-
1
-
-
77958487260
-
Cellular strategies for controlling protein aggregation
-
Tyedmers, J., Mogk, A. & Bukau, B. Cellular strategies for controlling protein aggregation. Nat. Rev. Mol. Cell Biol. 11, 777-788 (2010).
-
(2010)
Nat. Rev. Mol. Cell Biol.
, vol.11
, pp. 777-788
-
-
Tyedmers, J.1
Mogk, A.2
Bukau, B.3
-
2
-
-
0032503968
-
Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins
-
Glover, J.R. & Lindquist, S. Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 94, 73-82 (1998).
-
(1998)
Cell
, vol.94
, pp. 73-82
-
-
Glover, J.R.1
Lindquist, S.2
-
3
-
-
0033598703
-
Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network
-
Goloubinoff, P., Mogk, A., Peres Ben Zvi, A., Tomoyasu, T. & Bukau, B. Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network. Proc. Natl. Acad. Sci. USA 96, 13732-13737 (1999).
-
(1999)
Proc. Natl. Acad. Sci. USA
, vol.96
, pp. 13732-13737
-
-
Goloubinoff, P.1
Mogk, A.2
Peres Ben Zvi, A.3
Tomoyasu, T.4
Bukau, B.5
-
4
-
-
0033214052
-
ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi-chaperone system from Escherichia coli
-
Zolkiewski, M. ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi-chaperone system from Escherichia coli. J. Biol. Chem. 274, 28083-28086 (1999).
-
(1999)
J. Biol. Chem.
, vol.274
, pp. 28083-28086
-
-
Zolkiewski, M.1
-
5
-
-
0033594880
-
Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperones
-
Motohashi, K., Watanabe, Y., Yohda, M. & Yoshida, M. Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperones. Proc. Natl. Acad. Sci. USA 96, 7184-7189 (1999).
-
(1999)
Proc. Natl. Acad. Sci. USA
, vol.96
, pp. 7184-7189
-
-
Motohashi, K.1
Watanabe, Y.2
Yohda, M.3
Yoshida, M.4
-
6
-
-
0034636040
-
Mutants of Arabidopsis thaliana defective in the acquisition of tolerance to high temperature stress
-
Hong, S.W. & Vierling, E. Mutants of Arabidopsis thaliana defective in the acquisition of tolerance to high temperature stress. Proc. Natl. Acad. Sci. USA 97, 4392-4397 (2000).
-
(2000)
Proc. Natl. Acad. Sci. USA
, vol.97
, pp. 4392-4397
-
-
Hong, S.W.1
Vierling, E.2
-
7
-
-
0034119621
-
Heat shock protein 101 plays a crucial role in thermotolerance in Arabidopsis
-
Queitsch, C., Hong, S.W., Vierling, E. & Lindquist, S. Heat shock protein 101 plays a crucial role in thermotolerance in Arabidopsis. Plant Cell 12, 479-492 (2000).
-
(2000)
Plant Cell
, vol.12
, pp. 479-492
-
-
Queitsch, C.1
Hong, S.W.2
Vierling, E.3
Lindquist, S.4
-
8
-
-
0025193343
-
HSP104 required for induced thermotolerance
-
Sanchez, Y. & Lindquist, S.L. HSP104 required for induced thermotolerance. Science 248, 1112-1115 (1990).
-
(1990)
Science
, vol.248
, pp. 1112-1115
-
-
Sanchez, Y.1
Lindquist, S.L.2
-
9
-
-
0025799542
-
ClpB is the Escherichia coli heat shock protein F84
-
Squires, C.L., Pedersen, S., Ross, B.M. & Squires, C. ClpB is the Escherichia coli heat shock protein F84. J. Bacteriol. 173, 4254-4262 (1991).
-
(1991)
J. Bacteriol.
, vol.173
, pp. 4254-4262
-
-
Squires, C.L.1
Pedersen, S.2
Ross, B.M.3
Squires, C.4
-
10
-
-
3142657524
-
Evidence for an unfolding/threading mechanism for protein disaggregation by Saccharomyces cerevisiae Hsp104
-
Lum, R., Tkach, J.M., Vierling, E. & Glover, J.R. Evidence for an unfolding/threading mechanism for protein disaggregation by Saccharomyces cerevisiae Hsp104. J. Biol. Chem. 279, 29139-29146 (2004).
