-
1
-
-
0015859467
-
Principles that govern the folding of protein chains
-
Anfinsen, C. B. Principles that govern the folding of protein chains. Science 181, 223-230 (1973).
-
(1973)
Science
, vol.181
, pp. 223-230
-
-
Anfinsen, C.B.1
-
2
-
-
0032842870
-
The fundamentals of protein folding: Bringing together theory and experiment
-
Dobson, C. M. & Karpius, M. The fundamentals of protein folding: bringing together theory and experiment. Curr. Opin. Struct. Biol. 9, 92-101 (1999).
-
(1999)
Curr. Opin. Struct. Biol.
, vol.9
, pp. 92-101
-
-
Dobson, C.M.1
Karpius, M.2
-
3
-
-
0035478585
-
Macromolecular crowding: Obvious but under-appreciated
-
Bus, R. J. Macromolecular crowding: obvious but under-appreciated. Trends Bochem. Sci. 26, 597-604 (2001).
-
(2001)
Trends Bochem. Sci.
, vol.26
, pp. 597-604
-
-
Bus, R.J.1
-
4
-
-
0034637161
-
The structural basis of ribosome activity in peptide bond synthesis
-
Nissen, P., Hansen, J., Ban, N., Moore, P. B. & Steitz, T. A. The structural basis of ribosome activity in peptide bond synthesis. Science 289, 920-930 (2000).
-
(2000)
Science
, vol.289
, pp. 920-930
-
-
Nissen, P.1
Hansen, J.2
Ban, N.3
Moore, P.B.4
Steitz, T.A.5
-
5
-
-
1842766175
-
Three-dimensional structures of translating ribosomes by cryo-EM
-
Gilbert. R. J. C. et al. Three-dimensional structures of translating ribosomes by cryo-EM. Mol. Cell 14, 57-66 (2004).
-
(2004)
Mol. Cell
, vol.14
, pp. 57-66
-
-
Gilbert, R.J.C.1
-
6
-
-
0347357617
-
Protein folding and misfolding
-
Dobson, C. M. Protein folding and misfolding. Nature 426, 884-890 (2003).
-
(2003)
Nature
, vol.426
, pp. 884-890
-
-
Dobson, C.M.1
-
7
-
-
0347987853
-
Folding proteins in fatal ways
-
Selkoe, D. J. Folding proteins in fatal ways. Nature 426, 900-904 (2003).
-
(2003)
Nature
, vol.426
, pp. 900-904
-
-
Selkoe, D.J.1
-
8
-
-
0031029046
-
Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding
-
Schob, C., Stoller, G., Zarnt, T., Fischer, G. & Schmid, F. X. Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding. EMBO J. 16, 54-58 (1997).
-
(1997)
EMBO J.
, vol.16
, pp. 54-58
-
-
Schob, C.1
Stoller, G.2
Zarnt, T.3
Fischer, G.4
Schmid, F.X.5
-
9
-
-
0030805752
-
Nascent membrane and presecretory proteins synthesized in Escherichia coli associate with signal recognition partide and trigger factor
-
Valent, Q. A. et al. Nascent membrane and presecretory proteins synthesized in Escherichia coli associate with signal recognition partide and trigger factor. Mol. Microbiol. 25, 53-64 (1997).
-
(1997)
Mol. Microbiol.
, vol.25
, pp. 53-64
-
-
Valent, Q.A.1
-
10
-
-
0029913836
-
Escherichia coli trigger factor is a protyl isomerase that associates with nascent polypeptide chains
-
Hesterkamp, T., Hauser, S., Lutcke, H. & Bukau, B. Escherichia coli trigger factor is a protyl isomerase that associates with nascent polypeptide chains. Proc. Natl Acad. Sci. USA 93, 4437-4441 (1996).
-
(1996)
Proc. Natl. Acad. Sci. USA
, vol.93
, pp. 4437-4441
-
-
Hesterkamp, T.1
Hauser, S.2
Lutcke, H.3
Bukau, B.4
-
11
-
-
0035807963
-
Binding specificity of Escherichia coli trigger factor
-
Patzelt H. et al. Binding specificity of Escherichia coli trigger factor. Proc. Natl Acad. Sci. USA 98, 14244-14249 (2001).
-
(2001)
Proc. Natl. Acad. Sci. USA
, vol.98
, pp. 14244-14249
-
-
Patzelt, H.1
-
12
-
-
0030881913
-
The amino-terminal 118 amino acids of Escherichia coli trigger factor constitute a domain that is necessary and sufficient for binding to ribosomes
-
Hesterkamp, T., Deuerling, E. & Bukau, B. The amino-terminal 118 amino acids of Escherichia coli trigger factor constitute a domain that is necessary and sufficient for binding to ribosomes. J. Biol. Chem. 272, 21865-21871 (1997).
-
(1997)
J. Biol. Chem.
, vol.272
, pp. 21865-21871
-
-
Hesterkamp, T.1
Deuerling, E.2
Bukau, B.3
-
13
-
-
0037068441
-
L23 protein functions as a chaperone docking site on the ribosome
-
Kramer, G. et al. L23 protein functions as a chaperone docking site on the ribosome. Nature 419, 171-174 (2002). The nature of the specific interaction between ribosomes and the nascent-chain-binding chaperone TF is determined.
-
(2002)
Nature
, vol.419
, pp. 171-174
-
-
Kramer, G.1
-
14
-
-
0037459119
-
Localization of the trigger factor binding site on the ribosomal 50S subunit
-
Blaha, G. et al. Localization of the trigger factor binding site on the ribosomal 50S subunit. J. Mol. Biol. 326, 887-897 (2003).
-
(2003)
J. Mol. Biol.
, vol.326
, pp. 887-897
-
-
Blaha, G.1
-
15
-
-
0035861999
-
Dynamic association of trigger factor with protein substrates
-
Maier, R., Scholz, C. & Schmid, F. X. Dynamic association of trigger factor with protein substrates. J. Mol. Biol. 314. 1181-1190 (2001).
-
(2001)
J. Mol. Biol.
, vol.314
, pp. 1181-1190
-
-
Maier, R.1
Scholz, C.2
Schmid, F.X.3
-
16
-
-
1642487106
-
In vivo analysis of the overlapping functions of DnaK and trigger factor
-
Genevaux, P. et al. In vivo analysis of the overlapping functions of DnaK and trigger factor. EMBO Rep. 5, 195-200 (2004).
-
(2004)
EMBO Rep.
, vol.5
, pp. 195-200
-
-
Genevaux, P.1
-
17
-
-
1842639447
-
Trigger factor's peptidyl-protyl isomerase activity is not essential for the folding of cytosolic proteins in Escherichia coli
-
Kramer, G. et al. Trigger factor's peptidyl-protyl isomerase activity is not essential for the folding of cytosolic proteins in Escherichia coli. J. Biol. Chem. 279, 14165-14170 (2004).
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 14165-14170
-
-
Kramer, G.1
-
18
-
-
0033032592
-
Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains
-
Teter, S. A. et al. Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains. Cell 97, 755-765 (1999). Shows that both TF and Hsp70 (DnaK) bind nascent polypeptides and are crucial for the folding of newly synthesized proteins.
-
(1999)
Cell
, vol.97
, pp. 755-765
-
-
Teter, S.A.1
-
19
-
-
0032489016
-
The Hsp70 and Hsp60 chaperone machines
-
Bukau, B. & Horwich, A. L. The Hsp70 and Hsp60 chaperone machines. Cell 92, 351-366 (1998).
-
(1998)
Cell
, vol.92
, pp. 351-366
-
-
Bukau, B.1
Horwich, A.L.2
-
20
-
-
0037040541
-
Molecular chaperones in the cytosol: From nascent chain to folded protein
-
Hartl, F. U. & Hayer-Hartl, M. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295, 1852-1585 (2002).
