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Volumn 46, Issue 5, 2014, Pages 347-356

Chaperone function and mechanism of small heat-shock proteins

Author keywords

molecular chaperone; oligomer; protein aggregation; protein quality control; small heat shock protein

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN; PROTEIN BINDING;

EID: 84899808625     PISSN: 16729145     EISSN: 17457270     Source Type: Journal    
DOI: 10.1093/abbs/gmt152     Document Type: Review
Times cited : (48)

References (134)
  • 1
    • 0018221572 scopus 로고
    • Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA
    • Laskey RA, Honda BM, Mills AD and Finch JT. Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA. Nature 1978, 275: 416-420.
    • (1978) Nature , vol.275 , pp. 416-420
    • Laskey, R.A.1    Honda, B.M.2    Mills, A.D.3    Finch, J.T.4
  • 2
    • 0030224998 scopus 로고    scopus 로고
    • Discovery of molecular chaperones
    • Ellis RJ. Discovery of molecular chaperones. Cell Stress Chaperones 1996, 1: 155-160.
    • (1996) Cell Stress Chaperones , vol.1 , pp. 155-160
    • Ellis, R.J.1
  • 3
    • 0027925677 scopus 로고
    • The general concept of molecular chaperones
    • Ellis RJ. The general concept of molecular chaperones. Philos Trans R Soc Lond B Biol Sci 1993, 339: 257-261.
    • (1993) Philos Trans R Soc Lond B Biol Sci , vol.339 , pp. 257-261
    • Ellis, R.J.1
  • 4
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl FU, Bracher A and Hayer-Hartl M. Molecular chaperones in protein folding and proteostasis. Nature 2011, 475: 324-332.
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 5
    • 0027472047 scopus 로고
    • Evolution of the alphacrystallin/ small heat-shock protein family
    • de Jong WW, Leunissen JA and Voorter CE. Evolution of the alphacrystallin/ small heat-shock protein family. Mol Biol Evol 1993, 10: 103-126.
    • (1993) Mol Biol Evol , vol.10 , pp. 103-126
    • De Jong, W.W.1    Leunissen, J.A.2    Voorter, C.E.3
  • 6
    • 0026483279 scopus 로고
    • Alpha-crystallin can function as a molecular chaperone
    • Horwitz J. Alpha-crystallin can function as a molecular chaperone. Proc Natl Acad Sci USA 1992, 89: 10449-10453.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10449-10453
    • Horwitz, J.1
  • 7
    • 0027391629 scopus 로고
    • Small heat shock proteins are molecular chaperones
    • Jakob U, Gaestel M, Engel K and Buchner J. Small heat shock proteins are molecular chaperones. J Biol Chem 1993, 268: 1517-1520.
    • (1993) J Biol Chem , vol.268 , pp. 1517-1520
    • Jakob, U.1    Gaestel, M.2    Engel, K.3    Buchner, J.4
  • 8
    • 0035853131 scopus 로고    scopus 로고
    • Synechocystis HSP17 is an amphitropic protein that stabilizes heat-stressed membranes and binds denatured proteins for subsequent chaperone-mediated refolding
    • Torok Z, Goloubinoff P, Horvath I, Tsvetkova NM, Glatz A, Balogh G and Varvasovszki V, et al. Synechocystis HSP17 is an amphitropic protein that stabilizes heat-stressed membranes and binds denatured proteins for subsequent chaperone-mediated refolding. Proc Natl Acad Sci USA 2001, 98: 3098-3103.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 3098-3103
    • Torok, Z.1    Goloubinoff, P.2    Horvath, I.3    Tsvetkova, N.M.4    Glatz, A.5    Balogh, G.6    Varvasovszki, V.7
  • 9
    • 77956006894 scopus 로고    scopus 로고
    • Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function
    • Welker S, Rudolph B, Frenzel E, Hagn F, Liebisch G, Schmitz G and Scheuring J, et al. Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function. Mol Cell 2010, 39: 507-520.
    • (2010) Mol Cell , vol.39 , pp. 507-520
    • Welker, S.1    Rudolph, B.2    Frenzel, E.3    Hagn, F.4    Liebisch, G.5    Schmitz, G.6    Scheuring, J.7
  • 11
    • 0032079487 scopus 로고    scopus 로고
    • The small heatshock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network
    • Veinger L, Diamant S, Buchner J and Goloubinoff P. The small heatshock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network. J Biol Chem 1998, 273: 11032-11037.
    • (1998) J Biol Chem , vol.273 , pp. 11032-11037
    • Veinger, L.1    Diamant, S.2    Buchner, J.3    Goloubinoff, P.4
  • 12
    • 0142125283 scopus 로고    scopus 로고
    • Small heat shock proteins ClpB and the DnaK system form a functional triade in reversing protein aggregation
    • Mogk A, Deuerling E, Vorderwulbecke S, Vierling E and Bukau B. Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation. Mol Microbiol 2003, 50: 585-595.
    • (2003) Mol Microbiol , vol.50 , pp. 585-595
    • Mogk, A.1    Deuerling, E.2    Vorderwulbecke, S.3    Vierling, E.4    Bukau, B.5
  • 13
    • 0031024691 scopus 로고    scopus 로고
    • A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state
    • Lee GJ, Roseman AM, Saibil HR and Vierling E. A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state. EMBO J 1997, 16: 659-671.
    • (1997) EMBO J , vol.16 , pp. 659-671
    • Lee, G.J.1    Roseman, A.M.2    Saibil, H.R.3    Vierling, E.4
  • 14
    • 21244466032 scopus 로고    scopus 로고
    • A chaperone pathway in protein disaggregation. Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104
    • Cashikar AG, Duennwald M and Lindquist SL. A chaperone pathway in protein disaggregation. Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104. J Biol Chem 2005, 280: 23869-23875.
    • (2005) J Biol Chem , vol.280 , pp. 23869-23875
    • Cashikar, A.G.1    Duennwald, M.2    Lindquist, S.L.3
  • 15
    • 0343742639 scopus 로고    scopus 로고
    • Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation
    • Ehrnsperger M, Graber S, Gaestel M and Buchner J. Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation. EMBO J 1997, 16: 221-229.
    • (1997) EMBO J , vol.16 , pp. 221-229
    • Ehrnsperger, M.1    Graber, S.2    Gaestel, M.3    Buchner, J.4
  • 16
    • 53149098981 scopus 로고    scopus 로고
    • A mutant small heat shock protein with increased thylakoid association provides an elevated resistance against UV-B damage in synechocystis 6803
    • Balogi Z, Cheregi O, Giese KC, Juhasz K, Vierling E, Vass I and V?gh L, et al. A mutant small heat shock protein with increased thylakoid association provides an elevated resistance against UV-B damage in synechocystis 6803. J Biol Chem 2008, 283: 22983-22991.
    • (2008) J Biol Chem , vol.283 , pp. 22983-22991
    • Balogi, Z.1    Cheregi, O.2    Giese, K.C.3    Juhasz, K.4    Vierling, E.5    Vass, I.6    Vgh, L.7
  • 17
    • 84864366257 scopus 로고    scopus 로고
    • ZmHSP16.9, a cytosolic class i small heat shock protein in maize (Zea mays), confers heat tolerance in transgenic tobacco
    • Sun L, Liu Y, Kong X, Zhang D, Pan J, Zhou Y and Wang L, et al. ZmHSP16.9, a cytosolic class I small heat shock protein in maize (Zea mays), confers heat tolerance in transgenic tobacco. Plant Cell Rep 2012, 31: 1473-1484.
    • (2012) Plant Cell Rep , vol.31 , pp. 1473-1484
    • Sun, L.1    Liu, Y.2    Kong, X.3    Zhang, D.4    Pan, J.5    Zhou, Y.6    Wang, L.7
  • 18
    • 34447278582 scopus 로고    scopus 로고
    • The heterologous overexpression of hsp23, a small heat-shock protein gene from Trichoderma virens, confers thermotolerance to T. Harzianum
    • Montero-Barrientos M, Cardoza RE, Gutierrez S, Monte E and Hermosa R. The heterologous overexpression of hsp23, a small heat-shock protein gene from Trichoderma virens, confers thermotolerance to T. harzianum. Curr Genet 2007, 52: 45-53.
