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Volumn 48, Issue 2, 2009, Pages 442-453

Abnormal assemblies and subunit exchange of αB-crystallin R120 mutants could be associated with destabilization of the dimeric substructure

Author keywords

[No Author keywords available]

Indexed keywords

LIGHT SCATTERING; MOLECULAR DYNAMICS; SIMULATED ANNEALING; STRUCTURAL DYNAMICS; X RAY SCATTERING;

EID: 59849129128     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi8014967     Document Type: Article
Times cited : (43)

References (56)
  • 1
    • 0035718677 scopus 로고    scopus 로고
    • Structure and function of the small heat shock protein/α-crystallin family of molecular chaperones
    • van Montfort, R., Slingsby, C., and Vierling, E. (2001) Structure and function of the small heat shock protein/α-crystallin family of molecular chaperones. AdV. Protein Chem. 59, 105-156.
    • (2001) AdV. Protein Chem , vol.59 , pp. 105-156
    • van Montfort, R.1    Slingsby, C.2    Vierling, E.3
  • 2
    • 27144448839 scopus 로고    scopus 로고
    • Some like it hot: The structure and function of small heat shock proteins
    • Haslbeck, M., Franzmann, T., Weinfurtner, D., and Buchner, J. (2005) Some like it hot: The structure and function of small heat shock proteins. Nat. Struct. Mol. Biol. 12, 842-846.
    • (2005) Nat. Struct. Mol. Biol , vol.12 , pp. 842-846
    • Haslbeck, M.1    Franzmann, T.2    Weinfurtner, D.3    Buchner, J.4
  • 6
    • 0031934121 scopus 로고    scopus 로고
    • Autosomal dominant congenital cataract associated with a missense mutation in the human α-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 α-crystallin gene CRYAA. Hum. Mol. Genet. 7, 471-474.
    • (1998) Hum. Mol. Genet , vol.7 , pp. 471-474
    • Litt, M.1    Kramer, P.2    LaMorticella, D.M.3    Murphey, W.4    Lovrien, E.W.5    Weleber, R.G.6
  • 8
    • 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.
  • 10
    • 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.
    • (1998) Int. J. Biol. Macromol , vol.22 , pp. 151-162
    • de Jong, W.W.1    Caspers, G.J.2    Leunissen, J.A.3
  • 11
    • 1342292267 scopus 로고    scopus 로고
    • Crystal structure of a small heat-shock protein
    • Kim, K. K, Kim, R., and Kim, S. H. (1998) Crystal structure of a small heat-shock protein. Nature 394, 595-599.
    • (1998) Nature , vol.394 , pp. 595-599
    • Kim, K.K.1    Kim, R.2    Kim, S.H.3
  • 13
    • 25144461582 scopus 로고    scopus 로고
    • Wrapping the α-crystallin domain fold in a chaperone assembly
    • Stamler, R., Kappe, G., Boelens, W., and Slingsby, C. (2005) Wrapping the α-crystallin domain fold in a chaperone assembly. J. Mol. Biol. 353, 68-79.
    • (2005) J. Mol. Biol , vol.353 , pp. 68-79
    • Stamler, R.1    Kappe, G.2    Boelens, W.3    Slingsby, C.4
  • 16
    • 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.
    • (2006) J. Biol. Chem , vol.281 , pp. 40420-40428
    • Shi, J.1    Koteiche, H.A.2    McHaourab, H.S.3    Stewart, P.L.4
  • 18
    • 0141703310 scopus 로고    scopus 로고
    • Polydispersity of a mammalian chaperone: Mass spectrometry reveals the population of oligomers in αB-crystallin
    • Aquilina, J. A., Benesch, J. L., Bateman, O. A., Slingsby, C., and Robinson, C. V. (2003) Polydispersity of a mammalian chaperone: Mass spectrometry reveals the population of oligomers in αB-crystallin. Proc. Natl. Acad. Sci. U.S.A. 100, 10611-10616.
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 10611-10616
    • Aquilina, J.A.1    Benesch, J.L.2    Bateman, O.A.3    Slingsby, C.4    Robinson, C.V.5
  • 19
    • 0037325497 scopus 로고    scopus 로고
    • α-crystallin
    • Horwitz, J. (2003) α-crystallin. Exp. Eye Res. 76, 145-153.