-
(2002)
Science
, vol.295
, pp. 1852-1585
-
-
Hartl, F.U.1
Hayer-Hartl, M.2
-
21
-
-
0027425585
-
Control of folding and membrane translocation by binding of the chaperone DnaJ to nascent polypeptides
-
Hendrick, J. P., Langer, T., Davis, T. A., Hartl, F. U. & Wiedmann, M. Control of folding and membrane translocation by binding of the chaperone DnaJ to nascent polypeptides. Proc. Natl Acad. Sci. USA 90, 10216-10220 (1993).
-
(1993)
Proc. Natl. Acad. Sci. USA
, vol.90
, pp. 10216-10220
-
-
Hendrick, J.P.1
Langer, T.2
Davis, T.A.3
Hartl, F.U.4
Wiedmann, M.5
-
22
-
-
0033549770
-
Trigger factor and DnaK cooperate in folding of newly synthesized proteins
-
Deuerling, E., Schulze-Specking, A., Tomoyasu, T., Mogk, A. & Bukau, B. Trigger factor and DnaK cooperate in folding of newly synthesized proteins. Nature 400, 693-696 (1999). Together with reference 18, this report shows a functional cooperation between TF and Hsp70 (DnaK).
-
(1999)
Nature
, vol.400
, pp. 693-696
-
-
Deuerling, E.1
Schulze-Specking, A.2
Tomoyasu, T.3
Mogk, A.4
Bukau, B.5
-
23
-
-
0442307793
-
Low temperature or GroEL/ES overproduction permits growth of Escherichia coli cells lacking trigger factor and DnaK
-
Vorderwûlbecke, S. et al. Low temperature or GroEL/ES overproduction permits growth of Escherichia coli cells lacking trigger factor and DnaK. FEBS Lett. 559, 181-187 (2004).
-
(2004)
FEBS Lett.
, vol.559
, pp. 181-187
-
-
Vorderwûlbecke, S.1
-
24
-
-
1942421714
-
Function of trigger factor and DnaK in multi-domain protein folding: Increase in yield at the expense of folding speed
-
Agashe, V. R. et al. Function of trigger factor and DnaK in multi-domain protein folding: increase in yield at the expense of folding speed. Cell 117, 199-209 (2004).
-
(2004)
Cell
, vol.117
, pp. 199-209
-
-
Agashe, V.R.1
-
25
-
-
0034680334
-
Yeast Pdr13p and Zuo1p molecular chaperones are new functional Hsp70 and Hsp40 partners
-
Michimoto, T., Aoki, T., Toh-e, A. & Kikuchi, Y. Yeast Pdr13p and Zuo1p molecular chaperones are new functional Hsp70 and Hsp40 partners. Gene 257, 131-137 (2000).
-
(2000)
Gene
, vol.257
, pp. 131-137
-
-
Michimoto, T.1
Aoki, T.2
Toh-E, A.3
Kikuchi, Y.4
-
26
-
-
0035957355
-
RAC, a stable ribosome-associated complex in yeast formed by the DnaK-DnaJ homologs Ssz1p and zuotin
-
Gautschi, M. et al. RAC, a stable ribosome-associated complex in yeast formed by the DnaK-DnaJ homologs Ssz1p and zuotin. Proc. Natl Acad. Sci. USA 98, 3762-3767 (2001).
-
(2001)
Proc. Natl. Acad. Sci. USA
, vol.98
, pp. 3762-3767
-
-
Gautschi, M.1
-
27
-
-
0037007008
-
The in vivo function of the ribosome-associated Hsp70, Ssz1, does not require its putative peptide-binding domain
-
Hundley, H. et al. The in vivo function of the ribosome-associated Hsp70, Ssz1, does not require its putative peptide-binding domain. Proc. Natl Acad. Sci. USA 99, 4203-4208 (2002).
-
(2002)
Proc. Natl. Acad. Sci. USA
, vol.99
, pp. 4203-4208
-
-
Hundley, H.1
-
28
-
-
0032541489
-
Zuotin, a ribosome-associated DnaJ molecular chaperone
-
Yan, W. et al. Zuotin, a ribosome-associated DnaJ molecular chaperone. EMBO J. 17, 4809-4817 (1998).
-
(1998)
EMBO J.
, vol.17
, pp. 4809-4817
-
-
Yan, W.1
-
29
-
-
0026649409
-
The translation machinery and 70 kD heat shock protein cooperate in protein synthesis
-
Nelson, R. J., Zegelhoffer, T., Nicolet, C., Werner-Washburne, M. & Craig, E. A. The translation machinery and 70 kD heat shock protein cooperate in protein synthesis. Cell 71, 97-105 (1992). Presents some of the earliest evidence for a functional cooperation of cytosolic chaperones with the translation machinery.
-
(1992)
Cell
, vol.71
, pp. 97-105
-
-
Nelson, R.J.1
Zegelhoffer, T.2
Nicolet, C.3
Werner-Washburne, M.4
Craig, E.A.5
-
30
-
-
0032528301
-
The molecular chaperone Ssb from Saccharomyces cerevisiae is a component of the ribosome-nascent chain complex
-
Pfund, C. et al. The molecular chaperone Ssb from Saccharomyces cerevisiae is a component of the ribosome-nascent chain complex. EMBO J. 17, 3981-3989 (1998).
-
(1998)
EMBO J.
, vol.17
, pp. 3981-3989
-
-
Pfund, C.1
-
31
-
-
0141613640
-
TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes
-
Siegers, K. et al. TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes. EMBO J. 22, 5230-5240 (2003). Shows that the chaperonin TRiC works with two types of chaperone, Hsp70 (Ssb) and GimC, to fold subsets of its substrates.
-
(2003)
EMBO J.
, vol.22
, pp. 5230-5240
-
-
Siegers, K.1
-
32
-
-
0037007060
-
A functional chaperone triad on the yeast ribosome
-
Gautschi, M., Mun, A., Ross, S. & Rospert, S. A functional chaperone triad on the yeast ribosome. Proc. Natl Acad. Sci. USA 99, 4209-4214 (2002).
-
(2002)
Proc. Natl. Acad. Sci. USA
, vol.99
, pp. 4209-4214
-
-
Gautschi, M.1
Mun, A.2
Ross, S.3
Rospert, S.4
-
33
-
-
0025303147
-
Interaction of Hsp70 with newly synthesized proteins: Implications for protein folding and assembly
-
Beckmann, R. P., Mizzen, L. E. & Welch, W. J. Interaction of Hsp70 with newly synthesized proteins: implications for protein folding and assembly. Science 248, 850-854 (1990).
-
(1990)
Science
, vol.248
, pp. 850-854
-
-
Beckmann, R.P.1
Mizzen, L.E.2
Welch, W.J.3
-
34
-
-
0028361309
-
Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones
-
Frydman, J., Nimmesgem, E., Ohtsuka, K. & Hartl, F. U. Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones. Nature 370. 111-117 (1994).
-
(1994)
Nature
, vol.370
, pp. 111-117
-
-
Frydman, J.1
Nimmesgem, E.2
Ohtsuka, K.3
Hartl, F.U.4
-
35
-
-
0030928059
-
Complexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cells
-
Eggers, D. K., Welch, W. J. & Hansen, W. J. Complexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cells. Mol. Biol. Cell 8, 1559-1573 (1997).
-
(1997)
Mol. Biol. Cell
, vol.8
, pp. 1559-1573
-
-
Eggers, D.K.1
Welch, W.J.2
Hansen, W.J.3
-
36
-
-
0030830249
-
The human DnaJ homologue dj2 facilitates mitochondrial protein import and luciferase refolding
-
Terada, K., Kanazawa, M., Bukau, B. & Mori, M. The human DnaJ homologue dj2 facilitates mitochondrial protein import and luciferase refolding. J. Cell Biol. 139, 1089-1095 (1997).
-
(1997)
J. Cell Biol.
, vol.139
, pp. 1089-1095
-
-
Terada, K.1
Kanazawa, M.2
Bukau, B.3
Mori, M.4
-
37
-
-
0032510812
-
Mammalian cytosolic DnaJ homologues affect the hsp70 chaperone-substrate reaction cycle, but do not interact directly with nascent or newly synthesized proteins
-
Nagata, H., Hansen, W. J., Freeman, B. & Welch, W. J. Mammalian cytosolic DnaJ homologues affect the hsp70 chaperone-substrate reaction cycle, but do not interact directly with nascent or newly synthesized proteins. Biochemistry 37, 6924-6938 (1998).
