-
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
-
-
84857059172
-
TRAP-1, the mitochondrial Hsp90
-
Altieri D.C., Stein G.S., Lian J.B., Languino L.R. TRAP-1, the mitochondrial Hsp90. Biochim. Biophys. Acta 2012, 1823:767-773.
-
(2012)
Biochim. Biophys. Acta
, vol.1823
, pp. 767-773
-
-
Altieri, D.C.1
Stein, G.S.2
Lian, J.B.3
Languino, L.R.4
-
3
-
-
84859169870
-
The mitochondrial chaperone protein TRAP1 mitigates α-Synuclein toxicity
-
Butler E.K., Voigt A., Lutz A.K., Toegel J.P., Gerhardt E., Karsten P., Falkenburger B., Reinartz A., Winklhofer K.F., Schulz J.B. The mitochondrial chaperone protein TRAP1 mitigates α-Synuclein toxicity. PLoS Genet. 2012, 8:e1002488.
-
(2012)
PLoS Genet.
, vol.8
-
-
Butler, E.K.1
Voigt, A.2
Lutz, A.K.3
Toegel, J.P.4
Gerhardt, E.5
Karsten, P.6
Falkenburger, B.7
Reinartz, A.8
Winklhofer, K.F.9
Schulz, J.B.10
-
4
-
-
0034633963
-
Immunoelectron microscopy provides evidence that tumor necrosis factor receptor-associated protein 1 (TRAP-1) is a mitochondrial protein which also localizes at specific extramitochondrial sites
-
Cechetto J.D., Gupta R.S. Immunoelectron microscopy provides evidence that tumor necrosis factor receptor-associated protein 1 (TRAP-1) is a mitochondrial protein which also localizes at specific extramitochondrial sites. Exp. Cell Res. 2000, 260:30-39.
-
(2000)
Exp. Cell Res.
, vol.260
, pp. 30-39
-
-
Cechetto, J.D.1
Gupta, R.S.2
-
5
-
-
33746660802
-
Comparative genomics and evolution of the HSP90 family of genes across all kingdoms of organisms
-
Chen B., Zhong D., Monteiro A. Comparative genomics and evolution of the HSP90 family of genes across all kingdoms of organisms. BMC Genomics 2006, 7:156.
-
(2006)
BMC Genomics
, vol.7
, pp. 156
-
-
Chen, B.1
Zhong, D.2
Monteiro, A.3
-
6
-
-
84878533362
-
Drosophila Trap1 protects against mitochondrial dysfunction in a PINK1/parkin model of Parkinson's disease
-
Costa A.C., Loh S.H., Martins L.M. Drosophila Trap1 protects against mitochondrial dysfunction in a PINK1/parkin model of Parkinson's disease. Cell Death Dis. 2013, 4:e467.
-
(2013)
Cell Death Dis.
, vol.4
-
-
Costa, A.C.1
Loh, S.H.2
Martins, L.M.3
-
7
-
-
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
-
8
-
-
34948893963
-
Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones
-
Dollins D.E., Warren J.J., Immormino R.M., Gewirth D.T. Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones. Mol. Cell 2007, 28:41-56.
-
(2007)
Mol. Cell
, vol.28
, pp. 41-56
-
-
Dollins, D.E.1
Warren, J.J.2
Immormino, R.M.3
Gewirth, D.T.4
-
9
-
-
80053976720
-
An interaction network predicted from public data as a discovery tool: application to the Hsp90 molecular chaperone machine
-
Echeverría P.C., Bernthaler A., Dupuis P., Mayer B., Picard D. An interaction network predicted from public data as a discovery tool: application to the Hsp90 molecular chaperone machine. PLoS ONE 2011, 6:e26044.
-
(2011)
PLoS ONE
, vol.6
-
-
Echeverría, P.C.1
Bernthaler, A.2
Dupuis, P.3
Mayer, B.4
Picard, D.5
-
10
-
-
0034603178
-
The hsp90-related protein TRAP1 is a mitochondrial protein with distinct functional properties
-
Felts S.J., Owen B.A., Nguyen P., Trepel J., Donner D.B., Toft D.O. The hsp90-related protein TRAP1 is a mitochondrial protein with distinct functional properties. J. Biol. Chem. 2000, 275:3305-3312.
