-
1
-
-
33845922099
-
Functional analysis of CbpA, a DnaJ homolog and nucleoid-associated DNA-binding protein
-
Bird JG, Sharma S, Roshwalb SC, Hoskins JR, Wickner S. Functional analysis of CbpA, a DnaJ homolog and nucleoid-associated DNA-binding protein. J. Biol. Chem. 2006, 281:34349-34356.
-
(2006)
J. Biol. Chem.
, vol.281
, pp. 34349-34356
-
-
Bird, J.G.1
Sharma, S.2
Roshwalb, S.C.3
Hoskins, J.R.4
Wickner, S.5
-
2
-
-
0032489016
-
The Hsp70 and Hsp60 chaperone machines
-
Bukau B, Horwich AL. The Hsp70 and Hsp60 chaperone machines. Cell 1998, 92:351-366.
-
(1998)
Cell
, vol.92
, pp. 351-366
-
-
Bukau, B.1
Horwich, A.L.2
-
3
-
-
4043103993
-
CbpA, a DnaJ homolog, is a DnaK co-chaperone, and its activity is modulated by CbpM
-
Chae C, Sharma S, Hoskins JR, Wickner S. CbpA, a DnaJ homolog, is a DnaK co-chaperone, and its activity is modulated by CbpM. J. Biol. Chem. 2004, 279:33147-33153.
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 33147-33153
-
-
Chae, C.1
Sharma, S.2
Hoskins, J.R.3
Wickner, S.4
-
4
-
-
34247632202
-
In vivo modulation of a DnaJ homolog, CbpA, by CbpM
-
Chenoweth MR, Trun N, Wickner S. In vivo modulation of a DnaJ homolog, CbpA, by CbpM. J. Bacteriol. 2007, 189:3635-3638.
-
(2007)
J. Bacteriol.
, vol.189
, pp. 3635-3638
-
-
Chenoweth, M.R.1
Trun, N.2
Wickner, S.3
-
5
-
-
48149104997
-
Complex regulation of the DnaJ homolog CbpA by the global regulators sigmaS and Lrp, by the specific inhibitor CbpM, and by the proteolytic degradation of CbpM
-
Chenoweth MR, Wickner S. Complex regulation of the DnaJ homolog CbpA by the global regulators sigmaS and Lrp, by the specific inhibitor CbpM, and by the proteolytic degradation of CbpM. J. Bacteriol. 2008, 190:5153-5161.
-
(2008)
J. Bacteriol.
, vol.190
, pp. 5153-5161
-
-
Chenoweth, M.R.1
Wickner, S.2
-
6
-
-
0034647887
-
Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery
-
Diamant S, Ben-Zvi AP, Bukau B, Goloubinoff P. Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery. J. Biol. Chem. 2000, 275:21107-21113.
-
(2000)
J. Biol. Chem.
, vol.275
, pp. 21107-21113
-
-
Diamant, S.1
Ben-Zvi, A.P.2
Bukau, B.3
Goloubinoff, P.4
-
7
-
-
3042533581
-
DafA cycles between the DnaK chaperone system and translational machinery
-
Dumitru GL, Groemping Y, Klostermeier D, Restle T, Deuerling E, Reinstein J. DafA cycles between the DnaK chaperone system and translational machinery. J. Mol. Biol. 2004, 339:1179-1189.
-
(2004)
J. Mol. Biol.
, vol.339
, pp. 1179-1189
-
-
Dumitru, G.L.1
Groemping, Y.2
Klostermeier, D.3
Restle, T.4
Deuerling, E.5
Reinstein, J.6
-
8
-
-
0032503968
-
Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins
-
Glover JR, Lindquist S. Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 1998, 94:73-82.
-
(1998)
Cell
, vol.94
, pp. 73-82
-
-
Glover, J.R.1
Lindquist, S.2
-
9
-
-
0033598703
-
Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network
-
Goloubinoff P, Mogk A, Zvi AP, Tomoyasu T, Bukau B. Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network. Proc. Natl Acad. Sci. USA 1999, 96:13732-13737.
