-
1
-
-
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
-
2
-
-
0029992278
-
Molecular chaperones in cellular protein folding
-
Hartl FU. Molecular chaperones in cellular protein folding. Nature 1996; 381:571-580.
-
(1996)
Nature
, vol.381
, pp. 571-580
-
-
Hartl, F.U.1
-
3
-
-
0037040541
-
Molecular chaperones in the cytosol: From nascent chain to folded protein
-
Hartl FU, Hayer-Hartl M. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 2002; 295:1852-1858.
-
(2002)
Science
, vol.295
, pp. 1852-1858
-
-
Hartl, F.U.1
Hayer-Hartl, M.2
-
4
-
-
0026596223
-
Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding
-
Langer T, Lu C, Echols H, Flanagan J, Hayer MK, Hartl FU. Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding. Nature 1992; 356:683-689.
-
(1992)
Nature
, vol.356
, pp. 683-689
-
-
Langer, T.1
Lu, C.2
Echols, H.3
Flanagan, J.4
Hayer, M.K.5
Hartl, F.U.6
-
6
-
-
0033545978
-
Mechanism of regulation of Hsp70 chaperones by DnaJ cochaperones
-
Laufen T, Mayer MP, Beisel C, Klostermeier D, Mogk A, Reinstein J, Bukau B. Mechanism of regulation of Hsp70 chaperones by DnaJ cochaperones. Proc Natl Acad Sci 1996; 96:5452-5457.
-
(1996)
Proc. Natl. Acad. Sci.
, vol.96
, pp. 5452-5457
-
-
Laufen, T.1
Mayer, M.P.2
Beisel, C.3
Klostermeier, D.4
Mogk, A.5
Reinstein, J.6
Bukau, B.7
-
7
-
-
0032214832
-
J proteins catalytically activate Hsp70 molecules to trap a wide range of peptide sequences
-
Misselwitz S, Staeck O, Rapoport TA. J proteins catalytically activate Hsp70 molecules to trap a wide range of peptide sequences. Mol Cell 1998; 2:593-603.
-
(1998)
Mol. Cell.
, vol.2
, pp. 593-603
-
-
Misselwitz, S.1
Staeck, O.2
Rapoport, T.A.3
-
8
-
-
0036177548
-
Direct interactions between molecular chaperones Hsp70 and Hsp40: Yeast Hsp70 Ssa1 binds the extreme C-terminal region of yeast Hsp40 Sis1
-
Qian X, Hou W, Li Z, Sha BD. Direct interactions between molecular chaperones Hsp70 and Hsp40: yeast Hsp70 Ssa1 binds the extreme C-terminal region of yeast Hsp40 Sis1. Biochem J 2002; 361:27-34.
-
(2002)
Biochem. J.
, vol.361
, pp. 27-34
-
-
Qian, X.1
Hou, W.2
Li, Z.3
Sha, B.D.4
-
9
-
-
0028170215
-
The N-terminal 108 amino acids of the E. coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for lamda replication
-
Wall D, Zylicz M, Georgopoulos C. The N-terminal 108 amino acids of the E. coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for lamda replication. J Biol Chem 1994; 269:5446-5451.
-
(1994)
J. Biol. Chem.
, vol.269
, pp. 5446-5451
-
-
Wall, D.1
Zylicz, M.2
Georgopoulos, C.3
-
10
-
-
0032489556
-
The conserved carboxyl terminus and zinc finger-like domain of the co-chaperone Ydj1 assist Hsp70 in protein folding
-
Lu Z, Cyr DM. The conserved carboxyl terminus and zinc finger-like domain of the co-chaperone Ydj1 assist Hsp70 in protein folding. J Biol Chem 1998; 273:5970-5978.
-
(1998)
J. Biol. Chem.
, vol.273
, pp. 5970-5978
-
-
Lu, Z.1
Cyr, D.M.2
-
11
-
-
0025745326
-
Characterization of Ydj1: A yeast homologue of the bacteria dnaJ protein
-
Caplan AJ, Douglas MG. Characterization of Ydj1: a yeast homologue of the bacteria dnaJ protein. J Cell Biol 1991; 114:609-621.
-
(1991)
J. Cell Biol.
, vol.114
, pp. 609-621
-
-
Caplan, A.J.1
Douglas, M.G.2
-
12
-
-
0032561360
-
Protein folding activity of Hsp70 is modified differentially by the Hsp40 co-chaperone Sis1 and Ydj1
-
Lu Z, Cyr DM. Protein folding activity of Hsp70 is modified differentially by the Hsp40 co-chaperone Sis1 and Ydj1. J Biol Chem 1998; 273:27824-27830.