-
(2000)
J. Biol. Chem.
, vol.275
, pp. 3305-3312
-
-
Felts, S.J.1
Owen, B.A.2
Nguyen, P.3
Trepel, J.4
Donner, D.B.5
Toft, D.O.6
-
11
-
-
84873420281
-
Uncovering a region of heat shock protein 90 important for client binding in E. coli and chaperone function in yeast
-
Genest O., Reidy M., Street T.O., Hoskins J.R., Camberg J.L., Agard D.A., Masison D.C., Wickner S. Uncovering a region of heat shock protein 90 important for client binding in E. coli and chaperone function in yeast. Mol. Cell 2013, 49:464-473.
-
(2013)
Mol. Cell
, vol.49
, pp. 464-473
-
-
Genest, O.1
Reidy, M.2
Street, T.O.3
Hoskins, J.R.4
Camberg, J.L.5
Agard, D.A.6
Masison, D.C.7
Wickner, S.8
-
12
-
-
0031585990
-
Characterization of long-range structure in the denatured state of staphylococcal nuclease. I. Paramagnetic relaxation enhancement by nitroxide spin labels
-
Gillespie J.R., Shortle D. Characterization of long-range structure in the denatured state of staphylococcal nuclease. I. Paramagnetic relaxation enhancement by nitroxide spin labels. J. Mol. Biol. 1997, 268:158-169.
-
(1997)
J. Mol. Biol.
, vol.268
, pp. 158-169
-
-
Gillespie, J.R.1
Shortle, D.2
-
13
-
-
79960652801
-
Molecular chaperones in protein folding and proteostasis
-
Hartl F.U., Bracher A., Hayer-Hartl M. Molecular chaperones in protein folding and proteostasis. Nature 2011, 475:324-332.
-
(2011)
Nature
, vol.475
, pp. 324-332
-
-
Hartl, F.U.1
Bracher, A.2
Hayer-Hartl, M.3
-
14
-
-
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
-
15
-
-
0029161506
-
The 23-kDa acidic protein in reticulocyte lysate is the weakly bound component of the hsp foldosome that is required for assembly of the glucocorticoid receptor into a functional heterocomplex with hsp90
-
Hutchison K.A., Stancato L.F., Owens-Grillo J.K., Johnson J.L., Krishna P., Toft D.O., Pratt W.B. The 23-kDa acidic protein in reticulocyte lysate is the weakly bound component of the hsp foldosome that is required for assembly of the glucocorticoid receptor into a functional heterocomplex with hsp90. J. Biol. Chem. 1995, 270:18841-18847.
-
(1995)
J. Biol. Chem.
, vol.270
, pp. 18841-18847
-
-
Hutchison, K.A.1
Stancato, L.F.2
Owens-Grillo, J.K.3
Johnson, J.L.4
Krishna, P.5
Toft, D.O.6
Pratt, W.B.7
-
16
-
-
0028940309
-
Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase. Implications for heat shock in vivo
-
Jakob U., Lilie H., Meyer I., Buchner J. Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase. Implications for heat shock in vivo. J. Biol. Chem. 1995, 270:7288-7294.
-
(1995)
J. Biol. Chem.
, vol.270
, pp. 7288-7294
-
-
Jakob, U.1
Lilie, H.2
Meyer, I.3
Buchner, J.4
-
17
-
-
84859888767
-
DEER distance measurements on proteins
-
Jeschke G. DEER distance measurements on proteins. Annu. Rev. Phys. Chem. 2012, 63:419-446.
-
(2012)
Annu. Rev. Phys. Chem.
, vol.63
, pp. 419-446
-
-
Jeschke, G.1
-
18
-
-
84857048585
-
Evolution and function of diverse Hsp90 homologs and cochaperone proteins
-
Johnson J.L. Evolution and function of diverse Hsp90 homologs and cochaperone proteins. Biochim. Biophys. Acta 2012, 1823:607-613.