    • (2007) Curr Genet , vol.52 , pp. 45-53
    • Montero-Barrientos, M.1    Cardoza, R.E.2    Gutierrez, S.3    Monte, E.4    Hermosa, R.5
  • 19
    • 84856209522 scopus 로고    scopus 로고
    • Overexpression of a chloroplast-localized small heat shock protein OsHSP26 confers enhanced tolerance against oxidative and heat stresses in tall fescue
    • Kim KH, Alam I, Kim YG, Sharmin SA, Lee KW, Lee SH and Lee BH. Overexpression of a chloroplast-localized small heat shock protein OsHSP26 confers enhanced tolerance against oxidative and heat stresses in tall fescue. Biotechnol Lett 2012, 34: 371-377.
    • (2012) Biotechnol Lett , vol.34 , pp. 371-377
    • Kim, K.H.1    Alam, I.2    Kim, Y.G.3    Sharmin, S.A.4    Lee, K.W.5    Lee, S.H.6    Lee, B.H.7
  • 20
    • 30144436776 scopus 로고    scopus 로고
    • The intertidal copepod Tigriopus japonicus small heat shock protein 20 gene (Hsp20) enhances thermotolerance of transformed Escherichia coli
    • Seo JS, Lee YM, Park HG and Lee JS. The intertidal copepod Tigriopus japonicus small heat shock protein 20 gene (Hsp20) enhances thermotolerance of transformed Escherichia coli. Biochem Biophys Res Commun 2006, 340: 901-908.
    • (2006) Biochem Biophys Res Commun , vol.340 , pp. 901-908
    • Seo, J.S.1    Lee, Y.M.2    Park, H.G.3    Lee, J.S.4
  • 21
    • 0030886055 scopus 로고    scopus 로고
    • Expression of a gene encoding a 16.9-kDa heat-shock protein, Oshsp16.9, in Escherichia coli enhances thermotolerance
    • Yeh CH, Chang PF, Yeh KW, Lin WC, Chen YM and Lin CY. Expression of a gene encoding a 16.9-kDa heat-shock protein, Oshsp16.9, in Escherichia coli enhances thermotolerance. Proc Natl Acad Sci USA 1997, 94: 10967-10972.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10967-10972
    • Yeh, C.H.1    Chang, P.F.2    Yeh, K.W.3    Lin, W.C.4    Chen, Y.M.5    Lin, C.Y.6
  • 22
    • 0034653760 scopus 로고    scopus 로고
    • Small heat shock proteins, IbpA and IbpB, are involved in resistances to heat and superoxide stresses in Escherichia coli
    • Kitagawa M, Matsumura Y and Tsuchido T. Small heat shock proteins, IbpA and IbpB, are involved in resistances to heat and superoxide stresses in Escherichia coli. FEMS Microbiol Lett 2000, 184: 165-171.
    • (2000) FEMS Microbiol Lett , vol.184 , pp. 165-171
    • Kitagawa, M.1    Matsumura, Y.2    Tsuchido, T.3
  • 23
    • 0024345716 scopus 로고
    • Heat shock resistance conferred by expression of the human HSP27 gene in rodent cells
    • Landry J, Chretien P, Lambert H, Hickey E and Weber LA. Heat shock resistance conferred by expression of the human HSP27 gene in rodent cells. J Cell Biol 1989, 109: 7-15.
    • (1989) J Cell Biol , vol.109 , pp. 7-15
    • Landry, J.1    Chretien, P.2    Lambert, H.3    Hickey, E.4    Weber, L.A.5
  • 24
    • 0034949588 scopus 로고    scopus 로고
    • Overexpression of murine small heat shock protein HSP25 interferes with chondrocyte differentiation and decreases cell adhesion
    • Favet N, Duverger O, Loones MT, Poliard A, Kellermann O and Morange M. Overexpression of murine small heat shock protein HSP25 interferes with chondrocyte differentiation and decreases cell adhesion. Cell Death Differ 2001, 8: 603-613.
    • (2001) Cell Death Differ , vol.8 , pp. 603-613
    • Favet, N.1    Duverger, O.2    Loones, M.T.3    Poliard, A.4    Kellermann, O.5    Morange, M.6
  • 25
    • 36349009441 scopus 로고    scopus 로고
    • Overexpression of human Hsp27 inhibits serum-induced proliferation in airway smooth muscle myocytes and confers resistance to hydrogen peroxide cytotoxicity
    • Salinthone S, Ba M, Hanson L, Martin JL, Halayko AJ and Gerthoffer WT. Overexpression of human Hsp27 inhibits serum-induced proliferation in airway smooth muscle myocytes and confers resistance to hydrogen peroxide cytotoxicity. Am J Physiol Lung Cell Mol Physiol 2007, 293: L1194-L1207.
    • (2007) Am J Physiol Lung Cell Mol Physiol , vol.293
    • Salinthone, S.1    Ba, M.2    Hanson, L.3    Martin, J.L.4    Halayko, A.J.5    Gerthoffer, W.T.6
  • 26
    • 6344286028 scopus 로고    scopus 로고
    • Decreased lifespan in the absence of expression of the mitochondrial small heat shock protein Hsp22 in Drosophila
    • Morrow G, Battistini S, Zhang P and Tanguay RM. Decreased lifespan in the absence of expression of the mitochondrial small heat shock protein Hsp22 in Drosophila. J Biol Chem 2004, 279: 43382-43385.
    • (2004) J Biol Chem , vol.279 , pp. 43382-43385
    • Morrow, G.1    Battistini, S.2    Zhang, P.3    Tanguay, R.M.4
  • 27
    • 0029882949 scopus 로고    scopus 로고
    • Effect of overexpression of the small heat shock protein HSP27 on the heat and drug sensitivities of human testis tumor cells
    • Richards EH, Hickey E, Weber L and Master JR. Effect of overexpression of the small heat shock protein HSP27 on the heat and drug sensitivities of human testis tumor cells. Cancer Res 1996, 56: 2446-2451.
    • (1996) Cancer Res , vol.56 , pp. 2446-2451
    • Richards, E.H.1    Hickey, E.2    Weber, L.3    Master, J.R.4
  • 28
    • 10044254417 scopus 로고    scopus 로고
    • Overexpression of wild-type heat shock protein 27 and a nonphosphorylatable heat shock protein 27 mutant protects against ischemia/reperfusion injury in a transgenic mouse model
    • Salinthone S, Ba M, Hanson L, Martin JL, Halayko AJ and Gerthoffer WT. Overexpression of wild-type heat shock protein 27 and a nonphosphorylatable heat shock protein 27 mutant protects against ischemia/reperfusion injury in a transgenic mouse model. Circulation 2004, 110: 3544-3552.
    • (2004) Circulation , vol.110 , pp. 3544-3552
    • Salinthone, S.1    Ba, M.2    Hanson, L.3    Martin, J.L.4    Halayko, A.J.5    Gerthoffer, W.T.6
  • 29
    • 84875996709 scopus 로고    scopus 로고
    • Phenotype of cardiomyopathy in cardiac-specific heat shock protein B8 K141N transgenic mouse
    • Sanbe A, Marunouchi T, Abe T, Tezuka Y, Okada M, Aoki S and Tsumura H, et al. Phenotype of cardiomyopathy in cardiac-specific heat shock protein B8 K141N transgenic mouse. J Biol Chem 2013, 288: 8910-8921.
    • (2013) J Biol Chem , vol.288 , pp. 8910-8921
    • Sanbe, A.1    Marunouchi, T.2    Abe, T.3    Tezuka, Y.4    Okada, M.5    Aoki, S.6    Tsumura, H.7
  • 30
    • 0031934121 scopus 로고    scopus 로고
    • Autosomal dominant congenital cataract associated with a missense mutation in the human alpha crystallin gene CRYAA
    • Litt M, Kramer P, LaMorticella DM, Murphey W, Lovrien EW and Weleber RG. Autosomal dominant congenital cataract associated with a missense mutation in the human alpha crystallin gene CRYAA. Hum Mol Genet 1998, 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
  • 31
    • 17344361902 scopus 로고    scopus 로고
    • A missense mutation in the alphaB-crystallin chaperone gene causes a desmin-related myopathy
    • Vicart P, Caron A, Guicheney P, Li Z, Prevost MC, Faure A and Chateau D, et al. A missense mutation in the alphaB-crystallin chaperone gene causes a desmin-related myopathy. Nat Genet 1998, 20: 92-95.
