gupta, K. C., Kuwabara, M., Takahashi, T., Benz, E. J., Jr., and Maede, Y. (1992) Deamidation of human erythrocyte protein 4.1: Possible role in aging. Blood 79, 3355-3361.
    • (1992) Blood , vol.79 , pp. 3355-3361
    • Inaba, M.1    Gupta, K.C.2    Kuwabara, M.3    Takahashi, T.4    Benz Jr., E.J.5    Maede, Y.6
  • 29
    • 0017122111 scopus 로고
    • Intracellular degradation and deamidation of α-crystallin subunits
    • van Kleef, F. S. M., Willems-Thijssen, W., and Hoenders, H. J. (1976) Intracellular degradation and deamidation of α-crystallin subunits. Eur. J. Biochem. 66, 477-483.
    • (1976) Eur. J. Biochem , vol.66 , pp. 477-483
    • van Kleef, F.S.M.1    Willems-Thijssen, W.2    Hoenders, H.J.3
  • 31
    • 0034714274 scopus 로고    scopus 로고
    • Specific glutamine and asparagines residues of gamma-S crystallin are resistant to in vivo deamidation
    • Takemoto, L., and Boyle, D. (2000) Specific glutamine and asparagines residues of gamma-S crystallin are resistant to in vivo deamidation. J. Biol. Chem. 275, 26109-26112.
    • (2000) J. Biol. Chem , vol.275 , pp. 26109-26112
    • Takemoto, L.1    Boyle, D.2
  • 32
    • 0030475908 scopus 로고    scopus 로고
    • Modifications of the water-insoluble human lens α-crystallin
    • Lund, A. L., Smith, J. B., and Smith, D. L. (1996) Modifications of the water-insoluble human lens α-crystallin. Exp. Eye Res. 63, 661-672.
    • (1996) Exp. Eye Res , vol.63 , pp. 661-672
    • Lund, A.L.1    Smith, J.B.2    Smith, D.L.3
  • 34
    • 0016259488 scopus 로고
    • Intracellular C-terminal degradation of αA chain of α-crystallin
    • de Jong, W. W., van Kleef, F. S. M., and Bloemendal, H. (1974) Intracellular C-terminal degradation of αA chain of α-crystallin. Eur. J. Biochem. 48, 271-276.
    • (1974) Eur. J. Biochem , vol.48 , pp. 271-276
    • de Jong, W.W.1    van Kleef, F.S.M.2    Bloemendal, H.3
  • 35
    • 0017122111 scopus 로고
    • Intracellular degradation and deamidation of α-crystallin subunits
    • Van Kleef, F. S. M., Willlems-Thyssen, W., and Hoenders, H. J. (1976) Intracellular degradation and deamidation of α-crystallin subunits. Eur. J. Biochem. 66, 477-483.
    • (1976) Eur. J. Biochem , vol.66 , pp. 477-483
    • Van Kleef, F.S.M.1    Willlems-Thyssen, W.2    Hoenders, H.J.3
  • 36
    • 0027982901 scopus 로고
    • Identification of origin of two polypeptides of 4 and 5 kDa isolated from human lenses
    • Srivastava, O. P., Srivastava, K., and Silney, C. (1994) Identification of origin of two polypeptides of 4 and 5 kDa isolated from human lenses. Invest. Ophthalmol. Visual Sci. 35, 207-214.
    • (1994) Invest. Ophthalmol. Visual Sci , vol.35 , pp. 207-214
    • Srivastava, O.P.1    Srivastava, K.2    Silney, C.3
  • 37
    • 0742305818 scopus 로고    scopus 로고
    • Myofibrillar myopathy: Clinical, morphological and genetic studies in 63 patients
    • Selcen, D., Ohno, K., and Engel, A. G. (2004) Myofibrillar myopathy: clinical, morphological and genetic studies in 63 patients. Brain 127, 439-451.
    • (2004) Brain , vol.127 , pp. 439-451
    • Selcen, D.1    Ohno, K.2    Engel, A.G.3
  • 38
    • 0344664368 scopus 로고    scopus 로고
    • Myofibrillar myopathies caused by novel dominant negative αB-crystallin mutation
    • Selcen, D., and Engel, A. G. (2003) Myofibrillar myopathies caused by novel dominant negative αB-crystallin mutation. Ann. Neurol. 54, 804-810.
    • (2003) Ann. Neurol , vol.54 , pp. 804-810
    • Selcen, D.1    Engel, A.G.2
  • 39
    • 20444478694 scopus 로고    scopus 로고
    • The small heat shock proteins and their role in human disease
    • Sun, Y., and MacRae, T. H. (2005) The small heat shock proteins and their role in human disease. FEBS J. 272, 2613-2627.