-
(1998)
Biochemistry
, vol.37
, pp. 6924-6938
-
-
Nagata, H.1
Hansen, W.J.2
Freeman, B.3
Welch, W.J.4
-
38
-
-
0034193525
-
The interaction of the chaperonin tailless complex polypeptide 1 (TCP1) ring complex (TRiC) win ribosome-bound nascent chans examined using photo-crosslinking
-
McCallum, C. D., Do, H., Johnson, A. E. & Frydman, J. The interaction of the chaperonin tailless complex polypeptide 1 (TCP1) ring complex (TRiC) win ribosome-bound nascent chans examined using photo-crosslinking. J. Cell Biol. 149, 591-602 (2000). The results in this paper indicate a tight coupling between translation and chaperone-assisted protein folding.
-
(2000)
J. Cell Biol.
, vol.149
, pp. 591-602
-
-
McCallum, C.D.1
Do, H.2
Johnson, A.E.3
Frydman, J.4
-
39
-
-
0027980239
-
A protein complex required for signal-sequence-specific sorting and translocation
-
Wiedmann, B., Sakai, H., Davis, T. A. & Wiedmann, M. A protein complex required for signal-sequence-specific sorting and translocation. Nature 370, 434-440 (1994).
-
(1994)
Nature
, vol.370
, pp. 434-440
-
-
Wiedmann, B.1
Sakai, H.2
Davis, T.A.3
Wiedmann, M.4
-
40
-
-
0028849908
-
The yeast EGD2 gene encodes a homologue of the α-NAC subunit of the human nascent-polypeptide-associated complex
-
Shi, X., Parthun, M. R. & Jaehning, J. A. The yeast EGD2 gene encodes a homologue of the α-NAC subunit of the human nascent-polypeptide- associated complex. Gene 165, 199-202 (1995).
-
(1995)
Gene
, vol.165
, pp. 199-202
-
-
Shi, X.1
Parthun, M.R.2
Jaehning, J.A.3
-
41
-
-
0027214204
-
Folding in vivo of bacterial cytoplasmic proteins: Role of GroEL
-
Horwich, A. L., Low, K. B., Fenton, W. A., Hirshfeld, I. N. & Furtak, K. Folding in vivo of bacterial cytoplasmic proteins: role of GroEL. Cell 74, 909-917 (1993).
-
(1993)
Cell
, vol.74
, pp. 909-917
-
-
Horwich, A.L.1
Low, K.B.2
Fenton, W.A.3
Hirshfeld, I.N.4
Furtak, K.5
-
42
-
-
0030750584
-
In vivo observation of polypeptide flux through the bacterial chaperonin system
-
Ewalt, K. L., Hendrick, J. P., Houry, W. A. & Hartl, F. U. In vivo observation of polypeptide flux through the bacterial chaperonin system. Cell 90, 491-500 (1997).
-
(1997)
Cell
, vol.90
, pp. 491-500
-
-
Ewalt, K.L.1
Hendrick, J.P.2
Houry, W.A.3
Hartl, F.U.4
-
43
-
-
0026596223
-
Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding
-
Langer, T. et al. Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding. Nature 356, 683-689 (1992). This early paper shows that Hsp70 (DnaK) and chaperonins cooperate mechanistically in polypeptide folding.
-
(1992)
Nature
, vol.356
, pp. 683-689
-
-
Langer, T.1
-
44
-
-
0033547324
-
Identification of in vivo substrates of the chaperonin GroEL
-
Houry, W. A., Frishman, D., Eckerskorn, D., Lottspeich, F. & Haro, F. U. Identification of in vivo substrates of the chaperonin GroEL. Nature 402, 147-154 (1999).
-
(1999)
Nature
, vol.402
, pp. 147-154
-
-
Houry, W.A.1
Frishman, D.2
Eckerskorn, D.3
Lottspeich, F.4
Haro, F.U.5
-
45
-
-
0030598919
-
Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding
-
Buchberger, A., Schröder, H., Hesterkamp, T, Schönfeld, H. J. & Bukau, B. Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding. J. Mol. Biol. 261, 328-333 (1996).
-
(1996)
J. Mol. Biol.
, vol.261
, pp. 328-333
-
-
Buchberger, A.1
Schröder, H.2
Hesterkamp, T.3
Schönfeld, H.J.4
Bukau, B.5
-
46
-
-
0031873712
-
Regulation of the heat-shook response in bacteria
-
Segal, G. & Ron, E. Z. Regulation of the heat-shook response in bacteria. Ann. NY Acad. Sci. 851, 147-151 (1998).
-
(1998)
Ann. NY Acad. Sci.
, vol.851
, pp. 147-151
-
-
Segal, G.1
Ron, E.Z.2
-
47
-
-
0032541496
-
Role of the DnaK and HscA homologs of Hsp70 chaperones in protein folding in E. coli
-
Hesterkamp, T. & Bukau, B. Role of the DnaK and HscA homologs of Hsp70 chaperones in protein folding in E. coli. EMBO J. 17, 4818-4828 (1998).
-
(1998)
EMBO J.
, vol.17
, pp. 4818-4828
-
-
Hesterkamp, T.1
Bukau, B.2
-
48
-
-
0035913910
-
GroEL/GroES-mediated folding of a protein too large to be encapsulated
-
Chaudhuri, T. K., Farr, G. W., Fenton, W. A., Rospert, S. & Horwich, A. L. GroEL/GroES-mediated folding of a protein too large to be encapsulated. Cell 107, 235-246 (2001). A new mechanism for bacterial GroEL/ES is described, in which the substrate is bound only by the open end of the chaperonin system. This raises the possibility of GroEL interactions with nascent chains.
-
(2001)
Cell
, vol.107
, pp. 235-246
-
-
Chaudhuri, T.K.1
Farr, G.W.2
Fenton, W.A.3
Rospert, S.4
Horwich, A.L.5
-
49
-
-
0037010171
-
Structure and function of a protein folding machine: The eukaryotic chaperonin CCT
-
Valpuesta, J. M., Martín-Benito, J., Gómez-Puertas, R, Carrascosa, J. L. & Willison, K. R. Structure and function of a protein folding machine: the eukaryotic chaperonin CCT. FEBS Lett. 529, 11-16 (2002).
-
(2002)
FEBS Lett.
, vol.529
, pp. 11-16
-
-
Valpuesta, J.M.1
Martín-Benito, J.2
Gómez-Puertas, R.3
Carrascosa, J.L.4
Willison, K.R.5
-
50
-
-
0035423032
-
The 'sequential allosteric ring' mechanism in the eukaryotic chaperonin-assisted folding of actin and tubulin
-
Llorca, O. et al. The 'sequential allosteric ring' mechanism in the eukaryotic chaperonin-assisted folding of actin and tubulin. EMBO J. 20, 4065-4075 (2001).
-
(2001)
EMBO J.
, vol.20
, pp. 4065-4075
-
-
Llorca, O.1
-
51
-
-
0030668929
-
Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin
-
Klumpp, M., Baumeister, W. & Essen, L.-O. Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin. Cell 91, 263-270 (1997).
-
(1997)
Cell
, vol.91
, pp. 263-270
-
-
Klumpp, M.1
Baumeister, W.2
Essen, L.-O.3
-
52
-
-
0032478545
-
Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT
-
Ditzel, L. et al. Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT. Cell 93, 125-138 (1998).
-
(1998)
Cell
, vol.93
, pp. 125-138
-
-
Ditzel, L.1
-
53
-
-
0038737003
-
Closing the folding chamber of the eukaryotic chaperonin requires the transition state of ATP hydrolysis
-
Meyer, A. S. et al. Closing the folding chamber of the eukaryotic chaperonin requires the transition state of ATP hydrolysis. Cell 113, 369-381 (2003). The eukaryotic chaperonin TRiC is shown to use an encapsulation mechanism to assist the folding of its substrates, which is conceptually similar to the mechanism that is used by the bacterial chaperonin system GroEL-GroES.
