SEARCH

SEARCH BY CITATION

References

  • 1
    Boelens, W.C. & de Jong, W.W. (1995) α-Crystallins, versatile stress-proteins. Mol. Biol. Report 21, 75 80.
  • 2
    Ehrnsperger, M., Buchner, J., Gaestel, M. (1997) Structure and function of small heat shock proteins. In Molecular Chaperones in the Life Cycle of Proteins. Structure, Function and Mode of Action (Fink, A.L. & Goto, Y., eds), pp. 533 575. Marcel Dekker, New York.
  • 3
    Carver, J.A., Aquilina, J.A., Cooper, P.G., Williams, G.A., Truscott, R.J.W. (1994) Alpha-crystallin: molecular chaperone and protein surfactant. Biochim. Biophys. Acta 1204, 195 206.
  • 4
    Ehrnsperger, M., Gräber, S., Gaestel, M., Buchner, J. (1997) Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation. EMBO J. 16, 221 229.
  • 5
    Groenen, P.J.T.A., Merck, K.B., de Jong, W.W., Bloemendal, H. (1994) Structure and modifications of the junior chaperone alpha-crystallin − from lens transparency to molecular pathology. Eur. J. Biochem. 225, 1 19.
  • 6
    Behlke, J., Lutsch, G., Gaestel, M., Bielka, H. (1991) Supramolecular structure of the recombinant murine small heat shock protein hsp25. FEBS Lett. 288, 119 122.
  • 7
    Kim, K.K., Kim, R., Kim, S.-H. (1998) Crystal structure of a small heat-shock protein. Nature 394, 595 599.
  • 8
    Brady, J.P., Garland, D., Duglas-Tabor, Y., Robison, W.G. Jr, Groome, A., Wawrousek, E.F. (1997) Targeted disruption of the mouse alpha-A-crystallin gene induces cataract and cytoplasmic inclusion bodies containing the small heat shock protein alpha-B-crystallin. Proc. Natl Acad. Sci. USA 94, 884 889.
  • 9
    Carver, J.A., Aquilina, J.A., Truscott, R.J.W., Ralston, G.B. (1992) Identification by 1H NMR spectroscopy of flexible C-terminal extensions in bovine lens alpha-crystallin. FEBS Lett. 311, 143 149.
  • 10
    Carver, J.A., Esposito, G., Schwedersky, G., Gaestel, M. (1995) 1H NMR spectroscopy reveals that mouse Hsp25 has a flexible C-terminal extension of 18 amino acids. FEBS Lett. 369, 305 310.DOI: 10.1016/0014-5793(95)00770-a
  • 11
    Esposito, G., Viglino, P., Fogolari, F., Gaestel, M., Carver, J.A. (1998) Selective NMR experiments on macromolecules − implementation and analysis of QUIET-NOESY. J. Magn. Reson. 132, 204 213.DOI: 10.1006/jmre.1998.1430
  • 12
    Smulders, R.H.P.H., Carver, J.A., Lindner, R.A., van Boekel, M.A.M., Bloemendal, H., de Jong, W.W. (1996) Immobilization of the C-terminal extension of bovine αA-crystallin reduces chaperone-like activity. J. Biol. Chem. 271, 29060 29066.
  • 13
    Carver, J.A., Nicholls, K.A., Aquilina, J.A., Truscott, R.J.W. (1996) Age-related changes in bovine α-crystallin and high-molecular-weight protein. Exp. Eye Res. 63, 639 647.DOI: 10.1006/exer.1996.0158
  • 14
    Carver, J.A., Guerreiro, N., Nicholls, K.A., Truscott, R.J.W. (1995) On the interaction of α-crystallin with unfolded proteins. Biochim. Biophys. Acta 1252, 251 260.
  • 15
    Lindner, R.A., Kapur, A., Mariani, M., Titmuss, S., Carver, J.A. (1998) Structural alterations of α-crystallin during its chaperone action. Eur. J. Biochem. 258, 170 183.
  • 16
    Slingsby, C. & Bateman, O.A. (1990) Rapid separation of bovine beta-crystallin subunits beta B1, beta B2, beta B3, beta A3 and beta A4. Exp. Eye Res. 51, 21 26.
  • 17
    Engel, K., Knauf, U., Gaestel, M. (1991) Generation of antibodies against human hsp27 and murine hsp25 by immunization with a chimeric small heat shock protein. Biomed. Biochim. Acta 50, 1065 1071.
  • 18
    Buchner, J., Ehrnsperger, M., Gaestel, M., Walke, S. (1998) Purification and characterization of small heat shock proteins. Methods Enzymol. 290, 339 349.
  • 19
    Farahbakhsh, Z.T., Huang, Q.L., Ding, L.L., Altenbach, C., Steinhoff, H.J., Horwitz, J., Hubbell, W.L. (1995) Interaction of alpha-crystallin with spin-labeled peptides. Biochemistry 34, 509 516.
  • 20
