PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 20829124-2 2010 An important role for Hsp90 is to facilitate the stable binding of steroid hormones to their respective receptors enabling the ligand-based signal to be carried to the nucleus and ultimately resulting in the up-regulation of gene expression. Steroids 67-83 heat shock protein 90 alpha family class A member 1 Homo sapiens 22-27 15046863-2 2004 It is known that in non-neuronal cells, the GFP-GR moves from cytoplasm to the nucleus in a steroid-dependent manner by a rapid, hsp90-dependent mechanism. Steroids 92-99 heat shock protein 90 alpha family class A member 1 Homo sapiens 129-134 19581287-8 2009 Importantly, GR cross-linked to the hsp90 heterocomplex was able to translocate to the nucleus in digitonin-permeabilized cells treated with steroid, suggesting that GR could pass through the pore in its untransformed state. Steroids 141-148 heat shock protein 90 alpha family class A member 1 Homo sapiens 36-41 18573821-10 2008 The amount of hsp90 in the GR complex in cytoplasm was significantly higher in steroid-resistant multiple sclerosis compared with steroid-sensitive multiple sclerosis. Steroids 79-86 heat shock protein 90 alpha family class A member 1 Homo sapiens 14-19 18573821-10 2008 The amount of hsp90 in the GR complex in cytoplasm was significantly higher in steroid-resistant multiple sclerosis compared with steroid-sensitive multiple sclerosis. Steroids 130-137 heat shock protein 90 alpha family class A member 1 Homo sapiens 14-19 16610357-3 2006 During GR-hsp90 heterocomplex assembly, the hydrophobic ligand-binding cleft is opened to access by steroid, and subsequent binding of steroid within the cleft triggers a transformation of the receptor such that it engages in more dynamic cycles of assembly/disassembly with hsp90 that are required for rapid dynein-dependent translocation to the nucleus. Steroids 100-107 heat shock protein 90 alpha family class A member 1 Homo sapiens 10-15 16610357-3 2006 During GR-hsp90 heterocomplex assembly, the hydrophobic ligand-binding cleft is opened to access by steroid, and subsequent binding of steroid within the cleft triggers a transformation of the receptor such that it engages in more dynamic cycles of assembly/disassembly with hsp90 that are required for rapid dynein-dependent translocation to the nucleus. Steroids 135-142 heat shock protein 90 alpha family class A member 1 Homo sapiens 10-15 16610357-3 2006 During GR-hsp90 heterocomplex assembly, the hydrophobic ligand-binding cleft is opened to access by steroid, and subsequent binding of steroid within the cleft triggers a transformation of the receptor such that it engages in more dynamic cycles of assembly/disassembly with hsp90 that are required for rapid dynein-dependent translocation to the nucleus. Steroids 135-142 heat shock protein 90 alpha family class A member 1 Homo sapiens 275-280 20166544-3 2010 We report here a 37-year-old female patient with HSP nephritis (HSPN) associated with steroid-resistant nephrotic syndrome and renal dysfunction despite conventional therapy. Steroids 86-93 heat shock protein 90 alpha family class A member 1 Homo sapiens 64-68 16431970-2 2006 GRalpha undergoes steroid-dependent nuclear translocation by associating with a heat shock protein (Hsp)90 multiprotein heterocomplex. Steroids 18-25 heat shock protein 90 alpha family class A member 1 Homo sapiens 80-106 16087666-9 2005 Thus, acetylation of hsp90 results in dynamic GR.hsp90 heterocomplex assembly/disassembly, and this is manifest in the cell as a approximately 100-fold shift to the right in the steroid dose response for gene activation. Steroids 178-185 heat shock protein 90 alpha family class A member 1 Homo sapiens 21-26 16087666-9 2005 Thus, acetylation of hsp90 results in dynamic GR.hsp90 heterocomplex assembly/disassembly, and this is manifest in the cell as a approximately 100-fold shift to the right in the steroid dose response for gene activation. Steroids 178-185 heat shock protein 90 alpha family class A member 1 Homo sapiens 49-54 15759036-0 2005 Regulation of glucocorticoid receptor steroid binding and trafficking by the hsp90/hsp70-based chaperone machinery: implications for clinical intervention. Steroids 38-45 heat shock protein 90 alpha family class A member 1 Homo sapiens 77-82 12563018-8 2003 Stepwise assembly experiments have shown that hsp70 and hsp40 first interact with the receptor in an ATP-dependent reaction to produce a receptor*hsp70*hsp40 complex that is "primed" to be activated to the steroid-binding state in a second ATP-dependent step with hsp90, Hop, and p23. Steroids 206-213 heat shock protein 90 alpha family class A member 1 Homo sapiens 264-269 15242338-3 2004 The hsp90-/hsp70-based chaperone machinery interacts with the unliganded glucocorticoid receptor to open the steroid-binding cleft to access by a steroid, and the machinery interacts in very dynamic fashion with the liganded, transformed receptor to facilitate its translocation along microtubular highways to the nucleus. Steroids 109-116 heat shock protein 90 alpha family class A member 1 Homo sapiens 4-9 15242338-3 2004 The hsp90-/hsp70-based chaperone machinery interacts with the unliganded glucocorticoid receptor to open the steroid-binding cleft to access by a steroid, and the machinery interacts in very dynamic fashion with the liganded, transformed receptor to facilitate its translocation along microtubular highways to the nucleus. Steroids 146-153 heat shock protein 90 alpha family class A member 1 Homo sapiens 4-9 12897402-6 2003 