-
(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
-
10
-
-
0037805634
-
Thermosensor action of GrpE. The DnaK chaperone system at heat shock temperatures
-
Grimshaw JP, Jelesarov I, Siegenthaler RK, Christen P. Thermosensor action of GrpE. The DnaK chaperone system at heat shock temperatures. J. Biol. Chem. 2003, 278:19048-19053.
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 19048-19053
-
-
Grimshaw, J.P.1
Jelesarov, I.2
Siegenthaler, R.K.3
Christen, P.4
-
11
-
-
0035793209
-
Regulation of ATPase and chaperone cycle of DnaK from Thermus thermophilus by the nucleotide exchange factor GrpE
-
Groemping Y, Klostermeier D, Herrmann C, Veit T, Seidel R, Reinstein J. Regulation of ATPase and chaperone cycle of DnaK from Thermus thermophilus by the nucleotide exchange factor GrpE. J. Mol. Biol. 2001, 305:1173-1183.
-
(2001)
J. Mol. Biol.
, vol.305
, pp. 1173-1183
-
-
Groemping, Y.1
Klostermeier, D.2
Herrmann, C.3
Veit, T.4
Seidel, R.5
Reinstein, J.6
-
12
-
-
0035900534
-
Folding properties of the nucleotide exchange factor GrpE from Thermus thermophilus: GrpE is a thermosensor that mediates heat shock response
-
Groemping Y, Reinstein J. Folding properties of the nucleotide exchange factor GrpE from Thermus thermophilus: GrpE is a thermosensor that mediates heat shock response. J. Mol. Biol. 2001, 314:167-178.
-
(2001)
J. Mol. Biol.
, vol.314
, pp. 167-178
-
-
Groemping, Y.1
Reinstein, J.2
-
13
-
-
0033515528
-
The functional cycle and regulation of the Thermus thermophilus DnaK chaperone system
-
Klostermeier D, Seidel R, Reinstein J. The functional cycle and regulation of the Thermus thermophilus DnaK chaperone system. J. Mol. Biol. 1999, 287:511-525.
-
(1999)
J. Mol. Biol.
, vol.287
, pp. 511-525
-
-
Klostermeier, D.1
Seidel, R.2
Reinstein, J.3
-
14
-
-
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, 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
-
15
-
-
0033573135
-
Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB
-
Mogk A, Tomoyasu T, Goloubinoff P, Rudiger S, Roder D, Langen H, Bukau B. Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB. EMBO J. 1999, 18:6934-6949.
-
(1999)
EMBO J.
, vol.18
, pp. 6934-6949
-
-
Mogk, A.1
Tomoyasu, T.2
Goloubinoff, P.3
Rudiger, S.4
Roder, D.5
Langen, H.6
Bukau, B.7
-
16
-
-
0027984270
-
Isolation of the stable hexameric DnaK.DnaJ complex from Thermus thermophilus
-
Motohashi K, Taguchi H, Ishii N, Yoshida M. Isolation of the stable hexameric DnaK.DnaJ complex from Thermus thermophilus. J. Biol. Chem. 1994, 269:27074-27079.
-
(1994)
J. Biol. Chem.
, vol.269
, pp. 27074-27079
-
-
Motohashi, K.1
Taguchi, H.2
Ishii, N.3
Yoshida, M.4
-
17
-
-
0030054723
-
A novel factor required for the assembly of the DnaK and DnaJ chaperones of Thermus thermophilus
-
Motohashi K, Yohda M, Endo I, Yoshida M. A novel factor required for the assembly of the DnaK and DnaJ chaperones of Thermus thermophilus. J. Biol. Chem. 1996, 271:17343-17348.
-
(1996)
J. Biol. Chem.
, vol.271
, pp. 17343-17348
-
-
Motohashi, K.1
Yohda, M.2
Endo, I.3
Yoshida, M.4
-
18
-
-
0030832411
-
K+ is an indispensable cofactor for GrpE stimulation of ATPase activity of DnaK x DnaJ complex from Thermus thermophilus
-
Motohashi K, Yohda M, Odaka M, Yoshida M. K+ is an indispensable cofactor for GrpE stimulation of ATPase activity of DnaK x DnaJ complex from Thermus thermophilus. FEBS Lett. 1997, 412:633-636.