    • (2003) Exp. Eye Res , vol.76 , pp. 145-153
    • Horwitz, J.1
  • 21
    • 16544382615 scopus 로고    scopus 로고
    • The IXI/V motif in the C-terminal extension of alpha-crystallins: Alternative interactions and oligomeric assemblies
    • Pasta, S. Y., Raman, B., Ramakrishna, T., and Rao, Ch. M. (2004) The IXI/V motif in the C-terminal extension of alpha-crystallins: alternative interactions and oligomeric assemblies. Mol Vis. 10, 655-662.
    • (2004) Mol Vis , vol.10 , pp. 655-662
    • Pasta, S.Y.1    Raman, B.2    Ramakrishna, T.3    Rao, C.M.4
  • 22
    • 0346435099 scopus 로고    scopus 로고
    • Role of the conserved SRLFDQFFG region of α-crystallin, a small heat shock protein. Effect on oligomeric size, subunit exchange, and chaperone-like activity
    • Pasta, S. Y., Raman, B., Ramakrishna, T., and Rao, Ch. M. (2003) Role of the conserved SRLFDQFFG region of α-crystallin, a small heat shock protein. Effect on oligomeric size, subunit exchange, and chaperone-like activity. J. Biol. Chem. 278, 51159-51166.
    • (2003) J. Biol. Chem , vol.278 , pp. 51159-51166
    • Pasta, S.Y.1    Raman, B.2    Ramakrishna, T.3    Rao, C.M.4
  • 23
    • 14144255401 scopus 로고    scopus 로고
    • Insights into the domains required for dimerization and assembly of human αB-crystallin
    • Ghosh, J. G., and Clark, J. I. (2005) Insights 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
  • 24
    • 24644480940 scopus 로고    scopus 로고
    • Recognition sequence 2 (residues 60-71) plays a role in oligomerization and exchange dynamics of αB-crystallin
    • Sreelakshmi, Y., and Sharma, K. K. (2005) Recognition sequence 2 (residues 60-71) plays a role in oligomerization and exchange dynamics of αB-crystallin. Biochemistry 44, 12245-12252.
    • (2005) Biochemistry , vol.44 , pp. 12245-12252
    • Sreelakshmi, Y.1    Sharma, K.K.2
  • 25
    • 3142543752 scopus 로고    scopus 로고
    • Phosphorylation of αB-crystallin. alters chaperone function through loss of dimeric substructure
    • Aquilina, J. A., Benesch, J. L., Ding, L. L., Yaron, O., Horwitz, J., and Robinson, C. V. (2004) Phosphorylation of αB-crystallin. alters chaperone function through loss of dimeric substructure. J. Biol. Chem. 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
  • 26
    • 27744485379 scopus 로고    scopus 로고
    • Interactive domains for chaperone activity in the small heat shock protein, human αB-crystallin
    • Ghosh, J. G., Estrada, M. R., and Clark, J. I. (2005) Interactive domains for chaperone activity in the small heat shock protein, human αB-crystallin. Biochemistry 44, 14854-14869.
    • (2005) Biochemistry , vol.44 , pp. 14854-14869
    • Ghosh, J.G.1    Estrada, M.R.2    Clark, J.I.3
  • 27
    • 33751244272 scopus 로고    scopus 로고
    • N- and C-Terminal motifs in human αB-crystallin. play an important role in the recognition, selection, and solubilization of substrates
    • Ghosh, J. G., Jr, and Clark, J. I. (2006) N- and C-Terminal motifs in human αB-crystallin. play an important role in the recognition, selection, and solubilization of substrates. Biochemistry 45, 13847-13854.
    • (2006) Biochemistry , vol.45 , pp. 13847-13854
    • Ghosh Jr, J.G.1    Clark, J.I.2
  • 28
    • 33751120442 scopus 로고    scopus 로고
    • Conserved F84 and P86 residues in alphaB-crystallin are essential to effectively prevent the aggregation of substrate proteins
    • Santhoshkumar, P., and Sharma, K. K. (2006) Conserved F84 and P86 residues in alphaB-crystallin are essential to effectively prevent the aggregation of substrate proteins. Protein Sci. 15, 2488-2498.