-
(2003)
Cell
, vol.113
, pp. 369-381
-
-
Meyer, A.S.1
-
54
-
-
0026776331
-
A cytoplasmic chaperonin that catalyzes β-actin folding
-
Gao, Y., Thomas, J. O., Chow, R. L. Lee, G. H. & Cowan, N. J. A cytoplasmic chaperonin that catalyzes β-actin folding. Cell 69, 1043-1050 (1992).
-
(1992)
Cell
, vol.69
, pp. 1043-1050
-
-
Gao, Y.1
Thomas, J.O.2
Chow, R.L.3
Lee, G.H.4
Cowan, N.J.5
-
55
-
-
0026650749
-
TCP1 complex is a molecular chaperons in tubulin biogenesis
-
Yaffe, M. B. et al. TCP1 complex is a molecular chaperons in tubulin biogenesis. Nature 358, 245-248 (1992).
-
(1992)
Nature
, vol.358
, pp. 245-248
-
-
Yaffe, M.B.1
-
56
-
-
0030730821
-
Chaperanin-mediated folding in the eukaryotic cytosol proceeds through rounds of release of nature and normative forms
-
Fair, G. W., Schart, E. C., Schumacher, R. J., Sondek, S. & Norwich, A. L. Chaperanin-mediated folding in the eukaryotic cytosol proceeds through rounds of release of nature and normative forms. Cell 89, 927-937 (1997).
-
(1997)
Cell
, vol.89
, pp. 927-937
-
-
Fair, G.W.1
Schart, E.C.2
Schumacher, R.J.3
Sondek, S.4
Norwich, A.L.5
-
57
-
-
0031725057
-
Maturation of human cyclin E requires the function of eukaryotic chaperonin CCT
-
Won, K. A., Schumacher, R. J., Fair, G. W., Norwich, A. L. & Reed, S. I. Maturation of human cyclin E requires the function of eukaryotic chaperonin CCT. Mol. Cell. Biol. 18, 7584-7589 (1998).
-
(1998)
Mol. Cell. Biol.
, vol.18
, pp. 7584-7589
-
-
Won, K.A.1
Schumacher, R.J.2
Fair, G.W.3
Norwich, A.L.4
Reed, S.I.5
-
58
-
-
0033400674
-
Formation of the VHL-elongin BC tumor suppressor complex is mediated by the chaperonin TRiC
-
Feldman, D. E., Thulasiraman, V., Ferreyra, R. G. & Frydman, J. Formation of the VHL-elongin BC tumor suppressor complex is mediated by the chaperonin TRiC. Mol. Cell 4, 1051-1061 (1999).
-
(1999)
Mol. Cell
, vol.4
, pp. 1051-1061
-
-
Feldman, D.E.1
Thulasiraman, V.2
Ferreyra, R.G.3
Frydman, J.4
-
59
-
-
0041669463
-
The CCT chaperonin promotes actuation of the anaphase-promoting complex through the generation of functional Cdc20
-
Camasses, A., Bogdanova, A., Shevchenko, A. & Zachariae, W. The CCT chaperonin promotes actuation of the anaphase-promoting complex through the generation of functional Cdc20. Mol. Cell 12, 87-100 (2003).
-
(2003)
Mol. Cell
, vol.12
, pp. 87-100
-
-
Camasses, A.1
Bogdanova, A.2
Shevchenko, A.3
Zachariae, W.4
-
60
-
-
0032573163
-
Folding in vivo of a newly translated yeast cytosolic enzyme B mediated by the SSA class of cytosolic yeast Hsp70 proteins
-
Kim, S., Schilke, B., Craig, E. A. & Norwich, A. L. Folding in vivo of a newly translated yeast cytosolic enzyme B mediated by the SSA class of cytosolic yeast Hsp70 proteins. Proc. Natl Acad. Sci. USA 95, 12860-12865 (1998).
-
(1998)
Proc. Natl. Acad. Sci. USA
, vol.95
, pp. 12860-12865
-
-
Kim, S.1
Schilke, B.2
Craig, E.A.3
Norwich, A.L.4
-
61
-
-
0035911158
-
An essential role for the substrate-binding region of Hsp40s in Saccharomyces cerevisiae
-
Johnson, J. L. & Craig, E. A. An essential role for the substrate-binding region of Hsp40s in Saccharomyces cerevisiae. J. Cell Biol. 152, 851-856 (2001).
-
(2001)
J. Cell Biol.
, vol.152
, pp. 851-856
-
-
Johnson, J.L.1
Craig, E.A.2
-
62
-
-
0037404423
-
The Hsp70 and TRiC/CCT chaperone systems cooperate in vivo to assemble the von Nippel-Lindau tumor suppressor complex
-
Melville, M. W., McClellan, A. J., Meyer, A. S., Darveau, A. & Frydman, J. The Hsp70 and TRiC/CCT chaperone systems cooperate in vivo to assemble the von Nippel-Lindau tumor suppressor complex. Mol. Cell. Biol. 23, 3141-3151 (2003).
-
(2003)
Mol. Cell. Biol.
, vol.23
, pp. 3141-3151
-
-
Melville, M.W.1
McClellan, A.J.2
Meyer, A.S.3
Darveau, A.4
Frydman, J.5
-
63
-
-
0032481303
-
A novel protein complex promoting formation of functional α- and γ-tubulin
-
Geissler, S., Siegers, K. & Schiebel, E. A novel protein complex promoting formation of functional α- and γ-tubulin. EMBO J. 17, 952-966 (1998).
-
(1998)
EMBO J.
, vol.17
, pp. 952-966
-
-
Geissler, S.1
Siegers, K.2
Schiebel, E.3
-
64
-
-
0032577573
-
Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin
-
Vanberg, I. E. et al. Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin. Cell 93, 863-873 (1998).
-
(1998)
Cell
, vol.93
, pp. 863-873
-
-
Vanberg, I.E.1
-
65
-
-
0033680802
-
Structure of the molecular chaperone prefoldin: Unique interaction of multiple coiled coil tentacles with unfolded proteins
-
Siegert, R., Leroux, M. R., Scheufler, C., Hart, F. U. & Moarefi, I. Structure of the molecular chaperone prefoldin: unique interaction of multiple coiled coil tentacles with unfolded proteins. Cell 103, 621-632 (2000).
-
(2000)
Cell
, vol.103
, pp. 621-632
-
-
Siegert, R.1
Leroux, M.R.2
Scheufler, C.3
Hart, F.U.4
Moarefi, I.5
-
66
-
-
0037011162
-
Structure of eukaryotic prefoldin and of its complexes with unfolded actin and the cytosolic chaperonin CCT
-
Martín-Benito, J. et al. Structure of eukaryotic prefoldin and of its complexes with unfolded actin and the cytosolic chaperonin CCT. EMBO J. 21, 6377-6386 (2002).
-
(2002)
EMBO J.
, vol.21
, pp. 6377-6386
-
-
Martín-Benito, J.1
-
67
-
-
0345518025
-
Prefoldin-nascent chain complexes in the folding of cytoskeletal proteins
-
Hansen, W. J., Cowan, N. J. & Welch, W. J. Prefoldin-nascent chain complexes in the folding of cytoskeletal proteins. J. Cell Biol. 145, 265-277 (1999).
-
(1999)
J. Cell Biol.
, vol.145
, pp. 265-277
-
-
Hansen, W.J.1
Cowan, N.J.2
Welch, W.J.3
-
68
-
-
0033521523
-
Compartmentation of protein folding in vivo: Sequestration of non-native polypeptide by the chaperonin-GimC system
-
Siegers, K. et al. Compartmentation of protein folding in vivo: sequestration of non-native polypeptide by the chaperonin-GimC system. EMBO J. 18, 75-84 (1999).
-
(1999)
EMBO J.
, vol.18
, pp. 75-84
-
-
Siegers, K.1
-
69
-
-
1042278172
-
Selective contribution of eukaryotic prefoldin subunits to actin and tubulin binding
-
Simons, C. T. et al. Selective contribution of eukaryotic prefoldin subunits to actin and tubulin binding. J. Biol. Chem. 179, 4196-4203 (2004).