    Manavalan, P. & Johnson, W.C. Jr (1987) Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra. Anal. Biochem. 167, 76 85.
  • 21
    Behlke, J., Ristau, O., Schönfeld, H.-J. (1997) Nucleotide-dependent complex formation between the Escherichia coli chaperonins GroEL and GroES studied under equilibrium conditions. Biochemistry 36, 5149 5156.
  • 22
    Behlke, J. & Ristau, O. (1997) Molecular mass determination by sedimentation velocity experiments and direct fitting of the concentration profiles. Biophys. J. 72, 428 434.
  • 23
    Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680 685.
  • 24
    Werten, P.J.L., Carver, J.A., Jaenicke, R., de Jong, W.W. (1996) The elusive role of the N-terminal extension βA3- and βA1-crystallin. Prot. Eng. 9, 1021 1028.
  • 25
    Merck, K.B., Horwitz, J., Kersten, M., Overkamp, P., Gaestel, M., Bloemendal, H., de Jong, W.W. (1993) Comparison of the homologous carboxy-terminal domain and tail of alpha-crystallin and small heat shock protein. Mol. Biol. Report 18, 209 215.
  • 26
    Kuwajima, K., Ikeguchi, M., Sugawara, T., Hiraoka, Y., Sugai, S. (1990) Kinetics of disulfide bond reduction in alpha-lactalbumin by dithiothreitol and molecular basis of superreactivity of the Cys6–Cys120 disulfide bond. Biochemistry 29, 8240 8249.
  • 27
    Lindner, R.A., Kapur, A., Carver, J.A. (1997) The interaction of the molecular chaperone, α-crystallin, with molten globule states of bovine α-lactalbumin. J. Biol. Chem. 272, 27722 27729.
  • 28
    Zavialov, A., Benndorf, R., Ehrnsperger, M., Zav’Yalov, V., Dudich, I., Buchner, J., Gaestel, M. (1998) The effect of the intersubunit disulfide bond on the structural and functional properties of the small heat shock protein Hsp25. Int. J. Biol. Macromol. 22, 163 173.DOI: 10.1016/s0141-8130(98)00014-2
  • 29
    Das, K.P. & Surewicz, W.K. (1995) Temperature-induced exposure of hydrophobic surfaces and its effect on the chaperone activity of alpha-crystallin. FEBS Lett. 369, 321 325.DOI: 10.1016/0014-5793(95)00775-5
  • 30
    Raman, B., Ramakrishna, T., Rao, CH.M. (1995) Temperature dependent chaperone-like activity of alpha-crystallin. FEBS Lett. 365, 133 136.DOI: 10.1016/0014-5793(95)00440-k
  • 31
    Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248 254.
  • 32
    Wüthrich, K. (1986) NMR of Proteins and Nucleic Acids. J. Wiley, New York.
  • 33
    Wishart, D.S., Bigam, C.G., Holm, A., Hodges, R.S., Sykes, B.D. (1995) 1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. 1. Investigations of nearest neighbor effects. J. Biomol. NMR 5, 67 81.
  • 34
    Caspers, G.J., Leunissen, J.A.M., de Jong, W.W. (1995) The expanding small heat-shock protein family, and structure predictions of the conserved alpha-crystallin domain. J. Mol. Evol. 40, 238 248.
  • 35
    Smulders, R.H.P.H., van Boekel, M.A., de Jong, W.W. (1998) Mutations and modifications support a ‘pitted-flexiball’ model for α-crystallin. Int. J. Biol. Macromol. 22, 187 196.DOI: 10.1016/s0141-8130(98)00016-6
  • 36
    van Boekel, M.A.M., Lange, F., de Grip, W.J., de Jong, W.W. (1999) Eye lens αA- and αB-crystallin: complex stability versus chaperone-like activity. Biochim. Biophys. Acta 1434, 114 123.
  • 37
    Lee, C.Y., McCammon, J.A., Rossky, P.J. (1984) The structure of liquid water at an extended hydrophobic surface. J. Chem. Phys. 80, 4448 4455.
  • 38
    Leroux, M.R., Melki, R., Gordon, B., Batelier, G., Candido, E.P.M. (1997) Structure–function studies on small heat shock protein oligomeric assembly and interaction with unfolded polypeptides. J. Biol. Chem. 272, 24646 24656.
  • 39
    Wistow, G. (1985) Domain structure and evolution in alpha-crystallins and small heat-shock proteins. FEBS Lett. 181, 1 6.
  • 40
    Siezen, R.J. & Hoenders, H.J. (1979) The quarternary structure of bovine alpha-crystallin. Surface probing by limited proteolysis in vitro. Eur. J. Biochem. 96, 431 440.