-
1
-
-
33646176246
-
Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex
-
Ali M.M., Roe S.M., Vaughan C.K., Meyer P., Panaretou B., Piper P.W., Prodromou C., Pearl L.H. Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex. Nature 2006, 440:1013-1017.
-
(2006)
Nature
, vol.440
, pp. 1013-1017
-
-
Ali, M.M.1
Roe, S.M.2
Vaughan, C.K.3
Meyer, P.4
Panaretou, B.5
Piper, P.W.6
Prodromou, C.7
Pearl, L.H.8
-
2
-
-
9144261127
-
Geldanamycin and 17-allylamino-17-demethoxygeldanamycin potentiate the in vitro and in vivo radiation response of cervical tumor cells via the heat shock protein 90-mediated intracellular signaling and cytotoxicity
-
Bisht K.S., Bradbury C.M., Mattson D., Kaushal A., Sowers A., Markovina S., Ortiz K.L., Sieck L.K., Isaacs J.S., Brechbiel M.W., et al. Geldanamycin and 17-allylamino-17-demethoxygeldanamycin potentiate the in vitro and in vivo radiation response of cervical tumor cells via the heat shock protein 90-mediated intracellular signaling and cytotoxicity. Cancer Res. 2003, 63:8984-8995.
-
(2003)
Cancer Res.
, vol.63
, pp. 8984-8995
-
-
Bisht, K.S.1
Bradbury, C.M.2
Mattson, D.3
Kaushal, A.4
Sowers, A.5
Markovina, S.6
Ortiz, K.L.7
Sieck, L.K.8
Isaacs, J.S.9
Brechbiel, M.W.10
-
3
-
-
80054756986
-
The role of p23, Hop, immunophilins, and other co-chaperones in regulating Hsp90 function
-
Cox M.B., Johnson J.L. The role of p23, Hop, immunophilins, and other co-chaperones in regulating Hsp90 function. Methods Mol. Biol. 2011, 787:45-66.
-
(2011)
Methods Mol. Biol.
, vol.787
, pp. 45-66
-
-
Cox, M.B.1
Johnson, J.L.2
-
4
-
-
51049093018
-
Intra- and intermonomer interactions are required to synergistically facilitate ATP hydrolysis in Hsp90
-
Cunningham C.N., Krukenberg K.A., Agard D.A. Intra- and intermonomer interactions are required to synergistically facilitate ATP hydrolysis in Hsp90. J. Biol. Chem. 2008, 283:21170-21178.
-
(2008)
J. Biol. Chem.
, vol.283
, pp. 21170-21178
-
-
Cunningham, C.N.1
Krukenberg, K.A.2
Agard, D.A.3
-
5
-
-
79960452274
-
Global functional map of the p23 molecular chaperone reveals an extensive cellular network
-
Echtenkamp F.J., Zelin E., Oxelmark E., Woo J.I., Andrews B.J., Garabedian M., Freeman B.C. Global functional map of the p23 molecular chaperone reveals an extensive cellular network. Mol. Cell 2011, 43:229-241.
-
(2011)
Mol. Cell
, vol.43
, pp. 229-241
-
-
Echtenkamp, F.J.1
Zelin, E.2
Oxelmark, E.3
Woo, J.I.4
Andrews, B.J.5
Garabedian, M.6
Freeman, B.C.7
-
6
-
-
59449095866
-
Farnesylation of Ydj1 is required for in vivo interaction with Hsp90 client proteins
-
Flom G.A., Lemieszek M., Fortunato E.A., Johnson J.L. Farnesylation of Ydj1 is required for in vivo interaction with Hsp90 client proteins. Mol. Biol. Cell 2008, 19:5249-5258.
-
(2008)
Mol. Biol. Cell
, vol.19
, pp. 5249-5258
-
-
Flom, G.A.1
Lemieszek, M.2
Fortunato, E.A.3
Johnson, J.L.4
-
7
-
-
0027073107
-
Genetic dissection of the signaling domain of a mammalian steroid receptor in yeast
-
Garabedian M.J., Yamamoto K.R. Genetic dissection of the signaling domain of a mammalian steroid receptor in yeast. Mol. Biol. Cell 1992, 3:1245-1257.
-
(1992)
Mol. Biol. Cell
, vol.3
, pp. 1245-1257
-
-
Garabedian, M.J.1
Yamamoto, K.R.2
-
8
-
-
0142215475
-
Global analysis of protein expression in yeast
-
Ghaemmaghami S., Huh W.K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Global analysis of protein expression in yeast. Nature 2003, 425:737-741.