Up-regulation of HSP90, a steroid receptor chaperone, in the AD CP may indicate abnormal hormone receptor expression in this secretory tissue. Steroids 26-33 heat shock protein 90 alpha family class A member 1 Homo sapiens 17-22 12807878-0 2003 Visualization and mechanism of assembly of a glucocorticoid receptor.Hsp70 complex that is primed for subsequent Hsp90-dependent opening of the steroid binding cleft. Steroids 144-151 heat shock protein 90 alpha family class A member 1 Homo sapiens 113-118 12807878-1 2003 A minimal system of five proteins, hsp90, hsp70, Hop, hsp40, and p23, assembles glucocorticoid receptor (GR).hsp90 heterocomplexes and causes the simultaneous opening of the steroid binding cleft to access by steroid. Steroids 174-181 heat shock protein 90 alpha family class A member 1 Homo sapiens 35-40 12807878-1 2003 A minimal system of five proteins, hsp90, hsp70, Hop, hsp40, and p23, assembles glucocorticoid receptor (GR).hsp90 heterocomplexes and causes the simultaneous opening of the steroid binding cleft to access by steroid. Steroids 174-181 heat shock protein 90 alpha family class A member 1 Homo sapiens 109-114 12807878-1 2003 A minimal system of five proteins, hsp90, hsp70, Hop, hsp40, and p23, assembles glucocorticoid receptor (GR).hsp90 heterocomplexes and causes the simultaneous opening of the steroid binding cleft to access by steroid. Steroids 209-216 heat shock protein 90 alpha family class A member 1 Homo sapiens 35-40 12807878-1 2003 A minimal system of five proteins, hsp90, hsp70, Hop, hsp40, and p23, assembles glucocorticoid receptor (GR).hsp90 heterocomplexes and causes the simultaneous opening of the steroid binding cleft to access by steroid. Steroids 209-216 heat shock protein 90 alpha family class A member 1 Homo sapiens 109-114 11677765-1 2001 OBJECTIVE: To investigate the expression of glucocorticoid receptor (GR) and heat shock protein 90 (HSP90) mRNA in peripheral blood mononuclear cells (PBMCs) from steroid-sensitive (SS), steroid-dependent (SD) and steroid-resistant (SR) asthmatics patients, and to evaluate the role of GR and HSP90 in the pathogenesis of SR. METHODS: Reverse transcription-polymerase chain reaction (RT-PCR) was used to determine the expressions of GR and HSP90 mRNA in PBMC stimulated with IL-2 and/or IL-4 from 10 normal volunteers, 10 SS, 5 SD and 6 SR patients. Steroids 163-170 heat shock protein 90 alpha family class A member 1 Homo sapiens 77-98 12093808-1 2002 A minimal system of five purified proteins, hsp90, hsp70, Hop, hsp40, and p23, assembles glucocorticoid receptor (GR).hsp90 heterocomplexes and causes the simultaneous opening of the steroid binding cleft to access by steroid. Steroids 183-190 heat shock protein 90 alpha family class A member 1 Homo sapiens 44-49 12093808-1 2002 A minimal system of five purified proteins, hsp90, hsp70, Hop, hsp40, and p23, assembles glucocorticoid receptor (GR).hsp90 heterocomplexes and causes the simultaneous opening of the steroid binding cleft to access by steroid. Steroids 183-190 heat shock protein 90 alpha family class A member 1 Homo sapiens 118-123 12093808-1 2002 A minimal system of five purified proteins, hsp90, hsp70, Hop, hsp40, and p23, assembles glucocorticoid receptor (GR).hsp90 heterocomplexes and causes the simultaneous opening of the steroid binding cleft to access by steroid. Steroids 218-225 heat shock protein 90 alpha family class A member 1 Homo sapiens 44-49 12093808-1 2002 A minimal system of five purified proteins, hsp90, hsp70, Hop, hsp40, and p23, assembles glucocorticoid receptor (GR).hsp90 heterocomplexes and causes the simultaneous opening of the steroid binding cleft to access by steroid. Steroids 218-225 heat shock protein 90 alpha family class A member 1 Homo sapiens 118-123 12093808-9 2002 The rate-limiting step is the ATP-dependent opening of the steroid binding cleft after hsp90 binding. Steroids 59-66 heat shock protein 90 alpha family class A member 1 Homo sapiens 87-92 12093808-11 2002 The reported specific inhibitors of the C-terminal ATP site on hsp90 inhibit the generation of steroid binding, but they have other effects in this multiprotein system that could explain the inhibition. Steroids 95-102 heat shock protein 90 alpha family class A member 1 Homo sapiens 63-68 11677765-1 2001 OBJECTIVE: To investigate the expression of glucocorticoid receptor (GR) and heat shock protein 90 (HSP90) mRNA in peripheral blood mononuclear cells (PBMCs) from steroid-sensitive (SS), steroid-dependent (SD) and steroid-resistant (SR) asthmatics patients, and to evaluate the role of GR and HSP90 in the pathogenesis of SR. METHODS: Reverse transcription-polymerase chain reaction (RT-PCR) was used to determine the expressions of GR and HSP90 mRNA in PBMC stimulated with IL-2 and/or IL-4 from 10 normal volunteers, 10 SS, 5 SD and 6 SR patients. Steroids 163-170 heat shock protein 90 alpha family class A member 1 Homo sapiens 100-105 11803001-0 2001 [Glucocorticoid receptor and HSP 90 mRNA expression in peripheral blood mononuclear cell from steroid resistant asthmatics]. Steroids 94-101 heat shock protein 90 alpha family class A member 1 Homo sapiens 29-35 11803001-1 2001 OBJECTIVE: To investigate the expression of glucocorticoid receptor (GR) and HSP 90 mRNA in peripheral blood mononuclear cells (PBMC) from steroid-sensitive asthma (SS), steroid-dependant asthma (SD) and steroid-resistant asthma (SR) and assess the role of GR and HSP 90 in the pathogenesis of SR. METHODS: With reverse transcription-polymerase chain reaction (RT-PCR), expression of GR and HSP 90 mRNA were