-
(2012)
Biochim. Biophys. Acta
, vol.1823
, pp. 607-613
-
-
Johnson, J.L.1
-
19
-
-
84857699267
-
TRAP1 regulation of mitochondrial life or death decision in cancer cells and mitochondria-targeted TRAP1 inhibitors
-
Kang B.H. TRAP1 regulation of mitochondrial life or death decision in cancer cells and mitochondria-targeted TRAP1 inhibitors. BMB Rep. 2012, 45:1-6.
-
(2012)
BMB Rep.
, vol.45
, pp. 1-6
-
-
Kang, B.H.1
-
20
-
-
35348887850
-
Regulation of tumor cell mitochondrial homeostasis by an organelle-specific Hsp90 chaperone network
-
Kang B.H., Plescia J., Dohi T., Rosa J., Doxsey S.J., Altieri D.C. Regulation of tumor cell mitochondrial homeostasis by an organelle-specific Hsp90 chaperone network. Cell 2007, 131:257-270.
-
(2007)
Cell
, vol.131
, pp. 257-270
-
-
Kang, B.H.1
Plescia, J.2
Dohi, T.3
Rosa, J.4
Doxsey, S.J.5
Altieri, D.C.6
-
21
-
-
79551666466
-
N-terminal domain of human Hsp90 triggers binding to the cochaperone p23
-
Karagöz G.E., Duarte A.M., Ippel H., Uetrecht C., Sinnige T., van Rosmalen M., Hausmann J., Heck A.J., Boelens R., Rüdiger S.G. N-terminal domain of human Hsp90 triggers binding to the cochaperone p23. Proc. Natl. Acad. Sci. USA 2011, 108:580-585.
-
(2011)
Proc. Natl. Acad. Sci. USA
, vol.108
, pp. 580-585
-
-
Karagöz, G.E.1
Duarte, A.M.2
Ippel, H.3
Uetrecht, C.4
Sinnige, T.5
van Rosmalen, M.6
Hausmann, J.7
Heck, A.J.8
Boelens, R.9
Rüdiger, S.G.10
-
22
-
-
34548232365
-
Inference of macromolecular assemblies from crystalline state
-
Krissinel E., Henrick K. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 2007, 372:774-797.
-
(2007)
J. Mol. Biol.
, vol.372
, pp. 774-797
-
-
Krissinel, E.1
Henrick, K.2
-
23
-
-
42949147146
-
Multiple conformations of E. coli Hsp90 in solution: insights into the conformational dynamics of Hsp90
-
Krukenberg K.A., Förster F., Rice L.M., Sali A., Agard D.A. Multiple conformations of E. coli Hsp90 in solution: insights into the conformational dynamics of Hsp90. Structure 2008, 16:755-765.
-
(2008)
Structure
, vol.16
, pp. 755-765
-
-
Krukenberg, K.A.1
Förster, F.2
Rice, L.M.3
Sali, A.4
Agard, D.A.5
-
24
-
-
67349184994
-
PH-dependent conformational changes in bacterial Hsp90 reveal a Grp94-like conformation at pH 6 that is highly active in suppression of citrate synthase aggregation
-
Krukenberg K.A., Southworth D.R., Street T.O., Agard D.A. pH-dependent conformational changes in bacterial Hsp90 reveal a Grp94-like conformation at pH 6 that is highly active in suppression of citrate synthase aggregation. J. Mol. Biol. 2009, 390:278-291.
-
(2009)
J. Mol. Biol.
, vol.390
, pp. 278-291
-
-
Krukenberg, K.A.1
Southworth, D.R.2
Street, T.O.3
Agard, D.A.4
-
25
-
-
79955984427
-
Conformational dynamics of the molecular chaperone Hsp90
-
Krukenberg K.A., Street T.O., Lavery L.A., Agard D.A. Conformational dynamics of the molecular chaperone Hsp90. Q. Rev. Biophys. 2011, 44:229-255.
-
(2011)
Q. Rev. Biophys.
, vol.44
, pp. 229-255
-
-
Krukenberg, K.A.1
Street, T.O.2
Lavery, L.A.3
Agard, D.A.4
-
26
-
-
45549104450
-
The ATPase cycle of the mitochondrial Hsp90 analog Trap1
-
Leskovar A., Wegele H., Werbeck N.D., Buchner J., Reinstein J. The ATPase cycle of the mitochondrial Hsp90 analog Trap1. J. Biol. Chem. 2008, 283:11677-11688.
