-
1
-
-
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
-
2
-
-
0032538995
-
In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis
-
Obermann, W. M. J., Sondermann, H., Russo, A. A., Pavletich, N. P. & Hartl, F. U. In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis. J. Cell Biol. 143, 901-910 (1998).
-
(1998)
J. Cell Biol.
, vol.143
, pp. 901-910
-
-
Obermann, W.M.J.1
Sondermann, H.2
Russo, A.A.3
Pavletich, N.P.4
Hartl, F.U.5
-
3
-
-
0029812759
-
Polyubiquitination and proteasomal degradation of the p185c-erbB-2 receptor protein-tyrosine kinase induced by geldanamycin
-
Mimnaugh, E. G., Chavany, C. & Neckers, L. Polyubiquitination and proteasomal degradation of the p185c-erbB-2 receptor protein-tyrosine kinase induced by geldanamycin. J. Biol. Chem. 271, 22796-22801 (1996).
-
(1996)
J. Biol. Chem.
, vol.271
, pp. 22796-22801
-
-
Mimnaugh, E.G.1
Chavany, C.2
Neckers, L.3
-
4
-
-
0029963674
-
Pharmacologic shifting of a balance between protein folding and degradation mediated by Hsp90
-
Schneider, C. et al. Pharmacologic shifting of a balance between protein folding and degradation mediated by Hsp90. Proc. Natl Acad. Sci. USA 93, 14536-14541 (1996).
-
(1996)
Proc. Natl Acad. Sci. USA
, vol.93
, pp. 14536-14541
-
-
Schneider, C.1
-
5
-
-
12344291243
-
Hsp90 and Cdc37 - A chaperone cancer conspiracy
-
Pearl, L. H. Hsp90 and Cdc37 - a chaperone cancer conspiracy. Curr. Opin. Genet. Dev. 15, 55-61 (2005).
-
(2005)
Curr. Opin. Genet. Dev.
, vol.15
, pp. 55-61
-
-
Pearl, L.H.1
-
6
-
-
1542298267
-
Combinatorial attack on multistep oncogenesis by inhibiting the Hsp90 molecular chaperone
-
Workman, P. Combinatorial attack on multistep oncogenesis by inhibiting the Hsp90 molecular chaperone. Cancer Lett. 206, 149-157 (2004).
-
(2004)
Cancer Lett.
, vol.206
, pp. 149-157
-
-
Workman, P.1
-
7
-
-
0036931438
-
Activation of the ATPase activity of Hsp90 by the stress-regulated co-chaperone Aha1
-
Panaretou, B. et al. Activation of the ATPase activity of Hsp90 by the stress-regulated co-chaperone Aha1. Mol. Cell 10, 1307-1318 (2002).
-
(2002)
Mol. Cell
, vol.10
, pp. 1307-1318
-
-
Panaretou, B.1
-
8
-
-
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
-
10
-
-
0029075280
-
Binding of p23 and hsp90 during assembly with the progesterone receptor
-
Johnson, J. L. & Toft, D. O. Binding of p23 and hsp90 during assembly with the progesterone receptor. Mol. Endocrinol. 9, 670-678 (1995).
-
(1995)
Mol. Endocrinol.
, vol.9
, pp. 670-678
-
-
Johnson, J.L.1
Toft, D.O.2
-
11
-
-
0031832233
-
SBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23 proteins
-
Fang, Y., Fliss, A. E., Rao, J. & Caplan, A. J. SBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23 proteins. Mol. Cell. Biol. 18, 3727-3734 (1998).
-
(1998)
Mol. Cell. Biol.
, vol.18
, pp. 3727-3734
-
-
Fang, Y.1
Fliss, A.E.2
Rao, J.3
Caplan, A.J.4
-
12
-
-
0030938717
-
Nucleotides and two functional states of hsp90
-
Sullivan, W. et al. Nucleotides and two functional states of hsp90. J. Biol. Chem. 272, 8007-8012 (1997).
-
(1997)
J. Biol. Chem.
, vol.272
, pp. 8007-8012
-
-
Sullivan, W.1
-
13
-
-
10644265069
-
Co-chaperone regulation of conformational switching in the Hsp90 ATPase cycle
-
Siligardi, G. et al. Co-chaperone regulation of conformational switching in the Hsp90 ATPase cycle. J. Biol. Chem. 279, 51989-51998 (2004).