    • (2005) FEBS J , vol.272 , pp. 2613-2627
    • Sun, Y.1    MacRae, T.H.2
  • 40
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 41
    • 0033042935 scopus 로고    scopus 로고
    • Estimation of number of α-helical and beta strand segments in proteins using circular dichroism spectroscopy
    • Sreerama, N., Venyaminov, S. Y., and Woody, R. W. (1999) Estimation of number of α-helical and beta strand segments in proteins using circular dichroism spectroscopy. Protein Sci. 8, 370-380.
    • (1999) Protein Sci , vol.8 , pp. 370-380
    • Sreerama, N.1    Venyaminov, S.Y.2    Woody, R.W.3
  • 42
    • 0037108280 scopus 로고    scopus 로고
    • A positive charge preservation at position 116 of αA crystallin is critical for its structural and functional integrity
    • Bera, S., Thampi, P., Cho, W. J., and Abraham, E. C. (2002) A positive charge preservation at position 116 of αA crystallin is critical for its structural and functional integrity. Biochemistry 41, 12421-12426.
    • (2002) Biochemistry , vol.41 , pp. 12421-12426
    • Bera, S.1    Thampi, P.2    Cho, W.J.3    Abraham, E.C.4
  • 43
  • 44
    • 17644408766 scopus 로고    scopus 로고
    • Subunit exchange of polydisperse proteins. Mass spectrometry reveals consequences of αA-crystallin truncation
    • Aquilina, J. A., Benesch, J. L. P., Ding, L. L., Yaron, O., Horwitz, J., and Robinson, C. V. (2005) Subunit exchange of polydisperse proteins. Mass spectrometry reveals consequences of αA-crystallin truncation. J. Biol. Chem. 280, 14485-144919.
    • (2005) J. Biol. Chem , vol.280 , pp. 14485-144919
    • Aquilina, J.A.1    Benesch, J.L.P.2    Ding, L.L.3    Yaron, O.4    Horwitz, J.5    Robinson, C.V.6
  • 45
    • 0141988870 scopus 로고    scopus 로고
    • Influence of the C-terminal residues on oligomerization of αA-crystallin
    • Thampi, P., and Abraham, E. C. (2003) Influence of the C-terminal residues on oligomerization of αA-crystallin. Biochemistry 42, 11857-11863.
    • (2003) Biochemistry , vol.42 , pp. 11857-11863
    • Thampi, P.1    Abraham, E.C.2
  • 46
    • 2642563501 scopus 로고    scopus 로고
    • Evgrafov, O. V., Mersiyanova, I., Irobi, J., Van Den Bosch, L., Dierick, I., Leung, C. L., Schagina, O., Verpoorten, N., Van Impe, K., Fedotov, V., Dadali, E., Auer-Grumbach, M., Windpassinger, C., Wagner, K., Mitrovic, Z., Hilton-Jones, D., Talbot, K., Martin, J. J., Vasserman, N., Tverskaya, S., Polyakov, A., Liem, R. K., Gettemans, J., Robberecht, W., De Jonghe, P., and Timmerman, V. (2004) Mutant small heat-shock protein 27 causes axonal Charcot-Marie-Tooth disease and distal hereditary motor neuropathy. Nat. Genet. 36, 602-606.
    • Evgrafov, O. V., Mersiyanova, I., Irobi, J., Van Den Bosch, L., Dierick, I., Leung, C. L., Schagina, O., Verpoorten, N., Van Impe, K., Fedotov, V., Dadali, E., Auer-Grumbach, M., Windpassinger, C., Wagner, K., Mitrovic, Z., Hilton-Jones, D., Talbot, K., Martin, J. J., Vasserman, N., Tverskaya, S., Polyakov, A., Liem, R. K., Gettemans, J., Robberecht, W., De Jonghe, P., and Timmerman, V. (2004) Mutant small heat-shock protein 27 causes axonal Charcot-Marie-Tooth disease and distal hereditary motor neuropathy. Nat. Genet. 36, 602-606.
  • 47
    • 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., and Quinn, P. T. (2000) Synthesis and characterization of a peptide identified as a functional element in αA-crystallin. J. Biol. Chem. 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
  • 48
    • 0032546801 scopus 로고    scopus 로고
    • Identification of 1,1′-Bi(4-anilino) naphthalene-5,5′-disulfonic acid binding sequence in α-crystallin
    • Sharma, K. K., Kumar, G. S., Murphy, A. S., and Kester, K. (1998) Identification of 1,1′-Bi(4-anilino) naphthalene-5,5′-disulfonic acid binding sequence in α-crystallin. J. Biol. Chem. 273, 15474-15478.