-
(2008)
J. Biol. Chem.
, vol.283
, pp. 11677-11688
-
-
Leskovar, A.1
Wegele, H.2
Werbeck, N.D.3
Buchner, J.4
Reinstein, J.5
-
27
-
-
78650983812
-
Mixed Hsp90-cochaperone complexes are important for the progression of the reaction cycle
-
Li J., Richter K., Buchner J. Mixed Hsp90-cochaperone complexes are important for the progression of the reaction cycle. Nat. Struct. Mol. Biol. 2011, 18:61-66.
-
(2011)
Nat. Struct. Mol. Biol.
, vol.18
, pp. 61-66
-
-
Li, J.1
Richter, K.2
Buchner, J.3
-
28
-
-
84865072277
-
Structure insights into mechanisms of ATP hydrolysis and the activation of human heat-shock protein 90
-
Li J., Sun L., Xu C., Yu F., Zhou H., Zhao Y., Zhang J., Cai J., Mao C., Tang L., et al. Structure insights into mechanisms of ATP hydrolysis and the activation of human heat-shock protein 90. Acta Biochim. Biophys. Sin. (Shanghai) 2012, 44:300-306.
-
(2012)
Acta Biochim. Biophys. Sin. (Shanghai)
, vol.44
, pp. 300-306
-
-
Li, J.1
Sun, L.2
Xu, C.3
Yu, F.4
Zhou, H.5
Zhao, Y.6
Zhang, J.7
Cai, J.8
Mao, C.9
Tang, L.10
-
29
-
-
77957740228
-
Protein folding sculpting evolutionary change
-
Lindquist S. Protein folding sculpting evolutionary change. Cold Spring Harb. Symp. Quant. Biol. 2009, 74:103-108.
-
(2009)
Cold Spring Harb. Symp. Quant. Biol.
, vol.74
, pp. 103-108
-
-
Lindquist, S.1
-
30
-
-
84857475033
-
Folding of Toll-like receptors by the HSP90 paralogue gp96 requires a substrate-specific cochaperone
-
Liu B., Yang Y., Qiu Z., Staron M., Hong F., Li Y., Wu S., Li Y., Hao B., Bona R., et al. Folding of Toll-like receptors by the HSP90 paralogue gp96 requires a substrate-specific cochaperone. Nat. Commun. 2010, 1:79.
-
(2010)
Nat. Commun.
, vol.1
, pp. 79
-
-
Liu, B.1
Yang, Y.2
Qiu, Z.3
Staron, M.4
Hong, F.5
Li, Y.6
Wu, S.7
Li, Y.8
Hao, B.9
Bona, R.10
-
31
-
-
77953012604
-
Heat shock protein 90 in neurodegenerative diseases
-
Luo W., Sun W., Taldone T., Rodina A., Chiosis G. Heat shock protein 90 in neurodegenerative diseases. Mol. Neurodegener. 2010, 5:24.
-
(2010)
Mol. Neurodegener.
, vol.5
, pp. 24
-
-
Luo, W.1
Sun, W.2
Taldone, T.3
Rodina, A.4
Chiosis, G.5
-
32
-
-
20844444338
-
S-nitrosylation of Hsp90 promotes the inhibition of its ATPase and endothelial nitric oxide synthase regulatory activities
-
Martínez-Ruiz A., Villanueva L., González de Orduña C., López-Ferrer D., Higueras M.A., Tarín C., Rodríguez-Crespo I., Vázquez J., Lamas S. S-nitrosylation of Hsp90 promotes the inhibition of its ATPase and endothelial nitric oxide synthase regulatory activities. Proc. Natl. Acad. Sci. USA 2005, 102:8525-8530.