detected in PBMC without or with IL-2 and (or) IL-4 stimulation from 10 normal volunteers, 10 SS, 5 SD and 6 SR patients. Steroids 139-146 heat shock protein 90 alpha family class A member 1 Homo sapiens 77-83 11146632-7 2001 Here we show that CHIP abolishes the steroid-binding activity and transactivation potential of the glucocorticoid receptor, a well-characterized Hsp90 substrate, even though it has little effect on its synthesis. Steroids 37-44 heat shock protein 90 alpha family class A member 1 Homo sapiens 145-150 11170435-1 2001 hsp90 and hsp70 are essential components of a five-protein system, including also the nonessential cochaperones Hop, hsp40, and p23, that assembles glucocorticoid receptor (GR).hsp90 heterocomplexes and causes the simultaneous opening of the steroid binding pocket to access by steroid. Steroids 242-249 heat shock protein 90 alpha family class A member 1 Homo sapiens 0-5 11170435-1 2001 hsp90 and hsp70 are essential components of a five-protein system, including also the nonessential cochaperones Hop, hsp40, and p23, that assembles glucocorticoid receptor (GR).hsp90 heterocomplexes and causes the simultaneous opening of the steroid binding pocket to access by steroid. Steroids 242-249 heat shock protein 90 alpha family class A member 1 Homo sapiens 177-182 11170435-1 2001 hsp90 and hsp70 are essential components of a five-protein system, including also the nonessential cochaperones Hop, hsp40, and p23, that assembles glucocorticoid receptor (GR).hsp90 heterocomplexes and causes the simultaneous opening of the steroid binding pocket to access by steroid. Steroids 278-285 heat shock protein 90 alpha family class A member 1 Homo sapiens 0-5 11170435-1 2001 hsp90 and hsp70 are essential components of a five-protein system, including also the nonessential cochaperones Hop, hsp40, and p23, that assembles glucocorticoid receptor (GR).hsp90 heterocomplexes and causes the simultaneous opening of the steroid binding pocket to access by steroid. Steroids 278-285 heat shock protein 90 alpha family class A member 1 Homo sapiens 177-182 11170435-10 2001 This suggests that GR-bound hsp70 is also converted from the ATP-dependent to the ADP-dependent conformation while it cooperates with hsp90 to activate steroid binding activity. Steroids 152-159 heat shock protein 90 alpha family class A member 1 Homo sapiens 134-139 11123263-12 2001 Activation of HSF-1 by steroid hormones, resulting from a change in the interaction of HSP90 and HSF-1, represents a novel pathway for regulating expression of HSPs. Steroids 23-30 heat shock protein 90 alpha family class A member 1 Homo sapiens 87-92 10764743-0 2000 Stepwise assembly of a glucocorticoid receptor.hsp90 heterocomplex resolves two sequential ATP-dependent events involving first hsp70 and then hsp90 in opening of the steroid binding pocket. Steroids 167-174 heat shock protein 90 alpha family class A member 1 Homo sapiens 47-52 10764743-0 2000 Stepwise assembly of a glucocorticoid receptor.hsp90 heterocomplex resolves two sequential ATP-dependent events involving first hsp70 and then hsp90 in opening of the steroid binding pocket. Steroids 167-174 heat shock protein 90 alpha family class A member 1 Homo sapiens 143-148 10764743-2 2000 Two proteins, hsp90 and hsp70, are required for the activation of steroid binding activity that occurs with heterocomplex assembly, and three proteins, Hop, hsp40, p23, act as co-chaperones that enhance activation and assembly (Morishima, Y., Kanelakis, K. C., Silverstein, A.M., Dittmar, K. D., Estrada, L., and Pratt, W. B. Steroids 66-73 heat shock protein 90 alpha family class A member 1 Homo sapiens 14-19 10764743-8 2000 hsp90 is required for opening of the steroid binding pocket and is converted to its ATP-dependent conformation during this second step. Steroids 37-44 heat shock protein 90 alpha family class A member 1 Homo sapiens 0-5 10764743-10 2000 This conversion initiates the opening of the hydrophobic steroid binding pocket such that it can now accept the hydrophobic binding form of hsp90, which in turn must be converted to its ATP-dependent conformation for the pocket to be accessible by steroid. Steroids 57-64 heat shock protein 90 alpha family class A member 1 Homo sapiens 140-145 10764743-10 2000 This conversion initiates the opening of the hydrophobic steroid binding pocket such that it can now accept the hydrophobic binding form of hsp90, which in turn must be converted to its ATP-dependent conformation for the pocket to be accessible by steroid. Steroids 248-255 heat shock protein 90 alpha family class A member 1 Homo sapiens 140-145 10702249-2 2000 Hop binds independently to Hsp90 and to Hsp70 to form a Hsp90.Hop.Hsp70.Hsp40 complex that is sufficient to convert the GR to its steroid binding form, and this four-protein complex will form stable GR.Hsp90 heterocomplexes if p23 is added to the system (Dittmar, K. D., Banach, M., Galigniana, M. D., and Pratt, W. B. Steroids 130-137 heat shock protein 90 alpha family class A member 1 Homo sapiens 27-32 10702249-2 2000 Hop binds independently to Hsp90 and to Hsp70 to form a Hsp90.Hop.Hsp70.Hsp40 complex that is sufficient to convert the GR to its steroid binding form, and this four-protein complex will form stable GR.Hsp90 heterocomplexes if p23 is added to the system (Dittmar, K. D., Banach, M., Galigniana, M. D., and Pratt, W. B. Steroids 130-137 heat shock protein 90 alpha family class A member 1 Homo sapiens 56-61 10702249-2 2000 Hop binds independently to Hsp90 and to Hsp70 to form a Hsp90.Hop.Hsp70.Hsp40 complex that is sufficient to