-
1
-
-
1242283848
-
Protein binding and disruption by Clp/Hsp100 chaperones
-
Maurizi M.R., and Xia D. Protein binding and disruption by Clp/Hsp100 chaperones. Structure 12 (2004) 175-183
-
(2004)
Structure
, vol.12
, pp. 175-183
-
-
Maurizi, M.R.1
Xia, D.2
-
2
-
-
5344269437
-
Sculpting the proteome with AAA(+) proteases and disassembly machines
-
Sauer R.T., et al. Sculpting the proteome with AAA(+) proteases and disassembly machines. Cell 119 (2004) 9-18
-
(2004)
Cell
, vol.119
, pp. 9-18
-
-
Sauer, R.T.1
-
3
-
-
39449097830
-
Common and specific mechanisms of AAA+ proteins involved in protein quality control
-
Mogk A., Haslberger T., Tessarz P., and Bukau B. Common and specific mechanisms of AAA+ proteins involved in protein quality control. Biochem. Soc. Trans. 36 (2008) 120-125
-
(2008)
Biochem. Soc. Trans.
, vol.36
, pp. 120-125
-
-
Mogk, A.1
Haslberger, T.2
Tessarz, P.3
Bukau, B.4
-
4
-
-
0032503968
-
Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins
-
Glover J.R., and Lindquist S. Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 94 (1998) 73-82
-
(1998)
Cell
, vol.94
, pp. 73-82
-
-
Glover, J.R.1
Lindquist, S.2
-
5
-
-
0033598703
-
Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network
-
Goloubinoff P., Mogk A., Zvi A.P., Tomoyasu T., and Bukau B. Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network. Proc. Natl. Acad. Sci. USA 96 (1999) 13732-13737
-
(1999)
Proc. Natl. Acad. Sci. USA
, vol.96
, pp. 13732-13737
-
-
Goloubinoff, P.1
Mogk, A.2
Zvi, A.P.3
Tomoyasu, T.4
Bukau, B.5
-
6
-
-
0033594880
-
Heat-inactivated proteins are rescued by the DnaK. J-GrpE set and ClpB chaperones
-
Motohashi K., Watanabe Y., Yohda M., and Yoshida M. Heat-inactivated proteins are rescued by the DnaK. J-GrpE set and ClpB chaperones. Proc. Natl. Acad. Sci. USA 96 (1999) 7184-7189
-
(1999)
Proc. Natl. Acad. Sci. USA
, vol.96
, pp. 7184-7189
-
-
Motohashi, K.1
Watanabe, Y.2
Yohda, M.3
Yoshida, M.4
-
7
-
-
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 (1999) 28083-28086
-
(1999)
J. Biol. Chem.
, vol.274
, pp. 28083-28086
-
-
Zolkiewski, M.1
-
9
-
-
0037033053
-
The N terminus of ClpB from Thermus thermophilus is not essential for the chaperone activity
-
Beinker P., Schlee S., Groemping Y., Seidel R., and Reinstein J. The N terminus of ClpB from Thermus thermophilus is not essential for the chaperone activity. J. Biol. Chem. 277 (2002) 47160-47166
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 47160-47166
-
-
Beinker, P.1
Schlee, S.2
Groemping, Y.3
Seidel, R.4
Reinstein, J.5
-
10
-
-
27144456262
-
The amino-terminal domain of ClpB supports binding to strongly aggregated proteins
-
Barnett M.E., Nagy M., Kedzierska S., and Zolkiewski M. The amino-terminal domain of ClpB supports binding to strongly aggregated proteins. J. Biol. Chem. 280 (2005) 34940-34945
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 34940-34945
-
-
Barnett, M.E.1
Nagy, M.2
Kedzierska, S.3
Zolkiewski, M.4
-
11
-
-
0034529228
-
Structure and activity of ClpB from Escherichia coli. Role of the amino-and -carboxyl-terminal domains
-
Barnett M.E., Zolkiewska A., and Zolkiewski M. Structure and activity of ClpB from Escherichia coli. Role of the amino-and -carboxyl-terminal domains. J. Biol. Chem. 275 (2000) 37565-37571
-
(2000)