-
(2003)
Nature
, vol.425
, pp. 737-741
-
-
Ghaemmaghami, S.1
Huh, W.K.2
Bower, K.3
Howson, R.W.4
Belle, A.5
Dephoure, N.6
O'Shea, E.K.7
Weissman, J.S.8
-
9
-
-
61949349758
-
Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90
-
Hessling M., Richter K., Buchner J. Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90. Nat. Struct. Mol. Biol. 2009, 16:287-293.
-
(2009)
Nat. Struct. Mol. Biol.
, vol.16
, pp. 287-293
-
-
Hessling, M.1
Richter, K.2
Buchner, J.3
-
11
-
-
0035110553
-
Activation of heat shock transcription factor in yeast is not influenced by the levels of expression of heat shock proteins
-
Hjorth-Sørensen B., Hoffmann E.R., Lissin N.M., Sewell A.K., Jakobsen B.K. Activation of heat shock transcription factor in yeast is not influenced by the levels of expression of heat shock proteins. Mol. Microbiol. 2001, 39:914-923.
-
(2001)
Mol. Microbiol.
, vol.39
, pp. 914-923
-
-
Hjorth-Sørensen, B.1
Hoffmann, E.R.2
Lissin, N.M.3
Sewell, A.K.4
Jakobsen, B.K.5
-
12
-
-
40449089789
-
Silencing of HSP90 cochaperone AHA1 expression decreases client protein activation and increases cellular sensitivity to the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin
-
Holmes J.L., Sharp S.Y., Hobbs S., Workman P. Silencing of HSP90 cochaperone AHA1 expression decreases client protein activation and increases cellular sensitivity to the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin. Cancer Res. 2008, 68:1188-1197.
-
(2008)
Cancer Res.
, vol.68
, pp. 1188-1197
-
-
Holmes, J.L.1
Sharp, S.Y.2
Hobbs, S.3
Workman, P.4
-
13
-
-
3943099375
-
Protein modification by SUMO
-
Johnson E.S. Protein modification by SUMO. Annu. Rev. Biochem. 2004, 73:355-382.
-
(2004)
Annu. Rev. Biochem.
, vol.73
, pp. 355-382
-
-
Johnson, E.S.1
-
14
-
-
0141484615
-
A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors
-
Kamal A., Thao L., Sensintaffar J., Zhang L., Boehm M.F., Fritz L.C., Burrows F.J. A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors. Nature 2003, 425:407-410.
-
(2003)
Nature
, vol.425
, pp. 407-410
-
-
Kamal, A.1
Thao, L.2
Sensintaffar, J.3
Zhang, L.4
Boehm, M.F.5
Fritz, L.C.6
Burrows, F.J.7
-
15
-
-
0030745769
-
Cdc37 is a molecular chaperone with specific functions in signal transduction
-
Kimura Y., Rutherford S.L., Miyata Y., Yahara I., Freeman B.C., Yue L., Morimoto R.I., Lindquist S. Cdc37 is a molecular chaperone with specific functions in signal transduction. Genes Dev. 1997, 11:1775-1785.
-
(1997)
Genes Dev.
, vol.11
, pp. 1775-1785
-
-
Kimura, Y.1
Rutherford, S.L.2
Miyata, Y.3
Yahara, I.4
Freeman, B.C.5
Yue, L.6
Morimoto, R.I.7
Lindquist, S.8
-
16
-
-
77949438155
-
Biological and structural basis for Aha1 regulation of Hsp90 ATPase activity in maintaining proteostasis in the human disease cystic fibrosis
-
Koulov A.V., LaPointe P., Lu B., Razvi A., Coppinger J., Dong M.Q., Matteson J., Laister R., Arrowsmith C., Yates J.R., Balch W.E. Biological and structural basis for Aha1 regulation of Hsp90 ATPase activity in maintaining proteostasis in the human disease cystic fibrosis. Mol. Biol. Cell 2010, 21:871-884.