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 29139-29146
-
-
Lum, R.1
Tkach, J.M.2
Vierling, E.3
Glover, J.R.4
-
11
-
-
8844251486
-
Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB
-
Weibezahn, J. et al. Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB. Cell 119, 653-665 (2004).
-
(2004)
Cell
, vol.119
, pp. 653-665
-
-
Weibezahn, J.1
-
12
-
-
0142227208
-
The structure of ClpB. A molecular chaperone that rescues proteins from an aggregated state
-
Lee, S. et al. The structure of ClpB. A molecular chaperone that rescues proteins from an aggregated state. Cell 115, 229-240 (2003).
-
(2003)
Cell
, vol.115
, pp. 229-240
-
-
Lee, S.1
-
13
-
-
0037705402
-
Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP-hydrolysis and chaperone activity
-
Mogk, A. et al. Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP-hydrolysis and chaperone activity. J. Biol. Chem. 278, 17615-17624 (2003).
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 17615-17624
-
-
Mogk, A.1
-
14
-
-
0344629876
-
Structure and function of the middle domain of ClpB from Escherichia coli
-
Kedzierska, S., Akoev, V., Barnett, M.E. & Zolkiewski, M. Structure and function of the middle domain of ClpB from Escherichia coli. Biochemistry 42, 14242-14248 (2003).
-
(2003)
Biochemistry
, vol.42
, pp. 14242-14248
-
-
Kedzierska, S.1
Akoev, V.2
Barnett, M.E.3
Zolkiewski, M.4
-
15
-
-
77956178634
-
The M-domain controls Hsp104 protein remodeling activity in an Hsp70/Hsp40-dependent manner
-
Sielaff, B. & Tsai, F.T. The M-domain controls Hsp104 protein remodeling activity in an Hsp70/Hsp40-dependent manner. J. Mol. Biol. 402, 30-37 (2010).
-
(2010)
J. Mol. Biol.
, vol.402
, pp. 30-37
-
-
Sielaff, B.1
Tsai, F.T.2
-
16
-
-
79955563304
-
Species-specific collaboration of heat shock proteins (Hsp) 70 and 100 in thermotolerance and protein disaggregation
-
Miot, M. et al. Species-specific collaboration of heat shock proteins (Hsp) 70 and 100 in thermotolerance and protein disaggregation. Proc. Natl. Acad. Sci. USA 108, 6915-6920 (2011).
-
(2011)
Proc. Natl. Acad. Sci. USA
, vol.108
, pp. 6915-6920
-
-
Miot, M.1
-
17
-
-
33846231395
-
M domains couple the ClpB threading motor with the DnaK chaperone activity
-
Haslberger, T. et al. M domains couple the ClpB threading motor with the DnaK chaperone activity. Mol. Cell 25, 247-260 (2007).
-
(2007)
Mol. Cell
, vol.25
, pp. 247-260
-
-
Haslberger, T.1
-
18
-
-
33846188909
-
Visualizing the ATPase cycle in a protein disaggregating machine: Structural basis for substrate binding by ClpB
-
Lee, S., Choi, J.M. & Tsai, F.T. Visualizing the ATPase cycle in a protein disaggregating machine: structural basis for substrate binding by ClpB. Mol. Cell 25, 261-271 (2007).
-
(2007)
Mol. Cell
, vol.25
, pp. 261-271
-
-
Lee, S.1
Choi, J.M.2
Tsai, F.T.3
-
19
-
-
37449008520
-
Atypical AAA+ subunit packing creates an expanded cavity for disaggregation by the protein-remodeling factor Hsp104
-
Wendler, P. et al. Atypical AAA+ subunit packing creates an expanded cavity for disaggregation by the protein-remodeling factor Hsp104. Cell 131, 1366-1377 (2007).
-
(2007)
Cell
, vol.131
, pp. 1366-1377
-
-
Wendler, P.1
-
20
-
-
77952353727
-
CryoEM structure of Hsp104 and its mechanistic implication for protein disaggregation
-
Lee, S., Sielaff, B., Lee, J. & Tsai, F.T. CryoEM structure of Hsp104 and its mechanistic implication for protein disaggregation. Proc. Natl. Acad. Sci. USA 107, 8135-8140 (2010).
-
(2010)
Proc. Natl. Acad. Sci. USA
, vol.107
, pp. 8135-8140
-
-
Lee, S.1
Sielaff, B.2
Lee, J.3
Tsai, F.T.4
-
21
-
-
33644761306
-
Hydrogen exchange mass spectrometry for the analysis of protein dynamics
-
Wales, T.E. & Engen, J.R. Hydrogen exchange mass spectrometry for the analysis of protein dynamics. Mass Spectrom. Rev. 25, 158-170 (2006).