    • (1998) J. Biol. Chem , vol.273 , pp. 15474-15478
    • Sharma, K.K.1    Kumar, G.S.2    Murphy, A.S.3    Kester, K.4
  • 49
    • 0029083170 scopus 로고
    • Conversion from oligomers to tetramers enhances autophosphorylation by lens αA-crystallin
    • Kantorow, M., Horwitz, J., van Boekel, M. A., deJong, W. W., and Piatigorsky, J. (1995) Conversion from oligomers to tetramers enhances autophosphorylation by lens αA-crystallin. J. Biol. Chem. 270, 17215-17220.
    • (1995) J. Biol. Chem , vol.270 , pp. 17215-17220
    • Kantorow, M.1    Horwitz, J.2    van Boekel, M.A.3    deJong, W.W.4    Piatigorsky, J.5
  • 50
    • 0037040277 scopus 로고    scopus 로고
    • Detection of protein-protein interactions among lens crystallins in a mammalian two-hybrid system assay
    • Fu, L., and Liang, J. J.-N. (2002) Detection of protein-protein interactions among lens crystallins in a mammalian two-hybrid system assay. J. Biol. Chem. 277, 4255-4260.
    • (2002) J. Biol. Chem , vol.277 , pp. 4255-4260
    • Fu, L.1    Liang, J.J.-N.2
  • 51
    • 0034698120 scopus 로고    scopus 로고
    • Domain swapping in human alpha A and alpha B crystalline affects oligomerization and enhances chaperone-like activity
    • Kumar, L. V., and Rao, C. M. (2000) Domain swapping in human alpha A and alpha B crystalline affects oligomerization and enhances chaperone-like activity. J. Biol. Chem. 275, 22009-22013.
    • (2000) J. Biol. Chem , vol.275 , pp. 22009-22013
    • Kumar, L.V.1    Rao, C.M.2
  • 52
    • 0034731332 scopus 로고    scopus 로고
    • Packing-induced conformational and functional changes in subunit of α-crystallin
    • Datta, S. A., and Rao, C. M. (2000) Packing-induced conformational and functional changes in subunit of α-crystallin. J. Biol. Chem. 275, 41004-41010.
    • (2000) J. Biol. Chem , vol.275 , pp. 41004-41010
    • Datta, S.A.1    Rao, C.M.2
  • 53
    • 0034719154 scopus 로고    scopus 로고
    • Structural and functional changes in the αA-crystallin R116C mutant in hereditary cataracts
    • Cobb, B. A., and Petrash, J. M. (2000) Structural and functional changes in the αA-crystallin R116C mutant in hereditary cataracts. Biochemistry 39, 15791-15798.
    • (2000) Biochemistry , vol.39 , pp. 15791-15798
    • Cobb, B.A.1    Petrash, J.M.2
  • 54
    • 25444524072 scopus 로고    scopus 로고
    • Interaction and biophysical properties of human lens Q155*-βB2 mutant
    • Liu, B.-F., and Liand, J. J.-K. (2005) Interaction and biophysical properties of human lens Q155*-βB2 mutant. Mol. Vision 11, 321-327.
    • (2005) Mol. Vision , vol.11 , pp. 321-327
    • Liu, B.-F.1    Liand, J.J.-K.2
  • 55
    • 33744732089 scopus 로고    scopus 로고
    • A transgenic mouse model for human autosomal dominant cataract
    • Hsu, C.-D., Kymes, S., and Petrash, J. M. (2006) A transgenic mouse model for human autosomal dominant cataract. Invest. Ophthalmol. Visual Sci. 47, 2036-2044.
    • (2006) Invest. Ophthalmol. Visual Sci , vol.47 , pp. 2036-2044
    • Hsu, C.-D.1    Kymes, S.2    Petrash, J.M.3
  • 56
    • 0037039153 scopus 로고    scopus 로고
    • The αA-crystallin R116C mutant has a higher affinity for forming heteroaggregates with αB-crystallin
    • Bera, S., and Abraham, E. C. (2002) The αA-crystallin R116C mutant has a higher affinity for forming heteroaggregates with αB-crystallin. Biochemistry 41, 297-305.
    • (2002) Biochemistry , vol.41 , pp. 297-305
    • Bera, S.1    Abraham, E.C.2
  • 57
    • 0032077199 scopus 로고    scopus 로고
    • Hydrophobicity and flexibility of αA- and αB-crystallin are different
    • Bloemendal, M., and Bloemendal, H. (1998) Hydrophobicity and flexibility of αA- and αB-crystallin are different. Int. J. Biol. Macromol. 22, 239-245.
    • (1998) Int. J. Biol. Macromol , vol.22 , pp. 239-245
    • Bloemendal, M.1    Bloemendal, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.