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 51989-51998
-
-
Siligardi, G.1
-
14
-
-
0036303385
-
Stimulation of the weak ATPase activity of human Hsp90 by a client protein
-
McLaughlin, S. H., Smith, H. W. & Jackson, S. E. Stimulation of the weak ATPase activity of human Hsp90 by a client protein. J. Mol. Biol. 315, 787-798 (2002).
-
(2002)
J. Mol. Biol.
, vol.315
, pp. 787-798
-
-
McLaughlin, S.H.1
Smith, H.W.2
Jackson, S.E.3
-
15
-
-
4444291743
-
The co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle
-
Richter, K., Walter, S. & Buchner, J. The co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle. J. Mol. Biol. 342, 1403-1413 (2004).
-
(2004)
J. Mol. Biol.
, vol.342
, pp. 1403-1413
-
-
Richter, K.1
Walter, S.2
Buchner, J.3
-
16
-
-
0031871101
-
Studies with purified chaperones advance the understanding of the mechanism of glucocorticoid receptor hsp90 heterocomplex assembly
-
Pratt, W. B. & Dittmar, K. D. Studies with purified chaperones advance the understanding of the mechanism of glucocorticoid receptor hsp90 heterocomplex assembly. Trends Endocrinol. Metab. 9, 244-252 (1998).
-
(1998)
Trends Endocrinol. Metab.
, vol.9
, pp. 244-252
-
-
Pratt, W.B.1
Dittmar, K.D.2
-
17
-
-
0034329452
-
Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23
-
Young, J. C. & Hartl, 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
Hartl, F.U.2
-
18
-
-
0033741503
-
Dimerization and N-terminal domain proximity underlie the function of the molecular chaperone heat shock protein 90
-
Chadli, A. et al. Dimerization and N-terminal domain proximity underlie the function of the molecular chaperone heat shock protein 90. Proc. Natl Acad. Sci. USA 97, 12524-12529 (2000).
-
(2000)
Proc. Natl Acad. Sci. USA
, vol.97
, pp. 12524-12529
-
-
Chadli, A.1
-
19
-
-
0034663806
-
The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains
-
Prodromou, C. et al. The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains. EMBO J. 19, 4383-4392 (2000).
-
(2000)
EMBO J.
, vol.19
, pp. 4383-4392
-
-
Prodromou, C.1
-
20
-
-
17044403753
-
Structures of the N-terminal and middle domains of E. coli Hsp90 and conformation changes upon ADP binding
-
Huai, Q. et al. Structures of the N-terminal and middle domains of E. coli Hsp90 and conformation changes upon ADP binding. Structure 13, 579-590 (2005).
-
(2005)
Structure
, vol.13
, pp. 579-590
-
-
Huai, Q.1
-
21
-
-
8544249185
-
Ligand-induced conformational shift in the N-terminal domain of GRP94, an Hsp90 chaperone
-
Immormino, R. M. et al. Ligand-induced conformational shift in the N-terminal domain of GRP94, an Hsp90 chaperone. J. Biol. Chem. 279, 46162-46171 (2004).
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 46162-46171
-
-
Immormino, R.M.1
-
22
-
-
7944225978
-
Independent ATPase activity of Hsp90 subunits creates a flexible assembly platform
-
McLaughlin, S. H., Ventouras, L. A., Lobbezoo, B. & Jackson, S. E. Independent ATPase activity of Hsp90 subunits creates a flexible assembly platform. J. Mol. Biol. 344, 813-826 (2004).
-
(2004)
J. Mol. Biol.
, vol.344
, pp. 813-826
-
-
McLaughlin, S.H.1
Ventouras, L.A.2
Lobbezoo, B.3
Jackson, S.E.4
-
23
-
-
0030462612
-
Two eukaryote-specific regions of Hsp82 are dispensable for its viability and signal transduction functions in yeast
-
Louvion, J. F., Warth, R. & Picard, D. Two eukaryote-specific regions of Hsp82 are dispensable for its viability and signal transduction functions in yeast. Proc. Natl Acad. Sci. USA 93, 13937-13942 (1996).