-
(2004)
J. Biol. Chem.
, vol.179
, pp. 4196-4203
-
-
Simons, C.T.1
-
70
-
-
0033540034
-
Eukaryotic type II chaperonin CCT interacts with actin through specific subunits
-
Llorca, O. et al. Eukaryotic type II chaperonin CCT interacts with actin through specific subunits. Nature 402, 693-696 (1999).
-
(1999)
Nature
, vol.402
, pp. 693-696
-
-
Llorca, O.1
-
71
-
-
0034669110
-
Eukaryotic chaperonin CCT stabilizes actin and tubulin folding intermediates in open quasi-native conformations
-
LLorca, O. et al. Eukaryotic chaperonin CCT stabilizes actin and tubulin folding intermediates in open quasi-native conformations. EMBO J. 19, 5971-5979 (2000).
-
(2000)
EMBO J.
, vol.19
, pp. 5971-5979
-
-
Llorca, O.1
-
72
-
-
0035939668
-
Hsp90: A specialized but essential protein folding tool
-
Young, J. C., Moarefi, I. & Hard, F. U. Hsp90: a specialized but essential protein folding tool. J. Cell Biol. 154, 267-273 (2001).
-
(2001)
J. Cell Biol.
, vol.154
, pp. 267-273
-
-
Young, J.C.1
Moarefi, I.2
Hard, F.U.3
-
73
-
-
0034892432
-
Hsp90: Chaperoning signal transduction
-
Richter, K. & Buchner, J. Hsp90: chaperoning signal transduction. J. Cell. Phys. 188, 281-290 (2001).
-
(2001)
J. Cell. Phys.
, vol.188
, pp. 281-290
-
-
Richter, K.1
Buchner, J.2
-
74
-
-
0037315208
-
Regulation of signalling protein function and trafficking by the hsp90/hsp70-based chaperone machinery
-
Pratt, W. B. & Toft, D. O. Regulation of signalling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Exp. Biol. Med. 228, 111-133 (2003).
-
(2003)
Exp. Biol. Med.
, vol.228
, pp. 111-133
-
-
Pratt, W.B.1
Toft, D.O.2
-
75
-
-
0032541344
-
ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo
-
Panaretou, B. et al. ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo. EMBO J. 17, 4829-4836 (1998).
-
(1998)
EMBO J.
, vol.17
, pp. 4829-4836
-
-
Panaretou, B.1
-
76
-
-
0034329452
-
Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23
-
Young, J. C. & Hart, F. U. Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23. EMBO J. 19, 5930-5940 (2000).
-
(2000)
EMBO J.
, vol.19
, pp. 5930-5940
-
-
Young, J.C.1
Hart, F.U.2
-
77
-
-
1842782331
-
Under cover: Causes, effects and implications of Hsp90-mediated genetic capacitance
-
Sangster, T. A., Lindquist, S. & Queitsch, C. Under cover: causes, effects and implications of Hsp90-mediated genetic capacitance. BioEssays 26, 348-362 (2004).
-
(2004)
BioEssays
, vol.26
, pp. 348-362
-
-
Sangster, T.A.1
Lindquist, S.2
Queitsch, C.3
-
78
-
-
0037023732
-
HSP40 is the first step in the HSP90 chaperoning pathway for the progesterone receptor
-
Hernandez, M. P., Chadli, A. & Toft, D. O. HSP40 is the first step in the HSP90 chaperoning pathway for the progesterone receptor. J. Biol. Chem. 277, 11873-11881 (2002).
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 11873-11881
-
-
Hernandez, M.P.1
Chadli, A.2
Toft, D.O.3
-
79
-
-
0037416154
-
The Hsp90-binding peptidylprolyl isomerase FKBP52 potentiates glucocorticoid signaling in vivo
-
Riggs, D. L. et al. The Hsp90-binding peptidylprolyl isomerase FKBP52 potentiates glucocorticoid signaling in vivo. EMBO J. 22, 1158-1167 (2003).
-
(2003)
EMBO J.
, vol.22
, pp. 1158-1167
-
-
Riggs, D.L.1
-
80
-
-
0029665779
-
Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilized Cdk4
-
Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilized Cdk4. Genes Dev. 10, 1491-1502 (1996).
-
(1996)
Genes Dev.
, vol.10
, pp. 1491-1502
-
-
Stepanova, L.1
Leng, X.2
Parker, S.B.3
Harper, J.W.4
-
82
-
-
0029838168
-
Physical interaction of mammalian CDC37 with CDK4
-
Dai, K., Kobayashi, R. & Beach, D. Physical interaction of mammalian CDC37 with CDK4. J. Biol. Chem. 271, 22030-22034 (1996).
-
(1996)
J. Biol. Chem.
, vol.271
, pp. 22030-22034
-
-
Dai, K.1
Kobayashi, R.2
Beach, D.3
-
83
-
-
0036187476
-
TNF-induced recruitment and activation of the IKK comptex requires Cdc37 and Hsp90
-
Chen, G., Cao, P. & Goeddel, D. V. TNF-induced recruitment and activation of the IKK comptex requires Cdc37 and Hsp90. Mol. Cell 9, 401-410 (2002).
-
(2002)
Mol. Cell
, vol.9
, pp. 401-410
-
-
Chen, G.1
Cao, P.2
Goeddel, D.V.3
-
84
-
-
0037131187
-
Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function
-
Basso, A. D. et al. Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function. J. Biol. Chem. 277, 39858-39866 (2002).
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 39858-39866
-
-
Basso, A.D.1
-
85
-
-
0037107454
-
Cdc37 is essential for chromosome segregation and cytokinesis in higher eukaryotes
-
Lange, B. M., Rebollo, E., Herold, A. & González, C. Cdc37 is essential for chromosome segregation and cytokinesis in higher eukaryotes. EMBO J. 21, 5364-5374 (2002).
-
(2002)
EMBO J.
, vol.21
, pp. 5364-5374
-
-
Lange, B.M.1
Rebollo, E.2
Herold, A.3
González, C.4
-
86
-
-
0042092020
-
Identification of Cdc37 as a novel regulator of the stress-responsive mitogen-activated protein kinase
-
Tatebe, H. & Shiozaki, K. Identification of Cdc37 as a novel regulator of the stress-responsive mitogen-activated protein kinase. Mol. Cell. Biol. 23, 5132-5142 (2003).
-
(2003)
Mol. Cell. Biol.
, vol.23
, pp. 5132-5142
-
-
Tatebe, H.1
Shiozaki, K.2
-
87
-
-
0034720777
-
cdc37 is a nonexclusive Hsp90 cohort which participates intimately in Hsp90-mediated folding of immature kinase molecules
-
cdc37 is a nonexclusive Hsp90 cohort which participates intimately in Hsp90-mediated folding of immature kinase molecules. Biochemistry 39, 7631-7644 (2000).
-
(2000)
Biochemistry
, vol.39
, pp. 7631-7644
-
-
Hartson, S.D.1
-
88
-
-
0037164751
-
The Cdc37 protein kinase-binding domain is sufficient for protein kinase activity and cell viability
-
Lee, P. et al. The Cdc37 protein kinase-binding domain is sufficient for protein kinase activity and cell viability. J. Cell Biol. 159, 1051-1059 (2002).
-
(2002)
J. Cell Biol.
, vol.159
, pp. 1051-1059
-
-
Lee, P.1
-
89
-
-
1642505452
-
Sti1 and Cdc37 can stabilize Hsp90 in chaperone complexes with a protein kinase
-
Lee, P., Shabbir, A., Cardozo, C. & Caplan, A. J. Sti1 and Cdc37 can stabilize Hsp90 in chaperone complexes with a protein kinase. Mol. Biol. Cell 15, 1785-1792 (2004).
-
(2004)
Mol. Biol. Cell
, vol.15
, pp. 1785-1792
-
-
Lee, P.1
Shabbir, A.2
Cardozo, C.3
Caplan, A.J.4
-
90
-
-
0035104164
-
The hsp90 chaperone complex regulates intracellular localization of the dioxin receptor
-
Kazlauskas, A., Sundstrom, S., Poellinger, L. & Pongratz, I. The hsp90 chaperone complex regulates intracellular localization of the dioxin receptor. Mol. Cell. Biol. 21, 2594-2607 (2001).