-
(1997)
FEBS Lett.
, vol.412
, pp. 633-636
-
-
Motohashi, K.1
Yohda, M.2
Odaka, M.3
Yoshida, M.4
-
19
-
-
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 1999, 96:7184-7189.
-
(1999)
Proc. Natl Acad. Sci. USA
, vol.96
, pp. 7184-7189
-
-
Motohashi, K.1
Watanabe, Y.2
Yohda, M.3
Yoshida, M.4
-
20
-
-
0022349286
-
Purification and properties of glucose-6-phosphate dehydrogenase from Bacillus stearothermophilus
-
Okuno H, Nagata K, Nakajima H. Purification and properties of glucose-6-phosphate dehydrogenase from Bacillus stearothermophilus. J. Appl. Biochem. 1985, 7:192-201.
-
(1985)
J. Appl. Biochem.
, vol.7
, pp. 192-201
-
-
Okuno, H.1
Nagata, K.2
Nakajima, H.3
-
21
-
-
0023472472
-
Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
-
Schagger H, von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 1987, 166:368-379.
-
(1987)
Anal. Biochem.
, vol.166
, pp. 368-379
-
-
Schagger, H.1
von Jagow, G.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. 2001, 306:889-899.
-
(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
-
-
17644407779
-
The importance of having thermosensor control in the DnaK chaperone system
-
Siegenthaler RK, Christen P. The importance of having thermosensor control in the DnaK chaperone system. J. Biol. Chem. 2005, 280:14395-14401.
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 14395-14401
-
-
Siegenthaler, R.K.1
Christen, P.2
-
24
-
-
21644468868
-
ATP binding to nucleotide binding domain (NBD)1 of the ClpB chaperone induces motion of the long coiled-coil, stabilizes the hexamer, and activates NBD2
-
Watanabe YH, Takano M, Yoshida M. ATP binding to nucleotide binding domain (NBD)1 of the ClpB chaperone induces motion of the long coiled-coil, stabilizes the hexamer, and activates NBD2. J. Biol. Chem. 2005, 280:24562-24567.
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 24562-24567
-
-
Watanabe, Y.H.1
Takano, M.2
Yoshida, M.3
-
25
-
-
1942501822
-
Trigonal DnaK-DnaJ complex versus free DnaK and DnaJ: heat stress converts the former to the latter, and only the latter can do disaggregation in cooperation with ClpB
-
Watanabe YH, Yoshida M. Trigonal DnaK-DnaJ complex versus free DnaK and DnaJ: heat stress converts the former to the latter, and only the latter can do disaggregation in cooperation with ClpB. J. Biol. Chem. 2004, 279:15723-15727.
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 15723-15727
-
-
Watanabe, Y.H.1
Yoshida, M.2
-
26
-
-
0034724719
-
Heat-inactivated proteins managed by DnaKJ-GrpE-ClpB chaperones are released as a chaperonin-recognizable non-native form
-
Watanabe YH, Motohashi K, Taguchi H, Yoshida M. Heat-inactivated proteins managed by DnaKJ-GrpE-ClpB chaperones are released as a chaperonin-recognizable non-native form. J. Biol. Chem. 2000, 275:12388-12392.
-
(2000)
J. Biol. Chem.
, vol.275
, pp. 12388-12392
-
-
Watanabe, Y.H.1
Motohashi, K.2
Taguchi, H.3
Yoshida, M.4
-
27
-
-
0037155139
-
Roles of the two ATP binding sites of ClpB from Thermus thermophilus
-
Watanabe YH, Motohashi K, Yoshida M. Roles of the two ATP binding sites of ClpB from Thermus thermophilus. J. Biol. Chem. 2002, 277:5804-5809.
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 5804-5809
-
-
Watanabe, Y.H.1
Motohashi, K.2
Yoshida, M.3
-
28
-
-
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. 1999, 274:28083-28086.
-
(1999)
J. Biol. Chem.
, vol.274
, pp. 28083-28086
-
-
Zolkiewski, M.1
|