-
1
-
-
0018221572
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
10
-
-
0037108910
-
Small heat-shock proteins regulate membrane lipid polymorphism
-
Tsvetkova NM, Horvath I, Torok Z, Wolkers WF, Balogi Z, Shigapova N and Crowe LM, et al. Small heat-shock proteins regulate membrane lipid polymorphism. Proc Natl Acad Sci USA 2002, 99: 13504-13509.
-
(2002)
Proc Natl Acad Sci USA
, vol.99
, pp. 13504-13509
-
-
Tsvetkova, N.M.1
Horvath, I.2
Torok, Z.3
Wolkers, W.F.4
Balogi, Z.5
Shigapova, N.6
Crowe, L.M.7
-
11
-
-
0032079487
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
32
-
-
2642539919
-
Hot-spot residue in small heat-shock protein 22 causes distal motor neuropathy
-
Irobi J, Van Impe K, Seeman P, Jordanova A, Dierick I, Verpoorten N and Michalik A, et al. Hot-spot residue in small heat-shock protein 22 causes distal motor neuropathy. Nat Genet 2004, 36: 597-601.
-
(2004)
Nat Genet
, vol.36
, pp. 597-601
-
-
Irobi, J.1
Van Impe, K.2
Seeman, P.3
Jordanova, A.4
Dierick, I.5
Verpoorten, N.6
Michalik, A.7
-
33
-
-
2642563501
-
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
-
34
-
-
0035191639
-
Crystal structure and assembly of a eukaryotic small heat shock protein
-
van Montfort RL, Basha E, Friedrich KL, Slingsby C and Vierling E. Crystal structure and assembly of a eukaryotic small heat shock protein. Nat Struct Biol 2001, 8: 1025-1030.
-
(2001)
Nat Struct Biol
, vol.8
, pp. 1025-1030
-
-
Van Montfort, R.L.1
Basha, E.2
Friedrich, K.L.3
Slingsby, C.4
Vierling, E.5
-
35
-
-
1342292267
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
52
-
-
80255129390
-
Small heat shock protein AgsA forms dynamic fibrils
-
Shi X, Wang Z, Yan L, Ezemaduka AN, Fan G, Wang R and Fu X, et al. Small heat shock protein AgsA forms dynamic fibrils. FEBS Lett 2011, 585: 3396-3402.
-
(2011)
FEBS Lett
, vol.585
, pp. 3396-3402
-
-
Shi, X.1
Wang, Z.2
Yan, L.3
Ezemaduka, A.N.4
Fan, G.5
Wang, R.6
Fu, X.7
-
53
-
-
25144441023
-
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
-
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
-
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
-
56
-
-
84870917750
-
Alternative bacterial two-component small heat shock protein systems
-
Bepperling A, Alte F, Kriehuber T, Braun N, Weinkauf S, Groll M and Haslbeck M, et al. Alternative bacterial two-component small heat shock protein systems. Proc Natl Acad Sci USA 2012, 109: 20407-20412.
-
(2012)
Proc Natl Acad Sci USA
, vol.109
, pp. 20407-20412
-
-
Bepperling, A.1
Alte, F.2
Kriehuber, T.3
Braun, N.4
Weinkauf, S.5
Groll, M.6
Haslbeck, M.7
-
57
-
-
0032052239
-
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
-
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
-
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
-
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
-
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
-
64
-
-
84883003759
-
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
-
-
0027524175
-
Structural and functional similarities of bovine alpha-crystallin and mouse small heat-shock protein. A family of chaperones
-
Merck KB, Groenen PJ, Voorter CE, de Haard-Hoekman WA, Horwitz J, Bloemendal H and de Jong WW. Structural and functional similarities of bovine alpha-crystallin and mouse small heat-shock protein. A family of chaperones. J Biol Chem 1993, 268: 1046-1052.
-
(1993)
J Biol Chem
, vol.268
, pp. 1046-1052
-
-
Merck, K.B.1
Groenen, P.J.2
Voorter, C.E.3
De Haard-Hoekman, W.A.4
Horwitz, J.5
Bloemendal, H.6
De Jong, W.W.7
-
66
-
-
77953799932
-
Small heat-shock proteins interact with a flanking domain to suppress polyglutamine aggregation
-
Robertson AL, Headey SJ, Saunders HM, Ecroyd H, Scanlon MJ, Carver JA and Bottomley SP. Small heat-shock proteins interact with a flanking domain to suppress polyglutamine aggregation. Proc Natl Acad Sci USA 2010, 107: 10424-10429.
-
(2010)
Proc Natl Acad Sci USA
, vol.107
, pp. 10424-10429
-
-
Robertson, A.L.1
Headey, S.J.2
Saunders, H.M.3
Ecroyd, H.4
Scanlon, M.J.5
Carver, J.A.6
Bottomley, S.P.7
-
67
-
-
84863683967
-
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
-
68
-
-
0033485868
-
Hsp26: A temperature-regulated chaperone
-
Haslbeck M, Walke S, Stromer T, Ehrnsperger M, White HE, Chen S and Saibil HR, et al. Hsp26: a temperature-regulated chaperone. EMBO J 1999, 18: 6744-6751.
-
(1999)
EMBO J
, vol.18
, pp. 6744-6751
-
-
Haslbeck, M.1
Walke, S.2
Stromer, T.3
Ehrnsperger, M.4
White, H.E.5
Chen, S.6
Saibil, H.R.7
-
69
-
-
84874296899
-
Small heat shock protein AgsA: An effective stabilizer of enzyme activities
-
Tomoyasu T, Tabata A, Ishikawa Y, Whiley RA and Nagamune H. Small heat shock protein AgsA: an effective stabilizer of enzyme activities. J Biosci Bioeng 2013, 115: 15-19.