-
(1996)
Proc. Natl Acad. Sci. USA
, vol.93
, pp. 13937-13942
-
-
Louvion, J.F.1
Warth, R.2
Picard, D.3
-
24
-
-
0030901877
-
A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone
-
Prodromou, C., Roe, S. M., Piper, P. W. & Pearl, L. H. A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone. Nature Struct. Biol. 4, 477-482 (1997).
-
(1997)
Nature Struct. Biol.
, vol.4
, pp. 477-482
-
-
Prodromou, C.1
Roe, S.M.2
Piper, P.W.3
Pearl, L.H.4
-
25
-
-
0037352446
-
Structural and functional analysis of the middle segment of Hsp90: Implications for ATP hydrolysis and client-protein and co-chaperone interactions
-
Meyer, P. et al. Structural and functional analysis of the middle segment of Hsp90: Implications for ATP hydrolysis and client-protein and co-chaperone interactions. Mol. Cell 11, 647-658 (2003).
-
(2003)
Mol. Cell
, vol.11
, pp. 647-658
-
-
Meyer, P.1
-
26
-
-
0034725641
-
Crystal structure and activity of human p23, a heat shock protein 90 co-chaperone
-
Weaver, A. J., Sullivan, W. P., Felts, S. J., Owen, B. A. & Toft, D. O. Crystal structure and activity of human p23, a heat shock protein 90 co-chaperone. J. Biol. Chem. 275, 23045-23052 (2000).
-
(2000)
J. Biol. Chem.
, vol.275
, pp. 23045-23052
-
-
Weaver, A.J.1
Sullivan, W.P.2
Felts, S.J.3
Owen, B.A.4
Toft, D.O.5
-
27
-
-
0031444238
-
Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone
-
Prodromou, C. et al. Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell 90, 65-75 (1997).
-
(1997)
Cell
, vol.90
, pp. 65-75
-
-
Prodromou, C.1
-
28
-
-
0031005361
-
Crystal structure of an Hsp90-geldanamycin complex: Targetting of a protein chaperone by an antitumor agent
-
Stebbins, C. E. et al. Crystal structure of an Hsp90-geldanamycin complex: Targetting of a protein chaperone by an antitumor agent. Cell 89, 239-250 (1997).
-
(1997)
Cell
, vol.89
, pp. 239-250
-
-
Stebbins, C.E.1
-
29
-
-
0032959590
-
The structural basis for inhibition of the Hsp90 molecular chaperone, by the anti-tumour antibiotics radicicol and geldanamycin
-
Roe, S. M. et al. The structural basis for inhibition of the Hsp90 molecular chaperone, by the anti-tumour antibiotics radicicol and geldanamycin. J. Med. Chem. 42, 260-266 (1999).
-
(1999)
J. Med. Chem.
, vol.42
, pp. 260-266
-
-
Roe, S.M.1
-
30
-
-
20644448390
-
The identification, synthesis, protein crystal structure and in vitro biochemical evaluation of a new 3,4-diarylpyrazole class of Hsp90 inhibitors
-
Cheung, K. M. et al. The identification, synthesis, protein crystal structure and in vitro biochemical evaluation of a new 3,4-diarylpyrazole class of Hsp90 inhibitors. Bioorg. Med. Chem. Lett. 15, 3338-3343 (2005).
-
(2005)
Bioorg. Med. Chem. Lett.
, vol.15
, pp. 3338-3343
-
-
Cheung, K.M.1
-
31
-
-
3042637928
-
Structure-activity relationships in purine-based inhibitor binding to HSP90 isoforms
-
Wright, L. et al. Structure-activity relationships in purine-based inhibitor binding to HSP90 isoforms. Chem. Biol. 11, 775-785 (2004).
-
(2004)
Chem. Biol.
, vol.11
, pp. 775-785
-
-
Wright, L.1
-
32
-
-
2942533020
-
The crystal structure of the carboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site
-
Harris, S. F., Shiau, A. K. & Agard, D. A. The crystal structure of the carboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site. Structure 12, 1087-1097 (2004).
-
(2004)
Structure
, vol.12
, pp. 1087-1097
-
-
Harris, S.F.1
Shiau, A.K.2
Agard, D.A.3
-
33
-
-
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
-
34
-
-
0027359404
-
Isolation of Hsp90 mutants by screening for decreased steroid receptor function
-
Bohen, S. P. & Yamamoto, K. R. Isolation of Hsp90 mutants by screening for decreased steroid receptor function. Proc. Natl Acad. Sci. USA 90, 11424-11428 (1993).