    • (1998) Nat Genet , vol.20 , pp. 92-95
    • Vicart, P.1    Caron, A.2    Guicheney, P.3    Li, Z.4    Prevost, M.C.5    Faure, A.6    Chateau, D.7
  • 33
    • 2642563501 scopus 로고    scopus 로고
    • Mutant small heat-shock protein 27 causes axonal Charcot-Marie-Tooth disease and distal hereditary motor neuropathy
    • Evgrafov OV, Mersiyanova I, Irobi J, Van Den Bosch L, Dierick I, Leung CL and Schagina O, et al. Mutant small heat-shock protein 27 causes axonal Charcot-Marie-Tooth disease and distal hereditary motor neuropathy. Nat Genet 2004, 36: 602-606.
    • (2004) Nat Genet , vol.36 , pp. 602-606
    • Evgrafov, O.V.1    Mersiyanova, I.2    Irobi, J.3    Van Den Bosch, L.4    Dierick, I.5    Leung, C.L.6    Schagina, O.7
  • 35
    • 1342292267 scopus 로고    scopus 로고
    • Crystal structure of a small heat-shock protein
    • Kim KK, Kim R and Kim SH. Crystal structure of a small heat-shock protein. Nature 1998, 394: 595-599.
    • (1998) Nature , vol.394 , pp. 595-599
    • Kim, K.K.1    Kim, R.2    Kim, S.H.3
  • 36
    • 14844292563 scopus 로고    scopus 로고
    • A dual role for the N-terminal region of Mycobacterium tuberculosis Hsp16.3 in self-oligomerization and binding denaturing substrate proteins
    • Fu X, Zhang H, Zhang X, Cao Y, Jiao W, Liu C and Song Y, et al. A dual role for the N-terminal region of Mycobacterium tuberculosis Hsp16.3 in self-oligomerization and binding denaturing substrate proteins. J Biol Chem 2005, 280: 6337-6648.
    • (2005) J Biol Chem , vol.280 , pp. 6337-6648
    • Fu, X.1    Zhang, H.2    Zhang, X.3    Cao, Y.4    Jiao, W.5    Liu, C.6    Song, Y.7
  • 37
    • 55549133282 scopus 로고    scopus 로고
    • Insights into small heat shock protein and substrate structure during chaperone action derived from hydrogen/deuterium exchange and mass spectrometry
    • Cheng G, Basha E, Wysocki VH and Vierling E. Insights into small heat shock protein and substrate structure during chaperone action derived from hydrogen/deuterium exchange and mass spectrometry. J Biol Chem 2008, 283: 26634-26642.
    • (2008) J Biol Chem , vol.283 , pp. 26634-26642
    • Cheng, G.1    Basha, E.2    Wysocki, V.H.3    Vierling, E.4
  • 38
    • 0000899062 scopus 로고    scopus 로고
    • A spectroscopic study of glycated bovine alpha-crystallin: Investigation of flexibility of the C-terminal extension, chaperone activity and evidence for diglycation
    • Blakytny R, Carver JA, Harding JJ, Kilby GW and Sheil MM. A spectroscopic study of glycated bovine alpha-crystallin: investigation of flexibility of the C-terminal extension, chaperone activity and evidence for diglycation. Biochim Biophys Acta 1997, 1343: 299-315.
    • (1997) Biochim Biophys Acta , vol.1343 , pp. 299-315
    • Blakytny, R.1    Carver, J.A.2    Harding, J.J.3    Kilby, G.W.4    Sheil, M.M.5
  • 39
    • 0032078745 scopus 로고    scopus 로고
    • NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and chaperone action of small heatshock proteins
    • Carver JA and Lindner RA. NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and chaperone action of small heatshock proteins. Int J Biol Macromol 1998, 22: 197-209.
    • (1998) Int J Biol Macromol , vol.22 , pp. 197-209
    • Carver, J.A.1    Lindner, R.A.2
  • 40
    • 84858003372 scopus 로고    scopus 로고
    • Small heat shock proteins and alphacrystallins: Dynamic proteins with flexible functions
    • Basha E, ONeill H and Vierling E. Small heat shock proteins and alphacrystallins: dynamic proteins with flexible functions. Trends Biochem Sci 2012, 37: 106-117.
    • (2012) Trends Biochem Sci , vol.37 , pp. 106-117
    • Basha, E.1    Oneill, H.2    Vierling, E.3
  • 41
    • 0037064096 scopus 로고    scopus 로고
    • Subunit exchange of multimeric protein complexes. Real-time monitoring of subunit exchange between small heat shock proteins by using electrospray mass spectrometry
    • Sobott F, Benesch JL, Vierling E and Robinson CV. Subunit exchange of multimeric protein complexes. Real-time monitoring of subunit exchange between small heat shock proteins by using electrospray mass spectrometry. J Biol Chem 2002, 277: 38921-38929.
    • (2002) J Biol Chem , vol.277 , pp. 38921-38929
    • Sobott, F.1    Benesch, J.L.2    Vierling, E.3    Robinson, C.V.4
  • 42
    • 84864584745 scopus 로고    scopus 로고
    • Structural studies on the oligomeric transition of a small heat shock protein, StHsp14.0
    • Hanazono Y, Takeda K, Yohda M and Miki K. Structural studies on the oligomeric transition of a small heat shock protein, StHsp14.0. J Mol Biol 2012, 422: 100-108.
    • (2012) J Mol Biol , vol.422 , pp. 100-108
    • Hanazono, Y.1    Takeda, K.2    Yohda, M.3    Miki, K.4
  • 43
    • 84873390001 scopus 로고    scopus 로고
    • Nonequivalence observed for the 16-meric structure of a small heat shock protein, SpHsp16.0, from Schizosaccharomyces pombe
    • Hanazono Y, Takeda K, Oka T, Abe T, Tomonari T, Akiyama N and Aikawa Y, et al. Nonequivalence observed for the 16-meric structure of a small heat shock protein, SpHsp16.0, from Schizosaccharomyces pombe. Structure 2013, 21: 220-228.
    • (2013) Structure , vol.21 , pp. 220-228
    • Hanazono, Y.1    Takeda, K.2    Oka, T.3    Abe, T.4    Tomonari, T.5    Akiyama, N.6    Aikawa, Y.7
  • 44
    • 0032555364 scopus 로고    scopus 로고
    • Caenorhabditis elegans small heat-shock proteins Hsp12.2 and Hsp12.3 form tetramers and have no chaperone-like activity
    • Kokke BP, Leroux MR, Candido EP, Boelens WC and de Jong WW. Caenorhabditis elegans small heat-shock proteins Hsp12.2 and Hsp12.3 form tetramers and have no chaperone-like activity. FEBS Lett 1998, 433: 228-232.
    • (1998) FEBS Lett , vol.433 , pp. 228-232
    • Kokke, B.P.1    Leroux, M.R.2    Candido, E.P.3    Boelens, W.C.4    De Jong, W.W.5
  • 45
    • 84877577000 scopus 로고    scopus 로고
    • An unusual dimeric small heat shock protein provides insight into the mechanism of this class of chaperones
    • Basha E, Jones C, Blackwell AE, Cheng G, Waters ER, Samsel KA and Siddique M, et al. An unusual dimeric small heat shock protein provides insight into the mechanism of this class of chaperones. J Mol Biol 2013, 425: 1683-1696.
