-
1
-
-
0042733148
-
Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK
-
DOI 10.1074/jbc.M303587200
-
Mogk, A., Schlieker, C., Friedrich, K. L., Schönfeld, H. J., Vierling, E., and Bukau, B. (2003) Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK. J. Biol. Chem. 278, 31033-31042 (Pubitemid 36994617)
-
(2003)
Journal of Biological Chemistry
, vol.278
, Issue.33
, pp. 31033-31042
-
-
Mogk, A.1
Schlieker, C.2
Friedrich, K.L.3
Schonfeld, H.-J.4
Vierling, E.5
Bukau, B.6
-
2
-
-
21244497886
-
Disassembling protein aggregates in the yeast cytosol: The cooperation of HSP26 with SSA1 and HSP104
-
DOI 10.1074/jbc.M502697200
-
Haslbeck, M., Miess, A., Stromer, T., Walter, S., and Buchner, J. (2005) Disassembling protein aggregates in the yeast cytosol. The cooperation of Hsp26 with Ssa1 and Hsp104. J. Biol. Chem. 280, 23861-23868 (Pubitemid 40884873)
-
(2005)
Journal of Biological Chemistry
, vol.280
, Issue.25
, pp. 23861-23868
-
-
Haslbeck, M.1
Miess, A.2
Stromer, T.3
Walter, S.4
Buchner, J.5
-
3
-
-
0033765314
-
A small heat shock protein cooperates with heat shock protein 70 systems to reactivate a heat-denatured protein
-
Lee, G. J., and Vierling, E. (2000) A small heat shock protein cooperates with heat shock protein 70 systems to reactivate a heat-denatured protein. Plant Physiol. 122, 189-198
-
(2000)
Plant Physiol.
, vol.122
, pp. 189-198
-
-
Lee, G.J.1
Vierling, E.2
-
4
-
-
0142125283
-
Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation
-
DOI 10.1046/j.1365-2958.2003.03710.x
-
Mogk, A., Deuerling, E., Vorderwülbecke, S., Vierling, E., and Bukau, B. (2003) Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation. Mol. Microbiol. 50, 585-595 (Pubitemid 37297136)
-
(2003)
Molecular Microbiology
, vol.50
, Issue.2
, pp. 585-595
-
-
Mogk, A.1
Deuerling, E.2
Vorderwulbecke, S.3
Vierling, E.4
Bukau, B.5
-
5
-
-
16844368450
-
The small heat shock protein IbpA of Escherichia coli cooperates with IbpB in stabilization of thermally aggregated proteins in a disaggregation competent state
-
Matuszewska, M., Kuczyńska-Winik, D., Laskowska, E., and Liberek, K. (2005) The small heat shock protein IbpA of Escherichia coli cooperates with IbpB in stabilization of thermally aggregated proteins in a disaggregation competent state. J. Biol. Chem. 280, 12292-12298
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 12292-12298
-
-
Matuszewska, M.1
Kuczyńska-Winik, D.2
Laskowska, E.3
Liberek, K.4
-
6
-
-
0032079487
-
The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network
-
DOI 10.1074/jbc.273.18.11032
-
Veinger, L., Diamant, S., Buchner, J., and Goloubinoff, P. (1998) The small heat shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network. J. Biol. Chem. 273, 11032-11037 (Pubitemid 28204946)
-
(1998)
Journal of Biological Chemistry
, vol.273
, Issue.18
, pp. 11032-11037
-
-
Veinger, L.1
Diamant, S.2
Buchner, J.3
Goloubinoff, P.4
-
7
-
-
0031024691
-
A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state
-
DOI 10.1093/emboj/16.3.659
-
Lee, G. J., Roseman, A. M., Saibil, H. R., and Vierling, E. (1997)Asmall heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state. EMBO J. 16, 659-671 (Pubitemid 27067794)
-
(1997)
EMBO Journal
, vol.16
, Issue.3
, pp. 659-671
-
-
Lee, G.J.1
Roseman, A.M.2
Saibil, H.R.3
Vierling, E.4
-
8
-
-
0343742639
-
Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation
-
DOI 10.1093/emboj/16.2.221
-
Ehrnsperger, M., Gräber, S., Gaestel, M., and Buchner, J. (1997) Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation. EMBO J. 16, 221-229 (Pubitemid 27049380)
-
(1997)
EMBO Journal
, vol.16
, Issue.2
, pp. 221-229
-
-
Ehrnsperger, M.1
Graber, S.2
Gaestel, M.3
Buchner, J.4
-
9
-
-
58549098512
-
Distinct activities of Escherichia coli small heat shock proteins IbpA and IbpB promote efficient protein disaggregation
-
Ratajczak, E., Zietkiewicz, S., and Liberek, K. (2009) Distinct activities of Escherichia coli small heat shock proteins IbpA and IbpB promote efficient protein disaggregation. J. Mol. Biol. 386, 178-189
-
(2009)