-
(2010)
Mol. Biol. Cell
, vol.21
, pp. 871-884
-
-
Koulov, A.V.1
LaPointe, P.2
Lu, B.3
Razvi, A.4
Coppinger, J.5
Dong, M.Q.6
Matteson, J.7
Laister, R.8
Arrowsmith, C.9
Yates, J.R.10
Balch, W.E.11
-
17
-
-
84857042271
-
The Hsp90 chaperone machinery: conformational dynamics and regulation by co-chaperones
-
Li J., Soroka J., Buchner J. The Hsp90 chaperone machinery: conformational dynamics and regulation by co-chaperones. Biochim. Biophys. Acta 2012, 1823:624-635.
-
(2012)
Biochim. Biophys. Acta
, vol.1823
, pp. 624-635
-
-
Li, J.1
Soroka, J.2
Buchner, J.3
-
18
-
-
84875225582
-
Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle
-
Li J., Richter K., Reinstein J., Buchner J. Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle. Nat. Struct. Mol. Biol. 2013, 20:326-331.
-
(2013)
Nat. Struct. Mol. Biol.
, vol.20
, pp. 326-331
-
-
Li, J.1
Richter, K.2
Reinstein, J.3
Buchner, J.4
-
19
-
-
0032401771
-
Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome
-
Loo M.A., Jensen T.J., Cui L., Hou Y., Chang X.B., Riordan J.R. Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome. EMBO J. 1998, 17:6879-6887.
-
(1998)
EMBO J.
, vol.17
, pp. 6879-6887
-
-
Loo, M.A.1
Jensen, T.J.2
Cui, L.3
Hou, Y.4
Chang, X.B.5
Riordan, J.R.6
-
20
-
-
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. 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. 2003, 278:17228-17235.
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 17228-17235
-
-
Lotz, G.P.1
Lin, H.2
Harst, A.3
Obermann, W.M.4
-
22
-
-
77955506092
-
Gymnastics of molecular chaperones
-
Mayer M.P. Gymnastics of molecular chaperones. Mol. Cell 2010, 39:321-331.
-
(2010)
Mol. Cell
, vol.39
, pp. 321-331
-
-
Mayer, M.P.1
-
23
-
-
34848926209
-
Diverse cellular functions of the Hsp90 molecular chaperone uncovered using systems approaches
-
McClellan A.J., Xia Y., Deutschbauer A.M., Davis R.W., Gerstein M., Frydman J. Diverse cellular functions of the Hsp90 molecular chaperone uncovered using systems approaches. Cell 2007, 131:121-135.
-
(2007)
Cell
, vol.131
, pp. 121-135
-
-
McClellan, A.J.1
Xia, Y.2
Deutschbauer, A.M.3
Davis, R.W.4
Gerstein, M.5
Frydman, J.6
-
24
-
-
0037352446
-
Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions
-
Meyer P., Prodromou C., Hu B., Vaughan C., Roe S.M., Panaretou B., Piper P.W., Pearl L.H. Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions. Mol. Cell 2003, 11:647-658.
-
(2003)
Mol. Cell
, vol.11
, pp. 647-658
-
-
Meyer, P.1
Prodromou, C.2
Hu, B.3
Vaughan, C.4
Roe, S.M.5
Panaretou, B.6
Piper, P.W.7
Pearl, L.H.8
-
25
-
-
84857044092
-
Post-translational modifications of Hsp90 and their contributions to chaperone regulation
-
Mollapour M., Neckers L. Post-translational modifications of Hsp90 and their contributions to chaperone regulation. Biochim. Biophys. Acta 2012, 1823:648-655.
-
(2012)
Biochim. Biophys. Acta
, vol.1823
, pp. 648-655
-
-
Mollapour, M.1
Neckers, L.2
-
26
-
-
75949112264
-
Swe1Wee1-dependent tyrosine phosphorylation of Hsp90 regulates distinct facets of chaperone function
-
Mollapour M., Tsutsumi S., Donnelly A.C., Beebe K., Tokita M.J., Lee M.J., Lee S., Morra G., Bourboulia D., Scroggins B.T., et al. Swe1Wee1-dependent tyrosine phosphorylation of Hsp90 regulates distinct facets of chaperone function. Mol. Cell 2010, 37:333-343.
-
(2010)
Mol. Cell
, vol.37
, pp. 333-343
-
-
Mollapour, M.1
Tsutsumi, S.2
Donnelly, A.C.3
Beebe, K.4
Tokita, M.J.5
Lee, M.J.6
Lee, S.7
Morra, G.8
Bourboulia, D.9
Scroggins, B.T.10
-
27
-
-
80053425012
-
Casein kinase 2 phosphorylation of Hsp90 threonine 22 modulates chaperone function and drug sensitivity
-
Mollapour M., Tsutsumi S., Kim Y.S., Trepel J., Neckers L. Casein kinase 2 phosphorylation of Hsp90 threonine 22 modulates chaperone function and drug sensitivity. Oncotarget 2011, 2:407-417.