    • (2013) J Mol Biol , vol.425 , pp. 1683-1696
    • Basha, E.1    Jones, C.2    Blackwell, A.E.3    Cheng, G.4    Waters, E.R.5    Samsel, K.A.6    Siddique, M.7
  • 46
    • 0030973550 scopus 로고    scopus 로고
    • Unique structural features of a novel class of small heat shock proteins
    • Leroux MR, Ma BJ, Batelier G, Melki R and Candido EP. Unique structural features of a novel class of small heat shock proteins. J Biol Chem 1997, 272: 12847-12853.
    • (1997) J Biol Chem , vol.272 , pp. 12847-12853
    • Leroux, M.R.1    Ma, B.J.2    Batelier, G.3    Melki, R.4    Candido, E.P.5
  • 47
    • 0030002946 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis 16-kDa antigen (Hsp16.3) functions as an oligomeric structure in vitro to suppress thermal aggregation
    • Chang Z, Primm TP, Jakana J, Lee IH, Serysheva I, Chiu W and Gilbert HF, et al. Mycobacterium tuberculosis 16-kDa antigen (Hsp16.3) functions as an oligomeric structure in vitro to suppress thermal aggregation. J Biol Chem 1996, 271: 7218-7223.
    • (1996) J Biol Chem , vol.271 , pp. 7218-7223
    • Chang, Z.1    Primm, T.P.2    Jakana, J.3    Lee, I.H.4    Serysheva, I.5    Chiu, W.6    Gilbert, H.F.7
  • 48
    • 0032898210 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis small heat shock protein Hsp16.3 exposes hydrophobic surfaces at mild conditions: Conformational flexibility and molecular chaperone activity
    • Yang H, Huang S, Dai H, Gong Y, Zheng C and Chang Z. The Mycobacterium tuberculosis small heat shock protein Hsp16.3 exposes hydrophobic surfaces at mild conditions: conformational flexibility and molecular chaperone activity. Protein Sci 1999, 8: 174-179.
    • (1999) Protein Sci , vol.8 , pp. 174-179
    • Yang, H.1    Huang, S.2    Dai, H.3    Gong, Y.4    Zheng, C.5    Chang, Z.6
  • 49
    • 0036306310 scopus 로고    scopus 로고
    • Monodisperse Hsp16.3 nonamer exhibits dynamic dissociation and reassociation, with the nonamer dissociation prerequisite for chaperone-like activity
    • Gu L, Abulimiti A, Li W and Chang Z. Monodisperse Hsp16.3 nonamer exhibits dynamic dissociation and reassociation, with the nonamer dissociation prerequisite for chaperone-like activity. J Mol Biol 2002, 319: 517-526.
    • (2002) J Mol Biol , vol.319 , pp. 517-526
    • Gu, L.1    Abulimiti, A.2    Li, W.3    Chang, Z.4
  • 50
    • 14844355848 scopus 로고    scopus 로고
    • The essential role of the flexible termini in the temperature- responsiveness of the oligomeric state and chaperone-like activity for the polydisperse small heat shock protein IbpB from Escherichia coli
    • Jiao W, Qian M, Li P, Zhao L and Chang Z. The essential role of the flexible termini in the temperature-responsiveness of the oligomeric state and chaperone-like activity for the polydisperse small heat shock protein IbpB from Escherichia coli. J Mol Biol 2005, 347: 871-884.
    • (2005) J Mol Biol , vol.347 , pp. 871-884
    • Jiao, W.1    Qian, M.2    Li, P.3    Zhao, L.4    Chang, Z.5
  • 51
    • 39749148886 scopus 로고    scopus 로고
    • The dramatically increased chaperone activity of small heat-shock protein IbpB is retained for an extended period of time after the stress condition is removed
    • Jiao W, Hong W, Li P, Sun S, Ma J, Qian M and Hu M, et al. The dramatically increased chaperone activity of small heat-shock protein IbpB is retained for an extended period of time after the stress condition is removed. Biochem J 2008, 410: 63-70.
    • (2008) Biochem J , vol.410 , pp. 63-70
    • Jiao, W.1    Hong, W.2    Li, P.3    Sun, S.4    Ma, J.5    Qian, M.6    Hu, M.7
  • 53
    • 25144441023 scopus 로고    scopus 로고
    • Small heat-shock proteins function in the insoluble protein complex
    • Jiao W, Li P, Zhang J, Zhang H and Chang Z. Small heat-shock proteins function in the insoluble protein complex. Biochem Biophys Res Commun 2005, 335: 227-231.
    • (2005) Biochem Biophys Res Commun , vol.335 , pp. 227-231
    • Jiao, W.1    Li, P.2    Zhang, J.3    Zhang, H.4    Chang, Z.5
  • 54
    • 84887068645 scopus 로고    scopus 로고
    • In vivo substrate diversity and preference of small heat shock protein IbpB as revealed by using a genetically incorporated photo-crosslinker
    • Fu X, Shi X, Yan L, Zhang H and Chang Z. In vivo substrate diversity and preference of small heat shock protein IbpB as revealed by using a genetically incorporated photo-crosslinker. J Biol Chem 2013, 288: 31646-31654.
    • (2013) J Biol Chem , vol.288 , pp. 31646-31654
    • Fu, X.1    Shi, X.2    Yan, L.3    Zhang, H.4    Chang, Z.5
  • 55
    • 84876933888 scopus 로고    scopus 로고
    • Small heat shock protein IbpB acts as a robust chaperone in living cells by hierarchically activating its multi-type substrate-binding residues
    • Fu X, Shi X, Yin L, Liu J, Joo K, Lee J and Chang Z. Small heat shock protein IbpB acts as a robust chaperone in living cells by hierarchically activating its multi-type substrate-binding residues. J Biol Chem 2013, 288: 11897-11906.
    • (2013) J Biol Chem , vol.288 , pp. 11897-11906
    • Fu, X.1    Shi, X.2    Yin, L.3    Liu, J.4    Joo, K.5    Lee, J.6    Chang, Z.7
  • 57
    • 0032052239 scopus 로고    scopus 로고
    • The 16-kDa alpha-crystallin-like protein of Mycobacterium bovis BCG is produced under conditions of oxygen deficiency and is associated with ribosomes
    • Tabira Y, Ohara N, Ohara N, Kitaura H, Matsumoto S, Naito M and Yamada T. The 16-kDa alpha-crystallin-like protein of Mycobacterium bovis BCG is produced under conditions of oxygen deficiency and is associated with ribosomes. Res Microbiol 1998, 149: 255-264.
    • (1998) Res Microbiol , vol.149 , pp. 255-264
    • Tabira, Y.1    Ohara, N.2    Ohara, N.3    Kitaura, H.4    Matsumoto, S.5    Naito, M.6    Yamada, T.7
  • 58
    • 0000279337 scopus 로고
    • Cytoplasmic distribution of heat shock proteins in soybean
    • Mansfield MA and Key JL. Cytoplasmic distribution of heat shock proteins in soybean. Plant Physiol 1988, 86: 1240-1246.
    • (1988) Plant Physiol , vol.86 , pp. 1240-1246
    • Mansfield, M.A.1    Key, J.L.2
  • 59
    • 84857129568 scopus 로고    scopus 로고
    • The role of intrinsically disordered regions in the structure and functioning of small heat shock proteins
    • Sudnitsyna MV, Mymrikov EV, Seit-Nebi AS and Gusev NB. The role of intrinsically disordered regions in the structure and functioning of small heat shock proteins. Curr Protein Pept Sci 2012, 13: 76-85.
    • (2012) Curr Protein Pept Sci , vol.13 , pp. 76-85
    • Sudnitsyna, M.V.1    Mymrikov, E.V.2    Seit-Nebi, A.S.3    Gusev, N.B.4
  • 60
    • 0036195722 scopus 로고    scopus 로고
    • Alpha-crystallin-type heat shock proteins: Socializing minichaperones in the context of a multichaperone network
    • Narberhaus F. Alpha-crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network. Microbiol Mol Biol Rev 2002, 66: 64-93.
    • (2002) Microbiol Mol Biol Rev , vol.66 , pp. 64-93
    • Narberhaus, F.1
  • 61
    • 33846945050 scopus 로고    scopus 로고
    • The small heat shock proteins and their clients
    • Nakamoto H and Vigh L. The small heat shock proteins and their clients. Cell Mol Life Sci 2007, 64: 294-306.