J. Biol. Chem.
, vol.275
, pp. 37565-37571
-
-
Barnett, M.E.1
Zolkiewska, A.2
Zolkiewski, M.3
-
12
-
-
0037705402
-
Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP hydrolysis, and chaperone activity
-
Mogk A., Schlieker C., Strub C., Rist W., Weibezahn J., and Bukau B. Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP hydrolysis, and chaperone activity. J. Biol. Chem. 278 (2003) 17615-17624
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 17615-17624
-
-
Mogk, A.1
Schlieker, C.2
Strub, C.3
Rist, W.4
Weibezahn, J.5
Bukau, B.6
-
13
-
-
0344629876
-
Structure and function of the middle domain of ClpB from Escherichia coli
-
Kedzierska S., Akoev V., Barnett M.E., and Zolkiewski M. Structure and function of the middle domain of ClpB from Escherichia coli. Biochemistry 42 (2003) 14242-14248
-
(2003)
Biochemistry
, vol.42
, pp. 14242-14248
-
-
Kedzierska, S.1
Akoev, V.2
Barnett, M.E.3
Zolkiewski, M.4
-
14
-
-
2342485076
-
Dominant gain-of-function mutations in Hsp104p reveal crucial roles for the middle region
-
Schirmer E.C., Homann O.R., Kowal A.S., and Lindquist S. Dominant gain-of-function mutations in Hsp104p reveal crucial roles for the middle region. Mol. Biol. Cell 15 (2004) 2061-2072
-
(2004)
Mol. Biol. Cell
, vol.15
, pp. 2061-2072
-
-
Schirmer, E.C.1
Homann, O.R.2
Kowal, A.S.3
Lindquist, S.4
-
15
-
-
26844581179
-
Genetic analysis reveals domain interactions of Arabidopsis Hsp100/ClpB and cooperation with the small heat shock protein chaperone system
-
Lee U., Wie C., Escobar M., Williams B., Hong S.W., and Vierling E. Genetic analysis reveals domain interactions of Arabidopsis Hsp100/ClpB and cooperation with the small heat shock protein chaperone system. Plant Cell 17 (2005) 559-571
-
(2005)
Plant Cell
, vol.17
, pp. 559-571
-
-
Lee, U.1
Wie, C.2
Escobar, M.3
Williams, B.4
Hong, S.W.5
Vierling, E.6
-
16
-
-
41149169488
-
Coupling and dynamics of subunits in the hexameric AAA+ chaperone ClpB
-
Werbeck N.D., Schlee S., and Reinstein J. Coupling and dynamics of subunits in the hexameric AAA+ chaperone ClpB. J. Mol. Biol. 378 (2008) 178-190
-
(2008)
J. Mol. Biol.
, vol.378
, pp. 178-190
-
-
Werbeck, N.D.1
Schlee, S.2
Reinstein, J.3
-
17
-
-
44849138934
-
Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments
-
Haslberger T., Zdanowicz A., Brand I., Kirstein J., Turgay K., Mogk A., and Bukau B. Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments. Nat. Struct. Mol. Biol. 15 (2008) 641-650
-
(2008)
Nat. Struct. Mol. Biol.
, vol.15
, pp. 641-650
-
-
Haslberger, T.1
Zdanowicz, A.2
Brand, I.3
Kirstein, J.4
Turgay, K.5
Mogk, A.6
Bukau, B.7
-
18
-
-
76049127471
-
Coupling ATP utilization to protein remodeling by ClpB, a hexameric AAA+ protein
-
pnas.org/cgi/doi/10.1073/pnas.0911937106
-
Hoskins J.R., Doyle S.M., and Wickner S. Coupling ATP utilization to protein remodeling by ClpB, a hexameric AAA+ protein. Proc. Natl. Acad. Sci. USA (2009) pnas.org/cgi/doi/10.1073/pnas.0911937106
-
(2009)
Proc. Natl. Acad. Sci. USA
-
-
Hoskins, J.R.1
Doyle, S.M.2
Wickner, S.3
-
19
-
-
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. The heat-shock protein ClpB in Escherichia coli is a protein-activated ATPase. J. Biol. Chem. 267 (1992) 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
-
20
-
-
0037413822
-
Interdomain interaction through helices A and B of DnaK peptide binding domain
-
Moro F., Fernandez V., and Muga A. Interdomain interaction through helices A and B of DnaK peptide binding domain. FEBS Lett. 533 (2003) 119-123
-
(2003)
FEBS Lett.
, vol.533
, pp. 119-123
-
-
Moro, F.1
Fernandez, V.2
Muga, A.3
-
21
-
-
0021880465
-
Purification and properties of the dnaJ replication protein of Escherichia coli
-
Zylicz M., Yamamoto T., McKittrick N., Sell S., and Georgopoulos C. Purification and properties of the dnaJ replication protein of Escherichia coli. J. Biol. Chem. 260 (1985) 7591-7598
-
(1985)
J. Biol. Chem.
, vol.260
, pp. 7591-7598
-
-
Zylicz, M.1
Yamamoto, T.2
McKittrick, N.3
Sell, S.4
Georgopoulos, C.5
-
22
-
-
0034816295
-
A GrpE mutant containing the NH(2)-terminal "tail" region is able to displace bound polypeptide substrate from DnaK
-
Mehl A.F., Heskett L.D., and Neal K.M. A GrpE mutant containing the NH(2)-terminal "tail" region is able to displace bound polypeptide substrate from DnaK. Biochem. Biophys. Res. Commun. 282 (2001) 562-569
-
(2001)
Biochem. Biophys. Res. Commun.