-
(2011)
Oncotarget
, vol.2
, pp. 407-417
-
-
Mollapour, M.1
Tsutsumi, S.2
Kim, Y.S.3
Trepel, J.4
Neckers, L.5
-
28
-
-
79952665421
-
Threonine 22 phosphorylation attenuates Hsp90 interaction with cochaperones and affects its chaperone activity
-
Mollapour M., Tsutsumi S., Truman A.W., Xu W., Vaughan C.K., Beebe K., Konstantinova A., Vourganti S., Panaretou B., Piper P.W., et al. Threonine 22 phosphorylation attenuates Hsp90 interaction with cochaperones and affects its chaperone activity. Mol. Cell 2011, 41:672-681.
-
(2011)
Mol. Cell
, vol.41
, pp. 672-681
-
-
Mollapour, M.1
Tsutsumi, S.2
Truman, A.W.3
Xu, W.4
Vaughan, C.K.5
Beebe, K.6
Konstantinova, A.7
Vourganti, S.8
Panaretou, B.9
Piper, P.W.10
-
29
-
-
84879412911
-
C-terminal phosphorylation of Hsp70 and Hsp90 regulates alternate binding to co-chaperones CHIP and HOP to determine cellular protein folding/degradation balances
-
Muller P., Ruckova E., Halada P., Coates P.J., Hrstka R., Lane D.P., Vojtesek B. C-terminal phosphorylation of Hsp70 and Hsp90 regulates alternate binding to co-chaperones CHIP and HOP to determine cellular protein folding/degradation balances. Oncogene 2013, 32:3101-3110.
-
(2013)
Oncogene
, vol.32
, pp. 3101-3110
-
-
Muller, P.1
Ruckova, E.2
Halada, P.3
Coates, P.J.4
Hrstka, R.5
Lane, D.P.6
Vojtesek, B.7
-
30
-
-
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. 1995, 15:3917-3925.
-
(1995)
Mol. Cell. Biol.
, vol.15
, pp. 3917-3925
-
-
Nathan, D.F.1
Lindquist, S.2
-
31
-
-
84855457952
-
Hsp90 molecular chaperone inhibitors: are we there yetα
-
Neckers L., Workman P. Hsp90 molecular chaperone inhibitors: are we there yetα. Clin. Cancer Res. 2012, 18:64-76.
-
(2012)
Clin. Cancer Res.
, vol.18
, pp. 64-76
-
-
Neckers, L.1
Workman, P.2
-
32
-
-
0032538995
-
In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis
-
Obermann W.M., 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. 1998, 143:901-910.
-
(1998)
J. Cell Biol.
, vol.143
, pp. 901-910
-
-
Obermann, W.M.1
Sondermann, H.2
Russo, A.A.3
Pavletich, N.P.4
Hartl, F.U.5
-
33
-
-
0032541344
-
ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo
-
Panaretou B., Prodromou C., Roe S.M., O'Brien R., Ladbury J.E., Piper P.W., Pearl L.H. ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo. EMBO J. 1998, 17:4829-4836.
-
(1998)
EMBO J.
, vol.17
, pp. 4829-4836
-
-
Panaretou, B.1
Prodromou, C.2
Roe, S.M.3
O'Brien, R.4
Ladbury, J.E.5
Piper, P.W.6
Pearl, L.H.7
-
34
-
-
0036931438
-
Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1
-
Panaretou B., Siligardi G., Meyer P., Maloney A., Sullivan J.K., Singh S., Millson S.H., Clarke P.A., Naaby-Hansen S., Stein R., et al. Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1. Mol. Cell 2002, 10:1307-1318.
-
(2002)
Mol. Cell
, vol.10
, pp. 1307-1318
-
-
Panaretou, B.1
Siligardi, G.2
Meyer, P.3
Maloney, A.4
Sullivan, J.K.5
Singh, S.6
Millson, S.H.7
Clarke, P.A.8
Naaby-Hansen, S.9
Stein, R.10
-
35
-
-
4744360999
-
A proteome-wide approach identifies sumoylated substrate proteins in yeast
-
Panse V.G., Hardeland U., Werner T., Kuster B., Hurt E. A proteome-wide approach identifies sumoylated substrate proteins in yeast. J. Biol. Chem. 2004, 279:41346-41351.