    • (2007) Cell Mol Life Sci , vol.64 , pp. 294-306
    • Nakamoto, H.1    Vigh, L.2
  • 63
    • 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. Some like it hot: the structure and function of small heat-shock proteins. Nat Struct Mol Biol 2005, 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
  • 64
    • 84883003759 scopus 로고    scopus 로고
    • The potential role of small heat shock proteins in mitochondria
    • Zeng L, Tan J, Lu W, Lu T and Hu Z. The potential role of small heat shock proteins in mitochondria. Cell Signal 2013, 25: 2312-2319.
    • (2013) Cell Signal , vol.25 , pp. 2312-2319
    • Zeng, L.1    Tan, J.2    Lu, W.3    Lu, T.4    Hu, Z.5
  • 65
  • 67
    • 84863683967 scopus 로고    scopus 로고
    • Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humans
    • Duennwald ML, Echeverria A and Shorter J. Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humans. PLoS Biol 2012, 10: e1001346.
    • (2012) PLoS Biol , vol.10
    • Duennwald, M.L.1    Echeverria, A.2    Shorter, J.3
  • 69
  • 70
    • 15844414479 scopus 로고    scopus 로고
    • Conformational properties of substrate proteins bound to a molecular chaperone alpha-crystallin
    • Das KP, Petrash JM and Surewicz WK. Conformational properties of substrate proteins bound to a molecular chaperone alpha-crystallin. J Biol Chem 1996, 271: 10449-10452.
    • (1996) J Biol Chem , vol.271 , pp. 10449-10452
    • Das, K.P.1    Petrash, J.M.2    Surewicz, W.K.3
  • 71
    • 0037014666 scopus 로고    scopus 로고
    • Suppression of DTT-induced aggregation of abrin by alphaA- and alphaB-crystallins: A model aggregation assay for alpha-crystallin chaperone activity in vitro
    • Reddy GB, Narayanan S, Reddy PY and Surolia I. Suppression of DTT-induced aggregation of abrin by alphaA- and alphaB-crystallins: a model aggregation assay for alpha-crystallin chaperone activity in vitro. FEBS Lett 2002, 522: 59-64.
    • (2002) FEBS Lett , vol.522 , pp. 59-64
    • Reddy, G.B.1    Narayanan, S.2    Reddy, P.Y.3    Surolia, I.4
  • 72
    • 0030826325 scopus 로고    scopus 로고
    • Structure-function studies on small heat shock protein oligomeric assembly and interaction with unfolded polypeptides
    • Leroux MR, Melki R, Gordon B, Batelier G and Candido EP. Structure-function studies on small heat shock protein oligomeric assembly and interaction with unfolded polypeptides. J Biol Chem 1997, 272: 24646-24656.
    • (1997) J Biol Chem , vol.272 , pp. 24646-24656
    • Leroux, M.R.1    Melki, R.2    Gordon, B.3    Batelier, G.4    Candido, E.P.5
  • 73
    • 0032540350 scopus 로고    scopus 로고
    • Interactions of chaperone alpha-crystallin with the molten globule state of xylose reductase. Implications for reconstitution of the active enzyme
    • Rawat U and Rao M. Interactions of chaperone alpha-crystallin with the molten globule state of xylose reductase. Implications for reconstitution of the active enzyme. J Biol Chem 1998, 273: 9415-9423.
    • (1998) J Biol Chem , vol.273 , pp. 9415-9423
    • Rawat, U.1    Rao, M.2
  • 74
    • 0036306093 scopus 로고    scopus 로고
    • The interaction of the molecular chaperone alpha-crystallin with unfolding alpha-lactalbumin: A structural and kinetic spectroscopic study
    • Carver JA, Lindner RA, Lyon C, Canet D, Hernandez H, Dobson CM and Redfield C. The interaction of the molecular chaperone alpha-crystallin with unfolding alpha-lactalbumin: a structural and kinetic spectroscopic study. J Mol Biol 2002, 318: 815-827.
    • (2002) J Mol Biol , vol.318 , pp. 815-827
    • Carver, J.A.1    Lindner, R.A.2    Lyon, C.3    Canet, D.4    Hernandez, H.5    Dobson, C.M.6    Redfield, C.7
  • 76
    • 0034739275 scopus 로고    scopus 로고
    • The small heatshock chaperone protein, alpha-crystallin, does not recognize stable molten globule states of cytosolic proteins
    • Treweek TM, Lindner RA, Mariani M and Carver JA. The small heatshock chaperone protein, alpha-crystallin, does not recognize stable molten globule states of cytosolic proteins. Biochim Biophys Acta 2000, 1481: 175-188.
    • (2000) Biochim Biophys Acta , vol.1481 , pp. 175-188
    • Treweek, T.M.1    Lindner, R.A.2    Mariani, M.3    Carver, J.A.4
  • 78
    • 0030783517 scopus 로고    scopus 로고
    • The interaction of the molecular chaperone, alpha-crystallin, with molten globule states of bovine alphalactalbumin
    • Lindner RA, Kapur A and Carver JA. The interaction of the molecular chaperone, alpha-crystallin, with molten globule states of bovine alphalactalbumin. J Biol Chem 1997, 272: 27722-27729.
    • (1997) J Biol Chem , vol.272 , pp. 27722-27729
    • Lindner, R.A.1    Kapur, A.2    Carver, J.A.3
  • 79
    • 0033584959 scopus 로고    scopus 로고
    • Insight into the secondary structure of non-native proteins bound to a molecular chaperone alpha-crystallin. An isotope-edited infrared spectroscopic study
    • Das KP, Choo-Smith LP, Petrash JM and Surewicz WK. Insight into the secondary structure of non-native proteins bound to a molecular chaperone alpha-crystallin. An isotope-edited infrared spectroscopic study. J Biol Chem 1999, 274: 33209-33212.
    • (1999) J Biol Chem , vol.274 , pp. 33209-33212
    • Das, K.P.1    Choo-Smith, L.P.2    Petrash, J.M.3    Surewicz, W.K.4
  • 80
    • 0035865589 scopus 로고    scopus 로고
    • The molecular chaperone alphacrystallin is in kinetic competition with aggregation to stabilize a monomeric molten-globule form of alpha-lactalbumin
    • Lindner RA, Treweek TM and Carver JA. The molecular chaperone alphacrystallin is in kinetic competition with aggregation to stabilize a monomeric molten-globule form of alpha-lactalbumin. Biochem J 2001, 354: 79-87.
    • (2001) Biochem J , vol.354 , pp. 79-87
    • Lindner, R.A.1    Treweek, T.M.2    Carver, J.A.3
  • 81
    • 1542320089 scopus 로고    scopus 로고
    • The identity of proteins associated with a small heat shock protein during heat stress in vivo indicates that these chaperones protect a wide range of cellular functions
    • Basha E, Lee GJ, Breci LA, Hausrath AC, Buan NR, Giese KC and Vierling E. The identity of proteins associated with a small heat shock protein during heat stress in vivo indicates that these chaperones protect a wide range of cellular functions. J Biol Chem 2004, 279: 7566-7575.
    • (2004) J Biol Chem , vol.279 , pp. 7566-7575
    • Basha, E.1    Lee, G.J.2    Breci, L.A.3    Hausrath, A.C.4    Buan, N.R.5    Giese, K.C.6    Vierling, E.7
  • 82
    • 13444283630 scopus 로고    scopus 로고
    • Interaction network containing conserved and essential protein complexes in Escherichia coli
    • Butland G, Peregr?n-Alvarez JM, Li J, Yang W, Yang X, Canadien V and Starostine A, et al. Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 2005, 433: 531-537.
    • (2005) Nature , vol.433 , pp. 531-537
    • Butland, G.1    Peregrn-Alvarez, J.M.2    Li, J.3    Yang, W.4    Yang, X.5    Canadien, V.6    Starostine, A.7
  • 83
    • 42449153631 scopus 로고    scopus 로고
    • The recent evolution of a pseudogene: Diversity and divergence of a mitochondria-localized small heat shock protein in Arabidopsis thaliana
    • Waters ER, Nguyen SL, Eskandar R, Behan J and Sanders-Reed Z. The recent evolution of a pseudogene: diversity and divergence of a mitochondria-localized small heat shock protein in Arabidopsis thaliana. Genome 2008, 51: 177-186.
