參考文獻 |
Abulimiti, A., Qiu, X., Chen, J., Liu, Y., and Chang, Z. (2003). Reversible methionine sulfoxidation of Mycobacterium tuberculosis small heat shock protein Hsp16.3 and its possible role in scavenging oxidants. Biochem Biophys Res Commun 305, 87-93.
Anil, B., Sato, S., Cho, J.H., and Raleigh, D.P. (2005). Fine structure analysis of a protein folding transition state; distinguishing between hydrophobic stabilization and specific packing. J Mol Biol 354, 693-705.
Aufricht, C., Lu, E., Thulin, G., Kashgarian, M., Siegel, N.J., and Van Why, S.K. (1998). ATP releases HSP-72 from protein aggregates after renal ischemia. Am J Physiol 274, F268-274.
Augusteyn, R.C. (2004). alpha-crystallin: a review of its structure and function. Clin Exp Optom 87, 356-366.
Ayling, A., and Baneyx, F. (1996). Influence of the GroE molecular chaperone machine on the in vitro refolding of Escherichia coli beta-galactosidase. Protein Sci 5, 478-487.
Basha, E., Lee, G.J., Demeler, B., and Vierling, E. (2004). Chaperone activity of cytosolic small heat shock proteins from wheat. Eur J Biochem 271, 1426-1436.
Bhattacharyya, J., Padmanabha Udupa, E.G., Wang, J., and Sharma, K.K. (2006). Mini-alphaB-crystallin: a functional element of alphaB-crystallin with chaperone-like activity. Biochemistry 45, 3069-3076.
Buchner, J., Schmidt, M., Fuchs, M., Jaenicke, R., Rudolph, R., Schmid, F.X., and Kiefhaber, T. (1991). GroE facilitates refolding of citrate synthase by suppressing aggregation. Biochemistry 30, 1586-1591.
Craig, E.A. (1985). The heat shock response. CRC Crit Rev Biochem 18, 239-280.
Craig, W.S. (1988). Determination of quaternary structure of an active enzyme using chemical cross-linking with glutaraldehyde. Methods Enzymol 156, 333-345.
de Jong, W.W., Leunissen, J.A., and Voorter, C.E. (1993). Evolution of the alpha-crystallin/small heat-shock protein family. Mol Biol Evol 10, 103-126.
de Jong, W.W., Caspers, G.J., and Leunissen, J.A. (1998). Genealogy of the alpha-crystallin--small heat-shock protein superfamily. Int J Biol Macromol 22, 151-162.
Derocher, A.E., Helm, K.W., Lauzon, L.M., and Vierling, E. (1991). Expression of a Conserved Family of Cytoplasmic Low Molecular Weight Heat Shock Proteins during Heat Stress and Recovery. Plant Physiol 96, 1038-1047.
Ehrnsperger, M., Hergersberg, C., Wienhues, U., Nichtl, A., and Buchner, J. (1998). Stabilization of proteins and peptides in diagnostic immunological assays by the molecular chaperone Hsp25. Anal Biochem 259, 218-225.
Ghosh, J.G., and Clark, J.I. (2005). Insights into the domains required for dimerization and assembly of human alphaB crystallin. Protein Sci 14, 684-695.
Ghosh, J.G., Estrada, M.R., and Clark, J.I. (2005). Interactive domains for chaperone activity in the small heat shock protein, human alphaB crystallin. Biochemistry 44, 14854-14869.
Guan, J.C., Jinn, T.L., Yeh, C.H., Feng, S.P., Chen, Y.M., and Lin, C.Y. (2004). Characterization of the genomic structures and selective expression profiles of nine class I small heat shock protein genes clustered on two chromosomes in rice (Oryza sativa L.). Plant Mol Biol 56, 795-809.
Guruprasad, K., and Shukla, S. (2003). Prediction of beta-turns from amino acid sequences using the residue-coupled model. J Pept Res 61, 159-162.
Guruprasad, K., and Kumari, K. (2003). Three-dimensional models corresponding to the C-terminal domain of human alphaA- and alphaB-crystallins based on the crystal structure of the small heat-shock protein HSP16.9 from wheat. Int J Biol Macromol 33, 107-112.
Hartman, D.J., Surin, B.P., Dixon, N.E., Hoogenraad, N.J., and Hoj, P.B. (1993). Substoichiometric amounts of the molecular chaperones GroEL and GroES prevent thermal denaturation and aggregation of mammalian mitochondrial malate dehydrogenase in vitro. Proc Natl Acad Sci U S A 90, 2276-2280.