-
(1993)
Proc. Natl Acad. Sci. USA
, vol.90
, pp. 11424-11428
-
-
Bohen, S.P.1
Yamamoto, K.R.2
-
35
-
-
0029037110
-
Mutational analysis of Hsp90 function: Interactions with a steroid receptor and a protein kinase
-
Nathan, D. F. & Lindquist, S. Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase. Mol. Cell. Biol. 15, 3917-3925 (1995).
-
(1995)
Mol. Cell. Biol.
, vol.15
, pp. 3917-3925
-
-
Nathan, D.F.1
Lindquist, S.2
-
36
-
-
0033515522
-
Transformation of MutL by ATP binding and hydrolysis: A switch in DNA mismatch repair
-
Ban, C., Junop, M. & Yang, W. Transformation of MutL by ATP binding and hydrolysis: a switch in DNA mismatch repair. Cell 97, 85-97 (1999).
-
(1999)
Cell
, vol.97
, pp. 85-97
-
-
Ban, C.1
Junop, M.2
Yang, W.3
-
37
-
-
0026428621
-
Crystal structure of an N-terminal fragment of the DNA gyrase B protein
-
Wigley, D. B., Davies, G. J., Dodson, E. J., Maxwell, A. & Dodson, G. Crystal structure of an N-terminal fragment of the DNA gyrase B protein. Nature 351, 624-629 (1991).
-
(1991)
Nature
, vol.351
, pp. 624-629
-
-
Wigley, D.B.1
Davies, G.J.2
Dodson, E.J.3
Maxwell, A.4
Dodson, G.5
-
38
-
-
10744221887
-
Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery
-
Meyer, P. et al. Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery. EMBO J. 23, 511-519 (2004).
-
(2004)
EMBO J.
, vol.23
, pp. 511-519
-
-
Meyer, P.1
-
39
-
-
0141592432
-
Genetic dissection of p23, an Hsp90 cochaperone, reveals a distinct surface involved in estrogen receptor signaling
-
Oxelmark, E. et al. Genetic dissection of p23, an Hsp90 cochaperone, reveals a distinct surface involved in estrogen receptor signaling. J. Biol. Chem. 278, 36547-36555 (2003).
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 36547-36555
-
-
Oxelmark, E.1
-
40
-
-
0037593900
-
Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone
-
Lotz, G. P., Lin, H., Harst, A. & Obermann, W. M. J. Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity 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.J.4
-
41
-
-
18844406200
-
Aha1 competes with Hop, p50 and p23 for binding to the molecular chaperone Hsp90 and contributes to kinase and hormone receptor activation
-
Harst, A., Lin, H. & Obermann, W. M. Aha1 competes with Hop, p50 and p23 for binding to the molecular chaperone Hsp90 and contributes to kinase and hormone receptor activation. Biochem. J. 387, 789-796 (2005).
-
(2005)
Biochem. J.
, vol.387
, pp. 789-796
-
-
Harst, A.1
Lin, H.2
Obermann, W.M.3
-
42
-
-
3042598511
-
Biochemical and structural studies of the interaction of Cdc37 with Hsp90
-
Zhang, W. et al. Biochemical and structural studies of the interaction of Cdc37 with Hsp90. J. Mol. Biol. 340, 891-907 (2004).
-
(2004)
J. Mol. Biol.
, vol.340
, pp. 891-907
-
-
Zhang, W.1
-
43
-
-
0346037322
-
N-terminal residues regulate the catalytic efficiency of the Hsp90 ATPase cycle
-
Richter, K., Reinstein, J. & Buchner, J. N-terminal residues regulate the catalytic efficiency of the Hsp90 ATPase cycle. J. Biol. Chem. 277, 44905-44910 (2002).
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 44905-44910
-
-
Richter, K.1
Reinstein, J.2
Buchner, J.3
-
44
-
-
0742269688
-
cdc37
-
cdc37. Cell 116, 87-98 (2004).
-
(2004)
Cell
, vol.116
, pp. 87-98
-
-
Roe, S.M.1
|