    • (2006) Protein Sci , vol.15 , pp. 2488-2498
    • Santhoshkumar, P.1    Sharma, K.K.2
  • 29
    • 33644690454 scopus 로고    scopus 로고
    • Mini-alphaB-crystallin: A functional element of αB-crystallin. with chaperone-like activity
    • Bhattacharyya, J., Padmanabha Udupa, E. G., Wang, J., and Sharma, K. K. (2006) Mini-alphaB-crystallin: a functional element of αB-crystallin. with chaperone-like activity. Biochemistry 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
  • 31
    • 33646007016 scopus 로고    scopus 로고
    • sHSPs under temperature and pressure: The opposite behaviour of lens α-crystallins and yeast HSP26
    • Skouri-Panet, F., Quevillon-Cheruel, S., Michiel, M., Tardieu, A., and Finet, S. (2006) sHSPs under temperature and pressure: The opposite behaviour of lens α-crystallins and yeast HSP26. Biochim. Biophys. Acta 1764, 372-383.
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 372-383
    • Skouri-Panet, F.1    Quevillon-Cheruel, S.2    Michiel, M.3    Tardieu, A.4    Finet, S.5
  • 32
    • 38649115030 scopus 로고    scopus 로고
    • Activation of the Chaperone Hsp26 Is Controlled by the Rearrangement of Its Thermosensor Domain
    • Franzmann, T. M., Menhorn, P., Walter, S., and Buchner, J. (2008) Activation of the Chaperone Hsp26 Is Controlled by the Rearrangement of Its Thermosensor Domain. Mol. Cell 29, 207-216.
    • (2008) Mol. Cell , vol.29 , pp. 207-216
    • Franzmann, T.M.1    Menhorn, P.2    Walter, S.3    Buchner, J.4
  • 33
    • 0038529737 scopus 로고    scopus 로고
    • Subunit exchange demonstrates a differential chaperone activity of calf α-crystallin toward βLOW- and individual γ-crystallins
    • Putilina, T., Skouri-Panet, F., Prat, K., Lubsen, N. H., and Tardieu, A. (2003) Subunit exchange demonstrates a differential chaperone activity of calf α-crystallin toward βLOW- and individual γ-crystallins. J. Biol. Chem. 278, 13747-13756.
    • (2003) J. Biol. Chem , vol.278 , pp. 13747-13756
    • Putilina, T.1    Skouri-Panet, F.2    Prat, K.3    Lubsen, N.H.4    Tardieu, A.5
  • 34
    • 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., Ding, 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.3    Ding, L.4    Haley, D.A.5    Stewart, P.L.6    Horwitz, J.7
  • 36
    • 34548067977 scopus 로고    scopus 로고
    • Residue R120 is essential for the quaternary structure and functional integrity of human αB-crystallin
    • Simon, S., Michiel, M., Skouri-Panet, F., Lechaire, J. P., Vicart, P., and Tardieu, A. (2007) Residue R120 is essential for the quaternary structure and functional integrity of human αB-crystallin. Biochemistry 46, 9605-9614.
    • (2007) Biochemistry , vol.46 , pp. 9605-9614
    • Simon, S.1    Michiel, M.2    Skouri-Panet, F.3    Lechaire, J.P.4    Vicart, P.5    Tardieu, A.6
  • 37
    • 22844438853 scopus 로고    scopus 로고
    • Quasielas-tic light scattering for protein assembly studies
    • Lomakin, A., Teplow, D. B., and Benedek, G B. (2005) Quasielas-tic light scattering for protein assembly studies. Methods Mol. Biol. 299, 153-174.
    • (2005) Methods Mol. Biol , vol.299 , pp. 153-174
    • Lomakin, A.1    Teplow, D.B.2    Benedek, G.B.3
  • 38
  • 39
    • 34248372968 scopus 로고    scopus 로고
    • Reduction of two-dimensional small- and wide angle X-ray scattering data
    • Boesecke, P. (2007) Reduction of two-dimensional small- and wide angle X-ray scattering data. J. Appl. Crystallogr. 40, S423-427.
    • (2007) J. Appl. Crystallogr , vol.40
    • Boesecke, P.1
  • 41
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: Multiple sequence alignment with high accuracy and high throughput
    • Edgar, R. C. (2004) MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res. 32 (5), 1792-1797.