J. Mol. Biol.
, vol.386
, pp. 178-189
-
-
Ratajczak, E.1
Zietkiewicz, S.2
Liberek, K.3
-
10
-
-
0036195722
-
α-Crystallin-type heat shock proteins. Socializing minichaperones in the context of a multichaperone network
-
Narberhaus, F. (2002) α-Crystallin-type heat shock proteins. Socializing minichaperones in the context of a multichaperone network. Microbiol. Mol. Biol. Rev. 66, 64-93
-
(2002)
Microbiol. Mol. Biol. Rev.
, vol.66
, pp. 64-93
-
-
Narberhaus, F.1
-
11
-
-
0035718677
-
Structure and function of the small heat shock protein/α-crystallin family of molecular chaperones
-
DOI 10.1016/S0065-3233(01)59004-X
-
Van Montfort, R., Slingsby, C., and Vierling, E. (2001) Structure and function of the small heat shock protein/α-crystallin family of molecular chaperones. Adv. Protein Chem. 59, 105-156 (Pubitemid 34169303)
-
(2001)
Advances in Protein Chemistry
, vol.59
, pp. 105-156
-
-
Van Montfort, R.1
Slingsby, C.2
Vierling, E.3
-
12
-
-
0036809333
-
SHsps and their role in the chaperone network
-
Haslbeck, M. (2002) sHsps and their role in the chaperone network. Cell Mol. Life Sci. 59, 1649-1657
-
(2002)
Cell Mol. Life Sci.
, vol.59
, pp. 1649-1657
-
-
Haslbeck, M.1
-
13
-
-
27144448839
-
Some like it hot: The structure and function of small heat-shock proteins
-
DOI 10.1038/nsmb993, PII N993
-
Haslbeck, M., Franzmann, T., Weinfurtner, D., and Buchner, J. (2005) Some like it hot. The structure and function of small heat-shock proteins. Nat. Struct. Mol. Biol. 12, 842-846 (Pubitemid 41486706)
-
(2005)
Nature Structural and Molecular Biology
, vol.12
, Issue.10
, pp. 842-846
-
-
Haslbeck, M.1
Franzmann, T.2
Weinfurtner, D.3
Buchner, J.4
-
14
-
-
0026784986
-
Two novel heat shock genes encoding proteins produced in response to heterologous protein expression in Escherichia coli
-
Allen, S. P., Polazzi, J. O., Gierse, J. K., and Easton, A. M. (1992) Two novel heat shock genes encoding proteins produced in response to heterologous protein expression in Escherichia coli. J. Bacteriol. 174, 6938-6947
-
(1992)
J. Bacteriol.
, vol.174
, pp. 6938-6947
-
-
Allen, S.P.1
Polazzi, J.O.2
Gierse, J.K.3
Easton, A.M.4
-
15
-
-
0039870135
-
IbpA and IbpB, the new heat-shock proteins, bind to endogenous Escherichia coli proteins aggregated intracellularly by heat shock
-
DOI 10.1016/0300-9084(96)82643-5
-
Laskowska, E., Wawrzynów, A., and Taylor, A. (1996) IbpA and IbpB, the new heat-shock proteins, bind to endogenous Escherichia coli proteins aggregated intracellularly by heat shock. Biochimie 78, 117-122 (Pubitemid 26260836)
-
(1996)
Biochimie
, vol.78
, Issue.2
, pp. 117-122
-
-
Laskowska, E.1
Wawrzynow, A.2
Taylor, A.3
-
16
-
-
0035987265
-
The Escherichia coli small heat-shock proteins IbpA and IbpB prevent the aggregation of endogenous proteins denatured in vivo during extreme heat shock
-
Kuczyńska-Winik, D., Kedzierska, S., Matuszewska, E., Lund, P., Taylor, A., Lipińska, B., and Laskowska, E. (2002) The Escherichia coli small heat-shock proteins IbpA and IbpB prevent the aggregation of endogenous proteins denatured in vivo during extreme heat shock. Microbiology 148, 1757-1765 (Pubitemid 34679029)
-
(2002)
Microbiology
, vol.148
, Issue.6
, 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
-
17
-
-
0033537845
-
Biochemical characterization of the small heat shock protein IbpB from Escherichia coli
-
Shearstone, J. R., and Baneyx, F. (1999) Biochemical characterization of the small heat shock protein IbpB from Escherichia coli. J. Biol. Chem. 274, 9937-9945
-
(1999)