convert the GR to its steroid binding form, and this four-protein complex will form stable GR.Hsp90 heterocomplexes if p23 is added to the system (Dittmar, K. D., Banach, M., Galigniana, M. D., and Pratt, W. B. Steroids 130-137 heat shock protein 90 alpha family class A member 1 Homo sapiens 56-61 10702249-10 2000 By carrying out assembly in the presence of radiolabeled steroid to bind to the GR as soon as it is converted to the steroid binding state, we show that the folding change is brought about by only two essential components, Hsp90 and Hsp70, and that Hop, Hsp40, and p23 act as nonessential co-chaperones. Steroids 57-64 heat shock protein 90 alpha family class A member 1 Homo sapiens 223-228 10597896-11 1999 Interactions between Hsp90, histones, and high mobility group (HMG) protein-derived peptides raise the possibility of the involvement of Hsp90 in chromatin reorganization during steroid action, mitosis, or after cellular stress. Steroids 178-185 heat shock protein 90 alpha family class A member 1 Homo sapiens 21-26 10567384-7 1999 However, at molar ratios approaching stoichiometry with hsp70, BAG-1 produced a concentration-dependent inhibition of GR folding to the steroid-binding form with corresponding inhibition of GR.hsp90 heterocomplex assembly by the minimal five-protein chaperone system. Steroids 136-143 heat shock protein 90 alpha family class A member 1 Homo sapiens 193-198 9990042-1 1999 Hsp90, a molecular chaperone required for the functioning of glucocorticosteroid receptor (GR), ensures, by direct interaction, the conformational competence of the steroid-binding pocket. Steroids 73-80 heat shock protein 90 alpha family class A member 1 Homo sapiens 0-5 9880522-1 1999 It is established that the multiprotein heat shock protein 90 (hsp90)-based chaperone system acts on the ligand binding domain of the glucocorticoid receptor (GR) to form a GR.hsp90 heterocomplex and to convert the receptor ligand binding domain to the steroid-binding state. Steroids 253-260 heat shock protein 90 alpha family class A member 1 Homo sapiens 40-61 9880522-1 1999 It is established that the multiprotein heat shock protein 90 (hsp90)-based chaperone system acts on the ligand binding domain of the glucocorticoid receptor (GR) to form a GR.hsp90 heterocomplex and to convert the receptor ligand binding domain to the steroid-binding state. Steroids 253-260 heat shock protein 90 alpha family class A member 1 Homo sapiens 63-68 9880522-2 1999 Treatment of cells with the hsp90 inhibitor geldanamycin inactivates steroid binding activity and increases the rate of GR turnover. Steroids 69-76 heat shock protein 90 alpha family class A member 1 Homo sapiens 28-33 10597896-11 1999 Interactions between Hsp90, histones, and high mobility group (HMG) protein-derived peptides raise the possibility of the involvement of Hsp90 in chromatin reorganization during steroid action, mitosis, or after cellular stress. Steroids 178-185 heat shock protein 90 alpha family class A member 1 Homo sapiens 137-142 9228040-8 1997 These data support the view that hsp90 actively participates in steroid-induced signal transduction, and they suggest that geldanamycin affects receptor action without disrupting hsp90-containing heterocomplexes per se. Steroids 64-71 heat shock protein 90 alpha family class A member 1 Homo sapiens 33-38 9261129-7 1997 We have shown that hsp90, p60, and hsp70 are sufficient for carrying out the folding change that converts the glucocorticoid receptor (GR) hormone binding domain (HBD) from a non-steroid binding to a steroid binding conformation, but to form stable GR.hsp90 heterocomplexes, p23 must also be present in the incubation mix (Dittmar, K. D., and Pratt, W. B. Steroids 179-186 heat shock protein 90 alpha family class A member 1 Homo sapiens 19-24 9183567-7 1997 The observations that hsp90 binds to the receptors through their HBDs and that these domains can be fused to structurally different proteins bringing their function under hormonal control provided a powerful linkage between the hormonal regulation of receptor binding to hsp90 and the initial step in steroid hormone action. Steroids 301-316 heat shock protein 90 alpha family class A member 1 Homo sapiens 22-27 9183567-7 1997 The observations that hsp90 binds to the receptors through their HBDs and that these domains can be fused to structurally different proteins bringing their function under hormonal control provided a powerful linkage between the hormonal regulation of receptor binding to hsp90 and the initial step in steroid hormone action. Steroids 301-316 heat shock protein 90 alpha family class A member 1 Homo sapiens 271-276 9148915-1 1997 The initial hsp90.p60.hsp70-dependent step is sufficient for creating the steroid binding conformation. Steroids 74-81 heat shock protein 90 alpha family class A member 1 Homo sapiens 12-17 9148915-3 1997 The glucocorticoid receptor (GR) is bound to hsp90 via its hormone binding domain (HBD), which must be associated with hsp90 to have a steroid binding conformation. Steroids 135-142 heat shock protein 90 alpha family class A member 1 Homo sapiens 45-50 9148915-3 1997 The glucocorticoid receptor (GR) is bound to hsp90 via its hormone binding domain (HBD), which must be associated with hsp90 to have a steroid binding conformation. Steroids 135-142 heat shock protein 90 alpha family class A member 1 Homo sapiens 119-124 9148915-8 1997 In this work we show that when the GR is incubated with hsp90, hsp70, and p60, steroid binding sites are generated despite the absence of p23. Steroids 79-86 heat shock