    • (2008) Genome , vol.51 , pp. 177-186
    • Waters, E.R.1    Nguyen, S.L.2    Eskandar, R.3    Behan, J.4    Sanders-Reed, Z.5
  • 84
    • 0033453223 scopus 로고    scopus 로고
    • Chloroplast small heat shock proteins: Evidence for atypical evolution of an organelle-localized protein
    • Waters ER and Vierling E. Chloroplast small heat shock proteins: evidence for atypical evolution of an organelle-localized protein. Proc Natl Acad Sci USA 1999, 96: 14394-14399.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 14394-14399
    • Waters, E.R.1    Vierling, E.2
  • 85
    • 84864458203 scopus 로고    scopus 로고
    • Small heat shock protein expression and functions during development
    • Morrow G and Tanguay RM. Small heat shock protein expression and functions during development. Int J Biochem Cell Biol 2012, 44: 1613-1621.
    • (2012) Int J Biochem Cell Biol , vol.44 , pp. 1613-1621
    • Morrow, G.1    Tanguay, R.M.2
  • 86
    • 0037470554 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis Hsp16.3 nonamers are assembled and re-Assembled via trimer and hexamer intermediates
    • Abulimiti A, Fu X, Gu L, Feng X and Chang Z. Mycobacterium tuberculosis Hsp16.3 nonamers are assembled and re-Assembled via trimer and hexamer intermediates. J Mol Biol 2003, 326: 1013-1023.
    • (2003) J Mol Biol , vol.326 , pp. 1013-1023
    • Abulimiti, A.1    Fu, X.2    Gu, L.3    Feng, X.4    Chang, Z.5
  • 87
    • 78649346692 scopus 로고    scopus 로고
    • The heat shock response: Life on the verge of death
    • Richter K, Haslbeck M and Buchner J. The heat shock response: life on the verge of death. Mol Cell 2010, 40: 253-266.
    • (2010) Mol Cell , vol.40 , pp. 253-266
    • Richter, K.1    Haslbeck, M.2    Buchner, J.3
  • 88
    • 0034520437 scopus 로고    scopus 로고
    • Biochemical systems analysis of genomewide expression data
    • Voit EO and Radivoyevitch T. Biochemical systems analysis of genomewide expression data. Bioinformatics 2000, 16: 1023-1037.
    • (2000) Bioinformatics , vol.16 , pp. 1023-1037
    • Voit, E.O.1    Radivoyevitch, T.2
  • 89
    • 0032477726 scopus 로고    scopus 로고
    • ATP-enhanced molecular chaperone functions of the small heat shock protein human alpha-crystallin
    • Muchowski PJ and Clark JI. ATP-enhanced molecular chaperone functions of the small heat shock protein human alpha-crystallin. Proc Natl Acad Sci USA 1998, 95: 1004-1009.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 1004-1009
    • Muchowski, P.J.1    Clark, J.I.2
  • 90
    • 0033150267 scopus 로고    scopus 로고
    • Heterologous expression of a plant small heatshock protein enhances Escherichia coli viability under heat and cold stress
    • Soto A, Allona I, Collada C, Guevara MA, Casado R, Rodriguez-Cerezo E and Aragoncillo C, et al. Heterologous expression of a plant small heatshock protein enhances Escherichia coli viability under heat and cold stress. Plant Physiol 1999, 120: 521-528.
    • (1999) Plant Physiol , vol.120 , pp. 521-528
    • Soto, A.1    Allona, I.2    Collada, C.3    Guevara, M.A.4    Casado, R.5    Rodriguez-Cerezo, E.6    Aragoncillo, C.7
  • 91
    • 67249110296 scopus 로고    scopus 로고
    • Role of Escherichia coli heat shock proteins IbpA and IbpB in protection of alcohol dehydrogenase AdhE against heat inactivation in the presence of oxygen
    • Matuszewska E, Kwiatkowska J, Ratajczak E, Kuczynska-Wisnik D and Laskowska E. Role of Escherichia coli heat shock proteins IbpA and IbpB in protection of alcohol dehydrogenase AdhE against heat inactivation in the presence of oxygen. Acta Biochim Pol 2009, 56: 55-61.
    • (2009) Acta Biochim Pol , vol.56 , pp. 55-61
    • Matuszewska, E.1    Kwiatkowska, J.2    Ratajczak, E.3    Kuczynska-Wisnik, D.4    Laskowska, E.5
  • 92
    • 0035987265 scopus 로고    scopus 로고
    • The Escherichia coli small heat-shock proteins IbpA and IbpB prevent the aggregation of endogenous proteins denatured in vivo during extreme heat shock
    • Kuczynska-Wisnik D, Kedzierska S, Matuszewska E, Lund P, Taylor A, Lipinska B and Laskowska E. The Escherichia coli small heat-shock proteins IbpA and IbpB prevent the aggregation of endogenous proteins denatured in vivo during extreme heat shock. Microbiology 2002, 148: 1757-1765.
    • (2002) Microbiology , vol.148 , pp. 1757-1765
    • Kuczynska-Wisnik, D.1    Kedzierska, S.2    Matuszewska, E.3    Lund, P.4    Taylor, A.5    Lipinska, B.6    Laskowska, E.7
  • 93
    • 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 HA, Stein RA, Yang G and McHaourab HS. Mechanism of chaperone function in small heat-shock proteins. Fluorescence studies of the conformations of T4 lysozyme bound to alphaB-crystallin. J Biol Chem 2003, 278: 44214-44221.
    • (2003) J Biol Chem , vol.278 , pp. 44214-44221
    • Sathish, H.A.1    Stein, R.A.2    Yang, G.3    McHaourab, H.S.4
  • 94
    • 84861637257 scopus 로고    scopus 로고
    • Dissecting heterogeneous molecular chaperone complexes using a mass spectrum deconvolution approach
    • Stengel F, Baldwin AJ, Bush MF, Hilton GR, Lioe H, Basha E and Jaya N, et al. Dissecting heterogeneous molecular chaperone complexes using a mass spectrum deconvolution approach. Chem Biol 2012, 19: 599-607.
    • (2012) Chem Biol , vol.19 , pp. 599-607
    • Stengel, F.1    Baldwin, A.J.2    Bush, M.F.3    Hilton, G.R.4    Lioe, H.5    Basha, E.6    Jaya, N.7
  • 97
    • 0346463052 scopus 로고    scopus 로고
    • Interactions between small heat shock protein subunits and substrate in small heat shock protein-substrate complexes
    • Friedrich KL, Giese KC, Buan NR and Vierling E. Interactions between small heat shock protein subunits and substrate in small heat shock protein-substrate complexes. J Biol Chem 2004, 279: 1080-1089.
    • (2004) J Biol Chem , vol.279 , pp. 1080-1089
    • Friedrich, K.L.1    Giese, K.C.2    Buan, N.R.3    Vierling, E.4
  • 99
    • 0030870719 scopus 로고    scopus 로고
    • The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
    • Xu Z, Horwich AL and Sigler PB. The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature 1997, 388: 741-750.
    • (1997) Nature , vol.388 , pp. 741-750
    • Xu, Z.1    Horwich, A.L.2    Sigler, P.B.3
  • 100
    • 0027673091 scopus 로고
    • Comparison of the homologous carboxy-terminal domain and tail of alpha-crystallin and small heat shock protein
    • Merck KB, Horwitz J, Kersten M, Overkamp P, Gaestel M, Bloemendal H and de Jong WW. Comparison of the homologous carboxy-terminal domain and tail of alpha-crystallin and small heat shock protein. Mol Biol Rep 1993, 18: 209-215.