, vol.282
, pp. 562-569
-
-
Mehl, A.F.1
Heskett, L.D.2
Neal, K.M.3
-
23
-
-
0028914392
-
Modulation of the ATPase activity of the molecular chaperone DnaK by peptides and the DnaJ and GrpE heat shock proteins
-
Jordan R., and McMacken R. Modulation of the ATPase activity of the molecular chaperone DnaK by peptides and the DnaJ and GrpE heat shock proteins. J. Biol. Chem. 270 (1995) 4563-4569
-
(1995)
J. Biol. Chem.
, vol.270
, pp. 4563-4569
-
-
Jordan, R.1
McMacken, R.2
-
24
-
-
0023809599
-
Coupled assay of Na+, K+-ATPase activity
-
Norby J.G. Coupled assay of Na+, K+-ATPase activity. Methods Enzymol. 156 (1988) 116-119
-
(1988)
Methods Enzymol.
, vol.156
, pp. 116-119
-
-
Norby, J.G.1
-
25
-
-
10044275315
-
Solubilization of aggregated proteins by ClpB/DnaK relies on the continuous extraction of unfolded polypeptides
-
Schlieker C., Tews I., Bukau B., and Mogk A. Solubilization of aggregated proteins by ClpB/DnaK relies on the continuous extraction of unfolded polypeptides. FEBS Lett. 578 (2004) 351-356
-
(2004)
FEBS Lett.
, vol.578
, pp. 351-356
-
-
Schlieker, C.1
Tews, I.2
Bukau, B.3
Mogk, A.4
-
26
-
-
0035815699
-
Synchronized domain-opening motion of GroEL is essential for communication between the two rings
-
Shiseki K., Murai N., Motojima F., Hisabori T., Yoshida M., and Taguchi H. Synchronized domain-opening motion of GroEL is essential for communication between the two rings. J. Biol. Chem. 276 (2001) 11335-11338
-
(2001)
J. Biol. Chem.
, vol.276
, pp. 11335-11338
-
-
Shiseki, K.1
Murai, N.2
Motojima, F.3
Hisabori, T.4
Yoshida, M.5
Taguchi, H.6
-
27
-
-
0037072810
-
Salt bridges at the inter-ring interface regulate the thermostat of GroEL
-
Sot B., Galan A., Valpuesta J.M., Bertrand S., and Muga A. Salt bridges at the inter-ring interface regulate the thermostat of GroEL. J. Biol. Chem. 277 (2002) 34024-34029
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 34024-34029
-
-
Sot, B.1
Galan, A.2
Valpuesta, J.M.3
Bertrand, S.4
Muga, A.5
-
28
-
-
0042858475
-
Characterization of a trap mutant of the AAA+ chaperone ClpB
-
Weibezahn J., Schlieker C., Bukau B., and Mogk A. Characterization of a trap mutant of the AAA+ chaperone ClpB. J. Biol. Chem. 278 (2003) 32608-32617
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 32608-32617
-
-
Weibezahn, J.1
Schlieker, C.2
Bukau, B.3
Mogk, A.4
-
29
-
-
21244482459
-
Asymmetric interactions of ATP with the AAA+ ClpX6 unfoldase: allosteric control of a protein machine
-
Hersch G.L., Burton R.E., Bolon D.N., Baker T.A., and Sauer R.T. Asymmetric interactions of ATP with the AAA+ ClpX6 unfoldase: allosteric control of a protein machine. Cell 121 (2005) 1017-1027
-
(2005)
Cell
, vol.121
, pp. 1017-1027
-
-
Hersch, G.L.1
Burton, R.E.2
Bolon, D.N.3
Baker, T.A.4
Sauer, R.T.5
-
30
-
-
45849107940
-
Asymmetric nucleotide transactions of the HslUV protease
-
Yakamavich J.A., Baker T.A., and Sauer R.T. Asymmetric nucleotide transactions of the HslUV protease. J. Mol. Biol. 380 (2008) 946-957
-
(2008)
J. Mol. Biol.
, vol.380
, pp. 946-957
-
-
Yakamavich, J.A.1
Baker, T.A.2
Sauer, R.T.3
-
31
-
-
70350772363
-
Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine
-
Glynn S.E., Martin A., Nager A.R., Baker T.A., and Sauer R.T. Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine. Cell 139 (2009) 744-756
-
(2009)
Cell
, vol.139
, pp. 744-756
-
-
Glynn, S.E.1
Martin, A.2
Nager, A.R.3
Baker, T.A.4
Sauer, R.T.5
|