-
(2006)
Mass Spectrom. Rev.
, vol.25
, pp. 158-170
-
-
Wales, T.E.1
Engen, J.R.2
-
22
-
-
0035793721
-
The chaperone function of ClpB from Thermus thermophilus depends on allosteric interactions of its two ATP-binding sites
-
Schlee, S., Groemping, Y., Herde, P., Seidel, R. & Reinstein, J. The chaperone function of ClpB from Thermus thermophilus depends on allosteric interactions of its two ATP-binding sites. J. Mol. Biol. 306, 889-899 (2001).
-
(2001)
J. Mol. Biol.
, vol.306
, pp. 889-899
-
-
Schlee, S.1
Groemping, Y.2
Herde, P.3
Seidel, R.4
Reinstein, J.5
-
23
-
-
0034634334
-
Heptameric ring structure of the heat-shock protein ClpB, a protein-activated ATPase in Escherichia coli
-
Kim, K.I. et al. Heptameric ring structure of the heat-shock protein ClpB, a protein-activated ATPase in Escherichia coli. J. Mol. Biol. 303, 655-666 (2000).
-
(2000)
J. Mol. Biol.
, vol.303
, pp. 655-666
-
-
Kim, K.I.1
-
24
-
-
1342268093
-
Nucleotide-induced switch in oligomerization of the AAA+ ATPase ClpB
-
Akoev, V., Gogol, E.P., Barnett, M.E. & Zolkiewski, M. Nucleotide-induced switch in oligomerization of the AAA+ ATPase ClpB. Protein Sci. 13, 567-574 (2004).
-
(2004)
Protein Sci.
, vol.13
, pp. 567-574
-
-
Akoev, V.1
Gogol, E.P.2
Barnett, M.E.3
Zolkiewski, M.4
-
25
-
-
76749107015
-
Nucleotide utilization requirements that render ClpB active as a chaperone
-
del Castillo, U., Fernandez-Higuero, J.A., Perez-Acebron, S., Moro, F. & Muga, A. Nucleotide utilization requirements that render ClpB active as a chaperone. FEBS Lett. 584, 929-934 (2010).
-
(2010)
FEBS Lett.
, vol.584
, pp. 929-934
-
-
Del Castillo, U.1
Fernandez-Higuero, J.A.2
Perez-Acebron, S.3
Moro, F.4
Muga, A.5
-
26
-
-
73649102024
-
Conformational stability of the full-atom hexameric model of the ClpB chaperone from Escherichia coli
-
Zietkiewicz, S., Slusarz, M.J., Slusarz, R., Liberek, K. & Rodziewicz-Motowidlo, S. Conformational stability of the full-atom hexameric model of the ClpB chaperone from Escherichia coli. Biopolymers 93, 47-60 (2010).
-
(2010)
Biopolymers
, vol.93
, pp. 47-60
-
-
Zietkiewicz, S.1
Slusarz, M.J.2
Slusarz, R.3
Liberek, K.4
Rodziewicz-Motowidlo, S.5
-
27
-
-
44849138934
-
Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments
-
Haslberger, T. et al. Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments. Nat. Struct. Mol. Biol. 15, 641-650 (2008).
-
(2008)
Nat. Struct. Mol. Biol.
, vol.15
, pp. 641-650
-
-
Haslberger, T.1
-
28
-
-
33846941900
-
Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activity
-
Doyle, S.M. et al. Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activity. Nat. Struct. Mol. Biol. 14, 114-122 (2007).
-
(2007)
Nat. Struct. Mol. Biol.
, vol.14
, pp. 114-122
-
-
Doyle, S.M.1
-
29
-
-
84866438776
-
Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation
-
Winkler, J., Tyedmers, J., Bukau, B. & Mogk, A. Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation. J. Cell Biol. 198, 387-404 (2012).
-
(2012)
J. Cell Biol.
, vol.198
, pp. 387-404
-
-
Winkler, J.1
Tyedmers, J.2
Bukau, B.3
Mogk, A.4
-
30
-
-
54849425578
-
An intrinsic degradation tag on the ClpA C-terminus regulates the balance of ClpAP complexes with different substrate specificity
-
Maglica, Z., Striebel, F. & Weber-Ban, E. An intrinsic degradation tag on the ClpA C-terminus regulates the balance of ClpAP complexes with different substrate specificity. J. Mol. Biol. 384, 503-511 (2008).