Haslbeck, M. (2002). sHsps and their role in the chaperone network. Cell Mol Life Sci 59, 1649-1657.
Haslbeck, M., and Buchner, J. (2002). Chaperone function of sHsps. Prog Mol Subcell Biol 28, 37-59.
Horwitz, J., Emmons, T., and Takemoto, L. (1992). The ability of lens alpha crystallin to protect against heat-induced aggregation is age-dependent. Curr Eye Res 11, 817-822.
Iannotti, A.M., Rabideau, D.A., and Dougherty, J.J. (1988). Characterization of purified avian 90,000-Da heat shock protein. Arch Biochem Biophys 264, 54-60.
Jakob, U., and Buchner, J. (1994). Assisting spontaneity: the role of Hsp90 and small Hsps as molecular chaperones. Trends Biochem Sci 19, 205-211.
Jakob, U., Gaestel, M., Engel, K., and Buchner, J. (1993). Small heat shock proteins are molecular chaperones. J Biol Chem 268, 1517-1520.
Jinn, T.L., Chen, Y.M., and Lin, C.Y. (1995). Characterization and Physiological Function of Class I Low-Molecular-Mass, Heat-Shock Protein Complex in Soybean. Plant Physiol 108, 693-701.
Jinn, T.L., Chang, P., Chen, Y.M., Key, J.L., and Lin, C.Y. (1997). Tissue-Type-Specific Heat-Shock Response and Immunolocalization of Class I Low-Molecular-Weight Heat-Shock Proteins in Soybean. Plant Physiol 114, 429-438.
Kim, K.I., Woo, K.M., Seong, I.S., Lee, Z.W., Baek, S.H., and Chung, C.H. (1998a). Mutational analysis of the two ATP-binding sites in ClpB, a heat shock protein with protein-activated ATPase activity in Escherichia coli. Biochem J 333 ( Pt 3), 671-676.
Kim, K.K., Kim, R., and Kim, S.H. (1998b). Crystal structure of a small heat-shock protein. Nature 394, 595-599.
Kim, R., Kim, K.K., Yokota, H., and Kim, S.H. (1998c). Small heat shock protein of Methanococcus jannaschii, a hyperthermophile. Proc Natl Acad Sci U S A 95, 9129-9133.
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.
Larkindale, J., and Knight, M.R. (2002). Protection against heat stress-induced oxidative damage in Arabidopsis involves calcium, abscisic acid, ethylene, and salicylic acid. Plant Physiol 128, 682-695.
Lee, G.J., and Vierling, E. (2000). A small heat shock protein cooperates with heat shock protein 70 systems to reactivate a heat-denatured protein. Plant Physiol 122, 189-198.
Lee, G.J., Roseman, A.M., Saibil, H.R., and Vierling, E. (1997). A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state. Embo J 16, 659-671.
Ma, C., Haslbeck, M., Babujee, L., Jahn, O., and Reumann, S. (2006). Identification and characterization of a stress-inducible and a constitutive small heat-shock protein targeted to the matrix of plant peroxisomes. Plant Physiol 141, 47-60.
Merck, K.B., Horwitz, J., Kersten, M., Overkamp, P., Gaestel, M., Bloemendal, H., and de Jong, W.W. (1993). Comparison of the homologous carboxy-terminal domain and tail of alpha-crystallin and small heat shock protein. Mol Biol Rep 18, 209-215.
Miernyk, J.A., Duck, N.B., Shatters, R.G., Jr., and Folk, W.R. (1992). The 70-Kilodalton Heat Shock Cognate Can Act as a Molecular Chaperone during the Membrane Translocation of a Plant Secretory Protein Precursor. Plant Cell 4, 821-829.
Mogk, A., Mayer, M.P., and Deuerling, E. (2002). Mechanisms of protein folding: molecular chaperones and their application in biotechnology. Chembiochem 3, 807-814.
Mogk, A., Deuerling, E., Vorderwulbecke, S., Vierling, E., and Bukau, B. (2003). Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation. Mol Microbiol 50, 585-595.
Nieto-Sotelo, J., Kannan, K.B., Martinez, L.M., and Segal, C. (1999). Characterization of a maize heat-shock protein 101 gene, HSP101, encoding a ClpB/Hsp100 protein homologue. Gene 230, 187-195.