    • (2004) Nucleic Acids Res , vol.32 , Issue.5 , pp. 1792-1797
    • Edgar, R.C.1
  • 42
    • 38549141229 scopus 로고    scopus 로고
    • Exploring the extremes of sequence/structure space with ensemble fold recognition in the program Phyre
    • Bennett-Lovsey, R. M., Herbert, A. D., Sternberg, M. J. E., and Kelley, L. A. (2008) Exploring the extremes of sequence/structure space with ensemble fold recognition in the program Phyre. Proteins 703, 611-625.
    • (2008) Proteins , vol.703 , pp. 611-625
    • Bennett-Lovsey, R.M.1    Herbert, A.D.2    Sternberg, M.J.E.3    Kelley, L.A.4
  • 43
    • 0000009443 scopus 로고
    • Rapid comparison of protein structures
    • McLachlan, A. D. (1982) Rapid comparison of protein structures. Acta Crystallogr., Sect. A 38, 871-873.
    • (1982) Acta Crystallogr., Sect. A , vol.38 , pp. 871-873
    • McLachlan, A.D.1
  • 44
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: A package for molecular simulation and trajectory analysis
    • Lindahl, E., Hess, B., and van der Spoel, D. (2001) GROMACS 3.0: A package for molecular simulation and trajectory analysis. J. Mol. Model. 7, 306-317.
    • (2001) J. Mol. Model , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    van der Spoel, D.3
  • 45
    • 0028103275 scopus 로고    scopus 로고
    • Collaborative Computational Project, Number 4. (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr., Sect. D 50, 760-763.
    • Collaborative Computational Project, Number 4. (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr., Sect. D 50, 760-763.
  • 46
    • 0033588379 scopus 로고    scopus 로고
    • Structural and functional consequences of the mutation of a conserved arginine residue in RA and αB-crystallin.s
    • Kumar, L. V., Ramakrishna, T., and Rao, C. M. (1999) Structural and functional consequences of the mutation of a conserved arginine residue in RA and αB-crystallin.s. J. Biol. Chem. 274, 24137-24141.
    • (1999) J. Biol. Chem , vol.274 , pp. 24137-24141
    • Kumar, L.V.1    Ramakrishna, T.2    Rao, C.M.3
  • 47
    • 0000843475 scopus 로고    scopus 로고
    • The cardiomyopathy and lens cataract mutation in αB-crystallin. alters its protein structure, chaperone activity, and interaction with intermediate filaments in vitro
    • Perng, M. D., Muchowski, P. J., van Den, I. P., Wu, G J., Hutcheson, A. M., Clark, J. I., and Quinlan, R. A. (1999) The cardiomyopathy and lens cataract mutation in αB-crystallin. alters its protein structure, chaperone activity, and interaction with intermediate filaments in vitro. J. Biol. Chem. 274, 33235-33243.
    • (1999) J. Biol. Chem , vol.274 , pp. 33235-33243
    • Perng, M.D.1    Muchowski, P.J.2    van Den, I.P.3    Wu, G.J.4    Hutcheson, A.M.5    Clark, J.I.6    Quinlan, R.A.7
  • 48
    • 36348957457 scopus 로고    scopus 로고
    • Myopathy-associated alphaB-crystallin mutants: Abnormal phosphorylation, intracellular location, and interactions with other small heat shock proteins
    • Simon, S., Fontaine, J. M., Martin, J. L., Sun, X., Hoppe, A. D., Welsh, M. J., Benndorf, R., and Vicart, P. (2007) Myopathy-associated alphaB-crystallin mutants: abnormal phosphorylation, intracellular location, and interactions with other small heat shock proteins. J. Biol. Chem. 282, 34276-34287.
    • (2007) J. Biol. Chem , vol.282 , pp. 34276-34287
    • Simon, S.1    Fontaine, J.M.2    Martin, J.L.3    Sun, X.4    Hoppe, A.D.5    Welsh, M.J.6    Benndorf, R.7    Vicart, P.8
  • 50
    • 33745712767 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer study of subunit exchange in human lens crystallins and congenital cataract crystallin mutants
    • Liang, J. J., and Liu, B. F. (2006) Fluorescence resonance energy transfer study of subunit exchange in human lens crystallins and congenital cataract crystallin mutants. Protein Sci. 15, 1619-1627.