-
(2008)
J. Mol. Biol.
, vol.384
, pp. 503-511
-
-
Maglica, Z.1
Striebel, F.2
Weber-Ban, E.3
-
31
-
-
0037418224
-
MecA an adaptor protein necessary for ClpC chaperone activity
-
Schlothauer, T., Mogk, A., Dougan, D.A., Bukau, B. & Turgay, K. MecA, an adaptor protein necessary for ClpC chaperone activity. Proc. Natl. Acad. Sci. USA 100, 2306-2311 (2003).
-
(2003)
Proc. Natl. Acad. Sci. USA
, vol.100
, pp. 2306-2311
-
-
Schlothauer, T.1
Mogk, A.2
Dougan, D.A.3
Bukau, B.4
Turgay, K.5
-
32
-
-
27144474906
-
Rebuilt AAA+ motors reveal operating principles for ATP-fuelled machines
-
Martin, A., Baker, T.A. & Sauer, R.T. Rebuilt AAA+ motors reveal operating principles for ATP-fuelled machines. Nature 437, 1115-1120 (2005).
-
(2005)
Nature
, vol.437
, pp. 1115-1120
-
-
Martin, A.1
Baker, T.A.2
Sauer, R.T.3
-
33
-
-
84870792675
-
Hsp70 proteins bind Hsp100 regulatory M domains to activate AAA+ disaggregase at aggregate surfaces
-
advance online publication doi:10.1038/nsmb.2442 18 November
-
Seyffer, F. et al. Hsp70 proteins bind Hsp100 regulatory M domains to activate AAA+ disaggregase at aggregate surfaces. Nat. Struct. Mol. Biol. advance online publication, doi:10.1038/nsmb.2442 (18 November 2012).
-
(2012)
Nat. Struct. Mol. Biol.
-
-
Seyffer, F.1
-
34
-
-
79952906659
-
A quantitative analysis of the effect of nucleotides and the M domain on the association equilibrium of ClpB
-
del Castillo, U. et al. A quantitative analysis of the effect of nucleotides and the M domain on the association equilibrium of ClpB. Biochemistry 50, 1991-2003 (2011).
-
(2011)
Biochemistry
, vol.50
, pp. 1991-2003
-
-
Del Castillo, U.1
-
35
-
-
79959389010
-
AAA+ proteases: ATP-fueled machines of protein destruction
-
Sauer, R.T. & Baker, T.A. AAA+ proteases: ATP-fueled machines of protein destruction. Annu. Rev. Biochem. 80, 587-612 (2011).
-
(2011)
Annu. Rev. Biochem.
, vol.80
, pp. 587-612
-
-
Sauer, R.T.1
Baker, T.A.2
-
36
-
-
2342485076
-
Dominant gain-of-function mutations in Hsp104p reveal crucial roles for the middle region
-
Schirmer, E.C., Homann, O.R., Kowal, A.S. & Lindquist, S. Dominant gain-of-function mutations in Hsp104p reveal crucial roles for the middle region. Mol. Biol. Cell 15, 2061-2072 (2004).
-
(2004)
Mol. Biol. Cell
, vol.15
, pp. 2061-2072
-
-
Schirmer, E.C.1
Homann, O.R.2
Kowal, A.S.3
Lindquist, S.4
-
37
-
-
26844581179
-
Genetic analysis reveals domain interactions of Arabidopsis Hsp100/ClpB and cooperation with the small heat shock protein chaperone system
-
Lee, U. et al. Genetic analysis reveals domain interactions of Arabidopsis Hsp100/ClpB and cooperation with the small heat shock protein chaperone system. Plant Cell 17, 559-571 (2005).
-
(2005)
Plant Cell
, vol.17
, pp. 559-571
-
-
Lee, U.1
-
38
-
-
0345803934
-
Mapping temperature-induced conformational changes in the Escherichia coli heat shock transcription factor sigma 32 by amide hydrogen exchange
-
Rist, W., Jorgensen, T.J., Roepstorff, P., Bukau, B. & Mayer, M.P. Mapping temperature-induced conformational changes in the Escherichia coli heat shock transcription factor sigma 32 by amide hydrogen exchange. J. Biol. Chem. 278, 51415-51421 (2003).