-
(2001)
Mol. Cell. Biol.
, vol.21
, pp. 2594-2607
-
-
Kazlauskas, A.1
Sundstrom, S.2
Poellinger, L.3
Pongratz, I.4
-
91
-
-
0141704410
-
Defining the role for XAP2 in stabilization of the dioxin receptor
-
Lees, M. J., Peet, D. J. & Whitelaw, M. L. Defining the role for XAP2 in stabilization of the dioxin receptor. J. Biol. Chem. 278, 35878-35888 (2003).
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 35878-35888
-
-
Lees, M.J.1
Peet, D.J.2
Whitelaw, M.L.3
-
92
-
-
0037169028
-
Role of the myosin assembly protein UNC-45 as a molecular chaperone for myosin
-
Barra, J. M., Hutagalung, A. H., Blinker, A., Hartl, F. U. & Epstein, H. F. Role of the myosin assembly protein UNC-45 as a molecular chaperone for myosin. Science 295, 669-671 (2002).
-
(2002)
Science
, vol.295
, pp. 669-671
-
-
Barra, J.M.1
Hutagalung, A.H.2
Blinker, A.3
Hartl, F.U.4
Epstein, H.F.5
-
93
-
-
0141705339
-
HSP90 interacts with RAR1 and SGT1 and is essential for RP32-mediated disease resistance in Arabidopsis
-
Takahashi, A., Casas, C., Ichimura, K. & Shirasu, K. HSP90 interacts with RAR1 and SGT1 and is essential for RP32-mediated disease resistance in Arabidopsis. Proc. Natl Acad. Sci. USA 100, 11777-11782 (2003).
-
(2003)
Proc. Natl. Acad. Sci. USA
, vol.100
, pp. 11777-11782
-
-
Takahashi, A.1
Casas, C.2
Ichimura, K.3
Shirasu, K.4
-
94
-
-
0242556837
-
Cytosolic HSP90 associates with and modulates the Arabidopsis RPM1 disease resistance protein
-
Hubert, D. A. et al. Cytosolic HSP90 associates with and modulates the Arabidopsis RPM1 disease resistance protein. EMBO J. 22, 5679-5689 (2003).
-
(2003)
EMBO J.
, vol.22
, pp. 5679-5689
-
-
Hubert, D.A.1
-
95
-
-
0242641582
-
High throughput virus-induced gene silencing implicates heat shock protein 90 in plant disease resistance
-
Lu, R. et al. High throughput virus-induced gene silencing implicates heat shock protein 90 in plant disease resistance. EMBO J. 22, 5690-5699 (2003).
-
(2003)
EMBO J.
, vol.22
, pp. 5690-5699
-
-
Lu, R.1
-
96
-
-
0347087451
-
Molecular chaperone Hsp90 associates with resistance protein N and its signaling proteins SGT1 and RAR1 to modulate an innate immune response in plants
-
Liu, Y., Burch-Smith, T., Schiff, M., Feng, S. & Dinesh-Kumar, S. P. Molecular chaperone Hsp90 associates with resistance protein N and its signaling proteins SGT1 and RAR1 to modulate an innate immune response in plants. J. Biol. Chem. 279, 2101-2108 (2004).
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 2101-2108
-
-
Liu, Y.1
Burch-Smith, T.2
Schiff, M.3
Feng, S.4
Dinesh-Kumar, S.P.5
-
97
-
-
0033166694
-
STG1 encodes an essential component of the yeast kinetochore assembly pathway and a novel subunit of the SCF ubiquitin ligase complex
-
Kitagawa, K., Skowyra, D., Elledge, S. J., Harper, J. W. & Hieter, P. STG1 encodes an essential component of the yeast kinetochore assembly pathway and a novel subunit of the SCF ubiquitin ligase complex. Mol. Cell 4, 21-33 (1999).
-
(1999)
Mol. Cell
, vol.4
, pp. 21-33
-
-
Kitagawa, K.1
Skowyra, D.2
Elledge, S.J.3
Harper, J.W.4
Hieter, P.5
-
98
-
-
0037173049
-
Hsp90 enables Ctf13p/Skp1p to nucleate the budding yeast kinetochore
-
Stemmann, O., Neidig, A., Köcher, T., Wilm, M. & Lechner, J. Hsp90 enables Ctf13p/Skp1p to nucleate the budding yeast kinetochore. Proc. Natl Acad. Sci. USA 99, 8585-8590 (2002).
-
(2002)
Proc. Natl. Acad. Sci. USA
, vol.99
, pp. 8585-8590
-
-
Stemmann, O.1
Neidig, A.2
Köcher, T.3
Wilm, M.4
Lechner, J.5
-
99
-
-
0141484615
-
A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors
-
Kama, A. et al. A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors. Nature 425, 407-410 (2003). Shows that HSP90 in complexes in tumour cells is much more active than in untransformed cells, in which it is largely uncomplexed. This increased activity involves interactions with Hsp70 (HSC70) and co-chaperones of both HSP90 and HSC70.
-
(2003)
Nature
, vol.425
, pp. 407-410
-
-
Kama, A.1
-
100
-
-
0034756104
-
From the cradle to the grave: Molecular chaperones that may choose between folding and degradation
-
Höhfeld, J., Cyr, D. M. & Patterson, C. From the cradle to the grave: molecular chaperones that may choose between folding and degradation. EMBO Rep. 2, 885-890 (2001).
-
(2001)
EMBO Rep.
, vol.2
, pp. 885-890
-
-
Höhfeld, J.1
Cyr, D.M.2
Patterson, C.3
-
101
-
-
0036629253
-
Protein quality control: U-box-containing E3 ubiquitin ligases join the fold
-
Cyr, D. M., Höhfeld, J. & Patterson, C. Protein quality control: U-box-containing E3 ubiquitin ligases join the fold. Trends Biochem. Sci. 27, 368-375 (2002).
-
(2002)
Trends Biochem. Sci.
, vol.27
, pp. 368-375
-
-
Cyr, D.M.1
Höhfeld, J.2
Patterson, C.3
-
102
-
-
0642377466
-
More than folding: Localized functions of cytosolic chaperones
-
Young, J. C., Barrai, J. M. & Hart, F. U. More than folding: localized functions of cytosolic chaperones. Trends Biochem. Sci. 28, 541-547 (2003).
-
(2003)
Trends Biochem. Sci.
, vol.28
, pp. 541-547
-
-
Young, J.C.1
Barrai, J.M.2
Hart, F.U.3
-
104
-
-
0024298711
-
A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides
-
Deshaies, R. J., Koch, B. C., Werner-Washburne, M., Craig, E. A. & Schekman, R. W. A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides. Nature 332, 800-805 (1988).
-
(1988)
Nature
, vol.332
, pp. 800-805
-
-
Deshaies, R.J.1
Koch, B.C.2
Werner-Washburne, M.3
Craig, E.A.4
Schekman, R.W.5
-
105
-
-
0029845194
-
The requirement of heat shock cognate 70 protein for mitochondrial import varies among precursor proteins and depends on precursor length
-
Terada, K. et al. The requirement of heat shock cognate 70 protein for mitochondrial import varies among precursor proteins and depends on precursor length. Mol. Cell. Biol. 16, 6103-6109 (1996).
-
(1996)
Mol. Cell. Biol.
, vol.16
, pp. 6103-6109
-
-
Terada, K.1
-
106
-
-
0037428164
-
Molecular chaperones Hsp90 and Hsp70 deliver pre proteins to the mitochondrial import receptor Tom70
-
Young, J. C., Hoogenraad, N. J. & Hartl, F. U. Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70. Cell 112, 41-50 (2003). Reports the discovery of a specific interaction that directs the HSC70-HSPSO chaperone machinery to the mitochondrial outer membrane for the purpose of protein targeting.