-
(2005)
Proc. Natl. Acad. Sci. USA
, vol.102
, pp. 8525-8530
-
-
Martínez-Ruiz, A.1
Villanueva, L.2
González de Orduña, C.3
López-Ferrer, D.4
Higueras, M.A.5
Tarín, C.6
Rodríguez-Crespo, I.7
Vázquez, J.8
Lamas, S.9
-
33
-
-
31344474558
-
The co-chaperone p23 arrests the Hsp90 ATPase cycle to trap client proteins
-
McLaughlin S.H., Sobott F., Yao Z.P., Zhang W., Nielsen P.R., Grossmann J.G., Laue E.D., Robinson C.V., Jackson S.E. The co-chaperone p23 arrests the Hsp90 ATPase cycle to trap client proteins. J. Mol. Biol. 2006, 356:746-758.
-
(2006)
J. Mol. Biol.
, vol.356
, pp. 746-758
-
-
McLaughlin, S.H.1
Sobott, F.2
Yao, Z.P.3
Zhang, W.4
Nielsen, P.R.5
Grossmann, J.G.6
Laue, E.D.7
Robinson, C.V.8
Jackson, S.E.9
-
34
-
-
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
-
35
-
-
84861005184
-
Corresponding functional dynamics across the Hsp90 Chaperone family: insights from a multiscale analysis of MD simulations
-
Morra G., Potestio R., Micheletti C., Colombo G. Corresponding functional dynamics across the Hsp90 Chaperone family: insights from a multiscale analysis of MD simulations. PLoS Comput. Biol. 2012, 8:e1002433.
-
(2012)
PLoS Comput. Biol.
, vol.8
-
-
Morra, G.1
Potestio, R.2
Micheletti, C.3
Colombo, G.4
-
36
-
-
77956766997
-
Ribosomal protein L2 associates with E. coli HtpG and activates its ATPase activity
-
Motojima-Miyazaki Y., Yoshida M., Motojima F. Ribosomal protein L2 associates with E. coli HtpG and activates its ATPase activity. Biochem. Biophys. Res. Commun. 2010, 400:241-245.
-
(2010)
Biochem. Biophys. Res. Commun.
, vol.400
, pp. 241-245
-
-
Motojima-Miyazaki, Y.1
Yoshida, M.2
Motojima, F.3
-
37
-
-
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
-
38
-
-
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
-
39
-
-
77958005847
-
Dynamics of heat shock protein 90 C-terminal dimerization is an important part of its conformational cycle
-
Ratzke C., Mickler M., Hellenkamp B., Buchner J., Hugel T. Dynamics of heat shock protein 90 C-terminal dimerization is an important part of its conformational cycle. Proc. Natl. Acad. Sci. USA 2010, 107:16101-16106.
-
(2010)
Proc. Natl. Acad. Sci. USA
, vol.107
, pp. 16101-16106
-
-
Ratzke, C.1
Mickler, M.2
Hellenkamp, B.3
Buchner, J.4
Hugel, T.5
-
40
-
-
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
-
41
-
-
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. 2002, 277:44905-44910.
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 44905-44910
-
-
Richter, K.1
Reinstein, J.2
Buchner, J.3
-
42
-
-
33744956564
-
Intrinsic inhibition of the Hsp90 ATPase activity
-
Richter K., Moser S., Hagn F., Friedrich R., Hainzl O., Heller M., Schlee S., Kessler H., Reinstein J., Buchner J. Intrinsic inhibition of the Hsp90 ATPase activity. J. Biol. Chem. 2006, 281:11301-11311.
-
(2006)
J. Biol. Chem.
, vol.281
, pp. 11301-11311
-
-
Richter, K.1
Moser, S.2
Hagn, F.3
Friedrich, R.4
Hainzl, O.5
Heller, M.6
Schlee, S.7
Kessler, H.8
Reinstein, J.9
Buchner, J.10
-
43
-
-
28844455588
-
Recent advances in understanding structure-function relationships in the type II topoisomerase mechanism
-
Schoeffler A.J., Berger J.M. Recent advances in understanding structure-function relationships in the type II topoisomerase mechanism. Biochem. Soc. Trans. 2005, 33:1465-1470.
-
(2005)
Biochem. Soc. Trans.