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 51415-51421
-
-
Rist, W.1
Jorgensen, T.J.2
Roepstorff, P.3
Bukau, B.4
Mayer, M.P.5
-
39
-
-
0032010153
-
A universal algorithm for fast and automated charge state deconvolution of electrospray mass-to-charge ratio spectra
-
Zhang, Z. & Marshall, A.G. A universal algorithm for fast and automated charge state deconvolution of electrospray mass-to-charge ratio spectra. J. Am. Soc. Mass Spectrom. 9, 225-233 (1998).
-
(1998)
J. Am. Soc. Mass Spectrom.
, vol.9
, pp. 225-233
-
-
Zhang, Z.1
Marshall, A.G.2
-
40
-
-
0027136282
-
Comparative protein modelling by satisfaction of spatial restraints
-
Sali, A. & Blundell, T.L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234, 779-815 (1993).
-
(1993)
J. Mol. Biol.
, vol.234
, pp. 779-815
-
-
Sali, A.1
Blundell, T.L.2
-
41
-
-
0000243829
-
PROCHECK: A program to check the stereochemical quality of protein structures
-
Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291 (1993).
-
(1993)
J. Appl. Crystallogr.
, vol.26
, pp. 283-291
-
-
Laskowski, R.A.1
MacArthur, M.W.2
Moss, D.S.3
Thornton, J.M.4
-
42
-
-
46249092554
-
GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
-
Hess, B., Kutzner, C., van der Spoel, D. & Lindahl, E. GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation. J. Chem. Theory Comput. 4, 435-447 (2008).
-
(2008)
J. Chem. Theory Comput.
, vol.4
, pp. 435-447
-
-
Hess, B.1
Kutzner, C.2
Van Der Spoel, D.3
Lindahl, E.4
-
43
-
-
0242593434
-
Development and current status of the CHARMM force field for nucleic acids
-
MacKerell, A.D., Banavali, N. & Foloppe, N. Development and current status of the CHARMM force field for nucleic acids. Biopolymers 56, 257-265 (2001).
-
(2001)
Biopolymers
, vol.56
, pp. 257-265
-
-
MacKerell, A.D.1
Banavali, N.2
Foloppe, N.3
-
44
-
-
1842479952
-
Exploring protein native states and large-scale conformational changes with a modified generalized born model
-
Onufriev, A., Bashford, D. & Case, D.A. Exploring protein native states and large-scale conformational changes with a modified generalized born model. Proteins 55, 383-394 (2004).
-
(2004)
Proteins
, vol.55
, pp. 383-394
-
-
Onufriev, A.1
Bashford, D.2
Case, D.A.3
-
45
-
-
49449113010
-
The MARTINI coarse grained forcefield: Extension to proteins
-
Monticelli, L. et al. The MARTINI coarse grained forcefield: extension to proteins. J. Chem. Theory Comput. 4, 819-834 (2008).
-
(2008)
J. Chem. Theory Comput.
, vol.4
, pp. 819-834
-
-
Monticelli, L.1
-
46
-
-
73349084983
-
Combining an elastic network with a coarse-grained molecular force field: Structure, dynamics and intermolecular recognition
-
Periole, X., Cavalli, M., Marrink, S.J. & Ceruso, M. Combining an elastic network with a coarse-grained molecular force field: structure, dynamics and intermolecular recognition. J. Chem. Theory Comput. 5, 2531-2543 (2009).
-
(2009)
J. Chem. Theory Comput.
, vol.5
, pp. 2531-2543
-
-
Periole, X.1
Cavalli, M.2
Marrink, S.J.3
Ceruso, M.4
-
47
-
-
33747858757
-
NOMAD-Ref: Visualization, deformation and refinement of macromolecular structures based on all-atom normal mode analysis
-
Lindahl, E., Azuara, C., Koehl, P. & Delarue, M. NOMAD-Ref: visualization, deformation and refinement of macromolecular structures based on all-atom normal mode analysis. Nucleic Acids Res. 34, W52-W56 (2006).
-
(2006)
Nucleic Acids Res.
, vol.34
-
-
Lindahl, E.1
Azuara, C.2
Koehl, P.3
Delarue, M.4
-
48
-
-
0030870994
-
Conformational analysis of galanin using end to end distance distribution observed by Forster resonance energy transfer
-
Kulinski, T. et al. Conformational analysis of galanin using end to end distance distribution observed by Forster resonance energy transfer. Eur. Biophys. J. 26, 145-154 (1997).
-
(1997)
Eur. Biophys. J.
, vol.26
, pp. 145-154
-
-
Kulinski, T.1
|