protein 90 alpha family class A member 1 Homo sapiens 56-61 9148915-11 1997 Mixture of purified rabbit hsp90 and hsp70 with bacterial lysate containing human p60 results in spontaneous formation of an hsp90.p60.hsp70 complex that can be adsorbed with anti-p60 antibody, and the resulting immune complex converts the GR HBD to a steroid binding state in an ATP-dependent and K+-dependent manner. Steroids 252-259 heat shock protein 90 alpha family class A member 1 Homo sapiens 27-32 9148915-11 1997 Mixture of purified rabbit hsp90 and hsp70 with bacterial lysate containing human p60 results in spontaneous formation of an hsp90.p60.hsp70 complex that can be adsorbed with anti-p60 antibody, and the resulting immune complex converts the GR HBD to a steroid binding state in an ATP-dependent and K+-dependent manner. Steroids 252-259 heat shock protein 90 alpha family class A member 1 Homo sapiens 125-130 9261129-7 1997 We have shown that hsp90, p60, and hsp70 are sufficient for carrying out the folding change that converts the glucocorticoid receptor (GR) hormone binding domain (HBD) from a non-steroid binding to a steroid binding conformation, but to form stable GR.hsp90 heterocomplexes, p23 must also be present in the incubation mix (Dittmar, K. D., and Pratt, W. B. Steroids 179-186 heat shock protein 90 alpha family class A member 1 Homo sapiens 252-257 9261129-7 1997 We have shown that hsp90, p60, and hsp70 are sufficient for carrying out the folding change that converts the glucocorticoid receptor (GR) hormone binding domain (HBD) from a non-steroid binding to a steroid binding conformation, but to form stable GR.hsp90 heterocomplexes, p23 must also be present in the incubation mix (Dittmar, K. D., and Pratt, W. B. Steroids 200-207 heat shock protein 90 alpha family class A member 1 Homo sapiens 19-24 9261129-7 1997 We have shown that hsp90, p60, and hsp70 are sufficient for carrying out the folding change that converts the glucocorticoid receptor (GR) hormone binding domain (HBD) from a non-steroid binding to a steroid binding conformation, but to form stable GR.hsp90 heterocomplexes, p23 must also be present in the incubation mix (Dittmar, K. D., and Pratt, W. B. Steroids 200-207 heat shock protein 90 alpha family class A member 1 Homo sapiens 252-257 9261129-17 1997 The ATP-dependent conformation of hsp90 is required for the hormone binding domain to have a steroid binding site, and binding of p23 to that state of hsp90 stabilizes the GR.hsp90 heterocomplex to inactivation and disassembly. Steroids 93-100 heat shock protein 90 alpha family class A member 1 Homo sapiens 34-39 9148915-14 1997 Our data suggest that hsp90, hsp70, and p60 work together as a chaperone complex that possesses all of the folding/unfolding activity necessary to generate the high affinity steroid binding conformation of the receptor. Steroids 174-181 heat shock protein 90 alpha family class A member 1 Homo sapiens 22-27 8939864-2 1996 The steroid aporeceptor complex contains the molecular chaperones Hsp90 and Hsp70, p48, the cyclophilin Cyp-40, and the associated proteins p23 and p60. Steroids 4-11 heat shock protein 90 alpha family class A member 1 Homo sapiens 66-71 8856970-2 1996 For steroid receptors, the hsp90 chaperone system determines both repression of transcriptional activity in the absence of hormone and the proper folding of the hormone binding domain to produce the steroid binding conformation. Steroids 4-11 heat shock protein 90 alpha family class A member 1 Homo sapiens 27-32 8776730-10 1996 Overall, these findings provide direct pharmacological evidence that hsp90 function is required to maintain both the hormone-binding activity and stability of the GR protein in intact cells and suggest that hsp90 function may provide a novel target for the modulation of steroid hormone signaling. Steroids 271-286 heat shock protein 90 alpha family class A member 1 Homo sapiens 69-74 8776730-10 1996 Overall, these findings provide direct pharmacological evidence that hsp90 function is required to maintain both the hormone-binding activity and stability of the GR protein in intact cells and suggest that hsp90 function may provide a novel target for the modulation of steroid hormone signaling. Steroids 271-286 heat shock protein 90 alpha family class A member 1 Homo sapiens 207-212 8621522-2 1996 The HBD also contains the contact region for the chaperone protein hsp90, which must be bound to the GR for it to have a steroid binding conformation. Steroids 121-128 heat shock protein 90 alpha family class A member 1 Homo sapiens 67-72 8621522-6 1996 We report that N-iodoacetyltyrosine (IAT) inactivates steroid binding activity of the immunopurified, untransformed GR.hsp90 complex in a manner that is prevented by the sulfhydryl reagents cysteine and dithiothreitol but is not reversed by them. Steroids 54-61 heat shock protein 90 alpha family class A member 1 Homo sapiens 119-124 7521210-1 1994 The nontransformed steroid receptors contain several non-steroid binding proteins, such as hsp90, hsp70, and p59. Steroids 19-26 heat shock protein 90 alpha family class A member 1 Homo sapiens 91-96 7706757-6 1995 Hsp90 may have a unique role, binding to the glucocorticoid receptor in a manner essential for proper steroid hormone action. Steroids 102-117 heat shock protein 90 alpha family class A member 1 Homo sapiens 0-5 7625750-0 1995 Connection between immunosuppressants and steroids via HSP90. Steroids 42-50 heat shock protein 90 alpha family class A member 1 Homo sapiens 55-60 7510997-4 1994 Immunopurification from cytosol of [3H]steroid-labeled tungstate-stabilized PR with anti-PR immunoadsorbent yielded "9S"-PR species in which hsp90, hsp70 and p59/HBI were present. Steroids 39-46 heat shock protein 90 alpha family class A member 1 Homo sapiens 141-146 8142313-6 1994 These results are consistent with (1) the possible involvement of the "A" region in the interaction of hsp90 with steroid receptors and (2) a role of B and Z regions in the hsp90 structure for maintaining the steroid binding property of the hGR. Steroids 114-121 heat shock protein 90 alpha family class A member 1 Homo sapiens 103-108 2191718-10 1990 These results support the proposal that hsp90 is required for the receptor to bind steroid and dissociation of hsp90 is sufficient to inactivate the unoccupied receptor. Steroids 83-90 heat shock protein 90 alpha family class A member 1 Homo sapiens 40-45 8466913-4 1993 The vicinally spaced dithiol lies in a region of the receptor that appears to be a contact site for hsp90, which is required for the high-affinity steroid binding conformation of the glucocorticoid receptor [Dalman, F. C., Scherrer, L. C., Taylor, L. P., Akil, H., & Pratt, W. B. Steroids 147-154 heat shock protein 90 alpha family class A member 1 Homo sapiens 100-105 1314085-5 1992 Using sedimentation gradient analysis, we showed that the interaction between hsp90 and the steroid binding subunit of MR is highly dependent upon the nature of the steroid ligand since the binding of aldosterone antagonists results in an easy release of hsp90. Steroids 92-99 heat shock protein 90 alpha family class A member 1 Homo sapiens 78-83 1314085-5 1992 Using sedimentation gradient analysis, we showed that the interaction between hsp90 and the steroid binding subunit of MR is highly dependent upon the nature of the steroid ligand since the binding of aldosterone antagonists results in an easy release of hsp90. Steroids 92-99 heat shock protein 90 alpha family class A member 1 Homo sapiens 255-260 1314085-5 1992 Using sedimentation gradient analysis, we showed that the interaction between hsp90 and the steroid binding subunit of MR is highly dependent upon the nature of the steroid ligand since the binding of aldosterone antagonists results in an easy release of hsp90. Steroids 165-172 heat shock protein 90 alpha family class A member 1 Homo sapiens 78-83 1314085-5 1992 Using sedimentation gradient analysis, we showed that the interaction between hsp90 and the steroid binding subunit of MR is highly dependent upon the nature of the steroid ligand since the binding of aldosterone antagonists results in an easy release of hsp90. Steroids 165-172 heat shock protein 90 alpha family class A member 1 Homo sapiens 255-260 1310944-4 1992 The complex isolated from HeLa cells contained 2.2 mol hsp90/mol steroid-binding subunit. Steroids 65-72 heat shock protein 90 alpha family class A member 1 Homo sapiens 55-60 2204090-1 1990 The functional importance of the interaction of hsp90 with receptors for steroid hormones in the action of these hormones has been suggested. Steroids 73-89 heat shock protein 90 alpha family class A member 1 Homo sapiens 48-53 2770294-2 1989 The steroid is believed to function by releasing the receptor from hsp90 allowing the receptor to bind to DNA and activate transcription. Steroids 4-11 heat shock protein 90 alpha family class A member 1 Homo sapiens 67-72 2130517-1 1990 The functional importance of the interaction of hsp90 with receptors for steroid hormones in the action of these hormones has been suggested. Steroids 73-89 heat shock protein 90 alpha family class A member 1 Homo sapiens 48-53 34420854-1 2021 Steroid receptors form soluble heterocomplexes with the 90-kDa heat-shock protein (Hsp90) and other chaperones and co-chaperones. Steroids 0-7 heat shock protein 90 alpha family class A member 1 Homo sapiens 83-88 34420854-4 2021 Upon steroid binding, receptors become localized to the nucleus via the transportosome, a retrotransport molecular machinery that comprises Hsp90, a high-molecular-weight immunophilin, and dynein motors. Steroids 5-12 heat shock protein 90 alpha family class A member 1 Homo sapiens 140-145 34432285-7 2022 Furthermore, the association of Hsp90 with steroid receptors and signaling proteins in patients with breast cancer directed research to focus on Hsp-based treatments. Steroids 43-50 heat shock protein 90 alpha family class A member 1 Homo sapiens 32-37 2770294-5 1989 However, increased levels of hsp90 in response to steroid were observed in a number of cell lines. Steroids 50-57 heat shock protein 90 alpha family class A member 1 Homo sapiens 29-34 2647745-9 1989 Under no conditions does an hsp90-free receptor bind steroid. Steroids 53-60 heat shock protein 90 alpha family class A member 1 Homo sapiens 28-33 2647745-10 1989 Receptor bound to hsp90 can be cleaved to the 27-kDa meroreceptor in the presence of molybdate with retention of both hsp90 and steroid-binding activity. Steroids 128-135 heat shock protein 90 alpha family class A member 1 Homo sapiens 18-23 3293991-2 1988 One is the demonstration that cellular 90K hsp (hsp-90) can complex with steroid receptors in vitro and inhibit their ability to interact with DNA, and second, the demonstration that in avian oviduct sex steroids can regulate the synthesis of hsp-108. Steroids 204-212 heat shock protein 90 alpha family class A member 1 Homo sapiens 48-54 2843290-7 1988 We speculate that the inhibitory effect of the unliganded steroid binding domain may be mediated by heat shock protein hsp90, which binds selectively to the unliganded receptor. Steroids 58-65 