, vol.33
, pp. 1465-1470
-
-
Schoeffler, A.J.1
Berger, J.M.2
-
44
-
-
84878813471
-
The mitochondrial chaperone TRAP1 promotes neoplastic growth by inhibiting succinate dehydrogenase
-
Sciacovelli M., Guzzo G., Morello V., Frezza C., Zheng L., Nannini N., Calabrese F., Laudiero G., Esposito F., Landriscina M., et al. The mitochondrial chaperone TRAP1 promotes neoplastic growth by inhibiting succinate dehydrogenase. Cell Metab. 2013, 17:988-999.
-
(2013)
Cell Metab.
, vol.17
, pp. 988-999
-
-
Sciacovelli, M.1
Guzzo, G.2
Morello, V.3
Frezza, C.4
Zheng, L.5
Nannini, N.6
Calabrese, F.7
Laudiero, G.8
Esposito, F.9
Landriscina, M.10
-
45
-
-
0032883956
-
Hsp90 regulation of endothelial nitric oxide synthase contributes to vascular control in portal hypertension
-
Shah V., Wiest R., Garcia-Cardena G., Cadelina G., Groszmann R.J., Sessa W.C. Hsp90 regulation of endothelial nitric oxide synthase contributes to vascular control in portal hypertension. Am. J. Physiol. 1999, 277:G463-G468.
-
(1999)
Am. J. Physiol.
, vol.277
-
-
Shah, V.1
Wiest, R.2
Garcia-Cardena, G.3
Cadelina, G.4
Groszmann, R.J.5
Sessa, W.C.6
-
46
-
-
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
-
47
-
-
0028954475
-
Identification of a protein with homology to hsp90 that binds the type 1 tumor necrosis factor receptor
-
Song H.Y., Dunbar J.D., Zhang Y.X., Guo D., Donner D.B. Identification of a protein with homology to hsp90 that binds the type 1 tumor necrosis factor receptor. J. Biol. Chem. 1995, 270:3574-3581.
-
(1995)
J. Biol. Chem.
, vol.270
, pp. 3574-3581
-
-
Song, H.Y.1
Dunbar, J.D.2
Zhang, Y.X.3
Guo, D.4
Donner, D.B.5
-
48
-
-
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
-
49
-
-
56849131626
-
Species-dependent ensembles of conserved conformational states define the Hsp90 chaperone ATPase cycle
-
Southworth D.R., Agard D.A. Species-dependent ensembles of conserved conformational states define the Hsp90 chaperone ATPase cycle. Mol. Cell 2008, 32:631-640.
-
(2008)
Mol. Cell
, vol.32
, pp. 631-640
-
-
Southworth, D.R.1
Agard, D.A.2
-
50
-
-
79959344309
-
Client-loading conformation of the Hsp90 molecular chaperone revealed in the cryo-EM structure of the human Hsp90:Hop complex
-
Southworth D.R., Agard D.A. Client-loading conformation of the Hsp90 molecular chaperone revealed in the cryo-EM structure of the human Hsp90:Hop complex. Mol. Cell 2011, 42:771-781.
-
(2011)
Mol. Cell
, vol.42
, pp. 771-781
-
-
Southworth, D.R.1
Agard, D.A.2
-
51
-
-
79953308070
-
Substrate binding drives large-scale conformational changes in the Hsp90 molecular chaperone
-
Street T.O., Lavery L.A., Agard D.A. Substrate binding drives large-scale conformational changes in the Hsp90 molecular chaperone. Mol. Cell 2011, 42:96-105.
-
(2011)
Mol. Cell
, vol.42
, pp. 96-105
-
-
Street, T.O.1
Lavery, L.A.2
Agard, D.A.3
-
52
-
-
84855293594
-
Cross-monomer substrate contacts reposition the Hsp90 N-terminal domain and prime the chaperone activity
-
Street T.O., Lavery L.A., Verba K.A., Lee C.T., Mayer M.P., Agard D.A. Cross-monomer substrate contacts reposition the Hsp90 N-terminal domain and prime the chaperone activity. J. Mol. Biol. 2012, 415:3-15.