-
(2013)
J Biosci Bioeng
, vol.115
, pp. 15-19
-
-
Tomoyasu, T.1
Tabata, A.2
Ishikawa, Y.3
Whiley, R.A.4
Nagamune, H.5
-
70
-
-
15844414479
-
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
-
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
-
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
-
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
-
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
-
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
-
77
-
-
0028988412
-
Interaction of alpha-crystallin with spinlabeled peptides
-
Farahbakhsh ZT, Huang QL, Ding LL, Altenbach C, Steinhoff HJ, Horwitz J and Hubbell WL. Interaction of alpha-crystallin with spinlabeled peptides. Biochemistry 1995, 34: 509-516.
-
(1995)
Biochemistry
, vol.34
, pp. 509-516
-
-
Farahbakhsh, Z.T.1
Huang, Q.L.2
Ding, L.L.3
Altenbach, C.4
Steinhoff, H.J.5
Horwitz, J.6
Hubbell, W.L.7
-
78
-
-
0030783517
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
96
-
-
0033547324
-
Identification of in vivo substrates of the chaperonin GroEL
-
Houry WA, Frishman D, Eckerskorn C, Lottspeich F and Hartl FU. Identification of in vivo substrates of the chaperonin GroEL. Nature 1999, 402: 147-154.
-
(1999)
Nature
, vol.402
, pp. 147-154
-
-
Houry, W.A.1
Frishman, D.2
Eckerskorn, C.3
Lottspeich, F.4
Hartl, F.U.5
-
97
-
-
0346463052
-
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
-
98
-
-
76649084269
-
Quaternary dynamics and plasticity underlie small heat shock protein chaperone function 2007-2012
-
Stengel F, Baldwin AJ, Painter AJ, Jaya N, Basha E, Kay LE and Vierling E, et al. Quaternary dynamics and plasticity underlie small heat shock protein chaperone function. Proc Natl Acad Sci USA 2010, 107: 2007-2012.
-
Proc Natl Acad Sci USA
, vol.2010
, pp. 107
-
-
Stengel, F.1
Baldwin, A.J.2
Painter, A.J.3
Jaya, N.4
Basha, E.5
Kay, L.E.6
Vierling, E.7
-
99
-
-
0030870719
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
117
-
-
3042711961
-
Desmin-related cardiomyopathy in transgenic mice: A cardiac amyloidosis
-
Sanbe A, Osinska H, Saffitz JE, Glabe CG, Kayed R, Maloyan A and Robbins J. Desmin-related cardiomyopathy in transgenic mice: a cardiac amyloidosis. Proc Natl Acad Sci USA 2004, 101: 10132-10136.
-
(2004)
Proc Natl Acad Sci USA
, vol.101
, pp. 10132-10136
-
-
Sanbe, A.1
Osinska, H.2
Saffitz, J.E.3
Glabe, C.G.4
Kayed, R.5
Maloyan, A.6
Robbins, J.7
-
118
-
-
70349470609
-
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
-
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
-
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
-
121
-
-
0028979976
-
The mutation Asp69-.Ser affects the chaperonelike activity of alpha A-crystallin
-
Smulders RH,Merck KB, Aendekerk J, Horwitz J, Takemoto L, Slingsby C and Bloemendal H, et al. The mutation Asp69-.Ser affects the chaperonelike activity of alpha A-crystallin. Eur J Biochem 1995, 232: 834-838.
-
(1995)
Eur J Biochem
, vol.232
, pp. 834-838
-
-
Smulders, R.H.1
Merck, K.B.2
Aendekerk, J.3
Horwitz, J.4
Takemoto, L.5
Slingsby, C.6
Bloemendal, H.7
-
122
-
-
0042733148
-
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
-
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
-
124
-
-
41249084876
-
Structural dynamics of archaeal small heat shock proteins
-
Haslbeck M, Kastenmuller A, Buchner J, Weinkauf S and Braun N. Structural dynamics of archaeal small heat shock proteins. J Mol Biol 2008, 378: 362-374.
-
(2008)
J Mol Biol
, vol.378
, pp. 362-374
-
-
Haslbeck, M.1
Kastenmuller, A.2
Buchner, J.3
Weinkauf, S.4
Braun, N.5
-
125
-
-
0037064015
-
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
-
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
-
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
-
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
-
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
-
130
-
-
33846278382
-
Mimicking phosphorylation of alphaB-crystallin affects its chaperone activity
-
Ecroyd H, Meehan S, Horwitz J, Aquilina JA, Benesch JL, Robinson CV and Macphee CE, et al. Mimicking phosphorylation of alphaB-crystallin affects its chaperone activity. Biochem J 2007, 401: 129-141.
-
(2007)
Biochem J
, vol.401
, pp. 129-141
-
-
Ecroyd, H.1
Meehan, S.2
Horwitz, J.3
Aquilina, J.A.4
Benesch, J.L.5
Robinson, C.V.6
Macphee, C.E.7
-
132
-
-
14044272992
-
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
-
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
-
134
-
-
84885081139
-
Regulated structural transitions unleash the chaperone activity of alphaB-crystallin
-
Peschek J, Braun N, Rohrberg J, Back KC, Kriehuber T, Kastenmu ller A and Weinkauf S, et al. Regulated structural transitions unleash the chaperone activity of alphaB-crystallin. Proc Natl Acad Sci USA 2013, 110: E3780-E3789
-
(2013)
Proc Natl Acad Sci USA
, vol.110
-
-
Peschek, J.1
Braun, N.2
Rohrberg, J.3
Back, K.C.4
Kriehuber, T.5
Kastenmu Ller, A.6
Weinkauf, S.7
|