heat shock protein 90 alpha family class A member 1 Homo sapiens 119-124 3293991-3 1988 As yet, there is no report that sex steroids can regulate hsp-90 synthesis, especially in mammalian tissues. Steroids 36-44 heat shock protein 90 alpha family class A member 1 Homo sapiens 58-64 3293991-5 1988 We report that ovariectomy reduces the uterine concentration of hsp-90, and estradiol causes a time-dependent increase in uterine hsp-90 as early as 4 h after steroid administration, reaching a maximum increase of 4-fold between 18-24 h. The effect is specific to estrogens and not elicited by other steroid hormones. Steroids 159-166 heat shock protein 90 alpha family class A member 1 Homo sapiens 130-136 3293991-5 1988 We report that ovariectomy reduces the uterine concentration of hsp-90, and estradiol causes a time-dependent increase in uterine hsp-90 as early as 4 h after steroid administration, reaching a maximum increase of 4-fold between 18-24 h. The effect is specific to estrogens and not elicited by other steroid hormones. Steroids 300-307 heat shock protein 90 alpha family class A member 1 Homo sapiens 130-136 27769261-0 2016 Steroid resistance in COPD is associated with impaired molecular chaperone Hsp90 expression by pro-inflammatory lymphocytes. Steroids 0-7 heat shock protein 90 alpha family class A member 1 Homo sapiens 75-80 3374615-5 1988 Here we show that under conditions permitting minimal in vitro manipulation, the steroid-free glucocorticoid receptor in crude cytosol associates with the hsp90 heat shock protein (relative molecular mass Mr approximately equal to 90,000) to form a large 300K complex, rather than the 94K liganded receptor monomer. Steroids 81-88 heat shock protein 90 alpha family class A member 1 Homo sapiens 155-160 33846988-1 2022 Heat shock protein 90 (HSP90) is an indispensable molecular chaperone that facilitates the maturation of numerous oncoproteins in cancer cells, including protein kinases, ribonucleoproteins, steroid hormone receptors, and transcription factors. Steroids 191-198 heat shock protein 90 alpha family class A member 1 Homo sapiens 0-21 33846988-1 2022 Heat shock protein 90 (HSP90) is an indispensable molecular chaperone that facilitates the maturation of numerous oncoproteins in cancer cells, including protein kinases, ribonucleoproteins, steroid hormone receptors, and transcription factors. Steroids 191-198 heat shock protein 90 alpha family class A member 1 Homo sapiens 23-28 32776605-8 2021 During anoestrus, there was little immunostaining in the endometrium, suggesting that HSP90 is involved in the functional modulation of sex steroid receptors in cyclic mares. Steroids 140-147 heat shock protein 90 alpha family class A member 1 Homo sapiens 86-91 32776605-9 2021 Indeed, the function of HSP90 as a chaperone in the folding of proteins, such as steroid receptors, might explain the greater intensity of immunostaining during the oestrus and dioestrus phases, compared the anoestrus period. Steroids 81-88 heat shock protein 90 alpha family class A member 1 Homo sapiens 24-29 32612187-1 2020 The function of steroid receptors in the cell depends on the chaperone machinery of Hsp90, as Hsp90 primes steroid receptors for hormone binding and transcriptional activation. Steroids 16-23 heat shock protein 90 alpha family class A member 1 Homo sapiens 84-89 32612187-1 2020 The function of steroid receptors in the cell depends on the chaperone machinery of Hsp90, as Hsp90 primes steroid receptors for hormone binding and transcriptional activation. Steroids 16-23 heat shock protein 90 alpha family class A member 1 Homo sapiens 94-99 32612187-1 2020 The function of steroid receptors in the cell depends on the chaperone machinery of Hsp90, as Hsp90 primes steroid receptors for hormone binding and transcriptional activation. Steroids 107-114 heat shock protein 90 alpha family class A member 1 Homo sapiens 84-89 28700526-11 2017 An obvious decrease in urinary MIF concentrations among the children with HSPN was associated with steroid treatment. Steroids 99-106 heat shock protein 90 alpha family class A member 1 Homo sapiens 74-78 3312247-3 1987 When the receptors are transformed, the steroid-binding protein dissociates from hsp90. Steroids 40-47 heat shock protein 90 alpha family class A member 1 Homo sapiens 81-86 33245994-1 2021 Heat shock protein 90 (Hsp90) is a molecular chaperone that facilitates the maturation of its client proteins including protein kinases, transcription factors, and steroid hormone receptors which are structurally and functionally diverse. Steroids 164-171 heat shock protein 90 alpha family class A member 1 Homo sapiens 0-21 33245994-1 2021 Heat shock protein 90 (Hsp90) is a molecular chaperone that facilitates the maturation of its client proteins including protein kinases, transcription factors, and steroid hormone receptors which are structurally and functionally diverse. Steroids 164-171 heat shock protein 90 alpha family class A member 1 Homo sapiens 23-28 33390129-6 2021 Most of the family members of the latter group were first described as responsible of the immunosuppressive response or they were reported as members of the chaperone complex associated with HSP90 in steroid receptor oligomers. Steroids 200-207 heat shock protein 90 alpha family class A member 1 Homo sapiens 191-196 32612187-1 2020 The function of steroid receptors in the cell depends on the chaperone machinery of Hsp90, as Hsp90 primes steroid receptors for hormone binding and transcriptional activation. Steroids 107-114 heat shock protein 90 alpha family class