    • (1993) Mol Biol Rep , vol.18 , pp. 209-215
    • Merck, K.B.1    Horwitz, J.2    Kersten, M.3    Overkamp, P.4    Gaestel, M.5    Bloemendal, H.6    De Jong, W.W.7
  • 101
    • 33846018601 scopus 로고    scopus 로고
    • The N-terminal arm of small heat shock proteins is important for both chaperone activity and substrate specificity
    • Basha E, Friedrich KL and Vierling E. The N-terminal arm of small heat shock proteins is important for both chaperone activity and substrate specificity. J Biol Chem 2006, 281: 39943-39952.
    • (2006) J Biol Chem , vol.281 , pp. 39943-39952
    • Basha, E.1    Friedrich, K.L.2    Vierling, E.3
  • 102
    • 33751244272 scopus 로고    scopus 로고
    • N- and C-terminal motifs in human alpha B crystallin play an important role in the recognition, selection, and solubilization of substrates
    • Ghosh JG, Shenoy AK and Clark JI. N- and C-terminal motifs in human alpha B crystallin play an important role in the recognition, selection, and solubilization of substrates. Biochemistry 2006, 45: 13847-13854.
    • (2006) Biochemistry , vol.45 , pp. 13847-13854
    • Ghosh, J.G.1    Shenoy, A.K.2    Clark, J.I.3
  • 103
    • 84856071924 scopus 로고    scopus 로고
    • Importance of N- and C-terminal regions of IbpA, Escherichia coli small heat shock protein, for chaperone function and oligomerization
    • Strozecka J, Chrusciel E, Gorna E, Szymanska A, Zie?tkiewicz S and Liberek K. Importance of N- and C-terminal regions of IbpA, Escherichia coli small heat shock protein, for chaperone function and oligomerization. J Biol Chem 2012, 287: 2843-2853.
    • (2012) J Biol Chem , vol.287 , pp. 2843-2853
    • Strozecka, J.1    Chrusciel, E.2    Gorna, E.3    Szymanska, A.4    Zietkiewicz, S.5    Liberek, K.6
  • 104
    • 0036375506 scopus 로고    scopus 로고
    • A critical motif for oligomerization and chaperone activity of bacterial alpha-heat shock proteins
    • Studer S, Obrist M, Lentze N and Narberhaus F. A critical motif for oligomerization and chaperone activity of bacterial alpha-heat shock proteins. Eur J Biochem 2002, 269: 3578-3586.
    • (2002) Eur J Biochem , vol.269 , pp. 3578-3586
    • Studer, S.1    Obrist, M.2    Lentze, N.3    Narberhaus, F.4
  • 105
    • 33748296234 scopus 로고    scopus 로고
    • Identification of bis-ANS binding sites in Mycobacterium tuberculosis small heat shock protein Hsp16.3: Evidences for a two-step substrate-binding mechanism
    • Fu X and Chang Z. Identification of bis-ANS binding sites in Mycobacterium tuberculosis small heat shock protein Hsp16.3: evidences for a two-step substrate-binding mechanism. Biochem Biophys Res Commun 2006, 349: 167-171.
    • (2006) Biochem Biophys Res Commun , vol.349 , pp. 167-171
    • Fu, X.1    Chang, Z.2
  • 106
    • 84870450357 scopus 로고    scopus 로고
    • Probing the transient interaction between the small heatshock protein Hsp21 and a model substrate protein using crosslinking mass spectrometry
    • Lambert W, Rutsdottir G, Hussein R, Bernfur K, Kjellstrom S and Emanuelsson C. Probing the transient interaction between the small heatshock protein Hsp21 and a model substrate protein using crosslinking mass spectrometry. Cell Stress Chaperones 2013, 18: 75-85.
    • (2013) Cell Stress Chaperones , vol.18 , pp. 75-85
    • Lambert, W.1    Rutsdottir, G.2    Hussein, R.3    Bernfur, K.4    Kjellstrom, S.5    Emanuelsson, C.6
  • 107
    • 80051548039 scopus 로고    scopus 로고
    • Biochemical characterization of small heat shock protein HspB8 (Hsp22)-Bag3 interaction
    • Shemetov AA and Gusev NB. Biochemical characterization of small heat shock protein HspB8 (Hsp22)-Bag3 interaction. Arch Biochem Biophys 2011, 513: 1-9.
    • (2011) Arch Biochem Biophys , vol.513 , pp. 1-9
    • Shemetov, A.A.1    Gusev, N.B.2
  • 108
    • 0031561418 scopus 로고    scopus 로고
    • Functional elements in molecular chaperone alpha-crystallin: Identification of binding sites in alpha B-crystallin
    • Sharma KK, Kaur H and Kester K. Functional elements in molecular chaperone alpha-crystallin: identification of binding sites in alpha B-crystallin. Biochem Biophys Res Commun 1997, 239: 217-222.
    • (1997) Biochem Biophys Res Commun , vol.239 , pp. 217-222
    • Sharma, K.K.1    Kaur, H.2    Kester, K.3
  • 109
    • 0032546801 scopus 로고    scopus 로고
    • Identification of 1,10-bi(4-Anilino)naphthalene-5,50-disulfonic acid binding sequences in alpha-crystallin
    • Sharma KK, Kumar GS, Murphy AS and Kester K. Identification of 1,10-bi(4-Anilino)naphthalene-5,50-disulfonic acid binding sequences in alpha-crystallin. J Biol Chem 1998, 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
  • 110
    • 33646166507 scopus 로고    scopus 로고
    • Identification of a highly conserved pro-gly doublet in non-Animal small heat shock proteins and characterization of its structural and functional roles in Mycobacterium tuberculosis Hsp16.3
    • Fu X and Chang Z. Identification of a highly conserved pro-gly doublet in non-Animal small heat shock proteins and characterization of its structural and functional roles in Mycobacterium tuberculosis Hsp16.3. Biochemistry (Mosc) 2006, 71: S83-S90.
    • (2006) Biochemistry (Mosc) , vol.71
    • Fu, X.1    Chang, Z.2
  • 111
    • 3543039976 scopus 로고    scopus 로고
    • Mutants in a small heat shock protein that affect the oligomeric state. Analysis and allele-specific suppression
    • Giese KC and Vierling E. Mutants in a small heat shock protein that affect the oligomeric state. Analysis and allele-specific suppression. J Biol Chem 2004, 279: 32674-32683.
    • (2004) J Biol Chem , vol.279 , pp. 32674-32683
    • Giese, K.C.1    Vierling, E.2
  • 112
    • 0037427451 scopus 로고    scopus 로고
    • Structural and functional defects caused by point mutations in the alpha-crystallin domain of a bacterial alpha-heat shock protein
    • Lentze N, Studer S and Narberhaus F. Structural and functional defects caused by point mutations in the alpha-crystallin domain of a bacterial alpha-heat shock protein. J Mol Biol 2003, 328: 927-937.
    • (2003) J Mol Biol , vol.328 , pp. 927-937
    • Lentze, N.1    Studer, S.2    Narberhaus, F.3
  • 113
    • 41149087881 scopus 로고    scopus 로고
    • Role of the IXI/V motif in oligomer assembly and function of StHsp14.0, a small heat shock protein from the acidothermophilic archaeon, Sulfolobus tokodaii strain 7
    • Saji H, Iizuka R, Yoshida T, Abe T, Kidokoro S, Ishii N and Yohda M. Role of the IXI/V motif in oligomer assembly and function of StHsp14.0, a small heat shock protein from the acidothermophilic archaeon, Sulfolobus tokodaii strain 7. Proteins 2008, 71: 771-782.
    • (2008) Proteins , vol.71 , pp. 771-782
    • Saji, H.1    Iizuka, R.2    Yoshida, T.3    Abe, T.4    Kidokoro, S.5    Ishii, N.6    Yohda, M.7
  • 114
    • 42349107955 scopus 로고    scopus 로고
    • Site-directed mutations in the C-terminal extension of human alphaB-crystallin affect chaperone function and block amyloid fibril formation
    • Treweek TM, Ecroyd H, Williams DM, Meehan S, Carver JA and Walker MJ. Site-directed mutations in the C-terminal extension of human alphaB-crystallin affect chaperone function and block amyloid fibril formation. PLoS ONE 2007, 2: e1046.