    • (2006) Protein Sci , vol.15 , pp. 1619-1627
    • Liang, J.J.1    Liu, B.F.2
  • 51
    • 0031962334 scopus 로고    scopus 로고
    • Intermolecular exchange and stabilization of recombinant human alphaA- and alphaB-crystallin
    • Sun, T. X., and Liang, J. J. (1998) Intermolecular exchange and stabilization of recombinant human alphaA- and alphaB-crystallin. J. Biol. Chem. 273, 286-290.
    • (1998) J. Biol. Chem , vol.273 , pp. 286-290
    • Sun, T.X.1    Liang, J.J.2
  • 52
    • 0037064096 scopus 로고    scopus 로고
    • Subunit exchange of multimeric protein complexes. Realtime monitoring of subunit exchange between small heat shock proteins by using electrospray mass spectrometry
    • Sobott, F., Benesch, J. L. P., Vierling, E., and Robinson, C. V. (2002) Subunit exchange of multimeric protein complexes. Realtime monitoring of subunit exchange between small heat shock proteins by using electrospray mass spectrometry. J. Biol. Chem. 277 (41), 38921-38929.
    • (2002) J. Biol. Chem , vol.277 , Issue.41 , pp. 38921-38929
    • Sobott, F.1    Benesch, J.L.P.2    Vierling, E.3    Robinson, C.V.4
  • 53
    • 17644408766 scopus 로고    scopus 로고
    • Subunit exchange of polydisperse proteins: Mass spectrometry reveals consequences of αA-crystallin truncation
    • Aquilina, J. A., Benesch, J. L., 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, 14485-14491.
    • (2005) J. Biol. Chem , vol.280 , pp. 14485-14491
    • Aquilina, J.A.1    Benesch, J.L.2    Ding, L.L.3    Yaron, O.4    Horwitz, J.5    Robinson, C.V.6
  • 54
    • 17744391285 scopus 로고    scopus 로고
    • Unfolding crystallins: The destabilizing role of a β-hairpin cysteine in βB2-crystallin by simulation and experiment
    • MacDonald, J. T., Purkiss, A. G., Smith, M. A., Evans, P., Goodfellow, J. M., and Slingsby, C. (2005) Unfolding crystallins: The destabilizing role of a β-hairpin cysteine in βB2-crystallin by simulation and experiment. Protein Sci. 14, 1282-1293.
    • (2005) Protein Sci , vol.14 , pp. 1282-1293
    • MacDonald, J.T.1    Purkiss, A.G.2    Smith, M.A.3    Evans, P.4    Goodfellow, J.M.5    Slingsby, C.6
  • 55
    • 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 αB-crystallin. and its phosphorylation-mimicking mutant
    • Ahmad, M. F., Raman, B., Ramakrishna, T., and Rao, Ch. M. (2008) Effect of phosphorylation on alpha B-crystallin: differences in stability, subunit exchange and chaperone activity of homo and mixed oligomers of αB-crystallin. and its phosphorylation-mimicking mutant. J. Mol. Biol. 375, 1040-1051.
    • (2008) J. Mol. Biol , vol.375 , pp. 1040-1051
    • Ahmad, M.F.1    Raman, B.2    Ramakrishna, T.3    Rao, C.M.4
  • 56
    • 0038723738 scopus 로고    scopus 로고
    • Hsp27 suppresses the formation of inclusion bodies induced by expression of R120G αB-crystallin., a cause of desmin-related myopathy
    • Ito, H., Kamei, K., Iwamoto, I., Inaguma, Y., Tsuzuki, M., Kishikawa, M., Shimada, A., Hosokawa, M., and Kato, K. (2003) Hsp27 suppresses the formation of inclusion bodies induced by expression of R120G αB-crystallin., a cause of desmin-related myopathy. Cell. Mol. Life Sci. 60, 1217-1223.
    • (2003) Cell. Mol. Life Sci , vol.60 , pp. 1217-1223
    • Ito, H.1    Kamei, K.2    Iwamoto, I.3    Inaguma, Y.4    Tsuzuki, M.5    Kishikawa, M.6    Shimada, A.7    Hosokawa, M.8    Kato, K.9


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