J. Biol. Chem.
, vol.274
, pp. 9937-9945
-
-
Shearstone, J.R.1
Baneyx, F.2
-
18
-
-
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
-
DOI 10.1016/j.jmb.2005.01.029
-
Jiao, W., Qian, M., Li, P., Zhao, L., and Chang, Z. (2005) 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. 347, 871-884 (Pubitemid 40357925)
-
(2005)
Journal of Molecular Biology
, vol.347
, Issue.4
, pp. 871-884
-
-
Jiao, W.1
Qian, M.2
Li, P.3
Zhao, L.4
Chang, Z.5
-
19
-
-
0036315595
-
Escherichia coli small heat shock proteins, IbpA and IbpB, protect enzymes from inactivation by heat and oxidants
-
DOI 10.1046/j.1432-1033.2002.02958.x
-
Kitagawa, M., Miyakawa, M., Matsumura, Y., and Tsuchido, T. (2002) Escherichia coli small heat shock proteins, IbpA and IbpB, protect enzymes from inactivation by heat and oxidants. Eur. J. Biochem. 269, 2907-2917 (Pubitemid 34754019)
-
(2002)
European Journal of Biochemistry
, vol.269
, Issue.12
, pp. 2907-2917
-
-
Kitagawa, M.1
Miyakawa, M.2
Matsumura, Y.3
Tsuchido, T.4
-
20
-
-
77952959280
-
IbpA the small heat shock protein from Escherichia coli forms fibrils in the absence of its cochaperone IbpB
-
Ratajczak, E., Strózecka, J., Matuszewska, M., Zietkiewicz, S., Kuczyńska-Winik, D., Laskowska, E., Liberek, K. (2010) IbpA the small heat shock protein from Escherichia coli forms fibrils in the absence of its cochaperone IbpB. FEBS Lett. 584, 2253-2257
-
(2010)
FEBS Lett.
, vol.584
, pp. 2253-2257
-
-
Ratajczak, E.1
Strózecka, J.2
Matuszewska, M.3
Zietkiewicz, S.4
Kuczyńska-Winik, D.5
Laskowska, E.6
Liberek, K.7
-
21
-
-
0027445907
-
Sequence analysis of four new heat-shock genes constituting the hslTS/ibpAB and hslVU operons in Escherichia coli
-
Chuang, S. E., Burland, V., Plunkett, G., 3rd, Daniels, D. L., and Blattner, F. R. (1993) Sequence analysis of four new heat-shock genes constituting the hslTS/ibpAB and hslVU operons in Escherichia coli. Gene 134, 1-6
-
(1993)
Gene
, vol.134
, pp. 1-6
-
-
Chuang, S.E.1
Burland, V.2
Plunkett III, G.3
Daniels, D.L.4
Blattner, F.R.5
-
22
-
-
13444283630
-
Interaction network containing conserved and essential protein complexes in Escherichia coli
-
DOI 10.1038/nature03239
-
Butland, G., Peregrín-Alvarez, J. M., Li, J., Yang, W., Yang, X., Canadien, V., Starostine, A., Richards, D., Beattie, B., Krogan, N., Davey, M., Parkinson, J., Greenblatt, J., and Emili, A. (2005) Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433, 531-537 (Pubitemid 40204311)
-
(2005)
Nature
, vol.433
, Issue.7025
, pp. 531-537
-
-
Butland, G.1
Peregrin-Alvarez, J.M.2
Li, J.3
Yang, W.4
Yang, X.5
Canadien, V.6
Starostine, A.7
Richards, D.8
Beattie, B.9
Krogan, N.10
Davey, M.11
Parkinson, J.12
Greenblatt, J.13
Emili, A.14
-
23
-
-
0024316732
-
Initiation of λ DNA replication with purified host- and bacteriophage-encoded proteins: The role of the dnaK, dnaJ and grpE heat shock proteins
-
Zylicz, M., Ang, D., Liberek, K., and Georgopoulos, C. (1989) Initiation of λ DNA replication with purified host- and bacteriophage-encoded proteins. The role of the dnaK, dnaJ and grpE heat shock proteins. EMBO J. 8, 1601-1608 (Pubitemid 19274387)
-
(1989)
EMBO Journal
, vol.8
, Issue.5
, pp. 1601-1608
-
-
Zylicz, M.1
Ang, D.2
Liberek, K.3
Georgopoulos, C.4
-
24
-
-
0001592716
-
The heat-shock protein ClpB in Escherichia coli is a protein-activated ATPase
-
Woo, K. M., Kim, K. I., Goldberg, A. L., Ha, D. B., and Chung, C. H. (1992) The heat-shock protein ClpB in Escherichia coli is a protein-activated ATPase. J. Biol. Chem. 267, 20429-20434
-
(1992)