-
(1998)
J. Biol. Chem.
, vol.273
, pp. 27824-27830
-
-
Lu, Z.1
Cyr, D.M.2
-
13
-
-
0030030946
-
A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates
-
Szabo A, Korszun R, Hartl FU, Flanagan J. A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates. EMBO J 1996; 15:408-417.
-
(1996)
EMBO J.
, vol.15
, pp. 408-417
-
-
Szabo, A.1
Korszun, R.2
Hartl, F.U.3
Flanagan, J.4
-
14
-
-
0035911158
-
An essential role for the substratebinding region of Hsp40s in Saccharomyces cerevisiae
-
Johnson JL, Craig EA. An essential role for the substratebinding region of Hsp40s in Saccharomyces cerevisiae. J Cell Biol 2001; 152:851-856.
-
(2001)
J. Cell Biol.
, vol.152
, pp. 851-856
-
-
Johnson, J.L.1
Craig, E.A.2
-
15
-
-
0026059137
-
Peptide-binding specificity of the molecular chaperone Bip
-
Flynn GC, Pohl J, Flocco MT, Rothman JE. Peptide-binding specificity of the molecular chaperone Bip. Nature 1991; 353:726-730.
-
(1991)
Nature
, vol.353
, pp. 726-730
-
-
Flynn, G.C.1
Pohl, J.2
Flocco, M.T.3
Rothman, J.E.4
-
16
-
-
0029937037
-
Structural analysis of substrate binding by the molecular chaperone DnaK
-
Zhu X, Zhao X, Burkholder WF, Gragerov A, Ogata CM, Gottesman ME, Hendrickson WA. Structural analysis of substrate binding by the molecular chaperone DnaK. Science 1996; 272:1606-1614.
-
(1996)
Science
, vol.272
, pp. 1606-1614
-
-
Zhu, X.1
Zhao, X.2
Burkholder, W.F.3
Gragerov, A.4
Ogata, C.M.5
Gottesman, M.E.6
Hendrickson, W.A.7
-
17
-
-
0033598941
-
The crystal structure of a GroEL/peptide comlex: Plasticity as a basis for substrate diversity
-
Chen L, Sigler PB. The crystal structure of a GroEL/peptide comlex: plasticity as a basis for substrate diversity. Cell 1999; 99:757-768.
-
(1999)
Cell
, vol.99
, pp. 757-768
-
-
Chen, L.1
Sigler, P.B.2
-
18
-
-
0034662746
-
The crystal structure of the peptide-binding fragment from the yeast Hsp40 protein Sis1
-
Sha BD, Lee S, Cyr DM. The crystal structure of the peptide-binding fragment from the yeast Hsp40 protein Sis1. Structure 2000; 8:799-807.
-
(2000)
Structure
, vol.8
, pp. 799-807
-
-
Sha, B.D.1
Lee, S.2
Cyr, D.M.3
-
19
-
-
0345299781
-
The crystal structure of the yeast Hsp40 Ydj1 complexed with its peptide substrate
-
Li J, Qian X, Sha B. The crystal structure of the yeast Hsp40 Ydj1 complexed with its peptide substrate. Structure 2003; 11:1475-1483.
-
(2003)
Structure
, vol.11
, pp. 1475-1483
-
-
Li, J.1
Qian, X.2
Sha, B.3
-
20
-
-
0025112794
-
Searching for peptide ligands with an epitope library
-
Scott JK, Smith GP. Searching for peptide ligands with an epitope library. Science 1990; 249:386-390.
-
(1990)
Science
, vol.249
, pp. 386-390
-
-
Scott, J.K.1
Smith, G.P.2
-
21
-
-
0035283043
-
Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone
-
Rudiger S, Schneider-Mergener J, Bukau B. Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone. EMBO J 2001; 20:1042-1050.
-
(2001)
EMBO J.
, vol.20
, pp. 1042-1050
-
-
Rudiger, S.1
Schneider-Mergener, J.2
Bukau, B.3
-
23
-
-
0141613640
-
TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes
-
Siegers K, Bolter B, Schwarz JP, Bottcher UM, Guha S, Hartl FU. TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes. EMBO J 2003; 22: 5230-5240.
-
(2003)
EMBO J.
, vol.22
, pp. 5230-5240
-
-
Siegers, K.1
Bolter, B.2
Schwarz, J.P.3
Bottcher, U.M.4
Guha, S.5
Hartl, F.U.6
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