-
(2003)
Cell
, vol.112
, pp. 41-50
-
-
Young, J.C.1
Hoogenraad, N.J.2
Hartl, F.U.3
-
107
-
-
0142027923
-
AIP is a mitochondrial import mediator that binds to both import receptor Tom20 and preproteins
-
Yano, M., Terada, K. & Mon, M. AIP is a mitochondrial import mediator that binds to both import receptor Tom20 and preproteins. J. Cell Biol. 163, 45-56 (2003).
-
(2003)
J. Cell Biol.
, vol.163
, pp. 45-56
-
-
Yano, M.1
Terada, K.2
Mon, M.3
-
108
-
-
0029954823
-
Functional interaction of cytosolic hsp70 and a DnaJ related protein, Ydj1p, in protein translocation in vivo
-
Becker, J., Walter, W., Yan, W. & Craig, E. A. Functional interaction of cytosolic hsp70 and a DnaJ related protein, Ydj1p, in protein translocation in vivo. Mol. Cell Biol. 16, 4378-4386 (1996).
-
(1996)
Mol. Cell Biol.
, vol.16
, pp. 4378-4386
-
-
Becker, J.1
Walter, W.2
Yan, W.3
Craig, E.A.4
-
109
-
-
0036083396
-
The ubiquitin-proteasome proteorytic pathway: Destruction for the sake of construction
-
Glickman, M. H. & Ciechanover, A. The ubiquitin-proteasome proteorytic pathway: destruction for the sake of construction. Physiol. Rev. 82, 373-428 (2002).
-
(2002)
Physiol. Rev.
, vol.82
, pp. 373-428
-
-
Glickman, M.H.1
Ciechanover, A.2
-
110
-
-
0034790768
-
Molecular chaperone targeting and regulation by BAG family proteins
-
Takayama, S. & Reed, J. C. Molecular chaperone targeting and regulation by BAG family proteins. Nature Cell Biol. 3, E237-E241 (2001).
-
(2001)
Nature Cell Biol.
, vol.3
-
-
Takayama, S.1
Reed, J.C.2
-
111
-
-
0344039806
-
GrpE-like regulation of the Hsc70 chaperone by the anti-apoptotic protein BAG-1
-
Höhfeld, J. & Jentsch, S. GrpE-like regulation of the Hsc70 chaperone by the anti-apoptotic protein BAG-1. EMBO J. 16, 6209-6216 (1997).
-
(1997)
EMBO J.
, vol.16
, pp. 6209-6216
-
-
Höhfeld, J.1
Jentsch, S.2
-
112
-
-
0035936826
-
Structure of a Bag/Hsc70 complex: Convergent functional evolution of Hsp70 nucleotide exchange factors
-
Sondermann, H. et al. Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors. Science 291, 1553-1557 (2001).
-
(2001)
Science
, vol.291
, pp. 1553-1557
-
-
Sondermann, H.1
-
113
-
-
0035146685
-
Regulation of heat shock protein-mediated protein triage decisions by the co-chaperone CHIP
-
Connell, P. et al. Regulation of heat shock protein-mediated protein triage decisions by the co-chaperone CHIP. Nature Cell Biol. 3, 93-96 (2001).
-
(2001)
Nature Cell Biol.
, vol.3
, pp. 93-96
-
-
Connell, P.1
-
114
-
-
0035142877
-
The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
-
Meacham, G. C., Patterson, C., Zhang, W., Younger, J. M. & Cyr, D. The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation. Nature Cell Biol. 3, 100-105 (2001). References 113 and 114 show that the HSC70 and HSP90 chaperones are linked to the ubiquitin-mediated proteasome-degradation system through a ubiquitin-ligase co-chaperone. This indicates that these chaperones function in protein quality control.
-
(2001)
Nature Cell Biol.
, vol.3
, pp. 100-105
-
-
Meacham, G.C.1
Patterson, C.2
Zhang, W.3
Younger, J.M.4
Cyr, D.5
-
115
-
-
0035899897
-
Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling
-
Demand, J., Alberti, S., Patterson, C. & Höhfeld, J. Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling. Curr. Biol. 11, 1569-1577 (2002).
-
(2002)
Curr. Biol.
, vol.11
, pp. 1569-1577
-
-
Demand, J.1
Alberti, S.2
Patterson, C.3
Höhfeld, J.4
-
116
-
-
0037195907
-
Ubiquitylation of BAG-1 suggests a novel regulatory mechanism during the sorting of chaperone substrates to the proteasome
-
Alberti, S. et al. Ubiquitylation of BAG-1 suggests a novel regulatory mechanism during the sorting of chaperone substrates to the proteasome. J. Biol. Chem. 277, 45920-45927 (2002).
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 45920-45927
-
-
Alberti, S.1
-
117
-
-
0034745354
-
Bag1-Hsp70 mediates a physiological stress signaling pathway that regulates Raf-1/ERK and cell growth
-
Song, J., Takeda, M. & Morimoto, R. I. Bag1-Hsp70 mediates a physiological stress signaling pathway that regulates Raf-1/ERK and cell growth. Nature Cell Biol. 3, 276-282 (2001).
-
(2001)
Nature Cell Biol.
, vol.3
, pp. 276-282
-
-
Song, J.1
Takeda, M.2
Morimoto, R.I.3
-
118
-
-
10744223839
-
CHIP activates HSF1 and confers protection against apoptosis and cellular stress
-
Dai, Q. et al. CHIP activates HSF1 and confers protection against apoptosis and cellular stress. EMBO J. 22, 5446-5458 (2003).
-
(2003)
EMBO J.
, vol.22
, pp. 5446-5458
-
-
Dai, Q.1
-
119
-
-
0033933125
-
ClpB and HtpG facilitate de novo protein folding in stressed Escherichia coli cells
-
Thomas, J. G. & Baneyx, F. ClpB and HtpG facilitate de novo protein folding in stressed Escherichia coli cells. Mol. Microbiol. 36, 1360-1370 (2000).
-
(2000)
Mol. Microbiol.
, vol.36
, pp. 1360-1370
-
-
Thomas, J.G.1
Baneyx, F.2
-
120
-
-
0024421221
-
Hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperature
-
Borkovich, K. A., Farrelly, F. W., Finkelstein, D. B., Taulien, J. & Lindquist, S. Hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperature. Mol. Cell. Biol. 9, 3919-3930 (1989).
-
(1989)
Mol. Cell. Biol.
, vol.9
, pp. 3919-3930
-
-
Borkovich, K.A.1
Farrelly, F.W.2
Finkelstein, D.B.3
Taulien, J.4
Lindquist, S.5
-
121
-
-
0032980876
-
Genetic analysis of viable Hsp90 alleles reveals a critical role in Drosophila spermatogenesis
-
Yue, L et al. Genetic analysis of viable Hsp90 alleles reveals a critical role in Drosophila spermatogenesis. Genetics 151, 1065-1079 (1999).
-
(1999)
Genetics
, vol.151
, pp. 1065-1079
-
-
Yue, L.1
-
122
-
-
0037184939
-
Directed evolution of substrate-optimized GroEL/S chaperonins
-
Wang, J. D., Herman, C., Tipton, K. A., Gross, C. A. & Weissman, J. S. Directed evolution of substrate-optimized GroEL/S chaperonins. Cell 111, 1027-1039 (2002).
-
(2002)
Cell
, vol.111
, pp. 1027-1039
-
-
Wang, J.D.1
Herman, C.2
Tipton, K.A.3
Gross, C.A.4
Weissman, J.S.5
-
123
-
-
1142302227
-
Molecular chaperones: Structure of a protein disaggregase
-
Mogk, A. & Bukau, B. Molecular chaperones: structure of a protein disaggregase. Curr. Biol. 14, R78-R80 (2004).
-
(2004)
Curr. Biol.
, vol.14
-
-
Mogk, A.1
Bukau, B.2
-
124
-
-
0033573135
-
Identification of thermolabile Escherichia coli proteins: Prevention and reversion of aggregation by DnaK and ClpB
-
Mogk, A. et al. Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB. EMBO J. 18, 6934-6949 (1999).
-
(1999)
EMBO J.