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 41346-41351
-
-
Panse, V.G.1
Hardeland, U.2
Werner, T.3
Kuster, B.4
Hurt, E.5
-
36
-
-
0036810352
-
Heat-shock protein 90, a chaperone for folding and regulation
-
Picard D. Heat-shock protein 90, a chaperone for folding and regulation. Cell. Mol. Life Sci. 2002, 59:1640-1648.
-
(2002)
Cell. Mol. Life Sci.
, vol.59
, pp. 1640-1648
-
-
Picard, D.1
-
37
-
-
56749104316
-
NSF, Unc-18-1, dynamin-1 and HSP90 are inclusion body components in neuronal intranuclear inclusion disease identified by anti-SUMO-1-immunocapture
-
Pountney D.L., Raftery M.J., Chegini F., Blumbergs P.C., Gai W.P. NSF, Unc-18-1, dynamin-1 and HSP90 are inclusion body components in neuronal intranuclear inclusion disease identified by anti-SUMO-1-immunocapture. Acta Neuropathol. 2008, 116:603-614.
-
(2008)
Acta Neuropathol.
, vol.116
, pp. 603-614
-
-
Pountney, D.L.1
Raftery, M.J.2
Chegini, F.3
Blumbergs, P.C.4
Gai, W.P.5
-
38
-
-
84857051938
-
The 'active life' of Hsp90 complexes
-
Prodromou C. The 'active life' of Hsp90 complexes. Biochim. Biophys. Acta 2012, 1823:614-623.
-
(2012)
Biochim. Biophys. Acta
, vol.1823
, pp. 614-623
-
-
Prodromou, C.1
-
39
-
-
0034663806
-
The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains
-
Prodromou C., Panaretou B., Chohan S., Siligardi G., O'Brien R., Ladbury J.E., Roe S.M., Piper P.W., Pearl L.H. The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains. EMBO J. 2000, 19:4383-4392.
-
(2000)
EMBO J.
, vol.19
, pp. 4383-4392
-
-
Prodromou, C.1
Panaretou, B.2
Chohan, S.3
Siligardi, G.4
O'Brien, R.5
Ladbury, J.E.6
Roe, S.M.7
Piper, P.W.8
Pearl, L.H.9
-
40
-
-
79953202216
-
Enforced N-domain proximity stimulates Hsp90 ATPase activity and is compatible with function in vivo
-
Pullen L., Bolon D.N. Enforced N-domain proximity stimulates Hsp90 ATPase activity and is compatible with function in vivo. J. Biol. Chem. 2011, 286:11091-11098.
-
(2011)
J. Biol. Chem.
, vol.286
, pp. 11091-11098
-
-
Pullen, L.1
Bolon, D.N.2
-
41
-
-
75949106173
-
Asymmetric activation of the hsp90 dimer by its cochaperone aha1
-
Retzlaff M., Hagn F., Mitschke L., Hessling M., Gugel F., Kessler H., Richter K., Buchner J. Asymmetric activation of the hsp90 dimer by its cochaperone aha1. Mol. Cell 2010, 37:344-354.
-
(2010)
Mol. Cell
, vol.37
, pp. 344-354
-
-
Retzlaff, M.1
Hagn, F.2
Mitschke, L.3
Hessling, M.4
Gugel, F.5
Kessler, H.6
Richter, K.7
Buchner, J.8
-
42
-
-
0035877693
-
The small ubiquitin-like modifier-1 (SUMO-1) consensus sequence mediates Ubc9 binding and is essential for SUMO-1 modification
-
Sampson D.A., Wang M., Matunis M.J. The small ubiquitin-like modifier-1 (SUMO-1) consensus sequence mediates Ubc9 binding and is essential for SUMO-1 modification. J. Biol. Chem. 2001, 276:21664-21669.
-
(2001)
J. Biol. Chem.
, vol.276
, pp. 21664-21669
-
-
Sampson, D.A.1
Wang, M.2
Matunis, M.J.3
-
43
-
-
33846014703
-
An acetylation site in the middle domain of Hsp90 regulates chaperone function
-
Scroggins B.T., Robzyk K., Wang D., Marcu M.G., Tsutsumi S., Beebe K., Cotter R.J., Felts S., Toft D., Karnitz L., et al. An acetylation site in the middle domain of Hsp90 regulates chaperone function. Mol. Cell 2007, 25:151-159.