Ohtsuka, K., Utsumi, K.R., Kaneda, T., and Hattori, H. (1993). Effect of ATP on the release of hsp 70 and hsp 40 from the nucleus in heat-shocked HeLa cells. Exp Cell Res 209, 357-366.
Parsell, D.A., and Lindquist, S. (1993). The function of heat-shock proteins in stress tolerance: degradation and reactivation of damaged proteins. Annu Rev Genet 27, 437-496.
Parsell, D.A., Taulien, J., and Lindquist, S. (1993). The role of heat-shock proteins in thermotolerance. Philos Trans R Soc Lond B Biol Sci 339, 279-285; discussion 285-276.
Parsell, D.A., Kowal, A.S., and Lindquist, S. (1994a). Saccharomyces cerevisiae Hsp104 protein. Purification and characterization of ATP-induced structural changes. J Biol Chem 269, 4480-4487.
Parsell, D.A., Kowal, A.S., Singer, M.A., and Lindquist, S. (1994b). Protein disaggregation mediated by heat-shock protein Hsp104. Nature 372, 475-478.
Ritossa, P. (1962). [Problems of prophylactic vaccinations of infants.]. Riv Ist Sieroter Ital 37, 79-108.
Scharf, K.D., Siddique, M., and Vierling, E. (2001). The expanding family of Arabidopsis thaliana small heat stress proteins and a new family of proteins containing alpha-crystallin domains (Acd proteins). Cell Stress Chaperones 6, 225-237.
Schirmer, E.C., Glover, J.R., Singer, M.A., and Lindquist, S. (1996). HSP100/Clp proteins: a common mechanism explains diverse functions. Trends Biochem Sci 21, 289-296.
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 alphaA-crystallin. J Biol Chem 275, 3767-3771.
Sigler, P.B., Xu, Z., Rye, H.S., Burston, S.G., Fenton, W.A., and Horwich, A.L. (1998). Structure and function in GroEL-mediated protein folding. Annu Rev Biochem 67, 581-608.
Song, C.W., Kang, M.S., Rhee, J.G., and Levitt, S.H. (1980). The effect of hyperthermia on vascular function, pH, and cell survival. Radiology 137, 795-803.
Theriault, J.R., Lambert, H., Chavez-Zobel, A.T., Charest, G., Lavigne, P., and Landry, J. (2004). Essential role of the NH2-terminal WD/EPF motif in the phosphorylation-activated protective function of mammalian Hsp27. J Biol Chem 279, 23463-23471.
Van Montfort, R., Slingsby, C., and Vierling, E. (2001). Structure and function of the small heat shock protein/alpha-crystallin family of molecular chaperones. Adv Protein Chem 59, 105-156.
Van Montfort, R.L., Basha, E., Friedrich, K.L., Slingsby, C., and Vierling, E. (2001). Crystal structure and assembly of a eukaryotic small heat shock protein. Nat Struct Biol 8, 1025-1030.
Waters, E.R. (1995). The molecular evolution of the small heat-shock proteins in plants. Genetics 141, 785-795.
Waters, E.R., and Schaal, B.A. (1996). Heat shock induces a loss of rRNA-encoding DNA repeats in Brassica nigra. Proc Natl Acad Sci U S A 93, 1449-1452.
Waters, E.R., and Vierling, E. (1999). The diversification of plant cytosolic small heat shock proteins preceded the divergence of mosses. Mol Biol Evol 16, 127-139.
Yeh, C.H., Chen, Y.M., and Lin, C.Y. (2002). Functional regions of rice heat shock protein, Oshsp16.9, required for conferring thermotolerance in Escherichia coli. Plant Physiol 128, 661-668.
Yeh, C.H., Yeh, K.W., Wu, S.H., Chang, P.F., Chen, Y.M., and Lin, C.Y. (1995). A recombinant rice 16.9-kDa heat shock protein can provide thermoprotection in vitro. Plant Cell Physiol 36, 1341-1348.
Yeh, C.H., Chang, P.F., Yeh, K.W., Lin, W.C., Chen, Y.M., and Lin, C.Y. (1997). Expression of a gene encoding a 16.9-kDa heat-shock protein, Oshsp16.9, in Escherichia coli enhances thermotolerance. Proc Natl Acad Sci U S A 94, 10967-10972.
Yeh, K.W., Jinn, T.L., Yeh, C.H., Chen, Y.M., and Lin, C.Y. (1994). Plant low-molecular-mass heat-shock proteins: their relationship to the acquisition of thermotolerance in plants. Biotechnol Appl Biochem 19 ( Pt 1), 41-49. |