A member 1 Homo sapiens 94-99 29941666-3 2018 Here, we examined the activity of human Hsp90alpha and Hsp90beta in a purified five-protein chaperone machinery that assembles glucocorticoid receptor (GR) Hsp90 heterocomplexes to generate high-affinity steroid-binding activity. Steroids 204-211 heat shock protein 90 alpha family class A member 1 Homo sapiens 40-50 29941666-3 2018 Here, we examined the activity of human Hsp90alpha and Hsp90beta in a purified five-protein chaperone machinery that assembles glucocorticoid receptor (GR) Hsp90 heterocomplexes to generate high-affinity steroid-binding activity. Steroids 204-211 heat shock protein 90 alpha family class A member 1 Homo sapiens 40-45 29941666-9 2018 We showed that the phosphomimetic mutant Hsp90alpha T5/7D has the same intrinsic chaperone activity as wild-type human Hsp90alpha in activation of GR steroid-binding activity by the five-protein machinery, supporting the conclusion that T5/7 phosphorylation does not affect Hsp90alpha chaperone activity. Steroids 150-157 heat shock protein 90 alpha family class A member 1 Homo sapiens 41-51 29941666-9 2018 We showed that the phosphomimetic mutant Hsp90alpha T5/7D has the same intrinsic chaperone activity as wild-type human Hsp90alpha in activation of GR steroid-binding activity by the five-protein machinery, supporting the conclusion that T5/7 phosphorylation does not affect Hsp90alpha chaperone activity. Steroids 150-157 heat shock protein 90 alpha family class A member 1 Homo sapiens 119-129 29941666-9 2018 We showed that the phosphomimetic mutant Hsp90alpha T5/7D has the same intrinsic chaperone activity as wild-type human Hsp90alpha in activation of GR steroid-binding activity by the five-protein machinery, supporting the conclusion that T5/7 phosphorylation does not affect Hsp90alpha chaperone activity. Steroids 150-157 heat shock protein 90 alpha family class A member 1 Homo sapiens 119-129 28508980-12 2016 We present here a rare case of steroid-resistant HSPN treated with IVCY and tonsillectomy, with reference to some recent findings. Steroids 31-38 heat shock protein 90 alpha family class A member 1 Homo sapiens 49-53 27769261-3 2016 GCR must be bound to molecular chaperones heat shock proteins (Hsp) 70 and Hsp90 to acquire a high-affinity steroid binding conformation, and traffic to the nucleus. Steroids 108-115 heat shock protein 90 alpha family class A member 1 Homo sapiens 75-80 27769261-10 2016 CONCLUSIONS: Loss of Hsp90 from cytotoxic/pro-inflammatory CD28nullCD8+ T and NKT-like cells could contribute to steroid resistance in COPD. Steroids 113-120 heat shock protein 90 alpha family class A member 1 Homo sapiens 21-26 24171710-11 2014 CONCLUSION: Leflunomide combined with steroids is effective for treating adult HSPN with nephrotic proteinuria. Steroids 38-46 heat shock protein 90 alpha family class A member 1 Homo sapiens 79-83 25986567-3 2015 This review summaries the function of these proteins as cochaperones in steroid receptor-Hsp90 complexes and elaborates on their role in alternative, Hsp90-dependent and -independent signalling pathways not involving steroid receptors. Steroids 72-79 heat shock protein 90 alpha family class A member 1 Homo sapiens 89-94 25986567-3 2015 This review summaries the function of these proteins as cochaperones in steroid receptor-Hsp90 complexes and elaborates on their role in alternative, Hsp90-dependent and -independent signalling pathways not involving steroid receptors. Steroids 72-79 heat shock protein 90 alpha family class A member 1 Homo sapiens 150-155 21799260-5 2011 The larger members, FKBP51 and FKBP52, interact with Hsp90 and exhibit chaperone activity that is shown to regulate steroid hormone signalling. Steroids 116-123 heat shock protein 90 alpha family class A member 1 Homo sapiens 53-58 22447868-1 2012 PURPOSE: To characterize the roles of the cytoskeleton and heat shock protein 90 (HSP90) in steroid-induced glucocorticoid receptor alpha (GRalpha) translocation in cultured human trabecular meshwork cells. Steroids 92-99 heat shock protein 90 alpha family class A member 1 Homo sapiens 59-80 22447868-1 2012 PURPOSE: To characterize the roles of the cytoskeleton and heat shock protein 90 (HSP90) in steroid-induced glucocorticoid receptor alpha (GRalpha) translocation in cultured human trabecular meshwork cells. Steroids 92-99 heat shock protein 90 alpha family class A member 1 Homo sapiens 82-87 21968922-5 2011 The GR has been a particularly useful system for studying hsp90 because the receptor must be bound to hsp90 to have an open ligand binding cleft that is accessible to steroid (3). Steroids 167-174 heat shock protein 90 alpha family class A member 1 Homo sapiens 58-63 21968922-7 2011 As found in the endogenous GR hsp90 heterocomplex, the GR ligand binding cleft is open and capable of binding steroid. Steroids 111-118 heat shock protein 90 alpha family class A member 1 Homo sapiens 31-36 21968922-8 2011 If hsp90 dissociates from the GR or if its function is inhibited, the receptor is unable to bind steroid and requires reconstitution of the GR hsp90 heterocomplex before steroid binding activity is restored (4) . Steroids 170-177 heat shock protein 90 alpha family class A member 1 Homo sapiens 3-8 21968922-16 2011 This method can be utilized to test the effects of various chaperone cofactors, novel proteins, and experimental hsp90 or GR inhibitors in order to determine their functional significance on hsp90-mediated steroid binding (8-11). Steroids 206-213 heat shock protein 90 alpha family class A member 1 Homo sapiens 191-196