-
(2007)
Mol. Cell
, vol.25
, pp. 151-159
-
-
Scroggins, B.T.1
Robzyk, K.2
Wang, D.3
Marcu, M.G.4
Tsutsumi, S.5
Beebe, K.6
Cotter, R.J.7
Felts, S.8
Toft, D.9
Karnitz, L.10
-
44
-
-
33750008686
-
Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements
-
Shiau A.K., Harris S.F., Southworth D.R., Agard D.A. Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements. Cell 2006, 127:329-340.
-
(2006)
Cell
, vol.127
, pp. 329-340
-
-
Shiau, A.K.1
Harris, S.F.2
Southworth, D.R.3
Agard, D.A.4
-
45
-
-
10644265069
-
Co-chaperone regulation of conformational switching in the Hsp90 ATPase cycle
-
Siligardi G., Hu B., Panaretou B., Piper P.W., Pearl L.H., Prodromou C. Co-chaperone regulation of conformational switching in the Hsp90 ATPase cycle. J. Biol. Chem. 2004, 279:51989-51998.
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 51989-51998
-
-
Siligardi, G.1
Hu, B.2
Panaretou, B.3
Piper, P.W.4
Pearl, L.H.5
Prodromou, C.6
-
46
-
-
84857390643
-
Conformational switching of the molecular chaperone Hsp90 via regulated phosphorylation
-
Soroka J., Wandinger S.K., Mäusbacher N., Schreiber T., Richter K., Daub H., Buchner J. Conformational switching of the molecular chaperone Hsp90 via regulated phosphorylation. Mol. Cell 2012, 45:517-528.
-
(2012)
Mol. Cell
, vol.45
, pp. 517-528
-
-
Soroka, J.1
Wandinger, S.K.2
Mäusbacher, N.3
Schreiber, T.4
Richter, K.5
Daub, H.6
Buchner, J.7
-
47
-
-
0031005361
-
Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent
-
Stebbins C.E., Russo A.A., Schneider C., Rosen N., Hartl F.U., Pavletich N.P. Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent. Cell 1997, 89:239-250.
-
(1997)
Cell
, vol.89
, pp. 239-250
-
-
Stebbins, C.E.1
Russo, A.A.2
Schneider, C.3
Rosen, N.4
Hartl, F.U.5
Pavletich, N.P.6
-
48
-
-
84860356248
-
Characterization of the interaction of Aha1 with components of the Hsp90 chaperone machine and client proteins
-
Sun L., Prince T., Manjarrez J.R., Scroggins B.T., Matts R.L. Characterization of the interaction of Aha1 with components of the Hsp90 chaperone machine and client proteins. Biochim. Biophys. Acta 2012, 1823:1092-1101.
-
(2012)
Biochim. Biophys. Acta
, vol.1823
, pp. 1092-1101
-
-
Sun, L.1
Prince, T.2
Manjarrez, J.R.3
Scroggins, B.T.4
Matts, R.L.5
-
49
-
-
77953916528
-
HSP90 at the hub of protein homeostasis: emerging mechanistic insights
-
Taipale M., Jarosz D.F., Lindquist S. HSP90 at the hub of protein homeostasis: emerging mechanistic insights. Nat. Rev. Mol. Cell Biol. 2010, 11:515-528.
-
(2010)
Nat. Rev. Mol. Cell Biol.
, vol.11
, pp. 515-528
-
-
Taipale, M.1
Jarosz, D.F.2
Lindquist, S.3
-
50
-
-
77954945333
-
Targeting the dynamic HSP90 complex in cancer
-
Trepel J., Mollapour M., Giaccone G., Neckers L. Targeting the dynamic HSP90 complex in cancer. Nat. Rev. Cancer 2010, 10:537-549.
-
(2010)
Nat. Rev. Cancer
, vol.10
, pp. 537-549
-
-
Trepel, J.1
Mollapour, M.2
Giaccone, G.3
Neckers, L.4
-
51
-
-
59149107480
-
The SUMO system: an overview
-
Ulrich H.D. The SUMO system: an overview. Methods Mol. Biol. 2009, 497:3-16.
-
(2009)
Methods Mol. Biol.