, vol.18
, pp. 6934-6949
-
-
Mogk, A.1
-
125
-
-
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
-
126
-
-
0347130897
-
A chaperone network for the resolubilization of protein aggregates: Direct interaction of ClpB and DnaK
-
Schlee, S., Beinker, P., Akhrymuk, A. & Reinstein, J. A chaperone network for the resolubilization of protein aggregates: direct interaction of ClpB and DnaK. J. Mol. Biol. 336, 275-285 (2004).
-
(2004)
J. Mol. Biol.
, vol.336
, pp. 275-285
-
-
Schlee, S.1
Beinker, P.2
Akhrymuk, A.3
Reinstein, J.4
-
127
-
-
0037150683
-
Disassembty of transcriptional regulatory complexes by molecular chaperones
-
Freeman, B. C. & Yamamoto, K. R. Disassembty of transcriptional regulatory complexes by molecular chaperones. Science 298, 2232-2235 (2002).
-
(2002)
Science
, vol.298
, pp. 2232-2235
-
-
Freeman, B.C.1
Yamamoto, K.R.2
-
128
-
-
0032569851
-
Hsp90 as a capacitor for morphological evolution
-
Rutherford, S. L. & Lindquist, S. Hsp90 as a capacitor for morphological evolution. Nature 368, 336-342 (1998). Proposes a role for HSP90 in buffering widespread genetic variation in morphogenic pathways and, therefore, in potentiating evolutionary change through the occasional selection of an accumulated variation.
-
(1998)
Nature
, vol.368
, pp. 336-342
-
-
Rutherford, S.L.1
Lindquist, S.2
-
129
-
-
4944246094
-
Trigger factor in complex with the ribosome forms a molecular cradie for nascent proteins
-
29 Aug (doi:10.1038/nature02899)
-
Ferbitz, L. et al. Trigger factor in complex with the ribosome forms a molecular cradie for nascent proteins. Nature 29 Aug 2004 (doi:10.1038/ nature02899).
-
(2004)
Nature
-
-
Ferbitz, L.1
-
130
-
-
0032417527
-
The biochemical properties of the ATPase activity of a 70-kDa heat shock protein (Hsp70) are governed by the C-terminal domains
-
Lopez-Buesa, P., Pfund, C. & Craig, E. A. The biochemical properties of the ATPase activity of a 70-kDa heat shock protein (Hsp70) are governed by the C-terminal domains. Proc. Natl Acad. Sci. USA 95, 15253-15258 (1998).
-
(1998)
Proc. Natl. Acad. Sci. USA
, vol.95
, pp. 15253-15258
-
-
Lopez-Buesa, P.1
Pfund, C.2
Craig, E.A.3
-
131
-
-
0037032470
-
HspBP1, a homologue of the yeast Fes1 and Sis1 proteins, is an Hsc70 nucleotide exchange factor
-
Kabani, M., McLellan, C., Raynes, D. A., Guerriero, V. & Brodsky, J. L. HspBP1, a homologue of the yeast Fes1 and Sis1 proteins, is an Hsc70 nucleotide exchange factor. FEBS Lett. 531, 339-342 (2002).
-
(2002)
FEBS Lett.
, vol.531
, pp. 339-342
-
-
Kabani, M.1
McLellan, C.2
Raynes, D.A.3
Guerriero, V.4
Brodsky, J.L.5
-
132
-
-
0036275663
-
Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p
-
Kabani, M., Beckerich, J.-M. & Brodsky, J. L. Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p. Mol. Cell. Biol. 22, 4677-4689 (2002).
-
(2002)
Mol. Cell. Biol.
, vol.22
, pp. 4677-4689
-
-
Kabani, M.1
Beckerich, J.-M.2
Brodsky, J.L.3
-
133
-
-
0028842615
-
Hip, a novel cochaperone invoked in the eukaryotic Hsc70/Hsp40 cycle
-
Höhfeld, J., Minami, Y. & Hartl, F. U. Hip, a novel cochaperone invoked in the eukaryotic Hsc70/Hsp40 cycle. Cell 83, 589-598 (1995).
-
(1995)
Cell
, vol.83
, pp. 589-598
-
-
Höhfeld, J.1
Minami, Y.2
Hartl, F.U.3
-
134
-
-
0035895935
-
Modulation of in vivo Hsp70 chaperone activity by Hip and Bag-1
-
Nollen, E. A. A. et al. Modulation of in vivo Hsp70 chaperone activity by Hip and Bag-1. J. Biol. Chem. 276, 4677-4682 (2001).
-
(2001)
J. Biol. Chem.
, vol.276
, pp. 4677-4682
-
-
Nollen, E.A.A.1
-
135
-
-
0031911786
-
Regulation of transcription factor Pdr1p function by an Hsp70 protein in Saccharomyces cerevisiae
-
Hallstrom, T. C., Katzmann, D. J., Torres, R. J., Sharp, W. J. & Moye-Rowley, W. S. Regulation of transcription factor Pdr1p function by an Hsp70 protein in Saccharomyces cerevisiae. Mol. Cell. Biol. 18, 1147-1155 (1998).
-
(1998)
Mol. Cell. Biol.
, vol.18
, pp. 1147-1155
-
-
Hallstrom, T.C.1
Katzmann, D.J.2
Torres, R.J.3
Sharp, W.J.4
Moye-Rowley, W.S.5
-
136
-
-
2442707856
-
SecB is a bona fide generalized chaperone in Escherichia coli
-
Ullers, R. S. et al. SecB is a bona fide generalized chaperone in Escherichia coli. Proc. Natl Acad. Sci. USA 101, 7583-7588 (2004).
-
(2004)
Proc. Natl. Acad. Sci. USA
, vol.101
, pp. 7583-7588
-
-
Ullers, R.S.1
-
137
-
-
0035718899
-
Structure, function and mechanism of the Hsp90 molecular chaperone
-
Peart, L. H. & Prodromou, C. Structure, function and mechanism of the Hsp90 molecular chaperone. Adv. Protein Chem. 59, 157-186 (2001).
-
(2001)
Adv. Protein Chem.
, vol.59
, pp. 157-186
-
-
Peart, L.H.1
Prodromou, C.2
-
138
-
-
0034646511
-
Structure of TPR domain-peptide complexes: Critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine
-
Scheufler, C. et al. Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. Cell 101, 199-210 (2000).
-
(2000)
Cell
, vol.101
, pp. 199-210
-
-
Scheufler, C.1
-
139
-
-
0033081968
-
Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones
-
Prodromou, C. et al. Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones. EMBO J. 18, 754-762 (1999).
-
(1999)
EMBO J.
, vol.18
, pp. 754-762
-
-
Prodromou, C.1
-
140
-
-
0042815093
-
Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system
-
Brychzy, A. et al. Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system. EMBO J. 22, 3613-3623 (2003).
-
(2003)
EMBO J.
, vol.22
, pp. 3613-3623
-
-
Brychzy, A.1
-
141
-
-
0036931438
-
Actuation of the ATPase of hsp90 by the stress-regulated cochaperone Aha1
-
Panaretou, B. et al. Actuation of the ATPase of hsp90 by the stress-regulated cochaperone Aha1. Mol. Cell 10, 1307-1318 (2002).
-
(2002)
Mol. Cell
, vol.10
, pp. 1307-1318
-
-
Panaretou, B.1
-
142
-
-
0037593900
-
Aha1 binds to the middle domain of Hsp90, contributes to client protein actuation, and stimulates the ATPase of the molecular chaperone
-
Lotz, G. P., Lin, H., Harst, A. & Obermann, W. M. Aha1 binds to the middle domain of Hsp90, contributes to client protein actuation, and stimulates the ATPase of the molecular chaperone. J. Biol. Chem. 278, 17228-17235 (2003).
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 17228-17235
-
-
Lotz, G.P.1
Lin, H.2
Harst, A.3
Obermann, W.M.4
-
143
-
-
0742269688
-
cdc37
-
cdc37. Cell 116, 87-98 (2004).
-
(2004)
Cell
, vol.116
, pp. 87-98
-
-
Roe, S.M.1
|