J. Biol. Chem.
, vol.267
, pp. 20429-20434
-
-
Woo, K.M.1
Kim, K.I.2
Goldberg, A.L.3
Ha, D.B.4
Chung, C.H.5
-
25
-
-
33646354916
-
Hsp70 chaperone machine remodels protein aggregates at the initial step of Hsp70-Hsp100-dependent disaggregation
-
DOI 10.1074/jbc.M507893200
-
Zietkiewicz, S., Lewandowska, A., Stocki, P., and Liberek, K. (2006) Hsp70 chaperone machine remodels protein aggregates at the initial step of Hsp70-Hsp100-dependent disaggregation. J. Biol. Chem. 281, 7022-7029 (Pubitemid 43847465)
-
(2006)
Journal of Biological Chemistry
, vol.281
, Issue.11
, pp. 7022-7029
-
-
Zietkiewicz, S.1
Lewandowska, A.2
Stocki, P.3
Liberek, K.4
-
26
-
-
1342292267
-
Crystal structure of a small heat-shock protein
-
DOI 10.1038/29106
-
Kim, K. K., Kim, R., and Kim, S. H. (1998) Crystal structure of a small heat-shock protein. Nature 394, 595-599 (Pubitemid 28366837)
-
(1998)
Nature
, vol.394
, Issue.6693
, pp. 595-599
-
-
Kim, K.K.1
Kim, R.2
Kim, S.-H.3
-
27
-
-
3543039976
-
Mutants in a small heat shock protein that affect the oligomeric state: Analysis and allele-specific suppression
-
DOI 10.1074/jbc.M404455200
-
Giese, K. C., Vierling, E. (2004) Mutants in a small heat shock protein that affect the oligomeric state. Analysis and allele-specific suppression. J. Biol. Chem. 279, 32674-32683 (Pubitemid 39014726)
-
(2004)
Journal of Biological Chemistry
, vol.279
, Issue.31
, pp. 32674-32683
-
-
Giese, K.C.1
Vierling, E.2
-
28
-
-
70349470609
-
Substrate binding site flexibility of the small heat shock protein molecular chaperones
-
Jaya, N., Garcia, V., and Vierling, E. (2009) Substrate binding site flexibility of the small heat shock protein molecular chaperones. Proc. Natl. Acad. Sci. U.S.A. 106, 15604-15609
-
(2009)
Proc. Natl. Acad. Sci. U.S.A.