-
(2012)
J. Mol. Biol.
, vol.415
, pp. 3-15
-
-
Street, T.O.1
Lavery, L.A.2
Verba, K.A.3
Lee, C.T.4
Mayer, M.P.5
Agard, D.A.6
-
53
-
-
84861324339
-
Extent of structural asymmetry in homodimeric proteins: prevalence and relevance
-
Swapna L.S., Srikeerthana K., Srinivasan N. Extent of structural asymmetry in homodimeric proteins: prevalence and relevance. PLoS ONE 2012, 7:e36688.
-
(2012)
PLoS ONE
, vol.7
-
-
Swapna, L.S.1
Srikeerthana, K.2
Srinivasan, N.3
-
54
-
-
84865695733
-
Quantitative analysis of HSP90-client interactions reveals principles of substrate recognition
-
Taipale M., Krykbaeva I., Koeva M., Kayatekin C., Westover K.D., Karras G.I., Lindquist S. Quantitative analysis of HSP90-client interactions reveals principles of substrate recognition. Cell 2012, 150:987-1001.
-
(2012)
Cell
, vol.150
, pp. 987-1001
-
-
Taipale, M.1
Krykbaeva, I.2
Koeva, M.3
Kayatekin, C.4
Westover, K.D.5
Karras, G.I.6
Lindquist, S.7
-
55
-
-
84871458524
-
TRAP1 controls mitochondrial fusion/fission balance through Drp1 and Mff expression
-
Takamura H., Koyama Y., Matsuzaki S., Yamada K., Hattori T., Miyata S., Takemoto K., Tohyama M., Katayama T. TRAP1 controls mitochondrial fusion/fission balance through Drp1 and Mff expression. PLoS ONE 2012, 7:e51912.
-
(2012)
PLoS ONE
, vol.7
-
-
Takamura, H.1
Koyama, Y.2
Matsuzaki, S.3
Yamada, K.4
Hattori, T.5
Miyata, S.6
Takemoto, K.7
Tohyama, M.8
Katayama, T.9
-
56
-
-
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
-
58
-
-
84876862267
-
Molecular chaperone TRAP1 regulates a metabolic switch between mitochondrial respiration and aerobic glycolysis
-
Yoshida S., Tsutsumi S., Muhlebach G., Sourbier C., Lee M.J., Lee S., Vartholomaiou E., Tatokoro M., Beebe K., Miyajima N., et al. Molecular chaperone TRAP1 regulates a metabolic switch between mitochondrial respiration and aerobic glycolysis. Proc. Natl. Acad. Sci. USA 2013, 110:E1604-E1612.
-
(2013)
Proc. Natl. Acad. Sci. USA
, vol.110
-
-
Yoshida, S.1
Tsutsumi, S.2
Muhlebach, G.3
Sourbier, C.4
Lee, M.J.5
Lee, S.6
Vartholomaiou, E.7
Tatokoro, M.8
Beebe, K.9
Miyajima, N.10
-
59
-
-
84878529485
-
TRAP1 rescues PINK1 loss-of-function phenotypes
-
Zhang L., Karsten P., Hamm S., Pogson J.H., Müller-Rischart A.K., Exner N., Haass C., Whitworth A.J., Winklhofer K.F., Schulz J.B., Voigt A. TRAP1 rescues PINK1 loss-of-function phenotypes. Hum. Mol. Genet. 2013, 22:2829-2841.
-
(2013)
Hum. Mol. Genet.
, vol.22
, pp. 2829-2841
-
-
Zhang, L.1
Karsten, P.2
Hamm, S.3
Pogson, J.H.4
Müller-Rischart, A.K.5
Exner, N.6
Haass, C.7
Whitworth, A.J.8
Winklhofer, K.F.9
Schulz, J.B.10
Voigt, A.11
-
60
-
-
20044382800
-
Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone
-
Zhao R., Davey M., Hsu Y.C., Kaplanek P., Tong A., Parsons A.B., Krogan N., Cagney G., Mai D., Greenblatt J., et al. Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone. Cell 2005, 120:715-727.
-
(2005)
Cell
, vol.120
, pp. 715-727
-
-
Zhao, R.1
Davey, M.2
Hsu, Y.C.3
Kaplanek, P.4
Tong, A.5
Parsons, A.B.6
Krogan, N.7
Cagney, G.8
Mai, D.9
Greenblatt, J.10
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