    • (2007) PLoS ONE , vol.2
    • Treweek, T.M.1    Ecroyd, H.2    Williams, D.M.3    Meehan, S.4    Carver, J.A.5    Walker, M.J.6
  • 115
    • 0037155819 scopus 로고    scopus 로고
    • The R116C mutation in alpha A-crystallin diminishes its protective ability against stress-induced lens epithelial cell apoptosis
    • Andley UP, Patel HC and Xi JH. The R116C mutation in alpha A-crystallin diminishes its protective ability against stress-induced lens epithelial cell apoptosis. J Biol Chem 2002, 277: 10178-10186.
    • (2002) J Biol Chem , vol.277 , pp. 10178-10186
    • Andley, U.P.1    Patel, H.C.2    Xi, J.H.3
  • 116
    • 0033588379 scopus 로고    scopus 로고
    • Structural and functional consequences of the mutation of a conserved arginine residue in alphaA and alphaB crystallins
    • Kumar LV, Ramakrishna T and Rao CM. Structural and functional consequences of the mutation of a conserved arginine residue in alphaA and alphaB crystallins. J Biol Chem 1999, 274: 24137-24141.
    • (1999) J Biol Chem , vol.274 , pp. 24137-24141
    • Kumar, L.V.1    Ramakrishna, T.2    Rao, C.M.3
  • 118
    • 70349470609 scopus 로고    scopus 로고
    • Substrate binding site flexibility of the small heat shock protein molecular chaperones
    • Jaya N, Garcia V and Vierling E. Substrate binding site flexibility of the small heat shock protein molecular chaperones. Proc Natl Acad Sci USA 2009, 106: 15604-15609.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 15604-15609
    • Jaya, N.1    Garcia, V.2    Vierling, E.3
  • 119
    • 0037143649 scopus 로고    scopus 로고
    • Addition of a photocrosslinking amino acid to the genetic code of Escherichia coli
    • Chin JW, Martin AB, King DS, Wang L and Schultz PG. Addition of a photocrosslinking amino acid to the genetic code of Escherichia coli. Proc Natl Acad Sci USA 2002, 99: 11020-11024.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 11020-11024
    • Chin, J.W.1    Martin, A.B.2    King, D.S.3    Wang, L.4    Schultz, P.G.5
  • 120
    • 0029956553 scopus 로고    scopus 로고
    • Effects of site-directed mutations on the chaperone-like activity of alphaB-crystallin
    • Plater ML, Goode D and Crabbe MJ. Effects of site-directed mutations on the chaperone-like activity of alphaB-crystallin. J Biol Chem 1996, 271: 28558-62856.
    • (1996) J Biol Chem , vol.271 , pp. 28558-62856
    • Plater, M.L.1    Goode, D.2    Crabbe, M.J.3
  • 122
    • 0042733148 scopus 로고    scopus 로고
    • Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK
    • Mogk A, Schlieker C, Friedrich KL, Schonfeld HJ, Vierling E and Bukau B. Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK. J Biol Chem 2003, 278: 31033-31042.
    • (2003) J Biol Chem , vol.278 , pp. 31033-31042
    • Mogk, A.1    Schlieker, C.2    Friedrich, K.L.3    Schonfeld, H.J.4    Vierling, E.5    Bukau, B.6
  • 123
    • 1542617030 scopus 로고    scopus 로고
    • Temperature-dependent subunit exchange and chaperone-like activities of Hsp16.3, a small heat shock protein from Mycobacterium tuberculosis
    • Fu X and Chang Z. Temperature-dependent subunit exchange and chaperone-like activities of Hsp16.3, a small heat shock protein from Mycobacterium tuberculosis. Biochem Biophys Res Commun 2004, 316: 291-299.
    • (2004) Biochem Biophys Res Commun , vol.316 , pp. 291-299
    • Fu, X.1    Chang, Z.2
  • 125
    • 0037064015 scopus 로고    scopus 로고
    • Subunit exchange, conformational stability, and chaperone-like function of the small heat shock protein 16.5 from Methanococcus jannaschii
    • Bova MP, Huang Q, Ding L and Horwitz J. Subunit exchange, conformational stability, and chaperone-like function of the small heat shock protein 16.5 from Methanococcus jannaschii. J Biol Chem 2002, 277: 38468-38475.
    • (2002) J Biol Chem , vol.277 , pp. 38468-38475
    • Bova, M.P.1    Huang, Q.2    Ding, L.3    Horwitz, J.4
  • 126
    • 21744436278 scopus 로고    scopus 로고
    • The activation mechanism of Hsp26 does not require dissociation of the oligomer
    • Franzmann TM, Wuhr M, Richter K, Walter S and Buchner J. The activation mechanism of Hsp26 does not require dissociation of the oligomer. J Mol Biol 2005, 350: 1083-1093.
    • (2005) J Mol Biol , vol.350 , pp. 1083-1093
    • Franzmann, T.M.1    Wuhr, M.2    Richter, K.3    Walter, S.4    Buchner, J.5
  • 127
    • 38649115030 scopus 로고    scopus 로고
    • Activation of the chaperone Hsp26 is controlled by the rearrangement of its thermosensor domain
    • Franzmann TM, Menhorn P, Walter S and Buchner J. Activation of the chaperone Hsp26 is controlled by the rearrangement of its thermosensor domain. Mol Cell 2008, 29: 207-216.
    • (2008) Mol Cell , vol.29 , pp. 207-216
    • Franzmann, T.M.1    Menhorn, P.2    Walter, S.3    Buchner, J.4
  • 128
    • 77951228945 scopus 로고    scopus 로고
    • Mechanistic differences between two conserved classes of small heat shock proteins found in the plant cytosol
    • Basha E, Jones C, Wysocki V and Vierling E. Mechanistic differences between two conserved classes of small heat shock proteins found in the plant cytosol. J Biol Chem 2010, 285: 11489-11497.
    • (2010) J Biol Chem , vol.285 , pp. 11489-11497
    • Basha, E.1    Jones, C.2    Wysocki, V.3    Vierling, E.4
  • 129
    • 0030798628 scopus 로고    scopus 로고
    • Chaperone-like activity and temperature-induced structural changes of alpha-crystallin
    • Raman B and Rao CM. Chaperone-like activity and temperature-induced structural changes of alpha-crystallin. J Biol Chem 1997, 272: 23559-23564.
    • (1997) J Biol Chem , vol.272 , pp. 23559-23564
    • Raman, B.1    Rao, C.M.2
  • 131
    • 1342271074 scopus 로고    scopus 로고
    • Some properties of human small heat shock protein Hsp20 (HspB6)
    • Bukach OV, Seit-Nebi AS, Marston SB and Gusev NB. Some properties of human small heat shock protein Hsp20 (HspB6). Eur J Biochem 2004, 271: 291-302.
    • (2004) Eur J Biochem , vol.271 , pp. 291-302
    • Bukach, O.V.1    Seit-Nebi, A.S.2    Marston, S.B.3    Gusev, N.B.4
  • 132
    • 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 HA, Dong J and McHaourab HS. 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 2005, 280: 5281-5289.
    • (2005) J Biol Chem , vol.280 , pp. 5281-5289
    • Shashidharamurthy, R.1    Koteiche, H.A.2    Dong, J.3    McHaourab, H.S.4
  • 133
    • 79961031623 scopus 로고    scopus 로고
    • H11 kinase/heat shock protein 22 deletion impairs both nuclear and mitochondrial functions of STAT3 and accelerates the transition into heart failure on cardiac overload
    • Qiu H, Lizano P, Laure L, Sui X, Rashed E, Park JY and Hong C, et al. H11 kinase/heat shock protein 22 deletion impairs both nuclear and mitochondrial functions of STAT3 and accelerates the transition into heart failure on cardiac overload. Circulation 2011, 124: 406-415.
    • (2011) Circulation , vol.124 , pp. 406-415
    • Qiu, H.1    Lizano, P.2    Laure, L.3    Sui, X.4    Rashed, E.5    Park, J.Y.6    Hong, C.7


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