, vol.106
, pp. 15604-15609
-
-
Jaya, N.1
Garcia, V.2
Vierling, E.3
-
29
-
-
33846018601
-
The N-terminal arm of small heat shock proteins is important for both chaperone activity and substrate specificity
-
DOI 10.1074/jbc.M607677200
-
Basha, E., Friedrich, K. L., and Vierling, E. (2006) The N-terminal arm of small heat shock proteins is important for both chaperone activity and substrate specificity. J. Biol. Chem. 281, 39943-39952 (Pubitemid 46041798)
-
(2006)
Journal of Biological Chemistry
, vol.281
, Issue.52
, pp. 39943-39952
-
-
Basha, E.1
Friedrich, K.L.2
Vierling, E.3
-
30
-
-
14844292563
-
A dual role for the N-terminal region of Mycobacterium tuberculosis Hsp16.3 in self-oligomerization and binding denaturing substrate proteins
-
DOI 10.1074/jbc.M406319200
-
Fu, X., Zhang, H., Zhang, X., Cao, Y., Jiao, W., Liu, C., Song, Y., Abulimiti, A., and Chang, Z. (2005) A dual role for the N-terminal region of Mycobacterium tuberculosis Hsp16.3 in self-oligomerization and binding denaturing substrate proteins. J. Biol. Chem. 280, 6337-6348 (Pubitemid 40341180)
-
(2005)
Journal of Biological Chemistry
, vol.280
, Issue.8
, pp. 6337-6348
-
-
Fu, X.1
Zhang, H.2
Zhang, X.3
Cao, Y.4
Jiao, W.5
Liu, C.6
Song, Y.7
Abulimiti, A.8
Chang, Z.9
-
31
-
-
0030826325
-
Structure-function studies on small heat shock protein oligomeric assembly and interaction with unfolded polypeptides
-
Leroux, M. R., Melki, R., Gordon, B., Batelier, G., and Candido, E. P. (1997) Structure-function studies on small heat shock protein oligomeric assembly and interaction with unfolded polypeptides. J. Biol. Chem. 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
-
32
-
-
1642524277
-
Analysis of the regulation of the molecular chaperone Hsp26 by temperature-induced dissociation: The N-terminal domain is important for oligomer assembly and the binding of unfolding proteins
-
DOI 10.1074/jbc.M310149200
-
Stromer, T., Fischer, E., Richter, K., Haslbeck, M., and Buchner, J. (2004) Analysis of the regulation of the molecular chaperone Hsp26 by temperature-induced dissociation. The N-terminal domail is important for oligomer assembly and the binding of unfolding proteins. J. Biol. Chem. 279, 11222-11228 (Pubitemid 38401617)
-
(2004)
Journal of Biological Chemistry
, vol.279
, Issue.12
, pp. 11222-11228
-
-
Stromer, T.1
Fischer, E.2
Richter, K.3
Haslbeck, M.4
Buchner, J.5
-
33
-
-
0035191639
-
Crystal structure and assembly of a eukaryotic small heat shock protein
-
DOI 10.1038/nsb722
-
van Montfort, R. L., Basha, E., Friedrich, K. L., Slingsby, C., and Vierling, E. (2001) Crystal structure and assembly of a eukaryotic small heat shock protein. Nat. Struct. Biol. 8, 1025-1030 (Pubitemid 33101621)
-
(2001)
Nature Structural Biology
, vol.8
, Issue.12
, pp. 1025-1030
-
-
Van Montfort, R.L.M.1
Basha, E.2
Friedrich, K.L.3
Slingsby, C.4
Vierling, E.5
-
34
-
-
32144432437
-
The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling
-
DOI 10.1093/bioinformatics/bti770
-
Arnold, K., Bordoli, L., Kopp, J., and Schwede, T. (2006) The SWISS-MODEL workspace. A web-based environment for protein structure homology modelling. Bioinformatics 22, 195-201 (Pubitemid 43205406)
-
(2006)
Bioinformatics
, vol.22
, Issue.2
, pp. 195-201
-
-
Arnold, K.1
Bordoli, L.2
Kopp, J.3
Schwede, T.4
-
35
-
-
46249092554
-
GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
-
Hess, B., Kutzner, C., van der Spoel, D., and Lindahl, E. (2008) GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation. J. Chem. Theory Comput. 4, 435-447
-
(2008)
J. Chem. Theory Comput.
, vol.4
, pp. 435-447
-
-
Hess, B.1
Kutzner, C.2
Van Der Spoel, D.3
Lindahl, E.4
-
36
-
-
0029878720
-
VMD: Visual molecular dynamics
-
DOI 10.1016/0263-7855(96)00018-5
-
Humphrey, W., Dalke, A., and Schulten, K. (1996) VMD: visual molecular dynamics. J. Mol. Graphics 14, 33-38 (Pubitemid 26152973)
-
(1996)
Journal of Molecular Graphics
, vol.14
, Issue.1
, pp. 33-38
-
-
Humphrey, W.1
Dalke, A.2
Schulten, K.3
|