, vol.497
, pp. 3-16
-
-
Ulrich, H.D.1
-
52
-
-
33747878717
-
Structure of an Hsp90-Cdc37-Cdk4 complex
-
Vaughan C.K., Gohlke U., Sobott F., Good V.M., Ali M.M., Prodromou C., Robinson C.V., Saibil H.R., Pearl L.H. Structure of an Hsp90-Cdc37-Cdk4 complex. Mol. Cell 2006, 23:697-707.
-
(2006)
Mol. Cell
, vol.23
, pp. 697-707
-
-
Vaughan, C.K.1
Gohlke, U.2
Sobott, F.3
Good, V.M.4
Ali, M.M.5
Prodromou, C.6
Robinson, C.V.7
Saibil, H.R.8
Pearl, L.H.9
-
53
-
-
84878710811
-
Contributions of co-chaperones and post-translational modifications towards Hsp90 drug sensitivity
-
Walton-Diaz A., Khan S., Bourboulia D., Trepel J.B., Neckers L., Mollapour M. Contributions of co-chaperones and post-translational modifications towards Hsp90 drug sensitivity. Future Med Chem 2013, 5:1059-1071.
-
(2013)
Future Med Chem
, vol.5
, pp. 1059-1071
-
-
Walton-Diaz, A.1
Khan, S.2
Bourboulia, D.3
Trepel, J.B.4
Neckers, L.5
Mollapour, M.6
-
54
-
-
33750842131
-
Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis
-
Wang X., Venable J., LaPointe P., Hutt D.M., Koulov A.V., Coppinger J., Gurkan C., Kellner W., Matteson J., Plutner H., et al. Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis. Cell 2006, 127:803-815.
-
(2006)
Cell
, vol.127
, pp. 803-815
-
-
Wang, X.1
Venable, J.2
LaPointe, P.3
Hutt, D.M.4
Koulov, A.V.5
Coppinger, J.6
Gurkan, C.7
Kellner, W.8
Matteson, J.9
Plutner, H.10
-
55
-
-
84864910544
-
Dynamic tyrosine phosphorylation modulates cycling of the HSP90-P50(CDC37)-AHA1 chaperone machine
-
Xu W., Mollapour M., Prodromou C., Wang S., Scroggins B.T., Palchick Z., Beebe K., Siderius M., Lee M.J., Couvillon A., et al. Dynamic tyrosine phosphorylation modulates cycling of the HSP90-P50(CDC37)-AHA1 chaperone machine. Mol. Cell 2012, 47:434-443.
-
(2012)
Mol. Cell
, vol.47
, pp. 434-443
-
-
Xu, W.1
Mollapour, M.2
Prodromou, C.3
Wang, S.4
Scroggins, B.T.5
Palchick, Z.6
Beebe, K.7
Siderius, M.8
Lee, M.J.9
Couvillon, A.10
-
56
-
-
6344275303
-
Distinct roles for the Hsp40 and Hsp90 molecular chaperones during cystic fibrosis transmembrane conductance regulator degradation in yeast
-
Youker R.T., Walsh P., Beilharz T., Lithgow T., Brodsky J.L. Distinct roles for the Hsp40 and Hsp90 molecular chaperones during cystic fibrosis transmembrane conductance regulator degradation in yeast. Mol. Biol. Cell 2004, 15:4787-4797.
-
(2004)
Mol. Biol. Cell
, vol.15
, pp. 4787-4797
-
-
Youker, R.T.1
Walsh, P.2
Beilharz, T.3
Lithgow, T.4
Brodsky, J.L.5
-
57
-
-
3543018486
-
Global analyses of sumoylated proteins in Saccharomyces cerevisiae. Induction of protein sumoylation by cellular stresses
-
Zhou W., Ryan J.J., Zhou H. Global analyses of sumoylated proteins in Saccharomyces cerevisiae. Induction of protein sumoylation by cellular stresses. J. Biol. Chem. 2004, 279:32262-32268.
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 32262-32268
-
-
Zhou, W.1
Ryan, J.J.2
Zhou, H.3
-
58
-
-
0032555685
-
Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1
-
Zou J., Guo Y., Guettouche T., Smith D.F., Voellmy R. Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1. Cell 1998, 94:471-480.
-
(1998)
Cell
, vol.94
, pp. 471-480
-
-
Zou, J.1
Guo, Y.2
Guettouche, T.3
Smith, D.F.4
Voellmy, R.5
|